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Conserved domains on  [gi|2490581668|gb|WGG03889|]
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malonyl-ACP O-methyltransferase BioC [Pseudomonas sp. GD03721]

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 ...
 36-274 1.69e-82

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: 247.59  E-value: 1.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  36 YDSVAELQRSVGNQLLAYLPA--SLQPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHARPQGGAA-HFIAGD 112
Cdd:TIGR02072   9 YDRHAKIQREMAKRLLALLKEkgIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENvQFICGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 113 AEALPLHDASVDLLFSSLALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCVGTLQELRDSWLAvdgfvHVNRFRRFEDYQQ 192
Cdd:TIGR02072  89 AEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-----HGLRYLSLDELKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 193 LCAASGlQVLTLQREAEVLHFPDLRSLTTSLKELGAHNLNPGRpgglTGRSRIRALIEAYECFRQAQGLPATYQVVYGVL 272
Cdd:TIGR02072 164 LLKNSF-ELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR----TSRKQLKAFLERYEQEFQPDGLPLTYHVVYGIA 238


                  ..
gi 2490581668 273 QK 274
Cdd:TIGR02072 239 KK 240
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 36-274 1.69e-82

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: 247.59  E-value: 1.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  36 YDSVAELQRSVGNQLLAYLPA--SLQPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHARPQGGAA-HFIAGD 112
Cdd:TIGR02072   9 YDRHAKIQREMAKRLLALLKEkgIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENvQFICGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 113 AEALPLHDASVDLLFSSLALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCVGTLQELRDSWLAvdgfvHVNRFRRFEDYQQ 192
Cdd:TIGR02072  89 AEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-----HGLRYLSLDELKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 193 LCAASGlQVLTLQREAEVLHFPDLRSLTTSLKELGAHNLNPGRpgglTGRSRIRALIEAYECFRQAQGLPATYQVVYGVL 272
Cdd:TIGR02072 164 LLKNSF-ELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR----TSRKQLKAFLERYEQEFQPDGLPLTYHVVYGIA 238


                  ..
gi 2490581668 273 QK 274
Cdd:TIGR02072 239 KK 240
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 21-274 3.16e-49

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 163.01  E-value: 3.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  21 DKRQVAASFSRAAASYDSVAELQRSVGNQLLAYLPASlQPLRWLDLGSGTGHFTRALAERYapSEGLAVDIAEGMLRHAR 100
Cdd:PRK10258    5 NKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQR-KFTHVLDAGCGPGWMSRYWRERG--SQVTALDLSPPMLAQAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 101 PQGGAAHFIAGDAEALPLHDASVDLLFSSLALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCVGTLQELRDSWLAVDGFVH 180
Cdd:PRK10258   82 QKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDERPH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 181 VNRFRRFEDYQQlcAASGLQVlTLQREAEVLHFPDLRSLTTSLKELGAHNLNPGRPGGLTGRSRIRALIEAYEcfrQAQG 260
Cdd:PRK10258  162 ANRFLPPDAIEQ--ALNGWRY-QHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWP---QQQG 235

                         250
                  ....*....|....*
gi 2490581668 261 -LPATYQVVYGVLQK 274
Cdd:PRK10258  236 rYPLTYHLFLGVIER 250
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 36-178 2.16e-32

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: 116.25  E-value: 2.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  36 YDSVAElQRSVGNQLLAYLPASlQPLRWLDLGSGTGHFTRALAERYApsEGLAVDIAEGMLRHAR----PQGGAAHFIAG 111
Cdd:COG2226     1 FDRVAA-RYDGREALLAALGLR-PGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELAReraaEAGLNVEFVVG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490581668 112 DAEALPLHDASVDLLFSSLALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCVGTLQELRDsWLAVDGF 178
Cdd:COG2226    77 DAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEE-LLAEAGF 142
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 64-153 1.46e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 96.86  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYApSEGLAVDIAEGMLRHAR----PQGGAAHFIAGDAEALPLHDASVDLLFSSLALQWCG--D 137
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERAReraaEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPdpD 80

                          90
                  ....*....|....*.
gi 2490581668 138 FPRVLSEAQRVLRPGG 153
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 62-158 1.14e-15

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: 70.92  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  62 RWLDLGSGTGHFTRALAERYAPsEGLAVDIAEGMLRHARPQGGAA-----HFIAGDAEALPL-HDASVDLLFSSLALQW- 134
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA-RVTGVDISPVALELARKAAAALladnvEVLKGDAEELPPeADESFDVIISDPPLHHl 79

                          90       100
                  ....*....|....*....|....
gi 2490581668 135 CGDFPRVLSEAQRVLRPGGVLAFT 158
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 36-274 1.69e-82

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: 247.59  E-value: 1.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  36 YDSVAELQRSVGNQLLAYLPA--SLQPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHARPQGGAA-HFIAGD 112
Cdd:TIGR02072   9 YDRHAKIQREMAKRLLALLKEkgIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENvQFICGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 113 AEALPLHDASVDLLFSSLALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCVGTLQELRDSWLAvdgfvHVNRFRRFEDYQQ 192
Cdd:TIGR02072  89 AEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-----HGLRYLSLDELKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 193 LCAASGlQVLTLQREAEVLHFPDLRSLTTSLKELGAHNLNPGRpgglTGRSRIRALIEAYECFRQAQGLPATYQVVYGVL 272
Cdd:TIGR02072 164 LLKNSF-ELLTLEEELITLSFDDPLDVLRHLKKTGANGLSSGR----TSRKQLKAFLERYEQEFQPDGLPLTYHVVYGIA 238


                  ..
gi 2490581668 273 QK 274
Cdd:TIGR02072 239 KK 240
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 21-274 3.16e-49

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 163.01  E-value: 3.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  21 DKRQVAASFSRAAASYDSVAELQRSVGNQLLAYLPASlQPLRWLDLGSGTGHFTRALAERYapSEGLAVDIAEGMLRHAR 100
Cdd:PRK10258    5 NKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQR-KFTHVLDAGCGPGWMSRYWRERG--SQVTALDLSPPMLAQAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 101 PQGGAAHFIAGDAEALPLHDASVDLLFSSLALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCVGTLQELRDSWLAVDGFVH 180
Cdd:PRK10258   82 QKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDERPH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 181 VNRFRRFEDYQQlcAASGLQVlTLQREAEVLHFPDLRSLTTSLKELGAHNLNPGRPGGLTGRSRIRALIEAYEcfrQAQG 260
Cdd:PRK10258  162 ANRFLPPDAIEQ--ALNGWRY-QHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWP---QQQG 235

                         250
                  ....*....|....*
gi 2490581668 261 -LPATYQVVYGVLQK 274
Cdd:PRK10258  236 rYPLTYHLFLGVIER 250
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 36-178 2.16e-32

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: 116.25  E-value: 2.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  36 YDSVAElQRSVGNQLLAYLPASlQPLRWLDLGSGTGHFTRALAERYApsEGLAVDIAEGMLRHAR----PQGGAAHFIAG 111
Cdd:COG2226     1 FDRVAA-RYDGREALLAALGLR-PGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELAReraaEAGLNVEFVVG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490581668 112 DAEALPLHDASVDLLFSSLALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCVGTLQELRDsWLAVDGF 178
Cdd:COG2226    77 DAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEE-LLAEAGF 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
59-158 3.16e-28

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 103.75  E-value: 3.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  59 QPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHARPQGGAAHFIAGDAEALPLhDASVDLLFSSLALQWCGDF 138
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDP-PEPFDLVVSNAALHWLPDH 79

                          90       100
                  ....*....|....*....|
gi 2490581668 139 PRVLSEAQRVLRPGGVLAFT 158
Cdd:COG4106    80 AALLARLAAALAPGGVLAVQ 99
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 64-153 1.46e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 96.86  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYApSEGLAVDIAEGMLRHAR----PQGGAAHFIAGDAEALPLHDASVDLLFSSLALQWCG--D 137
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERAReraaEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPdpD 80

                          90
                  ....*....|....*.
gi 2490581668 138 FPRVLSEAQRVLRPGG 153
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 64-157 4.49e-25

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 95.42  E-value: 4.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYApsEGLAVDIAEGMLRHARPQGGAA--HFIAGDAEALPLHDASVDLLFSSLALQWCGDFPRV 141
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREglTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 2490581668 142 LSEAQRVLRPGGVLAF 157
Cdd:pfam08241  79 LREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
64-201 7.93e-22

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 89.67  E-value: 7.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYAPSEGlaVDIAEGMLRHARPQGGAAHFIAGDAEALPLHDASVDLLFSSLALQWCGDFPRVLS 143
Cdd:COG4976    51 LDLGCGTGLLGEALRPRGYRLTG--VDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFA 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2490581668 144 EAQRVLRPGGVLAFtslcvgTLQELRDSwlavdgfvhvNRFRRFEDY-QQLCAASGLQV 201
Cdd:COG4976   129 GVARALKPGGLFIF------SVEDADGS----------GRYAHSLDYvRDLLAAAGFEV 171
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 50-158 8.76e-21

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: 85.45  E-value: 8.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  50 LLAYL-PASLQPLRWLDLGSGTGHFTRALAERYApsEGLAVDIAEGMLRHARPQGGA--AHFIAGDAEALPLHDASVDLL 126
Cdd:COG2227    14 LAALLaRLLPAGGRVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIARERAAElnVDFVQGDLEDLPLEDGSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2490581668 127 FSSLALQWCGDFPRVLSEAQRVLRPGGVLAFT 158
Cdd:COG2227    92 ICSEVLEHLPDPAALLRELARLLKPGGLLLLS 123
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 64-173 9.59e-18

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 79.81  E-value: 9.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYAPS-EGLAVDIAEGMLRHAR------PQGGAAHFIAGDAEALPLHDASVDLLFSSLALQWCG 136
Cdd:PRK00216   56 LDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGReklrdlGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVP 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2490581668 137 DFPRVLSEAQRVLRPGGVLA---FTSLCVGTLQELRDSWL 173
Cdd:PRK00216  136 DIDKALREMYRVLKPGGRLVileFSKPTNPPLKKAYDFYL 175
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 60-156 2.04e-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: 78.84  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  60 PLRWLDLGSGTGHFTRALAeRYAPSEG--LAVDIAEGMLRHARPQGGA---AHFIAGDAEALPLHDASVDLLFSSLALQW 134
Cdd:TIGR01934  40 GQKVLDVACGTGDLAIELA-KSAPDRGkvTGVDFSSEMLEVAKKKSELplnIEFIQADAEALPFEDNSFDAVTIAFGLRN 118

                          90       100
                  ....*....|....*....|..
gi 2490581668 135 CGDFPRVLSEAQRVLRPGGVLA 156
Cdd:TIGR01934 119 VTDIQKALREMYRVLKPGGRLV 140
PRK08317 PRK08317
hypothetical protein; Provisional
 62-153 1.07e-16

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 77.28  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  62 RWLDLGSGTGHFTRALAERYAP-SEGLAVDIAEGML----RHARPQGGAAHFIAGDAEALPLHDASVDLLFSSLALQWCG 136
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVGPeGRVVGIDRSEAMLalakERAAGLGPNVEFVRGDADGLPFPDGSFDAVRSDRVLQHLE 101

                          90
                  ....*....|....*..
gi 2490581668 137 DFPRVLSEAQRVLRPGG 153
Cdd:PRK08317  102 DPARALAEIARVLRPGG 118
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 62-158 1.14e-15

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: 70.92  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  62 RWLDLGSGTGHFTRALAERYAPsEGLAVDIAEGMLRHARPQGGAA-----HFIAGDAEALPL-HDASVDLLFSSLALQW- 134
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA-RVTGVDISPVALELARKAAAALladnvEVLKGDAEELPPeADESFDVIISDPPLHHl 79

                          90       100
                  ....*....|....*....|....
gi 2490581668 135 CGDFPRVLSEAQRVLRPGGVLAFT 158
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVLT 103
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 64-174 1.22e-15

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 72.06  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYAP-SEGLAVDIAEGMLR----HARPQG-GAAHFIAGDAEALP--LHDASVDLLFSSLALQWC 135
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGPnAEVVGIDISEEAIEkareNAQKLGfDNVEFEQGDIEELPelLEDDKFDVVISNCVLNHI 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2490581668 136 GDFPRVLSEAQRVLRPGGVLAFTSLCvgTLQELRDSWLA 174
Cdd:pfam13847  88 PDPDKVLQEILRVLKPGGRLIISDPD--SLAELPAHVKE 124
arsM PRK11873
arsenite methyltransferase;
56-223 2.67e-15

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 73.83  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  56 ASLQP-LRWLDLGSGTGhFTRALAERYAPSEG--LAVDIAEGMLRHARP---QGGAAH--FIAGDAEALPLHDASVDLLF 127
Cdd:PRK11873   73 AELKPgETVLDLGSGGG-FDCFLAARRVGPTGkvIGVDMTPEMLAKARAnarKAGYTNveFRLGEIEALPVADNSVDVII 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 128 SSLALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCV-GTL-QELRDSWLA----VDGFVHVnrfrrfEDYQQLCAASGLQV 201
Cdd:PRK11873  152 SNCVINLSPDKERVFKEAFRVLKPGGRFAISDVVLrGELpEEIRNDAELyagcVAGALQE------EEYLAMLAEAGFVD 225

                         170       180
                  ....*....|....*....|..
gi 2490581668 202 LTLQREaEVLHFPDLRSLTTSL 223
Cdd:PRK11873  226 ITIQPK-REYRIPDAREFLEDW 246
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-160 1.41e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 70.33  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  49 QLLAYLPASLQPLRWLDLGSGTGHFTRALAERYApSEGLAVDIAEGMLRHAR----PQG-GAAHFIAGD-AEALPLHDAS 122
Cdd:COG0500    16 ALLALLERLPKGGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARaraaKAGlGNVEFLVADlAELDPLPAES 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2490581668 123 VDLLFSSLALQWCGDFPR--VLSEAQRVLRPGGVLAFTSL 160
Cdd:COG0500    95 FDLVVAFGVLHHLPPEEReaLLRELARALKPGGVLLLSAS 134
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 64-155 8.24e-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: 8.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYAPSEGLAVDIAEGML-----RHARPQGGAAHFIAGDAEALPLHD-ASVDLLFSSLALQWCGD 137
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALeaareRLAALGLLNAVRVELFQLDLGELDpGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 2490581668 138 FPRVLSEAQRVLRPGGVL 155
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 50-156 4.76e-12

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 64.19  E-value: 4.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  50 LLAYLPAsLQPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHARPQGGAAHFIAGD-AEALPlhDASVDLLFS 128
Cdd:PRK01683   23 LLARVPL-ENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRLPDCQFVEADiASWQP--PQALDLIFA 99

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2490581668 129 SLALQWCGD----FPRVLSeaqrVLRPGGVLA 156
Cdd:PRK01683  100 NASLQWLPDhlelFPRLVS----LLAPGGVLA 127
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
58-155 9.39e-11

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 60.15  E-value: 9.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  58 LQPLRWLDLGSGTGHFTRALAERYAPS-EGLAVDIAEGMLRHARPQ---GGAAH--FIAGDAEALPLHDASVDLLFSSLA 131
Cdd:pfam01209  41 KRGNKFLDVAGGTGDWTFGLSDSAGSSgKVVGLDINENMLKEGEKKakeEGKYNieFLQGNAEELPFEDDSFDIVTISFG 120

                          90       100
                  ....*....|....*....|....
gi 2490581668 132 LQWCGDFPRVLSEAQRVLRPGGVL 155
Cdd:pfam01209 121 LRNFPDYLKVLKEAFRVLKPGGRV 144
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 64-159 1.76e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 58.02  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYApSEGLAVDIAEGMLRHARPQGGAA------HFIAGDAEALPLhDASVDLLFSSLALQWCGD 137
Cdd:COG2230    56 LDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAEAgladrvEVRLADYRDLPA-DGQFDAIVSIGMFEHVGP 133

                          90       100
                  ....*....|....*....|....
gi 2490581668 138 --FPRVLSEAQRVLRPGGVLAFTS 159
Cdd:COG2230   134 enYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-203 3.73e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 57.44  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  50 LLAYLPASLQPLRWLDLGSGTGHFTRALAERYAPSEGlaVDIAEGMLRHARPQggAAHFIAGDAEALPLHDASvDLLFSS 129
Cdd:pfam13489  13 LLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTG--VDPSPIAIERALLN--VRFDQFDEQEAAVPAGKF-DVIVAR 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2490581668 130 LALQWCGDFPRVLSEAQRVLRPGGVLAFTSLCV--GTLQELRDSWLAVDGFVHVNRFRRfEDYQQLCAASGLQVLT 203
Cdd:pfam13489  88 EVLEHVPDPPALLRQIAALLKPGGLLLLSTPLAsdEADRLLLEWPYLRPRNGHISLFSA-RSLKRLLEEAGFEVVS 162
PRK05785 PRK05785
hypothetical protein; Provisional
 60-150 2.86e-08

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 53.15  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  60 PLRWLDLGSGTGHFTRALAERYaPSEGLAVDIAEGMLRHArpqggaahFIAGDA-----EALPLHDASVDLLFSSLALQW 134
Cdd:PRK05785   52 PKKVLDVAAGKGELSYHFKKVF-KYYVVALDYAENMLKMN--------LVADDKvvgsfEALPFRDKSFDVVMSSFALHA 122

                          90
                  ....*....|....*.
gi 2490581668 135 CGDFPRVLSEAQRVLR 150
Cdd:PRK05785  123 SDNIEKVIAEFTRVSR 138
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
66-158 5.68e-08

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 51.75  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  66 LGSGTGHFTRALAERYAPSEGL-AVDIAEGMLRHARPQGGAAHFIAGDAEALP-----LHDASVDLLFSSLALQWcgdFP 139
Cdd:COG3963    52 LGPGTGVFTRAILARGVPDARLlAVEINPEFAEHLRRRFPRVTVVNGDAEDLAellaeHGIGKVDAVVSGLPLLS---FP 128

                          90       100
                  ....*....|....*....|....*
gi 2490581668 140 -----RVLSEAQRVLRPGGV-LAFT 158
Cdd:COG3963   129 pelrrAILDAAFRVLAPGGVfVQFT 153
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
48-155 4.04e-07

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 49.96  E-value: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  48 NQLLAYLPAslQPLRWLDLGSGTGHFTRALAERyapseGLAV---DIAEGML----RHARPQG--GAAHFIAGDAEALPL 118
Cdd:PRK11036   35 DRLLAELPP--RPLRVLDAGGGEGQTAIKLAEL-----GHQVilcDLSAEMIqrakQAAEAKGvsDNMQFIHCAAQDIAQ 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2490581668 119 H-DASVDLLFSSLALQWCGDFPRVLSEAQRVLRPGGVL 155
Cdd:PRK11036  108 HlETPVDLILFHAVLEWVADPKSVLQTLWSVLRPGGAL 145
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 49-157 4.36e-07

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 48.64  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  49 QLLAYLPASLQPLRWLDLGSGTGHFTRALAeRYAPSEG--LAVDIAEGMLRHARP---QGGAAH---FIAGDA-EALP-L 118
Cdd:COG4122     6 RLLYLLARLLGAKRILEIGTGTGYSTLWLA-RALPDDGrlTTIEIDPERAAIAREnfaRAGLADrirLILGDAlEVLPrL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2490581668 119 HDASVDLLFsslalqwC----GDFPRVLSEAQRVLRPGGVLAF 157
Cdd:COG4122    85 ADGPFDLVF-------IdadkSNYPDYLELALPLLRPGGLIVA 120
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 50-157 9.40e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 48.92  E-value: 9.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  50 LLAYLPAsLQPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHARPQGgaAHFIAGDAEA-LPLHDasVDLLFS 128
Cdd:PRK14103   21 LLARVGA-ERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARERG--VDARTGDVRDwKPKPD--TDVVVS 95

                          90       100
                  ....*....|....*....|....*....
gi 2490581668 129 SLALQWCGDFPRVLSEAQRVLRPGGVLAF 157
Cdd:PRK14103   96 NAALQWVPEHADLLVRWVDELAPGSWIAV 124
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 59-155 1.53e-06

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 47.83  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  59 QPLrWLDLGSGTGHFTRALAERYaPSEG-LAVDI-AEGM---LRHARPQGGA-AHFIAGDAEALP--LHDASVD---LLF 127
Cdd:COG0220    33 APL-VLEIGFGKGEFLVELAAAN-PDINfIGIEVhEPGVakaLKKAEEEGLTnVRLLRGDAVELLelFPDGSLDriyLNF 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2490581668 128 SslalqwcgD-------------FPRVLSEAQRVLRPGGVL 155
Cdd:COG0220   111 P--------DpwpkkrhhkrrlvQPEFLALLARVLKPGGEL 143
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 87-159 6.29e-06

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: 45.32  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  87 LAVDIAEGMLRHAR-----PQGGAAHFIAGDAEALPLHDASVDLLfsslalqwCGDFP-----------------RVLSE 144
Cdd:COG1041    52 IGSDIDPKMVEGARenlehYGYEDADVIRGDARDLPLADESVDAI--------VTDPPygrsskisgeellelyeKALEE 123

                          90
                  ....*....|....*
gi 2490581668 145 AQRVLRPGGVLAFTS 159
Cdd:COG1041   124 AARVLKPGGRVVIVT 138
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 51-157 6.97e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 46.30  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  51 LAYLPASlQPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHAR----PQGGAA--HFIAGDA-EALPlHDASV 123
Cdd:COG2890   105 LALLPAG-APPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARrnaeRLGLEDrvRFLQGDLfEPLP-GDGRF 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2490581668 124 DLLFS----------------------SLALqWCG----DFPR-VLSEAQRVLRPGGVLAF 157
Cdd:COG2890   183 DLIVSnppyipedeiallppevrdhepRLAL-DGGedglDFYRrIIAQAPRLLKPGGWLLL 242
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 42-155 1.04e-05

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 45.67  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  42 LQRSVGNQLLAYLPASLQPLrwLDLGSGTGHFTRALAERYAPSEGLAV---DIAEGMLRHARPQGGAAHFIAGDAEALPL 118
Cdd:PRK11088   70 LRDAVANLLAERLDEKATAL--LDIGCGEGYYTHALADALPEITTMQLfglDISKVAIKYAAKRYPQVTFCVASSHRLPF 147

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2490581668 119 HDASVDLLFSSLAlqwcgdfPRVLSEAQRVLRPGGVL 155
Cdd:PRK11088  148 ADQSLDAIIRIYA-------PCKAEELARVVKPGGIV 177
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 48-116 3.39e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 44.06  E-value: 3.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2490581668  48 NQLLAYLPAS--LQPLRWLDLGSGTGHFTRALAERYApsEGLAVDIAEGML----RHARPQGGAA--HFIAGDAEAL 116
Cdd:PRK07580   50 DTVLSWLPADgdLTGLRILDAGCGVGSLSIPLARRGA--KVVASDISPQMVeearERAPEAGLAGniTFEVGDLESL 124
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
51-128 1.08e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 42.20  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  51 LAYLPASLQPLRWLDLGSGTGHFTRAlAERYAPSEGLAVDIAEGMLRHARP----QGGAAHFIAGDAEALPLhDASVDLL 126
Cdd:COG2263    37 LAYLRGDIEGKTVLDLGCGTGMLAIG-AALLGAKKVVGVDIDPEALEIAREnaerLGVRVDFIRADVTRIPL-GGSVDTV 114


                  ..
gi 2490581668 127 FS 128
Cdd:COG2263   115 VM 116
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 40-161 1.15e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 43.20  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  40 AELQRSVGNQLLAYLPaSLQPLRWLDLGSGTGHFTRALAERYApsEGLAVDIAEGMLRHARPQGGA---AHFIAGD--AE 114
Cdd:PLN02336   19 SDLDKEERPEILSLLP-PYEGKSVLELGAGIGRFTGELAKKAG--QVIALDFIESVIKKNESINGHyknVKFMCADvtSP 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2490581668 115 ALPLHDASVDLLFSSLALQWCGDfPRVLSEAQRV---LRPGGVLAFTSLC 161
Cdd:PLN02336   96 DLNISDGSVDLIFSNWLLMYLSD-KEVENLAERMvkwLKVGGYIFFRESC 144
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
109-155 3.47e-04

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 40.23  E-value: 3.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2490581668 109 IAGDA-EALPLHDASVDLLFSSLALQ--WCGDFPRVLSEAQRVLRPGGVL 155
Cdd:COG4627    32 IVGDLtDPLPFPDNSVDAIYSSHVLEhlDYEEAPLALKECYRVLKPGGIL 81
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 52-154 4.53e-04

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 41.03  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  52 AYLPASL--QPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHAR--PQGGAAHFIAGDAEALPLHDASVDLLF 127
Cdd:PLN02490  104 ALEPADLsdRNLKVVDVGGGTGFTTLGIVKHVDAKNVTILDQSPHQLAKAKqkEPLKECKIIEGDAEDLPFPTDYADRYV 183

                          90       100
                  ....*....|....*....|....*..
gi 2490581668 128 SSLALQWCGDFPRVLSEAQRVLRPGGV 154
Cdd:PLN02490  184 SAGSIEYWPDPQRGIKEAYRVLKIGGK 210
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 50-205 4.86e-04

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: 40.51  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  50 LLAYLPASLQPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHAR------PQGGAAHFIAGDAEALP--LHDA 121
Cdd:COG4123    28 LLAAFAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARrnvalnGLEDRITVIHGDLKEFAaeLPPG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668 122 SVDLLFS------------------SLALQW-CGDFPRVLSEAQRVLRPGGVLAftslcvgtlqelrdswlavdgFVHvn 182
Cdd:COG4123   108 SFDLVVSnppyfkagsgrkspdearAIARHEdALTLEDLIRAAARLLKPGGRFA---------------------LIH-- 164

                         170       180
                  ....*....|....*....|...
gi 2490581668 183 RFRRFEDYQQLCAASGLQVLTLQ 205
Cdd:COG4123   165 PAERLAEILAALRKYGLGPKRLR 187
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 50-155 8.45e-04

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: 39.40  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  50 LLAYLPASLQPlRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHAR-----PQGGAAHFIAGDAeALPLHDASVD 124
Cdd:COG2813    41 LLEHLPEPLGG-RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARanaaaNGLENVEVLWSDG-LSGVPDGSFD 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2490581668 125 LLFS----------SLALQWcgdfpRVLSEAQRVLRPGGVL 155
Cdd:COG2813   119 LILSnppfhagravDKEVAH-----ALIADAARHLRPGGEL 154
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 59-157 1.24e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.37  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  59 QPLRWLDLGSGTGHFTRALAERYAPSEGLAVDIAEGMLRHAR-----PQGGAAHFIAGDAEAlPLHDASVDLLFS----- 128
Cdd:PRK09328  108 EPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARrnakhGLGARVEFLQGDWFE-PLPGGRFDLIVSnppyi 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2490581668 129 -----------------SLALqwCG-----DFPR-VLSEAQRVLRPGGVLAF 157
Cdd:PRK09328  187 peadihllqpevrdhepHLAL--FGgedglDFYRrIIEQAPRYLKPGGWLLL 236
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 64-155 2.26e-03

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: 37.95  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  64 LDLGSGTGHFTRALAERYAPSeGLAVDIAEGMLRHARPQGGaAHFIAGDAEALPLHDA-------SVDLLFSSLA----L 132
Cdd:pfam01728  26 LDLGAAPGGWSQVALQRGAGK-VVGVDLGPMQLWKPRNDPG-VTFIQGDIRDPETLDLleellgrKVDLVLSDGSpfisG 103

                          90       100       110
                  ....*....|....*....|....*....|
gi 2490581668 133 QWCGDFPR--VLSEAQ-----RVLRPGGVL 155
Cdd:pfam01728 104 NKVLDHLRslDLVKAAlevalELLRKGGNF 133
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
37-130 7.06e-03

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 37.24  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2490581668  37 DSVAELqrsvgnqlLAYLPASL---QPLRWLDLGSGTGHFTRALAERYA-PSEGLAVDIAEGMLR----HARPQGGAAHF 108
Cdd:COG0827    98 DAIGLL--------IGYLVEKFtkkEGLRILDPAVGTGNLLTTVLNQLKkKVNAYGVEVDDLLIRlaavLANLQGHPVEL 169

                          90       100
                  ....*....|....*....|..
gi 2490581668 109 IAGDAEAlPLHDASVDLLFSSL 130
Cdd:COG0827   170 FHQDALQ-PLLIDPVDVVISDL 190
 
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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