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Conserved domains on  [gi|487940766|ref|WP_002014232|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Bacillus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 84-205 2.12e-25

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


:

Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 98.91  E-value: 2.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  84 VIEHLQLQGEEKILEVGCANGKFLSLLQTNGhkGQLTGFDQSKTMISEA----AITNNTIEWKLGDASKLPFEANCYDLI 159
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELAreraAEAGLNVEFVVGDAEDLPFPDGSFDLV 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 487940766 160 IARHMLYHMKDVEKTIQGFHKVIRPGGSLLATTNSKVSMPRIVEMC 205
Cdd:COG2226   92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 84-205 2.12e-25

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 98.91  E-value: 2.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  84 VIEHLQLQGEEKILEVGCANGKFLSLLQTNGhkGQLTGFDQSKTMISEA----AITNNTIEWKLGDASKLPFEANCYDLI 159
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELAreraAEAGLNVEFVVGDAEDLPFPDGSFDLV 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 487940766 160 IARHMLYHMKDVEKTIQGFHKVIRPGGSLLATTNSKVSMPRIVEMC 205
Cdd:COG2226   92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 97-189 3.88e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 85.79  E-value: 3.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766   97 LEVGCANGKFLSLLQTNGHkgQLTGFDQSKTMISEA--AITNNTIEWKLGDASKLPFEANCYDLIIARHMLYHMKDVEKT 174
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAreKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*
gi 487940766  175 IQGFHKVIRPGGSLL 189
Cdd:pfam08241  79 LREIARVLKPGGILI 93
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 95-191 4.66e-11

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: 58.98  E-value: 4.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  95 KILEVGCANGKFLSLLQtNGHKGQLTGFDQSKTMISEAAITNNT-----IEWKLGDASKLPFEA-NCYDLIIARHMLYH- 167
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAAlladnVEVLKGDAEELPPEAdESFDVIISDPPLHHl 79

                         90       100
                 ....*....|....*....|....
gi 487940766 168 MKDVEKTIQGFHKVIRPGGSLLAT 191
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 82-190 9.97e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 60.72  E-value: 9.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  82 EVVIEHLQLQGEEKILEVGCANGKFL-SLLQTNGHKGQLTGFDQSKTMISEA--AITNN--TIEWKLGDASKLPFEANCY 156
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDArELARRVGPEGRVVGIDRSEAMLALAkeRAAGLgpNVEFVRGDADGLPFPDGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 487940766 157 DLIIARHMLYHMKDVEKTIQGFHKVIRPGGSLLA 190
Cdd:PRK08317  89 DAVRSDRVLQHLEDPARALAEIARVLRPGGRVVV 122
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
94-190 8.92e-04

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 40.09  E-value: 8.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766    94 EKILEVGCANGKFLSLLQTNGHKGQLTGFDQSKtmiSEAAITNNTIEWKL---------GDASKLPFEANcYDLIIARHM 164
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPHLQLHGYTISP---EQAEVGRERIRALGlqgririfyRDSAKDPFPDT-YDLVFGFEV 76

                           90       100
                   ....*....|....*....|....*.
gi 487940766   165 LYHMKDVEKTIQGFHKVIRPGGSLLA 190
Cdd:smart00828  77 IHHIKDKMDLFSNISRHLKDGGHLVL 102
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 84-205 2.12e-25

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 98.91  E-value: 2.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  84 VIEHLQLQGEEKILEVGCANGKFLSLLQTNGhkGQLTGFDQSKTMISEA----AITNNTIEWKLGDASKLPFEANCYDLI 159
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELAreraAEAGLNVEFVVGDAEDLPFPDGSFDLV 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 487940766 160 IARHMLYHMKDVEKTIQGFHKVIRPGGSLLATTNSKVSMPRIVEMC 205
Cdd:COG2226   92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 95-192 7.49e-22

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: 88.92  E-value: 7.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  95 KILEVGCANGKFLSLLQTNGHkgQLTGFDQSKTMISEA--AITNNTIEWKLGDASKLPFEANCYDLIIARHMLYHMKDVE 172
Cdd:COG2227   27 RVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIAreRAAELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHLPDPA 104

                         90       100
                 ....*....|....*....|
gi 487940766 173 KTIQGFHKVIRPGGSLLATT 192
Cdd:COG2227  105 ALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 97-189 3.88e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 85.79  E-value: 3.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766   97 LEVGCANGKFLSLLQTNGHkgQLTGFDQSKTMISEA--AITNNTIEWKLGDASKLPFEANCYDLIIARHMLYHMKDVEKT 174
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAreKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*
gi 487940766  175 IQGFHKVIRPGGSLL 189
Cdd:pfam08241  79 LREIARVLKPGGILI 93
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 96-186 8.48e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 82.23  E-value: 8.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766   96 ILEVGCANGKFLSLLQTNGHkGQLTGFDQSKTMISEA----AITNNTIEWKLGDASKLPFEANCYDLIIARHMLYHM--K 169
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERAreraAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdP 79

                          90
                  ....*....|....*..
gi 487940766  170 DVEKTIQGFHKVIRPGG 186
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
94-192 2.22e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 76.02  E-value: 2.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  94 EKILEVGCANGKFLSLLQTNGHKGQLTGFDQSKTMISEAAITNNTIEWKLGDASKLPFEANcYDLIIARHMLYHMKDVEK 173
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEP-FDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*....
gi 487940766 174 TIQGFHKVIRPGGSLLATT 192
Cdd:COG4106   82 LLARLAAALAPGGVLAVQV 100
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
51-194 6.44e-16

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 74.26  E-value: 6.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  51 NDVKRQYN-VSDHLQTRIDTHKHYEEKQVNVDEVvIEHLQLQGEEKILEVGCANGKFLSLLQTNGHKgqLTGFDQSKTMI 129
Cdd:COG4976    5 AYVEALFDqYADSYDAALVEDLGYEAPALLAEEL-LARLPPGPFGRVLDLGCGTGLLGEALRPRGYR--LTGVDLSEEML 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487940766 130 SEAAITNNTIEWKLGDASKLPFEANCYDLIIARHMLYHMKDVEKTIQGFHKVIRPGGSLLATTNS 194
Cdd:COG4976   82 AKAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVED 146
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 95-192 8.01e-14

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 68.22  E-value: 8.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766   95 KILEVGCANGKFLSLLQTNGHkgQLTGFDQSKTMISEAAITNNTiewKLGDASKLPFEANCYDLIIARHMLYHMKDVEKT 174
Cdd:pfam13489  25 RVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERALLNVRF---DQFDEQEAAVPAGKFDVIVAREVLEHVPDPPAL 99

                          90
                  ....*....|....*...
gi 487940766  175 IQGFHKVIRPGGSLLATT 192
Cdd:pfam13489 100 LRQIAALLKPGGLLLLST 117
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 72-191 7.48e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 66.09  E-value: 7.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  72 HYEEKQVNVDEVVIEHLQLQGEEKILEVGCANGKFLSLLqTNGHKGQLTGFDQSKTMISEA-----AITNNTIEWKLGDA 146
Cdd:COG0500    6 YSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLAL-AARFGGRVIGIDLSPEAIALAraraaKAGLGNVEFLVADL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 487940766 147 SKL-PFEANCYDLIIARHMLYHMKDVE--KTIQGFHKVIRPGGSLLAT 191
Cdd:COG0500   85 AELdPLPAESFDLVVAFGVLHHLPPEEreALLRELARALKPGGVLLLS 132
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 95-192 2.75e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 63.59  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766   95 KILEVGCANGKFLSLL-QTNGHKGQLTGFDQSKTMISEA-------AITNntIEWKLGDASKLP--FEANCYDLIIARHM 164
Cdd:pfam13847   6 RVLDLGCGTGHLSFELaEELGPNAEVVGIDISEEAIEKArenaqklGFDN--VEFEQGDIEELPelLEDDKFDVVISNCV 83

                          90       100
                  ....*....|....*....|....*...
gi 487940766  165 LYHMKDVEKTIQGFHKVIRPGGSLLATT 192
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISD 111
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 97-188 3.06e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 62.00  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766   97 LEVGCANGKFLSLLQTNGHKGQLTGFDQSKTMISEAA--------ITNNTIEWKLGDASKLPFEAncYDLIIARHMLYHM 168
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARerlaalglLNAVRVELFQLDLGELDPGS--FDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|
gi 487940766  169 KDVEKTIQGFHKVIRPGGSL 188
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 95-191 4.66e-11

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: 58.98  E-value: 4.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  95 KILEVGCANGKFLSLLQtNGHKGQLTGFDQSKTMISEAAITNNT-----IEWKLGDASKLPFEA-NCYDLIIARHMLYH- 167
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAAlladnVEVLKGDAEELPPEAdESFDVIISDPPLHHl 79

                         90       100
                 ....*....|....*....|....
gi 487940766 168 MKDVEKTIQGFHKVIRPGGSLLAT 191
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLT 103
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 74-192 6.60e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 59.94  E-value: 6.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  74 EEKQVNVDEVVIEHLQLQGEEKILEVGCANGKFLSLL-QTNGHkgQLTGFDQSKTMIS------EAAITNNTIEWKLGDA 146
Cdd:COG2230   33 EEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLaRRYGV--RVTGVTLSPEQLEyareraAEAGLADRVEVRLADY 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 487940766 147 SKLPFEaNCYDLIIARHMLYHM--KDVEKTIQGFHKVIRPGGSLLATT 192
Cdd:COG2230  111 RDLPAD-GQFDAIVSIGMFEHVgpENYPAYFAKVARLLKPGGRLLLHT 157
PRK08317 PRK08317
hypothetical protein; Provisional
 82-190 9.97e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 60.72  E-value: 9.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  82 EVVIEHLQLQGEEKILEVGCANGKFL-SLLQTNGHKGQLTGFDQSKTMISEA--AITNN--TIEWKLGDASKLPFEANCY 156
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDArELARRVGPEGRVVGIDRSEAMLALAkeRAAGLgpNVEFVRGDADGLPFPDGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 487940766 157 DLIIARHMLYHMKDVEKTIQGFHKVIRPGGSLLA 190
Cdd:PRK08317  89 DAVRSDRVLQHLEDPARALAEIARVLRPGGRVVV 122
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
95-199 8.57e-08

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 52.06  E-value: 8.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766   95 KILEVGCANGKF-LSLLQTNGHKGQLTGFDQSKTMISEAA-----ITNNTIEWKLGDASKLPFEANCYDLIIARHMLYHM 168
Cdd:pfam01209  45 KFLDVAGGTGDWtFGLSDSAGSSGKVVGLDINENMLKEGEkkakeEGKYNIEFLQGNAEELPFEDDSFDIVTISFGLRNF 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 487940766  169 KDVEKTIQGFHKVIRPGGSLLATTNSKVSMP 199
Cdd:pfam01209 125 PDYLKVLKEAFRVLKPGGRVVCLEFSKPENP 155
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 84-189 2.54e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 50.54  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  84 VIEHLQLQGEEKILEVGCANGKF-LSLLQTNGHKGQLTGFDQSKTMIS------EAAITNNTIEWKLGDASKLPFEANCY 156
Cdd:PRK00216  43 TIKWLGVRPGDKVLDLACGTGDLaIALAKAVGKTGEVVGLDFSEGMLAvgreklRDLGLSGNVEFVQGDAEALPFPDNSF 122

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 487940766 157 DLI-IA---RhmlyHMKDVEKTIQGFHKVIRPGGSLL 189
Cdd:PRK00216 123 DAVtIAfglR----NVPDIDKALREMYRVLKPGGRLV 155
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 85-191 7.52e-07

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 50.13  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  85 IEHLQLQGEEKILEVGCA--NGKFLSLLQTNGHkgqLTGFDQSKTMIS---EAAITNN-TIEWKLGDASKLPFEANCYDL 158
Cdd:PLN02336 259 VDKLDLKPGQKVLDVGCGigGGDFYMAENFDVH---VVGIDLSVNMISfalERAIGRKcSVEFEVADCTKKTYPDNSFDV 335

                         90       100       110
                 ....*....|....*....|....*....|...
gi 487940766 159 IIARHMLYHMKDVEKTIQGFHKVIRPGGSLLAT 191
Cdd:PLN02336 336 IYSRDTILHIQDKPALFRSFFKWLKPGGKVLIS 368
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 72-199 3.09e-06

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 47.45  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  72 HYE---EKQVNVDEVVIEHLQLQGEEKILEVGCANGKFLSLLQTNGhkGQLTGFDQSKTMISEAAITNNTIEWKLGDASK 148
Cdd:PRK10258  19 HYEqhaELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERG--SQVTALDLSPPMLAQARQKDAADHYLAGDIES 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 487940766 149 LPFEANCYDLIIARHMLYHMKDVEKTIQGFHKVIRPGGSLLATTNSKVSMP 199
Cdd:PRK10258  97 LPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLP 147
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 94-215 5.13e-06

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 47.19  E-value: 5.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  94 EKILEVGCANGKFLSLL-QTNGHKGQLTGFDQSKTMISEAAITNN--------TIEWKLGDASKLPFEANCYDLIIARHM 164
Cdd:PLN02233  75 DRVLDLCCGSGDLAFLLsEKVGSDGKVMGLDFSSEQLAVAASRQElkakscykNIEWIEGDATDLPFDDCYFDAITMGYG 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 487940766 165 LYHMKDVEKTIQGFHKVIRPGGSLLATTNSKVSMPRIVEMCNSMLDAFDLP 215
Cdd:PLN02233 155 LRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEWMIDNVVVP 205
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
143-192 6.92e-05

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 42.55  E-value: 6.92e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487940766 143 LGDASK-LPFEANCYDLIIARHMLYHM--KDVEKTIQGFHKVIRPGGSLLATT 192
Cdd:COG4627   33 VGDLTDpLPFPDNSVDAIYSSHVLEHLdyEEAPLALKECYRVLKPGGILRIVV 85
PRK05785 PRK05785
hypothetical protein; Provisional
 95-236 7.57e-04

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 40.06  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  95 KILEVGCANGKfLSLLQTNGHKGQLTGFDQSKTMISEAAITNNTIewkLGDASKLPFEANCYDLIIARHMLYHMKDVEKT 174
Cdd:PRK05785  54 KVLDVAAGKGE-LSYHFKKVFKYYVVALDYAENMLKMNLVADDKV---VGSFEALPFRDKSFDVVMSSFALHASDNIEKV 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487940766 175 IQGFHKVIRPGGSLLATTNSKVSMPRIVEmcnSMLDAFDLPKTSPAVAPFCLENGK--EILQSI 236
Cdd:PRK05785 130 IAEFTRVSRKQVGFIAMGKPDNVIKRKYL---SFYLRYIMPYIACLAGAKCRDYKYiyYIYERL 190
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
94-190 8.92e-04

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 40.09  E-value: 8.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766    94 EKILEVGCANGKFLSLLQTNGHKGQLTGFDQSKtmiSEAAITNNTIEWKL---------GDASKLPFEANcYDLIIARHM 164
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPHLQLHGYTISP---EQAEVGRERIRALGlqgririfyRDSAKDPFPDT-YDLVFGFEV 76

                           90       100
                   ....*....|....*....|....*.
gi 487940766   165 LYHMKDVEKTIQGFHKVIRPGGSLLA 190
Cdd:smart00828  77 IHHIKDKMDLFSNISRHLKDGGHLVL 102
PLN02244 PLN02244
tocopherol O-methyltransferase
 95-192 9.11e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 40.50  E-value: 9.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  95 KILEVGCANG---KFLSllqtNGHKGQLTGFDQSKTMISEA-AIT-----NNTIEWKLGDASKLPFEANCYDLIIARHML 165
Cdd:PLN02244 121 RIVDVGCGIGgssRYLA----RKYGANVKGITLSPVQAARAnALAaaqglSDKVSFQVADALNQPFEDGQFDLVWSMESG 196

                         90       100
                 ....*....|....*....|....*..
gi 487940766 166 YHMKDVEKTIQGFHKVIRPGGSLLATT 192
Cdd:PLN02244 197 EHMPDKRKFVQELARVAAPGGRIIIVT 223
NodS pfam05401
Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The ...
 96-189 1.23e-03

Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involved in N methylation of LCOs. NodS uses N-deacetylated chitooligosaccharides, the products of the NodBC proteins, as its methyl acceptors.


Pssm-ID: 428457  Cd Length: 201  Bit Score: 39.22  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766   96 ILEVGCANGKFLSLLQTNGHKgqLTGFDQSKTMISEAAI-TNNT--IEWKLGDASKLPFEANcYDLIIARHMLYHMKDVE 172
Cdd:pfam05401  47 ALEIGCAAGAFTEMLAILCER--LTVVDLMPEAIAKAQErTGKWsdIIWHECDICQFDLNAK-FDLIICAEVLYYIHDKE 123

                          90       100
                  ....*....|....*....|
gi 487940766  173 K---TIQGFHKVIRPGGSLL 189
Cdd:pfam05401 124 ElhaAIENIVQLLAPDEQFI 143
arsM PRK11873
arsenite methyltransferase;
89-186 5.54e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 37.62  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487940766  89 QLQGEEKILEVGCANGK--FLSLLQTnGHKGQLTGFDQSKTMISEA-------AITNntIEWKLGDASKLPFEANCYDLI 159
Cdd:PRK11873  74 ELKPGETVLDLGSGGGFdcFLAARRV-GPTGKVIGVDMTPEMLAKAranarkaGYTN--VEFRLGEIEALPVADNSVDVI 150

                         90       100
                 ....*....|....*....|....*..
gi 487940766 160 IARHMLYHMKDVEKTIQGFHKVIRPGG 186
Cdd:PRK11873 151 ISNCVINLSPDKERVFKEAFRVLKPGG 177
 
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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