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Conserved domains on  [gi|122921436|pdb|2O57|D]
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Chain D, putative sarcosine dimethylglycine methyltransferase

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 1003603)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Catharanthus roseus 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase and picrinine-N-methytransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN02244 super family cl33438
tocopherol O-methyltransferase
 10-231 1.36e-29

tocopherol O-methyltransferase


The actual alignment was detected with superfamily member PLN02244:

Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 114.84  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        10 SQPAATSKTVKDNAEIYYDDddSDRFYFHVWGgEDIHVGLYKEPVDQDEIREASLRTDEwlaSELA*TGVLQRQAKG--- 86
Cdd:PLN02244  48 SPAPAATADLKEGIAEFYDE--SSGVWEDVWG-EHMHHGYYDPGASRGDHRQAQIRMIE---ESLAWAGVPDDDEKRpkr 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        87 -LDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIPCEDNSYDFIWSQDAFLHSPD 165
Cdd:PLN02244 122 iVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPD 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2O57_D       166 KLKVFQECARVLKPRG-V*AITDP*KEDGIDKSSIQP----ILDRIK----LHD*GSLGLYRSLAKECGLVTLRT 231
Cdd:PLN02244 202 KRKFVQELARVAAPGGrIIIVTWCHRDLEPGETSLKPdeqkLLDKICaayyLPAWCSTSDYVKLAESLGLQDIKT 276
 
Name Accession Description Interval E-value
PLN02244 PLN02244
tocopherol O-methyltransferase
 10-231 1.36e-29

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 114.84  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        10 SQPAATSKTVKDNAEIYYDDddSDRFYFHVWGgEDIHVGLYKEPVDQDEIREASLRTDEwlaSELA*TGVLQRQAKG--- 86
Cdd:PLN02244  48 SPAPAATADLKEGIAEFYDE--SSGVWEDVWG-EHMHHGYYDPGASRGDHRQAQIRMIE---ESLAWAGVPDDDEKRpkr 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        87 -LDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIPCEDNSYDFIWSQDAFLHSPD 165
Cdd:PLN02244 122 iVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPD 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2O57_D       166 KLKVFQECARVLKPRG-V*AITDP*KEDGIDKSSIQP----ILDRIK----LHD*GSLGLYRSLAKECGLVTLRT 231
Cdd:PLN02244 202 KRKFVQELARVAAPGGrIIIVTWCHRDLEPGETSLKPdeqkLLDKICaayyLPAWCSTSDYVKLAESLGLQDIKT 276
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 30-188 1.43e-27

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 104.63  E-value: 1.43e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       30 DDSDRFYFHVWG-GEDIHVGLYKEPvdQDEIREASLRTDEWLASELA*tgvLQRQAKGLDLGAGYGGAARFLVRKFGVSI 108
Cdd:COG2230   4 DLGNDFYRLFLDpTMTYSCAYFEDP--DDTLEEAQEAKLDLILRKLG----LKPGMRVLDIGCGWGGLALYLARRYGVRV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D      109 DCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIPcEDNSYDFIWSQDAFLHSPDK--LKVFQECARVLKPRGV*AIT 186
Cdd:COG2230  78 TGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLH 156


                ..
2O57_D      187 DP 188
Cdd:COG2230 157 TP 158
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 87-181 5.87e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 82.61  E-value: 5.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         87 LDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEYNNQAGLadNITVKYGSFLEIPCEDNSYDFIWSQDAFLH--SP 164
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpDP 79

                          90
                  ....*....|....*..
2O57_D        165 DKLKVFQECARVLKPRG 181
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 85-186 2.02e-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: 70.54  E-value: 2.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       85 KGLDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEyNNQAGLADNITVKYGSFLEIPC-EDNSYDFIWSQDAFLHS 163
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARK-AAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....
2O57_D      164 P-DKLKVFQECARVLKPRGV*AIT 186
Cdd:cd02440  80 VeDLARFLEEARRLLKPGGVLVLT 103
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 83-247 1.74e-07

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: 51.13  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         83 QAKGLDLGAGYGGAARFLVRKF-GVSIDCLNIAPVQNKRNEEYNNQagladNITVKYGSFLEIPCEDNSYDFIWSQDAF- 160
Cdd:TIGR02072  35 PASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTKLSE-----NVQFICGDAEKLPLEDSSFDLIVSNLALq 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        161 -LHSPDKlkVFQECARVLKPRGV*AITDP*KED--GIDKSSIQPILDRIKLHD*GSL--GLYRSLAKECGLVTLrTFSRP 235
Cdd:TIGR02072 110 wCDDLSQ--ALSELARVLKPGGLLAFSTFGPGTlhELRQSFGQHGLRYLSLDELKALlkNSFELLTLEEELITL-SFDDP 186

                         170
                  ....*....|..
2O57_D        236 DSLVHHYSKVKA 247
Cdd:TIGR02072 187 LDVLRHLKKTGA 198
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
87-188 7.79e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.01  E-value: 7.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D          87 LDLGAGYGGAARFLVRKFG-VSIDCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIPCEDNsYDFIWSQDAFLHSPD 165
Cdd:smart00828   4 LDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDT-YDLVFGFEVIHHIKD 82

                           90       100
                   ....*....|....*....|...
2O57_D         166 KLKVFQECARVLKPRGV*AITDP 188
Cdd:smart00828  83 KMDLFSNISRHLKDGGHLVLADF 105
 
Name Accession Description Interval E-value
PLN02244 PLN02244
tocopherol O-methyltransferase
 10-231 1.36e-29

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 114.84  E-value: 1.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        10 SQPAATSKTVKDNAEIYYDDddSDRFYFHVWGgEDIHVGLYKEPVDQDEIREASLRTDEwlaSELA*TGVLQRQAKG--- 86
Cdd:PLN02244  48 SPAPAATADLKEGIAEFYDE--SSGVWEDVWG-EHMHHGYYDPGASRGDHRQAQIRMIE---ESLAWAGVPDDDEKRpkr 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        87 -LDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIPCEDNSYDFIWSQDAFLHSPD 165
Cdd:PLN02244 122 iVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPD 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2O57_D       166 KLKVFQECARVLKPRG-V*AITDP*KEDGIDKSSIQP----ILDRIK----LHD*GSLGLYRSLAKECGLVTLRT 231
Cdd:PLN02244 202 KRKFVQELARVAAPGGrIIIVTWCHRDLEPGETSLKPdeqkLLDKICaayyLPAWCSTSDYVKLAESLGLQDIKT 276
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 30-188 1.43e-27

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 104.63  E-value: 1.43e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       30 DDSDRFYFHVWG-GEDIHVGLYKEPvdQDEIREASLRTDEWLASELA*tgvLQRQAKGLDLGAGYGGAARFLVRKFGVSI 108
Cdd:COG2230   4 DLGNDFYRLFLDpTMTYSCAYFEDP--DDTLEEAQEAKLDLILRKLG----LKPGMRVLDIGCGWGGLALYLARRYGVRV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D      109 DCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIPcEDNSYDFIWSQDAFLHSPDK--LKVFQECARVLKPRGV*AIT 186
Cdd:COG2230  78 TGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLH 156


                ..
2O57_D      187 DP 188
Cdd:COG2230 157 TP 158
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 87-181 5.87e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 82.61  E-value: 5.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         87 LDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEYNNQAGLadNITVKYGSFLEIPCEDNSYDFIWSQDAFLH--SP 164
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpDP 79

                          90
                  ....*....|....*..
2O57_D        165 DKLKVFQECARVLKPRG 181
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 80-195 5.75e-19

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: 81.19  E-value: 5.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       80 LQRQAKGLDLGAGYGGAARFLVRKfGVSIDCLNIAPVQNKRNEEYNNQAGLadNITVKYGSFLEIPCEDNSYDFIWSQDA 159
Cdd:COG2226  20 LRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFV 96

                        90       100       110
                ....*....|....*....|....*....|....*.
2O57_D      160 FLHSPDKLKVFQECARVLKPRGV*AITDP*KEDGID 195
Cdd:COG2226  97 LHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAE 132
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 87-185 3.98e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 72.31  E-value: 3.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         87 LDLGAGYGGAARFLvRKFGVSIDCLNIAPVQNKRNEEYNNQAGLADNItvkyGSFLEIPCEDNSYDFIWSQDAFLHSPDK 166
Cdd:pfam08241   1 LDVGCGTGLLTELL-ARLGARVTGVDISPEMLELAREKAPREGLTFVV----GDAEDLPFPDNSFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|....*....
2O57_D        167 LKVFQECARVLKPRGV*AI 185
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 85-186 2.02e-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: 70.54  E-value: 2.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       85 KGLDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEyNNQAGLADNITVKYGSFLEIPC-EDNSYDFIWSQDAFLHS 163
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARK-AAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....
2O57_D      164 P-DKLKVFQECARVLKPRGV*AIT 186
Cdd:cd02440  80 VeDLARFLEEARRLLKPGGVLVLT 103
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 67-188 1.39e-14

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: 68.89  E-value: 1.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       67 DEWLASELA*tgVLQRQAKGLDLGAGYGGAARFLVRKfGVSIDCLNIAPvqnkRNEEYNNQAGLADNITVKYGSFLEIPC 146
Cdd:COG2227  11 DRRLAALLAR--LLPAGGRVLDVGCGTGRLALALARR-GADVTGVDISP----EALEIARERAAELNVDFVQGDLEDLPL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
2O57_D      147 EDNSYDFIWSQDAFLHSPDKLKVFQECARVLKPRGV*AITDP 188
Cdd:COG2227  84 EDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTP 125
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 80-187 2.72e-13

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 68.46  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        80 LQRQAKGLDLGAGYGGAARFLVRKFGV---SID-CLNIAPVQNKRNEEYNNQAGLADNITVKygsflEIPceDNSYDFIW 155
Cdd:PTZ00098  50 LNENSKVLDIGSGLGGGCKYINEKYGAhvhGVDiCEKMVNIAKLRNSDKNKIEFEANDILKK-----DFP--ENTFDMIY 122

                         90       100       110
                 ....*....|....*....|....*....|....
2O57_D       156 SQDAFLHSP--DKLKVFQECARVLKPRGV*AITD 187
Cdd:PTZ00098 123 SRDAILHLSyaDKKKLFEKCYKWLKPNGILLITD 156
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 65-186 2.76e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 61.47  E-value: 2.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       65 RTDEWLASELA*TGVLQRQAKGLDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEYNNQAGLaDNITVKYGSFLEI 144
Cdd:COG0500   9 ELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAEL 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
2O57_D      145 -PCEDNSYDFIWSQDAFLH-SPDKL-KVFQECARVLKPRGV*AIT 186
Cdd:COG0500  88 dPLPAESFDLVVAFGVLHHlPPEEReALLRELARALKPGGVLLLS 132
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 87-188 4.44e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.04  E-value: 4.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         87 LDLGAGYGGAARFLVRKFG-----VSIDclnIAPVQNKRNEEYNNQAGLaDNITVKYGSFLEIPC--EDNSYDFIWSQDA 159
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGpnaevVGID---ISEEAIEKARENAQKLGF-DNVEFEQGDIEELPEllEDDKFDVVISNCV 83

                          90       100
                  ....*....|....*....|....*....
2O57_D        160 FLHSPDKLKVFQECARVLKPRGV*AITDP 188
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISDP 112
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 87-182 7.49e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.07  E-value: 7.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         87 LDLGAGYGGAARFLVRKF-GVSIDCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIPCEDNSYDFIWSQDAFLHSPD 165
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*..
2O57_D        166 KLKVFQECARVLKPRGV 182
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGV 97
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
50-186 1.85e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.08  E-value: 1.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       50 YKEPVDQDEIREASLRTDEWLASELA*TGVLQRQAKGLDLGAGYGGAARFLvRKFGVSIDC-------LNIApvqnKRNE 122
Cdd:COG4976  14 YADSYDAALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEAL-RPRGYRLTGvdlseemLAKA----REKG 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
2O57_D      123 EYnnqagladnITVKYGSFLEIPCEDNSYDFIWSQDAFLHSPDKLKVFQECARVLKPRGV*AIT 186
Cdd:COG4976  89 VY---------DRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFS 143
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
87-187 8.84e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.44  E-value: 8.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       87 LDLGAGYGGAARFLVRKF-GVSIDCLNIAPV---QNKRNeeynnqaglADNITVKYGSFLEIPCEDnSYDFIWSQDAFLH 162
Cdd:COG4106   6 LDLGCGTGRLTALLAERFpGARVTGVDLSPEmlaRARAR---------LPNVRFVVADLRDLDPPE-PFDLVVSNAALHW 75

                        90       100
                ....*....|....*....|....*
2O57_D      163 SPDKLKVFQECARVLKPRGV*AITD 187
Cdd:COG4106  76 LPDHAALLARLAAALAPGGVLAVQV 100
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 83-247 1.74e-07

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: 51.13  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         83 QAKGLDLGAGYGGAARFLVRKF-GVSIDCLNIAPVQNKRNEEYNNQagladNITVKYGSFLEIPCEDNSYDFIWSQDAF- 160
Cdd:TIGR02072  35 PASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTKLSE-----NVQFICGDAEKLPLEDSSFDLIVSNLALq 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        161 -LHSPDKlkVFQECARVLKPRGV*AITDP*KED--GIDKSSIQPILDRIKLHD*GSL--GLYRSLAKECGLVTLrTFSRP 235
Cdd:TIGR02072 110 wCDDLSQ--ALSELARVLKPGGLLAFSTFGPGTlhELRQSFGQHGLRYLSLDELKALlkNSFELLTLEEELITL-SFDDP 186

                         170
                  ....*....|..
2O57_D        236 DSLVHHYSKVKA 247
Cdd:TIGR02072 187 LDVLRHLKKTGA 198
arsM PRK11873
arsenite methyltransferase;
87-187 5.40e-07

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 49.95  E-value: 5.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        87 LDLGAGyGGAARFLVRK--------FGVSI--DCLNIApvqnKRNEEynnQAGlADNITVKYGSFLEIPCEDNSYDFIWS 156
Cdd:PRK11873  82 LDLGSG-GGFDCFLAARrvgptgkvIGVDMtpEMLAKA----RANAR---KAG-YTNVEFRLGEIEALPVADNSVDVIIS 152

                         90       100       110
                 ....*....|....*....|....*....|.
2O57_D       157 QDAFLHSPDKLKVFQECARVLKPRGV*AITD 187
Cdd:PRK11873 153 NCVINLSPDKERVFKEAFRVLKPGGRFAISD 183
PRK08317 PRK08317
hypothetical protein; Provisional
 80-235 1.31e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 48.39  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        80 LQRQAKGLDLGAGYGGAARFLVRKFG-----VSIDclniaPVQNKRNEEYNNQAGLADNITVKYGSFLEIPCEDNSYDFI 154
Cdd:PRK08317  17 VQPGDRVLDVGCGPGNDARELARRVGpegrvVGID-----RSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       155 WSQDAFLHSPDKLKVFQECARVLKPRGV*AITDP*KE----DGIDKSSIQPILDRIKLHD-*GSLGlyRSLAK---ECGL 226
Cdd:PRK08317  92 RSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWDtlvwHSGDRALMRKILNFWSDHFaDPWLG--RRLPGlfrEAGL 169


                 ....*....
2O57_D       227 VTLRTFSRP 235
Cdd:PRK08317 170 TDIEVEPYT 178
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 65-226 1.16e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 44.73  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         65 RTDEWLASELA*TG-VLQRQAKGLDLGAGYGGAARFLvRKFGVSIDCLNIAPVQNKRNEEYNNQAGLADNitvkygsflE 143
Cdd:pfam13489   4 QRERLLADLLLRLLpKLPSPGRVLDFGCGTGIFLRLL-RAQGFSVTGVDPSPIAIERALLNVRFDQFDEQ---------E 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        144 IPCEDNSYDFIWSQDAFLHSPDKLKVFQECARVLKPRGV*AITDP*KEDGIDKS-----SIQPILDRIKLHD*GSLglyR 218
Cdd:pfam13489  74 AAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLllewpYLRPRNGHISLFSARSL---K 150


                  ....*...
2O57_D        219 SLAKECGL 226
Cdd:pfam13489 151 RLLEEAGF 158
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 81-190 2.53e-05

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: 44.56  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         81 QRQAKGLDLGAGYGGAARFLVRKFGVSIDCLNIAPVQN------KRneeynnqAGLADNITVKYGSFLEIPCEDNSYDFI 154
Cdd:TIGR01934  38 FKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEmlevakKK-------SELPLNIEFIQADAEALPFEDNSFDAV 110

                          90       100       110
                  ....*....|....*....|....*....|....*.
2O57_D        155 WSQDAFLHSPDKLKVFQECARVLKPRGV*AITDP*K 190
Cdd:TIGR01934 111 TIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSK 146
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 85-193 3.12e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 45.13  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        85 KGLDLGAGYGGAARFLVRKFGV-------SIDCLNIA---PVQNKRNEEYNnqagLADNITVKYgsfleipcEDNSYDFI 154
Cdd:PLN02336 269 KVLDVGCGIGGGDFYMAENFDVhvvgidlSVNMISFAlerAIGRKCSVEFE----VADCTKKTY--------PDNSFDVI 336

                         90       100       110
                 ....*....|....*....|....*....|....*....
2O57_D       155 WSQDAFLHSPDKLKVFQECARVLKPRGV*AITDP*KEDG 193
Cdd:PLN02336 337 YSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPG 375
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 80-181 4.15e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 43.98  E-value: 4.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D       80 LQRQAKGLDLGAGYGGAARFLVRKF-GVSIDCLNIAPV---QNKRNEEYNnqaGLADNITVKYGSFLEIP--CEDNSYDF 153
Cdd:COG4123  35 VKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEaaeLARRNVALN---GLEDRITVIHGDLKEFAaeLPPGSFDL 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
2O57_D      154 I------WSQDAFLHSPDKLK-------------VFQECARVLKPRG 181
Cdd:COG4123 112 VvsnppyFKAGSGRKSPDEARaiarhedaltledLIRAAARLLKPGG 158
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 80-185 1.21e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 42.45  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        80 LQRQAKGLDLGAGYGGAARFLVRKFGVSIDC---------LNIApvqnkrnEEYNNQAGLADNITVKYGSFLEIPCEDNS 150
Cdd:PRK00216  49 VRPGDKVLDLACGTGDLAIALAKAVGKTGEVvgldfsegmLAVG-------REKLRDLGLSGNVEFVQGDAEALPFPDNS 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
2O57_D       151 YDFIwsqdaflhS--------PDKLKVFQECARVLKPRGV*AI 185
Cdd:PRK00216 122 FDAV--------TiafglrnvPDIDKALREMYRVLKPGGRLVI 156
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
144-182 1.68e-04

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 41.39  E-value: 1.68e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
2O57_D      144 IPCEDNSYDFIWSQDAF--LHSPDKLKVFQECARVLKPRGV 182
Cdd:COG4627  40 LPFPDNSVDAIYSSHVLehLDYEEAPLALKECYRVLKPGGI 80
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 87-244 1.84e-04

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 42.31  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         87 LDLGAGYGGAARFLVRKFGVSIDCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIpceDNSYDFIWSQDAFLH-SPD 165
Cdd:pfam02353  66 LDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF---DEPFDRIVSVGMFEHvGHE 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D        166 KLKV-FQECARVLKPRGV*---AITDP*KEDGIDKSSIQPILDRiKLHD*G---SLGLYRSLAKECGLvtlrTFSRPDSL 238
Cdd:pfam02353 143 NYDTfFKKLYNLLPPGGLMllhTITGLHPDETSERGLPLKFIDK-YIFPGGelpSISMIVESSSEAGF----TVEDVESL 217


                  ....*.
2O57_D        239 VHHYSK 244
Cdd:pfam02353 218 RPHYAK 223
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
82-181 1.62e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 38.96  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D         82 RQAKGLDLGAGYGGAARFLVRKFGVS--IDCLNIAPVQNKRNEEYNNQAGLAdNITVKYGSFLEIPCEDNSYDFIWSQDA 159
Cdd:pfam01209  42 RGNKFLDVAGGTGDWTFGLSDSAGSSgkVVGLDINENMLKEGEKKAKEEGKY-NIEFLQGNAEELPFEDDSFDIVTISFG 120

                          90       100
                  ....*....|....*....|..
2O57_D        160 FLHSPDKLKVFQECARVLKPRG 181
Cdd:pfam01209 121 LRNFPDYLKVLKEAFRVLKPGG 142
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
87-188 7.79e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.01  E-value: 7.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2O57_D          87 LDLGAGYGGAARFLVRKFG-VSIDCLNIAPVQNKRNEEYNNQAGLADNITVKYGSFLEIPCEDNsYDFIWSQDAFLHSPD 165
Cdd:smart00828   4 LDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDT-YDLVFGFEVIHHIKD 82

                           90       100
                   ....*....|....*....|...
2O57_D         166 KLKVFQECARVLKPRGV*AITDP 188
Cdd:smart00828  83 KMDLFSNISRHLKDGGHLVLADF 105
 
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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