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Conserved domains on  [gi|1327848535|ref|NP_001346465|]
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methyltransferase-like protein 27 isoform 1 [Mus musculus]

Protein Classification

class I SAM-dependent DNA methyltransferase( domain architecture ID 11471966)

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047
PubMed:  23180741|12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-192 8.24e-34

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


:

Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 119.72  E-value: 8.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976    11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535 111 LYHHLSLCTLGQepLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGGLVCLTTRTNPSNLPYKETLEATLDSLER 190
Cdd:COG4976    89 VYDRLLVADLAD--LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADGSGRYAHSLDYVRDLLAA 166


                  ..
gi 1327848535 191 AG 192
Cdd:COG4976   167 AG 168
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-192 8.24e-34

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 119.72  E-value: 8.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976    11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535 111 LYHHLSLCTLGQepLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGGLVCLTTRTNPSNLPYKETLEATLDSLER 190
Cdd:COG4976    89 VYDRLLVADLAD--LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADGSGRYAHSLDYVRDLLAA 166


                  ..
gi 1327848535 191 AG 192
Cdd:COG4976   167 AG 168
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-162 5.77e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 83.77  E-value: 5.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSlCTLGQ---EPLPDPEGTFDAVIIVGALS--EGQ 145
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN-VEFVQgdaEDLPFPDGSFDLVVSSGVLHhlPDP 79

                          90
                  ....*....|....*..
gi 1327848535 146 VPCSAIPELLRVTKPGG 162
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 33-172 9.10e-16

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 73.65  E-value: 9.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  33 DDWAPEYDQ--DVAAL----KYRapRLAVDCLsrafrGSPHDALILDVACGTGLVAVEL--QARGFLQVQGVDGSPEMLK 104
Cdd:PRK00216   18 DSIAPKYDLmnDLLSFglhrVWR--RKTIKWL-----GVRPGDKVLDLACGTGDLAIALakAVGKTGEVVGLDFSEGMLA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535 105 QARAR----GLYHHLSLCTLGQEPLPDPEGTFDAVII----------VGALSegqvpcsaipELLRVTKPGG-LVCL--T 167
Cdd:PRK00216   91 VGREKlrdlGLSGNVEFVQGDAEALPFPDNSFDAVTIafglrnvpdiDKALR----------EMYRVLKPGGrLVILefS 160


                  ....*
gi 1327848535 168 TRTNP 172
Cdd:PRK00216  161 KPTNP 165
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-166 1.88e-14

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: 69.98  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  30 RFYDDWAPEYDQDVAALKYRAPRL----AVDCLsRAFRGSPhdalILDVACGTGLVAVELQARG--FLQVQGVDGSPEML 103
Cdd:TIGR01934   3 EMFDRIAPKYDLLNDLLSFGLHRLwrrrAVKLI-GVFKGQK----VLDVACGTGDLAIELAKSApdRGKVTGVDFSSEML 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327848535 104 KQARARGLYH-HLSLCTLGQEPLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGG-LVCL 166
Cdd:TIGR01934  78 EVAKKKSELPlNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGrLVIL 142
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-167 4.02e-12

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 60.91  E-value: 4.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSLCTLGQ----EPLPDPEGTFDAVIIVGALS-EGQ 145
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKgdaeELPPEADESFDVIISDPPLHhLVE 81

                          90       100
                  ....*....|....*....|..
gi 1327848535 146 VPCSAIPELLRVTKPGGLVCLT 167
Cdd:cd02440    82 DLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-192 8.24e-34

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 119.72  E-value: 8.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976    11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535 111 LYHHLSLCTLGQepLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGGLVCLTTRTNPSNLPYKETLEATLDSLER 190
Cdd:COG4976    89 VYDRLLVADLAD--LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADGSGRYAHSLDYVRDLLAA 166


                  ..
gi 1327848535 191 AG 192
Cdd:COG4976   167 AG 168
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 32-183 1.61e-24

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: 94.68  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  32 YDDWAPEYDQDVAALKYRAPRlavdclsrafrgspHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARGL 111
Cdd:COG2226     1 FDRVAARYDGREALLAALGLR--------------PGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAA 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327848535 112 YHHLSLCTLGQ--EPLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGGLVCLTTRTNPSNLPYKETLEA 183
Cdd:COG2226    66 EAGLNVEFVVGdaEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-162 5.77e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 83.77  E-value: 5.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSlCTLGQ---EPLPDPEGTFDAVIIVGALS--EGQ 145
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN-VEFVQgdaEDLPFPDGSFDLVVSSGVLHhlPDP 79

                          90
                  ....*....|....*..
gi 1327848535 146 VPCSAIPELLRVTKPGG 162
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 66-168 5.79e-19

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 79.68  E-value: 5.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  66 PHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARGLYHHLSLCTLGQEPLPDPEGTFDAVIIVGALSEGQ 145
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHLP 101

                          90       100
                  ....*....|....*....|...
gi 1327848535 146 VPCSAIPELLRVTKPGGLVCLTT 168
Cdd:COG2227   102 DPAALLRELARLLKPGGLLLLST 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 30-194 2.95e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 76.88  E-value: 2.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  30 RFYDDWAPEYDQDVAALkyraPRLavdclsrafrgsPHDALILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARAR 109
Cdd:COG0500     5 YYSDELLPGLAALLALL----ERL------------PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARAR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535 110 GLYHHLSLCTLGQ----EPLPDPEGTFDAVIIVGALS--EGQVPCSAIPELLRVTKPGGLVCLT-TRTNPSNLPYKETLE 182
Cdd:COG0500    69 AAKAGLGNVEFLVadlaELDPLPAESFDLVVAFGVLHhlPPEEREALLRELARALKPGGVLLLSaSDAAAALSLARLLLL 148

                         170
                  ....*....|..
gi 1327848535 183 ATLDSLERAGVW 194
Cdd:COG0500   149 ATASLLELLLLL 160
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 33-172 9.10e-16

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 73.65  E-value: 9.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  33 DDWAPEYDQ--DVAAL----KYRapRLAVDCLsrafrGSPHDALILDVACGTGLVAVEL--QARGFLQVQGVDGSPEMLK 104
Cdd:PRK00216   18 DSIAPKYDLmnDLLSFglhrVWR--RKTIKWL-----GVRPGDKVLDLACGTGDLAIALakAVGKTGEVVGLDFSEGMLA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535 105 QARAR----GLYHHLSLCTLGQEPLPDPEGTFDAVII----------VGALSegqvpcsaipELLRVTKPGG-LVCL--T 167
Cdd:PRK00216   91 VGREKlrdlGLSGNVEFVQGDAEALPFPDNSFDAVTIafglrnvpdiDKALR----------EMYRVLKPGGrLVILefS 160


                  ....*
gi 1327848535 168 TRTNP 172
Cdd:PRK00216  161 KPTNP 165
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 72-166 1.44e-15

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 69.62  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  72 LDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG-----LYHHLSLCTLgqePLPDpeGTFDAVIIVGALSEGQV 146
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKApreglTFVVGDAEDL---PFPD--NSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 1327848535 147 PCSAIPELLRVTKPGGLVCL 166
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-166 1.88e-14

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: 69.98  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  30 RFYDDWAPEYDQDVAALKYRAPRL----AVDCLsRAFRGSPhdalILDVACGTGLVAVELQARG--FLQVQGVDGSPEML 103
Cdd:TIGR01934   3 EMFDRIAPKYDLLNDLLSFGLHRLwrrrAVKLI-GVFKGQK----VLDVACGTGDLAIELAKSApdRGKVTGVDFSSEML 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327848535 104 KQARARGLYH-HLSLCTLGQEPLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGG-LVCL 166
Cdd:TIGR01934  78 EVAKKKSELPlNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGrLVIL 142
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 36-176 9.07e-14

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 68.63  E-value: 9.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  36 APEYDQDVAALKYRAPRLAVDCLSRAFrgsphdALILDVACGTGLVAVELQARGfLQVQGVDGSPEMLKQARARGLYHHL 115
Cdd:PRK10258   17 AAHYEQHAELQRQSADALLAMLPQRKF------THVLDAGCGPGWMSRYWRERG-SQVTALDLSPPMLAQARQKDAADHY 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848535 116 SLCTLgqEPLPDPEGTFD------AVIIVGALSEgqvpcsAIPELLRVTKPGGLVCLTTRTNPSnLP 176
Cdd:PRK10258   90 LAGDI--ESLPLATATFDlawsnlAVQWCGNLST------ALRELYRVVRPGGVVAFTTLVQGS-LP 147
PRK08317 PRK08317
hypothetical protein; Provisional
 71-168 2.08e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 64.57  E-value: 2.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGLVAVELQAR----GflQVQGVDGSPEMLKQARARGLYHHLSLCTL--GQEPLPDPEGTFDAVIIVGALSEG 144
Cdd:PRK08317   23 VLDVGCGPGNDARELARRvgpeG--RVVGIDRSEAMLALAKERAAGLGPNVEFVrgDADGLPFPDGSFDAVRSDRVLQHL 100

                          90       100
                  ....*....|....*....|....*
gi 1327848535 145 QVPCSAIPELLRVTKPGG-LVCLTT 168
Cdd:PRK08317  101 EDPARALAEIARVLRPGGrVVVLDT 125
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-167 4.02e-12

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 60.91  E-value: 4.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSLCTLGQ----EPLPDPEGTFDAVIIVGALS-EGQ 145
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKgdaeELPPEADESFDVIISDPPLHhLVE 81

                          90       100
                  ....*....|....*....|..
gi 1327848535 146 VPCSAIPELLRVTKPGGLVCLT 167
Cdd:cd02440    82 DLARFLEEARRLLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
71-168 4.78e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 60.61  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGLVAVELQARG-FLQVQGVDGSPEMLKQARAR--GL-YHHLSLCTLgqeplpDPEGTFDAVIIVGALS--EG 144
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARlpNVrFVVADLRDL------DPPEPFDLVVSNAALHwlPD 78

                          90       100
                  ....*....|....*....|....
gi 1327848535 145 QVpcSAIPELLRVTKPGGLVCLTT 168
Cdd:COG4106    79 HA--ALLARLAAALAPGGVLAVQV 100
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 71-169 3.08e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 59.56  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARAR----GLYHHLSLCTLGQEPLPdPEGTFDAVIIVGALSegQV 146
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERaaeaGLADRVEVRLADYRDLP-ADGQFDAIVSIGMFE--HV 131

                          90       100
                  ....*....|....*....|....*..
gi 1327848535 147 PCSAIPELL----RVTKPGGLVCLTTR 169
Cdd:COG2230   132 GPENYPAYFakvaRLLKPGGRLLLHTP 158
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
71-183 5.71e-11

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 60.15  E-value: 5.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGLVAVEL--QARGFLQVQGVDGSPEMLKQARAR----GLYHHLSLCTLGQEpLPDPEGTFDAVIIVGALSEG 144
Cdd:pfam01209  46 FLDVAGGTGDWTFGLsdSAGSSGKVVGLDINENMLKEGEKKakeeGKYNIEFLQGNAEE-LPFEDDSFDIVTISFGLRNF 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1327848535 145 QVPCSAIPELLRVTKPGG-LVCLTTrTNPSNLPYKETLEA 183
Cdd:pfam01209 125 PDYLKVLKEAFRVLKPGGrVVCLEF-SKPENPLLSQAYEL 163
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 72-164 4.83e-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: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  72 LDVACGTGLVAVEL-QARGFLQVQGVDGSPEMLKQARARGL---YHHLSLCTLGQEPLPDPEG-TFDAVIIVGALSEGQV 146
Cdd:pfam08242   1 LEIGCGTGTLLRALlEALPGLEYTGLDISPAALEAARERLAalgLLNAVRVELFQLDLGELDPgSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1327848535 147 PCSAIPELLRVTKPGGLV 164
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 64-136 1.83e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 56.00  E-value: 1.83e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848535  64 GSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARAR----GLYHHLSLCTLGQEPLpdpEGTFDAVI 136
Cdd:PRK07580   60 GDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDISPQMVEEARERapeaGLAGNITFEVGDLESL---LGRFDTVV 132
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 63-196 8.52e-09

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: 54.21  E-value: 8.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  63 RGSPHDALILDVACGTGLVAVELQARgFLQVQ--GVDGSPEMLKQARarglyHHLS---LCTLGQ-EPLPDPEGTFDavI 136
Cdd:TIGR02072  30 KGIFIPASVLDIGCGTGYLTRALLKR-FPQAEfiALDISAGMLAQAK-----TKLSenvQFICGDaEKLPLEDSSFD--L 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327848535 137 IVGALSegqV-----PCSAIPELLRVTKPGGLVCLTT-------------RTNPSNLPYKETLEATLDSLERAGVWEC 196
Cdd:TIGR02072 102 IVSNLA---LqwcddLSQALSELARVLKPGGLLAFSTfgpgtlhelrqsfGQHGLRYLSLDELKALLKNSFELLTLEE 176
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 71-208 3.34e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 51.26  E-value: 3.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTG----LVAVELQARGflQVQGVDGSPEMLKQARARGLYHHLSLCTLGQE-----PLPDPEGTFDAVIIVGAL 141
Cdd:pfam13847   7 VLDLGCGTGhlsfELAEELGPNA--EVVGIDISEEAIEKARENAQKLGFDNVEFEQGdieelPELLEDDKFDVVISNCVL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848535 142 SEGQVPCSAIPELLRVTKPGGLVCLTTRTNPSNLPYketlEATLDSLERAGVWECLVTQPVDHWELA 208
Cdd:pfam13847  85 NHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPA----HVKEDSTYYAGCVGGAILKKKLYELLE 147
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-173 1.19e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 49.73  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  46 LKYRAPRLAVDCLSRAFRGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMlkQARARGLYHHLSLCtlgQEPL 125
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF-SVTGVDPSPIA--IERALLNVRFDQFD---EQEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1327848535 126 PDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGGLVCLTTRTNPS 173
Cdd:pfam13489  75 AVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASD 122
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 71-164 2.23e-07

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 50.30  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTGL----VAVELQARGFLQVQGVDGSPEMLKQARARglYHHLSLCTLGQEPLPDPEGTFDAVIIVGAlsegqv 146
Cdd:PRK11088   89 LLDIGCGEGYythaLADALPEITTMQLFGLDISKVAIKYAAKR--YPQVTFCVASSHRLPFADQSLDAIIRIYA------ 160

                          90
                  ....*....|....*...
gi 1327848535 147 PCSAiPELLRVTKPGGLV 164
Cdd:PRK11088  161 PCKA-EELARVVKPGGIV 177
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 51-168 2.26e-07

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: 49.18  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  51 PRLAvDCLSRAFRGSPHDaLILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARGLYHHLSLCTLGQEP---LPD 127
Cdd:COG1041    12 PRLA-RALVNLAGAKEGD-TVLDPFCGTGTILIEAGLLGR-RVIGSDIDPKMVEGARENLEHYGYEDADVIRGDardLPL 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327848535 128 PEGTFDAVII-----VGALSEGQVPC----SAIPELLRVTKPGGLVCLTT 168
Cdd:COG1041    89 ADESVDAIVTdppygRSSKISGEELLelyeKALEEAARVLKPGGRVVIVT 138
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 52-183 1.67e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 42.03  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  52 RLAV--DCLSRAFRGSPHDAL------ILDVACGTGLVAVELqARGFLQVQGVDGSPEMLKQARARG----LYHHLSLCT 119
Cdd:PLN02396  108 RLAFirSTLCRHFSKDPSSAKpfeglkFIDIGCGGGLLSEPL-ARMGATVTGVDAVDKNVKIARLHAdmdpVTSTIEYLC 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327848535 120 LGQEPLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGGLVCLTTrTNPSNLPYKETLEA 183
Cdd:PLN02396  187 TTAEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVLST-INRTMRAYASTIVG 249
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 63-177 2.37e-04

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


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 41.62  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  63 RGSPH-----DALILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARA----RGLYHHLSLCTLGQEPLPDPEGtFD 133
Cdd:pfam08003 106 RVLPHlsplkGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFLCQFEAvrklLGNDQRAHLLPLGIEQLPALAA-FD 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1327848535 134 AVIIVGALSEGQVPCSAIPELLRVTKPGGLVCLTTRTNPSNLPY 177
Cdd:pfam08003 185 TVFSMGVLYHRRSPLDHLLQLKDQLVKGGELVLETLVIDGDENT 228
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 68-173 4.92e-04

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 40.65  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  68 DALILDVACGTGL----VAVELQARgflQVQGVDGSPEMLKQARARglyHHLSLCTLGQ---EPLPDPEGTFDAVIIVGA 140
Cdd:PLN02490  114 NLKVVDVGGGTGFttlgIVKHVDAK---NVTILDQSPHQLAKAKQK---EPLKECKIIEgdaEDLPFPTDYADRYVSAGS 187

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1327848535 141 LSEGQVPCSAIPELLRVTKPGGLVCLTTRTNPS 173
Cdd:PLN02490  188 IEYWPDPQRGIKEAYRVLKIGGKACLIGPVHPT 220
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 35-111 9.49e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 39.29  E-value: 9.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327848535  35 WAPeyDQDVAALKYRApRLAVDCLSRAfrGSPHDALILDVACGTGLVAVELQAR-GFLQVQGVDGSPEMLKQARARGL 111
Cdd:PRK14103    2 WDP--DVYLAFADHRG-RPFYDLLARV--GAERARRVVDLGCGPGNLTRYLARRwPGAVIEALDSSPEMVAAARERGV 74
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 34-109 1.23e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 39.16  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  34 DWAPE-YdqdvaaLKYRAPRL--AVDCLSRAfrgsPHDAL--ILDVACGTGLVAVELQAR-GFLQVQGVDGSPEMLKQAR 107
Cdd:PRK01683    3 DWNPSlY------LKFEDERTrpARDLLARV----PLENPryVVDLGCGPGNSTELLVERwPAARITGIDSSPAMLAEAR 72


                  ..
gi 1327848535 108 AR 109
Cdd:PRK01683   73 SR 74
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 71-159 1.97e-03

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


Pssm-ID: 399779  Cd Length: 193  Bit Score: 38.21  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  71 ILDVACGTG----LVAVELQARGflqvQGVDGSPEMLKQARARGLYHHLSLCTLGQEPLPDpeGTFDAVIIVGALSEGQV 146
Cdd:pfam07021  17 VLDLGCGDGtllyLLKEEKGVDG----YGIELDAAGVAECVAKGLYVIQGDLDEGLEHFPD--KSFDYVILSQTLQATRN 90

                          90
                  ....*....|...
gi 1327848535 147 PCSAIPELLRVTK 159
Cdd:pfam07021  91 PREVLDEMLRIGR 103
PRK06202 PRK06202
hypothetical protein; Provisional
 29-109 9.83e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 36.13  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848535  29 LRFYDDWAPEY-DQ---DVAALK--YRAPRL---AVDCLSRAFRgsPHDAL---------ILDVACGTGLVAVELQA--- 87
Cdd:PRK06202    6 LSRRRDRQPEVmDDpgcDPARLDrtYAGFRRvnrIVAGWRGLYR--RLLRPalsadrpltLLDIGCGGGDLAIDLARwar 83

                          90       100
                  ....*....|....*....|....
gi 1327848535  88 -RGF-LQVQGVDGSPEMLKQARAR 109
Cdd:PRK06202   84 rDGLrLEVTAIDPDPRAVAFARAN 107
 
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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