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Conserved domains on  [gi|768811324|gb|AJV27928|]
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Crg1p [Saccharomyces cerevisiae YJM1190]

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]; ...
 16-155 5.09e-22

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: 89.28  E-value: 5.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  16 YNNVRPSYPL-SLVNEIMKFHKGTRksLVDIGCGTGKATFVVELYFKEVIGIDPSSAMLSIAEKETNERRLDkkIRFINA 94
Cdd:COG2226    1 FDRVAARYDGrEALLAALGLRPGAR--VLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768811324  95 PGEDLsSIRPESVDMVISAEAIHWC-NLERLFQQVSSILRSDGTFAFWFYIQPEFVDFPEAL 155
Cdd:COG2226   77 DAEDL-PFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 16-155 5.09e-22

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: 89.28  E-value: 5.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  16 YNNVRPSYPL-SLVNEIMKFHKGTRksLVDIGCGTGKATFVVELYFKEVIGIDPSSAMLSIAEKETNERRLDkkIRFINA 94
Cdd:COG2226    1 FDRVAARYDGrEALLAALGLRPGAR--VLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768811324  95 PGEDLsSIRPESVDMVISAEAIHWC-NLERLFQQVSSILRSDGTFAFWFYIQPEFVDFPEAL 155
Cdd:COG2226   77 DAEDL-PFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 44-136 6.47e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 79.53  E-value: 6.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   44 DIGCGTGKATF-VVELYFKEVIGIDPSSAMLSIAEKetNERRLDKKIRFINAPGEDLsSIRPESVDMVISAEAIHWCN-- 120
Cdd:pfam13649   3 DLGCGTGRLTLaLARRGGARVTGVDLSPEMLERARE--RAAEAGLNVEFVQGDAEDL-PFPDGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 768811324  121 -LERLFQQVSSILRSDG 136
Cdd:pfam13649  80 dLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 42-144 2.00e-16

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: 73.23  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  42 LVDIGCGTGKATF-VVELYFKEVIGIDPSSAMLSIAEKEtNERRLDKKIRFINAPGEDLSSIRPESVDMVISAEAIHWC- 119
Cdd:cd02440    2 VLDLGCGTGALALaLASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLv 80

                         90       100
                 ....*....|....*....|....*.
gi 768811324 120 -NLERLFQQVSSILRSDGTFAFWFYI 144
Cdd:cd02440   81 eDLARFLEEARRLLKPGGVLVLTLVL 106
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 26-140 4.29e-13

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: 67.31  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   26 SLVNEIMKFHKGTRKSLVDIGCGTGKATFVVELYFK--EVIGIDPSSAMLSIAEKetnerRLDKKIRFINAPGEDLsSIR 103
Cdd:TIGR02072  22 RLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPqaEFIALDISAGMLAQAKT-----KLSENVQFICGDAEKL-PLE 95

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 768811324  104 PESVDMVISAEAIHWCN-LERLFQQVSSILRSDGTFAF 140
Cdd:TIGR02072  96 DSSFDLIVSNLALQWCDdLSQALSELARVLKPGGLLAF 133
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 17-99 1.14e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 48.61  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  17 NNVRPSYplSLVNEIMKF--HKGTRKSLV------------DIGCGTGKATFvveLYFK------EVIGIDPSSAMLSIA 76
Cdd:PRK00216  18 DSIAPKY--DLMNDLLSFglHRVWRRKTIkwlgvrpgdkvlDLACGTGDLAI---ALAKavgktgEVVGLDFSEGMLAVG 92

                         90       100
                 ....*....|....*....|...
gi 768811324  77 EKETNERRLDKKIRFINAPGEDL 99
Cdd:PRK00216  93 REKLRDLGLSGNVEFVQGDAEAL 115
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 16-155 5.09e-22

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: 89.28  E-value: 5.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  16 YNNVRPSYPL-SLVNEIMKFHKGTRksLVDIGCGTGKATFVVELYFKEVIGIDPSSAMLSIAEKETNERRLDkkIRFINA 94
Cdd:COG2226    1 FDRVAARYDGrEALLAALGLRPGAR--VLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768811324  95 PGEDLsSIRPESVDMVISAEAIHWC-NLERLFQQVSSILRSDGTFAFWFYIQPEFVDFPEAL 155
Cdd:COG2226   77 DAEDL-PFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 44-136 6.47e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 79.53  E-value: 6.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   44 DIGCGTGKATF-VVELYFKEVIGIDPSSAMLSIAEKetNERRLDKKIRFINAPGEDLsSIRPESVDMVISAEAIHWCN-- 120
Cdd:pfam13649   3 DLGCGTGRLTLaLARRGGARVTGVDLSPEMLERARE--RAAEAGLNVEFVQGDAEDL-PFPDGSFDLVVSSGVLHHLPdp 79

                          90
                  ....*....|....*..
gi 768811324  121 -LERLFQQVSSILRSDG 136
Cdd:pfam13649  80 dLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 43-140 1.09e-18

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 78.86  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   43 VDIGCGTGKATFVVELYFKEVIGIDPSSAMLSIAEKETNERRLDkkirFINAPGEDLsSIRPESVDMVISAEAIHWC-NL 121
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLT----FVVGDAEDL-PFPDNSFDLVLSSEVLHHVeDP 75

                          90
                  ....*....|....*....
gi 768811324  122 ERLFQQVSSILRSDGTFAF 140
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
41-142 2.06e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 75.63  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  41 SLVDIGCGTGKAT--FVVELYFKEVIGIDPSSAMLSIAeketneRRLDKKIRFINApgeDLSSIRP-ESVDMVISAEAIH 117
Cdd:COG4106    4 RVLDLGCGTGRLTalLAERFPGARVTGVDLSPEMLARA------RARLPNVRFVVA---DLRDLDPpEPFDLVVSNAALH 74

                         90       100
                 ....*....|....*....|....*.
gi 768811324 118 WC-NLERLFQQVSSILRSDGTFAFWF 142
Cdd:COG4106   75 WLpDHAALLARLAAALAPGGVLAVQV 100
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
9-140 3.92e-17

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 77.35  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   9 KNFESAHYNNVRPSYPLSLVNEIMKFHKGTR-KSLVDIGCGTGKATFVVELYFKEVIGIDPSSAMLSIAEketnERRLDk 87
Cdd:COG4976   16 DSYDAALVEDLGYEAPALLAEELLARLPPGPfGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR----EKGVY- 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768811324  88 kIRFINApgeDLSSIR--PESVDMVISAEAIHWC-NLERLFQQVSSILRSDGTFAF 140
Cdd:COG4976   91 -DRLLVA---DLADLAepDGRFDLIVAADVLTYLgDLAAVFAGVARALKPGGLFIF 142
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-140 6.62e-17

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: 75.05  E-value: 6.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  28 VNEIMKFHKGTRKSLVDIGCGTGKATFVVELYFKEVIGIDPSSAMLSIAEKETNERRldkkIRFINAPGEDLsSIRPESV 107
Cdd:COG2227   14 LAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELN----VDFVQGDLEDL-PLEDGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 768811324 108 DMVISAEAIHWC-NLERLFQQVSSILRSDGTFAF 140
Cdd:COG2227   89 DLVICSEVLEHLpDPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 42-144 2.00e-16

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: 73.23  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  42 LVDIGCGTGKATF-VVELYFKEVIGIDPSSAMLSIAEKEtNERRLDKKIRFINAPGEDLSSIRPESVDMVISAEAIHWC- 119
Cdd:cd02440    2 VLDLGCGTGALALaLASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLv 80

                         90       100
                 ....*....|....*....|....*.
gi 768811324 120 -NLERLFQQVSSILRSDGTFAFWFYI 144
Cdd:cd02440   81 eDLARFLEEARRLLKPGGVLVLTLVL 106
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 41-140 1.32e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 73.41  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  41 SLVDIGCGTGKATFVV-ELYFKEVIGIDPSSAMLSIAEKETNERRLDKkIRFINAPGEDLSSIRPESVDMVISAEAIHWC 119
Cdd:COG0500   29 RVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIALARARAAKAGLGN-VEFLVADLAELDPLPAESFDLVVAFGVLHHL 107

                         90       100
                 ....*....|....*....|....
gi 768811324 120 NLE---RLFQQVSSILRSDGTFAF 140
Cdd:COG0500  108 PPEereALLRELARALKPGGVLLL 131
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 43-138 1.65e-14

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 67.78  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   43 VDIGCGTGKATFVV--ELYFKEVIGIDPSSAMLSIAEKETNERRLDKkIRFINAPGEDLSSIRPESVDMVISAEAIHWC- 119
Cdd:pfam08242   1 LEIGCGTGTLLRALleALPGLEYTGLDISPAALEAARERLAALGLLN-AVRVELFQLDLGELDPGSFDVVVASNVLHHLa 79

                          90
                  ....*....|....*....
gi 768811324  120 NLERLFQQVSSILRSDGTF 138
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 26-140 4.29e-13

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: 67.31  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   26 SLVNEIMKFHKGTRKSLVDIGCGTGKATFVVELYFK--EVIGIDPSSAMLSIAEKetnerRLDKKIRFINAPGEDLsSIR 103
Cdd:TIGR02072  22 RLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPqaEFIALDISAGMLAQAKT-----KLSENVQFICGDAEKL-PLE 95

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 768811324  104 PESVDMVISAEAIHWCN-LERLFQQVSSILRSDGTFAF 140
Cdd:TIGR02072  96 DSSFDLIVSNLALQWCDdLSQALSELARVLKPGGLLAF 133
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 42-140 7.55e-12

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 62.25  E-value: 7.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  42 LVDIGCGTGK-ATFVVELYFKEVIGIDPSSAMLSIAEKETNERRLDKKIRFINAPGEDLSSirPESVDMVISAEAIHWC- 119
Cdd:COG2230   55 VLDIGCGWGGlALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPA--DGQFDAIVSIGMFEHVg 132

                         90       100
                 ....*....|....*....|...
gi 768811324 120 --NLERLFQQVSSILRSDGTFAF 140
Cdd:COG2230  133 peNYPAYFAKVARLLKPGGRLLL 155
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 35-172 1.68e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.50  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   35 HKGTRksLVDIGCGTGKATFVV--ELYFK-EVIGIDPSSAMLSIAEKETNERRLDkKIRFINAPGEDL-SSIRPESVDMV 110
Cdd:pfam13847   2 DKGMR--VLDLGCGTGHLSFELaeELGPNaEVVGIDISEEAIEKARENAQKLGFD-NVEFEQGDIEELpELLEDDKFDVV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768811324  111 ISAEAI-HWCNLERLFQQVSSILRSDGTFA-FWFYIQPEFVDFPEALNVYYKYGWSKDYMGKYL 172
Cdd:pfam13847  79 ISNCVLnHIPDPDKVLQEILRVLKPGGRLIiSDPDSLAELPAHVKEDSTYYAGCVGGAILKKKL 142
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 17-99 1.14e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 48.61  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  17 NNVRPSYplSLVNEIMKF--HKGTRKSLV------------DIGCGTGKATFvveLYFK------EVIGIDPSSAMLSIA 76
Cdd:PRK00216  18 DSIAPKY--DLMNDLLSFglHRVWRRKTIkwlgvrpgdkvlDLACGTGDLAI---ALAKavgktgEVVGLDFSEGMLAVG 92

                         90       100
                 ....*....|....*....|...
gi 768811324  77 EKETNERRLDKKIRFINAPGEDL 99
Cdd:PRK00216  93 REKLRDLGLSGNVEFVQGDAEAL 115
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 39-163 4.16e-06

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: 47.06  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  39 RKSLVDIGCGTGKATFVVELYFK--EVIGIDPSSAMLSIAEKETNERRLDKKIRFINApgeDL----SSIRPESVDMVIS 112
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNGLEDRITVIHG---DLkefaAELPPGSFDLVVS 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768811324 113 ------------------AEAIHW--CNLERLFQQVSSILRSDGTFAFwfyIQPEFVdFPEALNVYYKYGW 163
Cdd:COG4123  115 nppyfkagsgrkspdearAIARHEdaLTLEDLIRAAARLLKPGGRFAL---IHPAER-LAEILAALRKYGL 181
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 36-180 1.90e-05

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 45.42  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   36 KGTRKSLVDIGCGTGKATFVVELYF--KEVIGIDPSSAMLSIAEKETNERRLDKKIRFINapGEDLSSIRPESVDMVIS- 112
Cdd:TIGR00536 112 QPPILHILDLGTGSGCIALALAYEFpnAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQ--SNLFEPLAGQKIDIIVSn 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  113 -----AEAIH--------------------WCNLERLFQQVSSILRSDGtfaFWFY-----IQPEFVDFPEALNVYYKYG 162
Cdd:TIGR00536 190 ppyidEEDLAdlpnvvrfepllalvggddgLNILRQIIELAPDYLKPNG---FLVCeignwQQKSLKELLRIKFTWYDVE 266

                         170
                  ....*....|....*...
gi 768811324  163 WSKDYmgkylNDNQREIL 180
Cdd:TIGR00536 267 NGRDL-----NGKERVVL 279
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 43-139 2.41e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 44.93  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  43 VDIGCGTGKATfvvELYFK-----EVIGIDPSSAMLSIAEKetnerRLdKKIRFINApgeDLSSIRP-ESVDmVISAEAI 116
Cdd:PRK01683  36 VDLGCGPGNST---ELLVErwpaaRITGIDSSPAMLAEARS-----RL-PDCQFVEA---DIASWQPpQALD-LIFANAS 102

                         90       100
                 ....*....|....*....|....*
gi 768811324 117 -HWC-NLERLFQQVSSILRSDGTFA 139
Cdd:PRK01683 103 lQWLpDHLELFPRLVSLLAPGGVLA 127
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
40-112 4.86e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 43.35  E-value: 4.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768811324  40 KSLVDIGCGTGKATFVVELY-FKEVIGIDPSSAMLSIAEKetNERRLDKKIRFINApgeDLSSIRP-ESVDMVIS 112
Cdd:COG2263   47 KTVLDLGCGTGMLAIGAALLgAKKVVGVDIDPEALEIARE--NAERLGVRVDFIRA---DVTRIPLgGSVDTVVM 116
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 42-139 6.65e-05

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: 43.47  E-value: 6.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   42 LVDIGCGTGK-ATFVVELYFKEVIGIDPSSAMLSIAEKETNERRLDKKIRFINAPGEDLssirPESVDMVISAEAI-HWC 119
Cdd:pfam02353  65 LLDIGCGWGGlMRRAAERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF----DEPFDRIVSVGMFeHVG 140

                          90       100
                  ....*....|....*....|..
gi 768811324  120 --NLERLFQQVSSILRSDGTFA 139
Cdd:pfam02353 141 heNYDTFFKKLYNLLPPGGLML 162
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 20-140 9.02e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 42.03  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   20 RPSYPLSLVNEIMKFHKgTRKSLVDIGCGTGKATFVVELYFKEVIGIDPSSAMLSIAeketnerrlDKKIRFINAPGEDL 99
Cdd:pfam13489   5 RERLLADLLLRLLPKLP-SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERA---------LLNVRFDQFDEQEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 768811324  100 SSiRPESVDMVISAEAIHWC-NLERLFQQVSSILRSDGTFAF 140
Cdd:pfam13489  75 AV-PAGKFDVIVAREVLEHVpDPPALLRQIAALLKPGGLLLL 115
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 26-120 1.70e-04

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 40.63  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   26 SLVNEIMKfhKGTRKSLVDIGCGTGKATFVveLYF----KEVIGIDPSSAMLSIAEKETNERRLDKKIRFINAP-GEDLS 100
Cdd:pfam13679  15 PLLKELLD--ENGPITIVDHGAGKGYLGFI--LYYlkygVRVYGIDTRAELVEKANALAQKLGFNKRMSFLEGTiAGSTP 90

                          90       100
                  ....*....|....*....|
gi 768811324  101 SIRPESVDMVIsaeAIHWCN 120
Cdd:pfam13679  91 VELPDRVDVVT---ALHACD 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
43-112 5.06e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.40  E-value: 5.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768811324  43 VDIGCGTG-KATFVVELYFKEVIGIDPSSAMLSIAEKETNERRLDKKIRFINAPGEDLSSirPESVDMVIS 112
Cdd:COG4076   40 LDIGTGSGlLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDL--PEKADVIIS 108
PRK08317 PRK08317
hypothetical protein; Provisional
 41-137 7.09e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 40.31  E-value: 7.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  41 SLVDIGCGTGkaTFVVELYFK-----EVIGIDPSSAMLSIAEKETNERRLdkKIRFINAPGEDLsSIRPESVDMVISAEA 115
Cdd:PRK08317  22 RVLDVGCGPG--NDARELARRvgpegRVVGIDRSEAMLALAKERAAGLGP--NVEFVRGDADGL-PFPDGSFDAVRSDRV 96

                         90       100
                 ....*....|....*....|...
gi 768811324 116 I-HWCNLERLFQQVSSILRSDGT 137
Cdd:PRK08317  97 LqHLEDPARALAEIARVLRPGGR 119
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 43-140 3.45e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 38.13  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324  43 VDIGCGTGKATFVVELYFKE--VIGIDPSSAMLSIAEketnERRLDkkirfinAPGEDLSSIRP-ESVDMVISAEAIHWC 119
Cdd:PRK14103  34 VDLGCGPGNLTRYLARRWPGavIEALDSSPEMVAAAR----ERGVD-------ARTGDVRDWKPkPDTDVVVSNAALQWV 102

                         90       100
                 ....*....|....*....|...
gi 768811324 120 --NLERLFQQVSSiLRSDGTFAF 140
Cdd:PRK14103 103 peHADLLVRWVDE-LAPGSWIAV 124
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
5-117 9.73e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 37.54  E-value: 9.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811324   5 SYLNKNFESAHYNNVrpsyplslvneIMKFHKGTRksLVDIGCGTGKATFVVE--LYFKEVIGIDPSSAMLSIAEKEtnE 82
Cdd:PRK06922 398 VYLEHMNSSADDKRI-----------ILDYIKGDT--IVDVGAGGGVMLDMIEeeTEDKRIYGIDISENVIDTLKKK--K 462

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 768811324  83 RRLDKKIRFINAPGEDL-SSIRPESVDMVISAEAIH 117
Cdd:PRK06922 463 QNEGRSWNVIKGDAINLsSSFEKESVDTIVYSSILH 498
 
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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