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Conserved domains on  [gi|502316134|ref|WP_012761548|]
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MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Ralstonia]

Protein Classification

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG( domain architecture ID 11493423)

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG is a class I SAM-dependent methyltransferase that catalyzes both methylation steps in ubiquinone biosynthesis

CATH:  3.40.50.150
EC:  2.1.1.222|2.1.1.64
Gene Ontology:  GO:0102208|GO:0008425|GO:0032259|GO:0006744
PubMed:  10419476|11583838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 12-229 3.07e-119

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


:

Pssm-ID: 273910  Cd Length: 224  Bit Score: 338.89  E-value: 3.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   12 ELEKFSELAHRWWDPNSEFKPLHEINPLRLDWIQSI------TPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKA 85
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRirknfkNPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   86 LRVADLHSLEAGVTVDYEEIAAEALAAREPGSFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTIHRNAKAYLLA 165
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502316134  166 VIGAEYVLNMLPRGTHDYAKFIRPSELSAFVRAAGLQAQEMRGLEYNPITARYALTQDTSVNYL 229
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 12-229 3.07e-119

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 338.89  E-value: 3.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   12 ELEKFSELAHRWWDPNSEFKPLHEINPLRLDWIQSI------TPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKA 85
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRirknfkNPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   86 LRVADLHSLEAGVTVDYEEIAAEALAAREPGSFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTIHRNAKAYLLA 165
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502316134  166 VIGAEYVLNMLPRGTHDYAKFIRPSELSAFVRAAGLQAQEMRGLEYNPITARYALTQDTSVNYL 229
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 2-229 2.55e-68

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 213.06  E-value: 2.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   2 TTTHANADpgELEKFSELAHRWWDPNSEFKPLHEINPLRLDWIQSI------------TPLAGKRIVDVGCGGGILSESM 69
Cdd:PLN02396  72 TTTSLNED--ELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTlcrhfskdpssaKPFEGLKFIDIGCGGGLLSEPL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  70 ARAGAIVKGIDLSRKALRVADLHSLEAGVTVDYEEIAAEALAAREPG-SFDVVTCMEMLEHVPDPASVVRACATLVKPGG 148
Cdd:PLN02396 150 ARMGATVTGVDAVDKNVKIARLHADMDPVTSTIEYLCTTAEKLADEGrKFDAVLSLEVIEHVANPAEFCKSLSALTIPNG 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134 149 YVFFSTIHRNAKAYLLAVIGAEYVLNMLPRGTHDYAKFIRPSELSAFVRAAGLQAQEMRGLEYNPITARYALTQDTSVNY 228
Cdd:PLN02396 230 ATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNY 309


                 .
gi 502316134 229 L 229
Cdd:PLN02396 310 I 310
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 20-156 2.35e-35

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: 122.05  E-value: 2.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  20 AHRWWDPnsefkplhEINPLRLDWIqsitpLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVT 99
Cdd:COG2227    6 ARDFWDR--------RLAALLARLL-----PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVD 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502316134 100 VdyeEIAAEALAAREPGSFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTIH 156
Cdd:COG2227   73 F---VQGDLEDLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-202 1.86e-21

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 87.10  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   48 TPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVTVDyeeiaaeaLAAREPGSFDVVTCMEML 127
Cdd:pfam13489  19 KLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQ--------EAAVPAGKFDVIVAREVL 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502316134  128 EHVPDPASVVRACATLVKPGGYVFFSTIHRNAKAYLLavigAEYVLNMLPRGTHdyAKFIRPSELSAFVRAAGLQ 202
Cdd:pfam13489  91 EHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGH--ISLFSARSLKRLLEEAGFE 159
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-156 6.01e-11

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 57.83  E-value: 6.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  54 RIVDVGCGGGILSESMARAGAI-VKGIDLSRKALRVADLHSLEAG-VTVDYEEIAAEALAAREPGSFDVVTCMEMLEH-V 130
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLaDNVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90       100
                 ....*....|....*....|....*.
gi 502316134 131 PDPASVVRACATLVKPGGYVFFSTIH 156
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 12-229 3.07e-119

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 338.89  E-value: 3.07e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   12 ELEKFSELAHRWWDPNSEFKPLHEINPLRLDWIQSI------TPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKA 85
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRirknfkNPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   86 LRVADLHSLEAGVTVDYEEIAAEALAAREPGSFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTIHRNAKAYLLA 165
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502316134  166 VIGAEYVLNMLPRGTHDYAKFIRPSELSAFVRAAGLQAQEMRGLEYNPITARYALTQDTSVNYL 229
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 2-229 2.55e-68

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 213.06  E-value: 2.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   2 TTTHANADpgELEKFSELAHRWWDPNSEFKPLHEINPLRLDWIQSI------------TPLAGKRIVDVGCGGGILSESM 69
Cdd:PLN02396  72 TTTSLNED--ELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTlcrhfskdpssaKPFEGLKFIDIGCGGGLLSEPL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  70 ARAGAIVKGIDLSRKALRVADLHSLEAGVTVDYEEIAAEALAAREPG-SFDVVTCMEMLEHVPDPASVVRACATLVKPGG 148
Cdd:PLN02396 150 ARMGATVTGVDAVDKNVKIARLHADMDPVTSTIEYLCTTAEKLADEGrKFDAVLSLEVIEHVANPAEFCKSLSALTIPNG 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134 149 YVFFSTIHRNAKAYLLAVIGAEYVLNMLPRGTHDYAKFIRPSELSAFVRAAGLQAQEMRGLEYNPITARYALTQDTSVNY 228
Cdd:PLN02396 230 ATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNY 309


                 .
gi 502316134 229 L 229
Cdd:PLN02396 310 I 310
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 20-156 2.35e-35

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: 122.05  E-value: 2.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  20 AHRWWDPnsefkplhEINPLRLDWIqsitpLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVT 99
Cdd:COG2227    6 ARDFWDR--------RLAALLARLL-----PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVD 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502316134 100 VdyeEIAAEALAAREPGSFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTIH 156
Cdd:COG2227   73 F---VQGDLEDLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 39-167 1.10e-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: 90.05  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  39 LRLDWIQSITPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVTVDYeEIAAEALAAREPGSF 118
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEF-VVGDAEDLPFPDGSF 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 502316134 119 DVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTIHRNAKAYLLAVI 167
Cdd:COG2226   89 DLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-202 1.86e-21

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 87.10  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   48 TPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVTVDyeeiaaeaLAAREPGSFDVVTCMEML 127
Cdd:pfam13489  19 KLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQ--------EAAVPAGKFDVIVAREVL 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502316134  128 EHVPDPASVVRACATLVKPGGYVFFSTIHRNAKAYLLavigAEYVLNMLPRGTHdyAKFIRPSELSAFVRAAGLQ 202
Cdd:pfam13489  91 EHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGH--ISLFSARSLKRLLEEAGFE 159
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-152 1.23e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 83.10  E-value: 1.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   56 VDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVTVdyeEIAAEALAAREPGSFDVVTCMEMLEHVPDPAS 135
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTF---VVGDAEDLPFPDNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 502316134  136 VVRACATLVKPGGYVFF 152
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-148 4.28e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.45  E-value: 4.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   55 IVDVGCGGGILSESMARA-GAIVKGIDLSRKALRVADLHSLEAGVTVDYEEIAAEALAARePGSFDVVTCMEMLEHVPDP 133
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 502316134  134 --ASVVRACATLVKPGG 148
Cdd:pfam13649  80 dlEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 18-154 3.01e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 76.12  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  18 ELAHRWWDPN---------SEFKPLHEINPLRLDWIQSITPL-AGKRIVDVGCGGGILSESMARA-GAIVKGIDLSRKAL 86
Cdd:COG2230    8 DFYRLFLDPTmtyscayfeDPDDTLEEAQEAKLDLILRKLGLkPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502316134  87 RVA----DLHSLEAGVTV---DYEEIAAealaarePGSFDVVTCMEMLEHVPDP--ASVVRACATLVKPGGYVFFST 154
Cdd:COG2230   88 EYAreraAEAGLADRVEVrlaDYRDLPA-------DGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
39-154 1.09e-16

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 75.03  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  39 LRLDWIQSITPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVTVDyeeiaAEALAAREPGSF 118
Cdd:COG4976   34 LAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLLVA-----DLADLAEPDGRF 108

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502316134 119 DVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFST 154
Cdd:COG4976  109 DLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
51-154 4.38e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 68.70  E-value: 4.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  51 AGKRIVDVGCGGGILSESMARA--GAIVKGIDLSRKAL------------RVADLHSLEAgvtvdyeeiaaealaarePG 116
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLarararlpnvrfVVADLRDLDP------------------PE 62

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 502316134 117 SFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFST 154
Cdd:COG4106   63 PFDLVVSNAALHWLPDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 35-153 4.94e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 65.71  E-value: 4.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  35 EINPLRLDWIQSITPL-AGKRIVDVGCGGGILSESMA-RAGAIVKGIDLSRKALRVADLHSLEAGVT-VDYEEIAAEALA 111
Cdd:COG0500    9 ELLPGLAALLALLERLpKGGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELD 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502316134 112 AREPGSFDVVTCMEMLEHVP--DPASVVRACATLVKPGGYVFFS 153
Cdd:COG0500   89 PLPAESFDLVVAFGVLHHLPpeEREALLRELARALKPGGVLLLS 132
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 41-143 1.98e-12

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 64.47  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  41 LDWIQSITPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVT--VDYEEIAAEALAarepGSF 118
Cdd:PRK07580  53 LSWLPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgnITFEVGDLESLL----GRF 128

                         90       100
                 ....*....|....*....|....*
gi 502316134 119 DVVTCMEMLEHVPDPAsVVRACATL 143
Cdd:PRK07580 129 DTVVCLDVLIHYPQED-AARMLAHL 152
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-150 2.92e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 60.84  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   56 VDVGCGGGILSESMARAGAIVK--GIDLSRKALRVADLHSLEAG-VTVDYEEIAAEALAAREPGSFDVVTCMEMLEHVPD 132
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEytGLDISPAALEAARERLAALGlLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 502316134  133 PASVVRACATLVKPGGYV 150
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
PLN02244 PLN02244
tocopherol O-methyltransferase
 53-158 9.91e-12

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 63.61  E-value: 9.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  53 KRIVDVGCGGGILSESMARA-GAIVKGIDLSRK-ALRVADLhSLEAGVTVDYEEIAAEALAAREP-GSFDVVTCMEMLEH 129
Cdd:PLN02244 120 KRIVDVGCGIGGSSRYLARKyGANVKGITLSPVqAARANAL-AAAQGLSDKVSFQVADALNQPFEdGQFDLVWSMESGEH 198

                         90       100       110
                 ....*....|....*....|....*....|
gi 502316134 130 VPDPASVVRACATLVKPGGYVFFST-IHRN 158
Cdd:PLN02244 199 MPDKRKFVQELARVAAPGGRIIIVTwCHRD 228
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-156 6.01e-11

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 57.83  E-value: 6.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  54 RIVDVGCGGGILSESMARAGAI-VKGIDLSRKALRVADLHSLEAG-VTVDYEEIAAEALAAREPGSFDVVTCMEMLEH-V 130
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLaDNVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90       100
                 ....*....|....*....|....*.
gi 502316134 131 PDPASVVRACATLVKPGGYVFFSTIH 156
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTLVL 106
PRK08317 PRK08317
hypothetical protein; Provisional
 47-150 2.30e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 55.71  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  47 ITPLAGKRIVDVGCGGGILSESMARA---GAIVKGIDLSRKALRVADLHSLEAGVTVDYEEIAAEALAAREpGSFDVVTC 123
Cdd:PRK08317  15 LAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPD-GSFDAVRS 93

                         90       100
                 ....*....|....*....|....*..
gi 502316134 124 MEMLEHVPDPASVVRACATLVKPGGYV 150
Cdd:PRK08317  94 DRVLQHLEDPARALAEIARVLRPGGRV 120
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 51-156 5.47e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 53.19  E-value: 5.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   51 AGKRIVDVGCGGGILSESMA---RAGAIVKGIDLSRKALRVA-----------------DLHSLEAGVTVDyeeiaaeal 110
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAeelGPNAEVVGIDISEEAIEKArenaqklgfdnvefeqgDIEELPELLEDD--------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 502316134  111 aarepgSFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTIH 156
Cdd:pfam13847  74 ------KFDVVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 41-155 2.79e-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: 49.98  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   41 LDWIQSITPLAGKRIVDVGCGGGILSESMARAGAIVKGI--DLSRKALRVADLHSleaGVTVDYEEIAAEALAARePGSF 118
Cdd:TIGR02072  24 LALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIalDISAGMLAQAKTKL---SENVQFICGDAEKLPLE-DSSF 99

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 502316134  119 DVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTI 155
Cdd:TIGR02072 100 DLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTF 136
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 34-155 4.55e-07

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 49.57  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   34 HEINPLRLDWIQSITpLAGKRIVDVGCGGGILSESMARAGAI-VKGIDLSRKALRVA----DLHSLEAGVTVdyeeiaaE 108
Cdd:pfam06325 145 HPTTKLCLEALERLV-KPGESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAkenaELNGVEARLEV-------Y 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502316134  109 ALAAREPGSFDVVTC-------MEMLEHVpdpasvvracATLVKPGGYVFFSTI 155
Cdd:pfam06325 217 LPGDLPKEKADVVVAniladplIELAPDI----------YALVKPGGYLILSGI 260
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 44-216 5.79e-07

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: 48.80  E-value: 5.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   44 IQSITPLAGKRIVDVGCGGGILSESMARAGAI---VKGIDLSRKALRVA-DLHSLEAGVTvdyeeiAAEALAAREP---G 116
Cdd:TIGR01934  32 VKLIGVFKGQKVLDVACGTGDLAIELAKSAPDrgkVTGVDFSSEMLEVAkKKSELPLNIE------FIQADAEALPfedN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  117 SFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTIHRNAKAyLLAVIGAEYVLNMLPR---------GTHDY---- 183
Cdd:TIGR01934 106 SFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANA-LLKKFYKFYLKNVLPSigglisknaEAYTYlpes 184

                         170       180       190
                  ....*....|....*....|....*....|....
gi 502316134  184 -AKFIRPSELSAFVRAAGLqaqemRGLEYNPITA 216
Cdd:TIGR01934 185 iRAFPSQEELAAMLKEAGF-----EEVRYRSLTF 213
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
41-153 7.23e-07

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 49.02  E-value: 7.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  41 LDWIQSItPLAGKRIVDVGCGGGILSESMARAGAI-VKGIDLSRKALRV----ADLHSLEAGVTVdyeeiaaEALAAREP 115
Cdd:COG2264  139 LEALEKL-LKPGKTVLDVGCGSGILAIAAAKLGAKrVLAVDIDPVAVEAarenAELNGVEDRIEV-------VLGDLLED 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502316134 116 GSFDVVTC-------MEMLEHVpdpasvvracATLVKPGGYVFFS 153
Cdd:COG2264  211 GPYDLVVAnilanplIELAPDL----------AALLKPGGYLILS 245
PRK06202 PRK06202
hypothetical protein; Provisional
 54-198 1.30e-06

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 47.69  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  54 RIVDVGCGGGILSESMARAGA------IVKGIDLSRKALRVADLHSLEAGVTVdyeEIAAEALAAREPGSFDVVTCMEML 127
Cdd:PRK06202  63 TLLDIGCGGGDLAIDLARWARrdglrlEVTAIDPDPRAVAFARANPRRPGVTF---RQAVSDELVAEGERFDVVTSNHFL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134 128 EHVpDPASVVR---ACATLVKpgGYVFFSTIHRNAKAYLLAVIGAEyvlnMLPRGT---HDYAKFIR----PSELSAFVR 197
Cdd:PRK06202 140 HHL-DDAEVVRllaDSAALAR--RLVLHNDLIRSRLAYALFWAGTR----LLSRSSfvhTDGLLSVRrsytPAELAALAP 212


                 .
gi 502316134 198 A 198
Cdd:PRK06202 213 Q 213
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
50-102 1.41e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.21  E-value: 1.41e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502316134  50 LAGKRIVDVGCGGGILSESMARAGA-IVKGIDLSRKALRVADLHSLEAGVTVDY 102
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRVDF 97
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
41-155 1.69e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 47.45  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  41 LDWIQSItPLAGKRIVDVGCGGGILSESMARAGAI-VKGIDLSRKALRV----ADLHSLEAGVTVDYEEIaaealaarep 115
Cdd:PRK00517 110 LEALEKL-VLPGKTVLDVGCGSGILAIAAAKLGAKkVLAVDIDPQAVEAarenAELNGVELNVYLPQGDL---------- 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 502316134 116 gSFDVVTC-------MEMLEHVpdpasvvracATLVKPGGYVFFSTI 155
Cdd:PRK00517 179 -KADVIVAnilanplLELAPDL----------ARLLKPGGRLILSGI 214
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 41-132 2.33e-06

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 47.54  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  41 LDWIQSITPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSrkALRVAdlhslEAgvTVDYEEIAAEALAAREP----- 115
Cdd:PLN02585 134 LLWLAEDGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDIS--AAMVA-----EA--ERRAKEALAALPPEVLPkfean 204

                         90       100
                 ....*....|....*....|...
gi 502316134 116 ------GSFDVVTCMEMLEHVPD 132
Cdd:PLN02585 205 dleslsGKYDTVTCLDVLIHYPQ 227
PRK14967 PRK14967
putative methyltransferase; Provisional
 52-123 3.30e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 46.58  E-value: 3.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502316134  52 GKRIVDVGCGGGILSESMARAGAI-VKGIDLSRKALRVADLHSLEAGVTVDYEEIAAEALAAREPgsFDVVTC 123
Cdd:PRK14967  37 GRRVLDLCTGSGALAVAAAAAGAGsVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEFRP--FDVVVS 107
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 34-155 5.34e-06

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 46.37  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   34 HEINPLRLDWIQSITpLAGKRIVDVGCGGGILSESMARAGAI-VKGIDLSRKALRVAdLHSLEAGVTVDYEEIAAEALAA 112
Cdd:TIGR00406 143 HPTTSLCLEWLEDLD-LKDKNVIDVGCGSGILSIAALKLGAAkVVGIDIDPLAVESA-RKNAELNQVSDRLQVKLIYLEQ 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 502316134  113 REPGSFDVVTCMEMLEHVPDPASVVracATLVKPGGYVFFSTI 155
Cdd:TIGR00406 221 PIEGKADVIVANILAEVIKELYPQF---SRLVKPGGWLILSGI 260
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 39-100 8.16e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 45.53  E-value: 8.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502316134  39 LRLDWIQSITPLagkRIVDVGCGGGILSESMARA--GAIVKGIDLSRKALRVA----DLHSLEAGVTV 100
Cdd:COG2890  103 LALALLPAGAPP---RVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVArrnaERLGLEDRVRF 167
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 51-157 1.85e-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: 44.37  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  51 AGKRIVDVGCGGGILSESMAR--AGAIVKGIDLSRK----ALRVADLHSLEAGVTVdYEEIAAEALAAREPGSFDVVTC- 123
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQrsPGARITGVEIQPEaaelARRNVALNGLEDRITV-IHGDLKEFAAELPPGSFDLVVSn 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502316134 124 ---MEMLEHV--PDPA-------------SVVRACATLVKPGGYVFFstIHR 157
Cdd:COG4123  116 ppyFKAGSGRksPDEAraiarhedaltleDLIRAAARLLKPGGRFAL--IHP 165
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
47-190 5.66e-05

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 43.31  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  47 ITPLAGKRIVDVGCGGGILSESMARAGA-IVKGIDLS-----------------RKA----LRVADLHSLEAgvtvdyee 104
Cdd:PRK15068 118 LSPLKGRTVLDVGCGNGYHMWRMLGAGAkLVVGIDPSqlflcqfeavrkllgndQRAhllpLGIEQLPALKA-------- 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134 105 iaaealaarepgsFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTihrnakaylLAVIG-AEYVLnmLPRGThdY 183
Cdd:PRK15068 190 -------------FDTVFSMGVLYHRRSPLDHLKQLKDQLVPGGELVLET---------LVIDGdENTVL--VPGDR--Y 243

                        170
                 ....*....|..
gi 502316134 184 AK-----FIrPS 190
Cdd:PRK15068 244 AKmrnvyFI-PS 254
PRK14968 PRK14968
putative methyltransferase; Provisional
 51-89 1.00e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.81  E-value: 1.00e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 502316134  51 AGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVA 89
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECA 61
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 42-102 1.63e-04

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 41.41  E-value: 1.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502316134  42 DWIQSITPLAGKRIVDVGCGGGILSESMARAGAI-VKGIDLSRKALRVADLHSLEAGVTVDY 102
Cdd:COG3897   61 RYLLDHPEVAGKRVLELGCGLGLVGIAAAKAGAAdVTATDYDPEALAALRLNAALNGVAITT 122
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 44-89 7.15e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.76  E-value: 7.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 502316134  44 IQSITPLAGKRIVDVGCGGGILSESMA--RAGAIVKGIDLSRKALRVA 89
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIALALAkeRPDAEVTAVDISPEALAVA 148
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
49-150 9.94e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 39.34  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   49 PLAGKRIVDVGCGGG----ILSESMARAGAIVkGIDLSRKALRVADLHSLEAGVT-VDYEEIAAEALAAREpGSFDVVTC 123
Cdd:pfam01209  40 VKRGNKFLDVAGGTGdwtfGLSDSAGSSGKVV-GLDINENMLKEGEKKAKEEGKYnIEFLQGNAEELPFED-DSFDIVTI 117

                          90       100
                  ....*....|....*....|....*..
gi 502316134  124 MEMLEHVPDPASVVRACATLVKPGGYV 150
Cdd:pfam01209 118 SFGLRNFPDYLKVLKEAFRVLKPGGRV 144
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 40-155 1.15e-03

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: 39.31  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   40 RLDW-----IQSITPLAGKRIVDVGCGGGILSESMARAGA-IVKGIDLSR------KALR---------------VADLH 92
Cdd:pfam08003  99 RSDWkwdrvLPHLSPLKGRTILDVGCGNGYHMWRMLGEGAaMVVGIDPSElflcqfEAVRkllgndqrahllplgIEQLP 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502316134   93 SLEAgvtvdyeeiaaealaarepgsFDVVTCMEMLEHVPDPASVVRACATLVKPGGYVFFSTI 155
Cdd:pfam08003 179 ALAA---------------------FDTVFSMGVLYHRRSPLDHLLQLKDQLVKGGELVLETL 220
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 51-155 2.12e-03

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: 38.46  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134   51 AGKRIVDVGCG-GGILSESMARAGAIVKGIDLSRKALRVA----DLHSLEAGVTVDYeeiaaeALAAREPGSFDVVTCME 125
Cdd:pfam02353  61 PGMTLLDIGCGwGGLMRRAAERYDVNVVGLTLSKNQYKLArkrvAAEGLARKVEVLL------QDYRDFDEPFDRIVSVG 134

                          90       100       110
                  ....*....|....*....|....*....|...
gi 502316134  126 MLEHVpDPASVVRACATL---VKPGGYVFFSTI 155
Cdd:pfam02353 135 MFEHV-GHENYDTFFKKLynlLPPGGLMLLHTI 166
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 50-152 3.79e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 37.75  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  50 LAGKRIVDVGCGGGILSESMAR--AGAIVKGIDLSRKALRVADLHSLEAGV--------TVDYeeiaaealaarepgsfD 119
Cdd:PRK14103  28 ERARRVVDLGCGPGNLTRYLARrwPGAVIEALDSSPEMVAAARERGVDARTgdvrdwkpKPDT----------------D 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 502316134 120 VVTCMEMLEHVPDPASVVRACATLVKPGGYVFF 152
Cdd:PRK14103  92 VVVSNAALQWVPEHADLLVRWVDELAPGSWIAV 124
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 51-160 3.87e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.81  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  51 AGKRIVDVGCGGGILSESMARA-GAIVKGIDLSRKALRVADLHSLEAGVTVDYEEIAAEALAAREpGSFDVVTCMEMLEH 129
Cdd:PLN02336 266 PGQKVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPD-NSFDVIYSRDTILH 344

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502316134 130 VPDPASVVRACATLVKPGGYVFFSTIHRNAK 160
Cdd:PLN02336 345 IQDKPALFRSFFKWLKPGGKVLISDYCRSPG 375
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 33-87 6.01e-03

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 36.64  E-value: 6.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 502316134   33 LHEINPLRLDWIQSITPLAGKRIVDVGCGGGILSESMARAGAIVKGIDLSRKALR 87
Cdd:pfam05724  19 QEGVNPLLVRHWDALKLPPGLRVLVPLCGKALDMVWLAEQGHFVVGVEISELAVE 73
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 44-89 6.44e-03

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 36.41  E-value: 6.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 502316134   44 IQSITPLAGKRIVDVGCGGGILSESMARAG--AIVKGIDLSRKALRVA 89
Cdd:pfam05175  24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESA 71
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
54-178 8.82e-03

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 36.48  E-value: 8.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502316134  54 RIVDVGCGGGILSESMARAGAIVKGIDLSRKALRVADLHSLEAGVTVDY--EEIAAEALAAREPGSFDVVTCMEMLEHVP 131
Cdd:PRK11036  47 RVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMqfIHCAAQDIAQHLETPVDLILFHAVLEWVA 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 502316134 132 DPASVVRACATLVKPGGYVffSTIHRNAKAYLL--AVIGA-EYVLNMLPR 178
Cdd:PRK11036 127 DPKSVLQTLWSVLRPGGAL--SLMFYNANGLLMhnMVAGNfDYVQAGMPK 174
 
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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