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Conserved domains on  [gi|446319745|ref|WP_000397600|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Bacillus thuringiensis]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-135 2.66e-21

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: 85.07  E-value: 2.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  36 KDILVPGIGYGRNAKVFIDNGINVTGIEISKTAIDLAMQNGLE-DISIYHGSVNEMPFNNKLYDGIYSHALLHLLnkQER 114
Cdd:COG2227   26 GRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElNVDFVQGDLEDLPLEDGSFDLVICSEVLEHL--PDP 103

                         90       100
                 ....*....|....*....|.
gi 446319745 115 EQFIKDCYNQLKPGGYMVFTT 135
Cdd:COG2227  104 AALLRELARLLKPGGLLLLST 124
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-135 2.66e-21

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: 85.07  E-value: 2.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  36 KDILVPGIGYGRNAKVFIDNGINVTGIEISKTAIDLAMQNGLE-DISIYHGSVNEMPFNNKLYDGIYSHALLHLLnkQER 114
Cdd:COG2227   26 GRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElNVDFVQGDLEDLPLEDGSFDLVICSEVLEHL--PDP 103

                         90       100
                 ....*....|....*....|.
gi 446319745 115 EQFIKDCYNQLKPGGYMVFTT 135
Cdd:COG2227  104 AALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 42-133 5.84e-18

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 75.39  E-value: 5.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   42 GIGYGRNAKVFIDNGINVTGIEISKTAIDLAMQNG-LEDISIYHGSVNEMPFNNKLYDGIYSHALLHLLNkqEREQFIKD 120
Cdd:pfam08241   4 GCGTGLLTELLARLGARVTGVDISPEMLELAREKApREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVE--DPERALRE 81

                          90
                  ....*....|...
gi 446319745  121 CYNQLKPGGYMVF 133
Cdd:pfam08241  82 IARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 37-136 1.19e-10

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: 56.28  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  37 DILVPGIGYGRNAKVFID-NGINVTGIEISKTAIDLAMQN----GLEDISIYHGSVNEMPFNNKL-YDGIYSHALLHLLn 110
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAaaalLADNVEVLKGDAEELPPEADEsFDVIISDPPLHHL- 79

                         90       100
                 ....*....|....*....|....*.
gi 446319745 111 KQEREQFIKDCYNQLKPGGYMVFTTV 136
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLTLV 105
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 55-138 3.30e-04

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: 40.35  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   55 NGINVTGIEISKTAIDLAMQNGLEDISIYHGSVNEMPFNNKLYDGIYSHALLHLLNKQEreQFIKDCYNQLKPGGYMVFT 134
Cdd:TIGR02072  57 PQAEFIALDISAGMLAQAKTKLSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLS--QALSELARVLKPGGLLAFS 134


                  ....
gi 446319745  135 TVSQ 138
Cdd:TIGR02072 135 TFGP 138
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-135 2.66e-21

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: 85.07  E-value: 2.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  36 KDILVPGIGYGRNAKVFIDNGINVTGIEISKTAIDLAMQNGLE-DISIYHGSVNEMPFNNKLYDGIYSHALLHLLnkQER 114
Cdd:COG2227   26 GRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElNVDFVQGDLEDLPLEDGSFDLVICSEVLEHL--PDP 103

                         90       100
                 ....*....|....*....|.
gi 446319745 115 EQFIKDCYNQLKPGGYMVFTT 135
Cdd:COG2227  104 AALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 42-133 5.84e-18

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 75.39  E-value: 5.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   42 GIGYGRNAKVFIDNGINVTGIEISKTAIDLAMQNG-LEDISIYHGSVNEMPFNNKLYDGIYSHALLHLLNkqEREQFIKD 120
Cdd:pfam08241   4 GCGTGLLTELLARLGARVTGVDISPEMLELAREKApREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVE--DPERALRE 81

                          90
                  ....*....|...
gi 446319745  121 CYNQLKPGGYMVF 133
Cdd:pfam08241  82 IARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 42-129 5.35e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.98  E-value: 5.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   42 GIGYGRNAKVFIDN-GINVTGIEISKTAIDLAMQNGLE---DISIYHGSVNEMPFNNKLYDGIYSHALLHLLNKQEREQF 117
Cdd:pfam13649   5 GCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEaglNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPDLEAA 84

                          90
                  ....*....|..
gi 446319745  118 IKDCYNQLKPGG 129
Cdd:pfam13649  85 LREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 3-168 7.72e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 72.64  E-value: 7.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   3 FWESSFIEKQTmwgfePTESAILTKDFFLEKNVKdILVPGIGYGRNAKVFID-NGINVTGIEISKTAIDLAMQN----GL 77
Cdd:COG0500    1 PWDSYYSDELL-----PGLAALLALLERLPKGGR-VLDLGCGTGRNLLALAArFGGRVIGIDLSPEAIALARARaakaGL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  78 EDISIYHGSVNE-MPFNNKLYDGIYSHALLHLLNKQEREQFIKDCYNQLKPGGYMVFTTVSQKAPMYGKGKQLEQDYYEI 156
Cdd:COG0500   75 GNVEFLVADLAElDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLL 154

                        170
                 ....*....|..
gi 446319745 157 MEGVKMFFYDSE 168
Cdd:COG0500  155 ELLLLLRLLALE 166
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 36-138 3.49e-14

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: 66.94  E-value: 3.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  36 KDILVPGIGYGRNAKVFIDNGINVTGIEISKTAIDLAMQNGLE---DISIYHGSVNEMPFNNKLYDGIYSHALLHLLnkQ 112
Cdd:COG2226   24 ARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEaglNVEFVVGDAEDLPFPDGSFDLVISSFVLHHL--P 101

                         90       100
                 ....*....|....*....|....*.
gi 446319745 113 EREQFIKDCYNQLKPGGYMVFTTVSQ 138
Cdd:COG2226  102 DPERALAEIARVLKPGGRLVVVDFSP 127
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 38-135 1.16e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 60.33  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  38 ILVPGIGYGRNAKVFIDN-GINVTGIEISKTAIDLAMQN----GLED-ISIYHGSVNEMPFNNKlYDGIYSHALLHLLNK 111
Cdd:COG2230   55 VLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERaaeaGLADrVEVRLADYRDLPADGQ-FDAIVSIGMFEHVGP 133

                         90       100
                 ....*....|....*....|....
gi 446319745 112 QEREQFIKDCYNQLKPGGYMVFTT 135
Cdd:COG2230  134 ENYPAYFAKVARLLKPGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
42-135 1.16e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 60.78  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  42 GIGYGRNAKVFIDNGINVTGIEISKTAIDLAMQNGLEDiSIYHGSVNEMPFNNKLYDGIYSHALLHLLNKQEReqFIKDC 121
Cdd:COG4976   54 GCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYD-RLLVADLADLAEPDGRFDLIVAADVLTYLGDLAA--VFAGV 130

                         90
                 ....*....|....
gi 446319745 122 YNQLKPGGYMVFTT 135
Cdd:COG4976  131 ARALKPGGLFIFSV 144
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 33-183 4.81e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 58.98  E-value: 4.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   33 KNVKDIlvpGIGYGRNAKVFIDNGINVTGIEISktaidLAMQNGLEDISIYHGSVNEMP-FNNKLYDGIYS-HALLHLLN 110
Cdd:pfam13489  24 GRVLDF---GCGTGIFLRLLRAQGFSVTGVDPS-----PIAIERALLNVRFDQFDEQEAaVPAGKFDVIVArEVLEHVPD 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446319745  111 KQEREQFIKDCynqLKPGGYMVFTTVSQKAPMygkGKQLEQDYYEIMEGVKMFFYDSESIKRDFNQYGLVQVS 183
Cdd:pfam13489  96 PPALLRQIAAL---LKPGGLLLLSTPLASDEA---DRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGFEVVS 162
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
38-135 9.62e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 56.37  E-value: 9.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  38 ILVPGIGYGRNAKVFIDN--GINVTGIEISKTAIDLAMQNgLEDISIYHGSVNEMPFNNKlYDGIYSHALLHLLnkQERE 115
Cdd:COG4106    5 VLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARAR-LPNVRFVVADLRDLDPPEP-FDLVVSNAALHWL--PDHA 80

                         90       100
                 ....*....|....*....|
gi 446319745 116 QFIKDCYNQLKPGGYMVFTT 135
Cdd:COG4106   81 ALLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 37-136 1.19e-10

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: 56.28  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  37 DILVPGIGYGRNAKVFID-NGINVTGIEISKTAIDLAMQN----GLEDISIYHGSVNEMPFNNKL-YDGIYSHALLHLLn 110
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAaaalLADNVEVLKGDAEELPPEADEsFDVIISDPPLHHL- 79

                         90       100
                 ....*....|....*....|....*.
gi 446319745 111 KQEREQFIKDCYNQLKPGGYMVFTTV 136
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLTLV 105
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 2-137 6.90e-06

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: 45.11  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745    2 EFWESSFIEKQTmwGFEPTESAILTKDFFLEKNVK---DILVPGIGYGRNAKVFIDNGINVTGIEISKTAI-DLAMQNGL 77
Cdd:pfam05724   4 DFWLKRWVEGQT--PFHQEGVNPLLVRHWDALKLPpglRVLVPLCGKALDMVWLAEQGHFVVGVEISELAVeKFFAEAGL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446319745   78 E---------------DISIYHGSVNEMPFNN-KLYDGIYSHALLHLLNKQEREQFIKDCYNQLKPGGYMVFTTVS 137
Cdd:pfam05724  82 SppitelsgfkeyssgNISLYCGDFFTLPREElGKFDLIYDRAALCALPPEMRPRYAKQMYELLPPGGRGLLITLD 157
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 31-162 1.38e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 43.56  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   31 LEKNVKdILVPGIGYGRNAKVFIDN---GINVTGIEISKTAIDLAMQN----GLEDISIYHGSVNEMP--FNNKLYDGIY 101
Cdd:pfam13847   1 IDKGMR-VLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENaqklGFDNVEFEQGDIEELPelLEDDKFDVVI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446319745  102 SHALLHLLNKQerEQFIKDCYNQLKPGGYMVFTTVSQKAPMYGKGKQLEQDYYEIMEGVKM 162
Cdd:pfam13847  80 SNCVLNHIPDP--DKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAIL 138
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 56-132 1.59e-05

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 43.64  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  56 GINVTGIEISKTAIDLA----MQNGLEDISIYHGSVNEmPFNNKLYDGIYS----HALlHLLNKQEREQFIKDCYNQLKP 127
Cdd:COG2813   73 EARVTLVDVNARAVELAranaAANGLENVEVLWSDGLS-GVPDGSFDLILSnppfHAG-RAVDKEVAHALIADAARHLRP 150


                 ....*..
gi 446319745 128 GG--YMV 132
Cdd:COG2813  151 GGelWLV 157
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 56-133 4.02e-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: 42.82  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745  56 GINVTGIEISKTAIDLAMQN----GLED-ISIYHGSVNEMP--FNNKLYDGI-----YSHALLHLLNKQER--------- 114
Cdd:COG4123   61 GARITGVEIQPEAAELARRNvalnGLEDrITVIHGDLKEFAaeLPPGSFDLVvsnppYFKAGSGRKSPDEAraiarheda 140

                         90       100
                 ....*....|....*....|..
gi 446319745 115 ---EQFIKDCYNQLKPGGYMVF 133
Cdd:COG4123  141 ltlEDLIRAAARLLKPGGRFAL 162
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 42-130 1.52e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 39.66  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   42 GIGYGRNAKVFIDN--GINVTGIEISKTAIDLA----MQNGLEDISIYHGSVNEMPFNNKL-YDGIYSHALLHLLNkqER 114
Cdd:pfam08242   4 GCGTGTLLRALLEAlpGLEYTGLDISPAALEAArerlAALGLLNAVRVELFQLDLGELDPGsFDVVVASNVLHHLA--DP 81

                          90
                  ....*....|....*.
gi 446319745  115 EQFIKDCYNQLKPGGY 130
Cdd:pfam08242  82 RAVLRNIRRLLKPGGV 97
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 55-138 3.30e-04

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: 40.35  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446319745   55 NGINVTGIEISKTAIDLAMQNGLEDISIYHGSVNEMPFNNKLYDGIYSHALLHLLNKQEreQFIKDCYNQLKPGGYMVFT 134
Cdd:TIGR02072  57 PQAEFIALDISAGMLAQAKTKLSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLS--QALSELARVLKPGGLLAFS 134


                  ....
gi 446319745  135 TVSQ 138
Cdd:TIGR02072 135 TFGP 138
 
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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