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Conserved domains on  [gi|446926627|ref|WP_001003883|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Bacillus]

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]; ...
 27-154 2.77e-17

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: 75.80  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  27 ETVGEIWDFYGEVKER--CKPSDILLDVGTGGGENVLNIASWAKLLIGIDNSNGMIETAHSNLKKSGVqNVEFLQMGSEA 104
Cdd:COG2226    2 DRVAARYDGREALLAAlgLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446926627 105 LTFPHAHFDIASSCHA--------PFLAsELAKVMKKGAFFLTQQVSENDKLNLKEAF 154
Cdd:COG2226   81 LPFPDGSFDLVISSFVlhhlpdpeRALA-EIARVLKPGGRLVVVDFSPPDLAELEELL 137
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 27-154 2.77e-17

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: 75.80  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  27 ETVGEIWDFYGEVKER--CKPSDILLDVGTGGGENVLNIASWAKLLIGIDNSNGMIETAHSNLKKSGVqNVEFLQMGSEA 104
Cdd:COG2226    2 DRVAARYDGREALLAAlgLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446926627 105 LTFPHAHFDIASSCHA--------PFLAsELAKVMKKGAFFLTQQVSENDKLNLKEAF 154
Cdd:COG2226   81 LPFPDGSFDLVISSFVlhhlpdpeRALA-EIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-134 1.91e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627   50 LDVGTGGGENVLNIASWAKL-LIGIDNSNGMIETAHSNLKKSGVqNVEFLQMGSEALTFPHAHFDIASSCHA-------- 120
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlpdpd 80

                          90
                  ....*....|....*
gi 446926627  121 -PFLASELAKVMKKG 134
Cdd:pfam13649  81 lEAALREIARVLKPG 95
PRK08317 PRK08317
hypothetical protein; Provisional
 44-134 5.65e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.94  E-value: 5.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  44 KPSDILLDVGTGGGENVLNIA---SWAKLLIGIDNSNGMIETAHSNLKKSGVqNVEFLQMGSEALTFPHAHFDIASSCHA 120
Cdd:PRK08317  18 QPGDRVLDVGCGPGNDARELArrvGPEGRVVGIDRSEAMLALAKERAAGLGP-NVEFVRGDADGLPFPDGSFDAVRSDRV 96

                         90       100
                 ....*....|....*....|.
gi 446926627 121 -------PFLASELAKVMKKG 134
Cdd:PRK08317  97 lqhledpARALAEIARVLRPG 117
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 49-142 3.15e-05

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: 42.03  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  49 LLDVGTGGGENVLNIASW-AKLLIGIDNSNGMIETAHSNLKKSGVQNVEFLQM-GSEALTFPHAHFDIASSCHAPF---- 122
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGdAEELPPEADESFDVIISDPPLHhlve 81

                         90       100
                 ....*....|....*....|....
gi 446926627 123 ----LASELAKVMKKGAFFLTQQV 142
Cdd:cd02440   82 dlarFLEEARRLLKPGGVLVLTLV 105
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 49-114 2.72e-04

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: 41.13  E-value: 2.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627   49 LLDVGTGGGenvLNIASWAKL---LIGIDNSNGMIETAHSNLKKSGVQnVEFLQMGSEALTFPHAH-FDI 114
Cdd:TIGR01983  50 VLDVGCGGG---LLSEPLARLganVTGIDASEENIEVAKLHAKKDPLQ-IDYRCTTVEDLAEKKAGsFDV 115
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 27-154 2.77e-17

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: 75.80  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  27 ETVGEIWDFYGEVKER--CKPSDILLDVGTGGGENVLNIASWAKLLIGIDNSNGMIETAHSNLKKSGVqNVEFLQMGSEA 104
Cdd:COG2226    2 DRVAARYDGREALLAAlgLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446926627 105 LTFPHAHFDIASSCHA--------PFLAsELAKVMKKGAFFLTQQVSENDKLNLKEAF 154
Cdd:COG2226   81 LPFPDGSFDLVISSFVlhhlpdpeRALA-EIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-134 1.91e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627   50 LDVGTGGGENVLNIASWAKL-LIGIDNSNGMIETAHSNLKKSGVqNVEFLQMGSEALTFPHAHFDIASSCHA-------- 120
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlpdpd 80

                          90
                  ....*....|....*
gi 446926627  121 -PFLASELAKVMKKG 134
Cdd:pfam13649  81 lEAALREIARVLKPG 95
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 50-138 1.46e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.22  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627   50 LDVGTGGGENVLNIASWAKLLIGIDNSNGMIETAHSNLKKSGvqnVEFLQMGSEALTFPHAHFDIASSCHA--------P 121
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG---LTFVVGDAEDLPFPDNSFDLVLSSEVlhhvedpeR 77

                          90
                  ....*....|....*..
gi 446926627  122 FLAsELAKVMKKGAFFL 138
Cdd:pfam08241  78 ALR-EIARVLKPGGILI 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 33-143 1.85e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.77  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  33 WDFYGEVKERCKPSDILLDVGTGGGENVLNIAS-WAKLLIGIDNSNGMIETAHSNLKKSGVQNVEFLQMG-SEALTFPHA 110
Cdd:COG0500   14 LAALLALLERLPKGGRVLDLGCGTGRNLLALAArFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADlAELDPLPAE 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446926627 111 HFDIASSCHA---------PFLASELAKVMKKGAFFLTQQVS 143
Cdd:COG0500   94 SFDLVVAFGVlhhlppeerEALLRELARALKPGGVLLLSASD 135
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 31-138 1.42e-09

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: 54.64  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  31 EIWD--FYGEVKERCKPSDILLDVGTGGGENVLNIASWAKLLIGIDNSNGMIETAHSNLKKsgvQNVEFLQMGSEALTFP 108
Cdd:COG2227    8 DFWDrrLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE---LNVDFVQGDLEDLPLE 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446926627 109 HAHFDIASSCH--------APFLAsELAKVMKKGAFFL 138
Cdd:COG2227   85 DGSFDLVICSEvlehlpdpAALLR-ELARLLKPGGLLL 121
PRK08317 PRK08317
hypothetical protein; Provisional
 44-134 5.65e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.94  E-value: 5.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  44 KPSDILLDVGTGGGENVLNIA---SWAKLLIGIDNSNGMIETAHSNLKKSGVqNVEFLQMGSEALTFPHAHFDIASSCHA 120
Cdd:PRK08317  18 QPGDRVLDVGCGPGNDARELArrvGPEGRVVGIDRSEAMLALAKERAAGLGP-NVEFVRGDADGLPFPDGSFDAVRSDRV 96

                         90       100
                 ....*....|....*....|.
gi 446926627 121 -------PFLASELAKVMKKG 134
Cdd:PRK08317  97 lqhledpARALAEIARVLRPG 117
arsM PRK11873
arsenite methyltransferase;
44-203 5.88e-07

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 49.18  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  44 KPSDILLDVGTGGGENVLnIAswAKLL------IGIDNSNGMIETAHSNLKKSGVQNVEFLQMGSEALTFPHAHFD-IAS 116
Cdd:PRK11873  76 KPGETVLDLGSGGGFDCF-LA--ARRVgptgkvIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEALPVADNSVDvIIS 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627 117 SC------HAPFLASELAKVMKKGAFF------LTQQVSENDKLNLKEAFGrgqCLGerdGTL-KEKYMDKLISAGFDLV 183
Cdd:PRK11873 153 NCvinlspDKERVFKEAFRVLKPGGRFaisdvvLRGELPEEIRNDAELYAG---CVA---GALqEEEYLAMLAEAGFVDI 226

                        170       180
                 ....*....|....*....|
gi 446926627 184 QVREydvTDYYSTPEDLIFL 203
Cdd:PRK11873 227 TIQP---KREYRIPDAREFL 243
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 44-179 1.30e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.64  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627   44 KPSDILLDVGTGGGENVLNIASWA---KLLIGIDNSNGMIETAHSNLKKSGVQNVEFLQ--MGSEALTFPHAHFDIASS- 117
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQgdIEELPELLEDDKFDVVISn 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446926627  118 ---CHAPFLAS---ELAKVMKKGAFFLTQ---QVSENDKLNLKEAFGRGQCLGERdgTLKEKYMDKLISAG 179
Cdd:pfam13847  82 cvlNHIPDPDKvlqEILRVLKPGGRLIISdpdSLAELPAHVKEDSTYYAGCVGGA--ILKKKLYELLEEAG 150
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 44-116 8.13e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 45.53  E-value: 8.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  44 KPSDILLDVGTGGGenVLNIAsWAKL------LIGIDNSNGMIETAHSNLKKSGVQ-NVEFLQMGSEALTFPHAHFDIAS 116
Cdd:PRK00216  50 RPGDKVLDLACGTG--DLAIA-LAKAvgktgeVVGLDFSEGMLAVGREKLRDLGLSgNVEFVQGDAEALPFPDNSFDAVT 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 49-142 3.15e-05

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: 42.03  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  49 LLDVGTGGGENVLNIASW-AKLLIGIDNSNGMIETAHSNLKKSGVQNVEFLQM-GSEALTFPHAHFDIASSCHAPF---- 122
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGdAEELPPEADESFDVIISDPPLHhlve 81

                         90       100
                 ....*....|....*....|....
gi 446926627 123 ----LASELAKVMKKGAFFLTQQV 142
Cdd:cd02440   82 dlarFLEEARRLLKPGGVLVLTLV 105
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
50-138 1.76e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.14  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  50 LDVGTGGGENVLNIASWAKLLIGIDNSNGMIETAhsnlKKSGVQnVEFLQMGSEALTFPHAHFDIASSCH--------AP 121
Cdd:COG4976   51 LDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA----REKGVY-DRLLVADLADLAEPDGRFDLIVAADvltylgdlAA 125

                         90
                 ....*....|....*..
gi 446926627 122 FLAsELAKVMKKGAFFL 138
Cdd:COG4976  126 VFA-GVARALKPGGLFI 141
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 44-140 1.80e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 40.68  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  44 KPSDILLDVGTGGGENVLNIASWAKL-LIGIDNSNGMIETAHSNLKKSGVQN-VEFLQMGSEALTFPhAHFDIASS---- 117
Cdd:COG2230   50 KPGMRVLDIGCGWGGLALYLARRYGVrVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLPAD-GQFDAIVSigmf 128

                         90       100
                 ....*....|....*....|....*....
gi 446926627 118 CHAP------FLAsELAKVMKKGAFFLTQ 140
Cdd:COG2230  129 EHVGpenypaYFA-KVARLLKPGGRLLLH 156
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 49-114 2.72e-04

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: 41.13  E-value: 2.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627   49 LLDVGTGGGenvLNIASWAKL---LIGIDNSNGMIETAHSNLKKSGVQnVEFLQMGSEALTFPHAH-FDI 114
Cdd:TIGR01983  50 VLDVGCGGG---LLSEPLARLganVTGIDASEENIEVAKLHAKKDPLQ-IDYRCTTVEDLAEKKAGsFDV 115
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 41-184 5.35e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 39.33  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627   41 ERCKPSDILLDVGTGGGENVLNIASWAKLLIGIDNSNGMIETAHSnlkksgvqNVEFLQMGSEALTFPHAHFDIASS--- 117
Cdd:pfam13489  18 PKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALL--------NVRFDQFDEQEAAVPAGKFDVIVArev 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446926627  118 -CHAPFLASEL---AKVMKKGAFFLTQQVSENDKLNlkEAFGRGQCLGERDG--------TLKEkYMDKlisAGFDLVQ 184
Cdd:pfam13489  90 lEHVPDPPALLrqiAALLKPGGLLLLSTPLASDEAD--RLLLEWPYLRPRNGhislfsarSLKR-LLEE---AGFEVVS 162
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
44-114 1.83e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 38.57  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446926627   44 KPSDILLDVGTGGGENVLNIASWAK---LLIGIDNSNGMIETAHSNLKKSGVQNVEFLQMGSEALTFPHAHFDI 114
Cdd:pfam01209  41 KRGNKFLDVAGGTGDWTFGLSDSAGssgKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDI 114
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 42-136 6.47e-03

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 36.47  E-value: 6.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  42 RCKPSDILLD--VGTGGgenVLNIASWAKL-LIGIDNSNGMIETAHSNLKKSGVQNVEFLQMGSEALTFPHAHFD----- 113
Cdd:COG1041   23 GAKEGDTVLDpfCGTGT---ILIEAGLLGRrVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDLPLADESVDaivtd 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446926627 114 -----IASSCHAPFL------ASELAKVMKKGAF 136
Cdd:COG1041  100 ppygrSSKISGEELLelyekaLEEAARVLKPGGR 133
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
44-138 9.82e-03

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 36.69  E-value: 9.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446926627  44 KPSDILLDVGTGGGenVLNIAS---WAKLLIGIDNSNGMIETAHSNLKKSGVQN-VEFLQmGSEaltFPHAHFDI----- 114
Cdd:COG2264  147 KPGKTVLDVGCGSG--ILAIAAaklGAKRVLAVDIDPVAVEAARENAELNGVEDrIEVVL-GDL---LEDGPYDLvvani 220

                         90       100
                 ....*....|....*....|....*..
gi 446926627 115 -ASschaPF--LASELAKVMKKGAFFL 138
Cdd:COG2264  221 lAN----PLieLAPDLAALLKPGGYLI 243
 
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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