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Conserved domains on  [gi|514881312|ref|WP_016613256|]
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MULTISPECIES: methyltransferase domain-containing protein [Enterococcus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 19-265 8.23e-38

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.).


The actual alignment was detected with superfamily member PRK11088:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 272  Bit Score: 134.27  E-value: 8.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  19 FECPLCRQAFFPTENGLVCPNRHRFDLSKKGTLFFLDHQVKADYD----QALFLPRQRMIASGMYAPVLETIKAAL---- 90
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDpgdnKEMMQARRAFLDAGHYQPLRDAVANLLaerl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  91 -GDAEYLLDVGCGEG---SFLAQMVNEKTQAAV-GFDIAKDGVYLATN--QNVpaFWCVADLTKLPFAEASFDTIFNLFS 163
Cdd:PRK11088  83 dEKATALLDIGCGEGyytHALADALPEITTMQLfGLDISKVAIKYAAKryPQV--TFCVASSHRLPFADQSLDAIIRIYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312 164 PSNYGEFNRILKKGGQLIKVVPAADYLKELRAAFYpdDETKQQYSNERVVSKF-FEHyptasRQRVTHVFAIPEENRQDL 242
Cdd:PRK11088 161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIY--DEVRLHAPEAEQLEGFeLQH-----SERLAYPMRLTGSEAVAL 233

                        250       260
                 ....*....|....*....|...
gi 514881312 243 LAMSPLEWGASEERKEKLRQTPL 265
Cdd:PRK11088 234 LQMTPFAWKATPEVKQQLAAKGV 256
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 19-265 8.23e-38

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 134.27  E-value: 8.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  19 FECPLCRQAFFPTENGLVCPNRHRFDLSKKGTLFFLDHQVKADYD----QALFLPRQRMIASGMYAPVLETIKAAL---- 90
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDpgdnKEMMQARRAFLDAGHYQPLRDAVANLLaerl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  91 -GDAEYLLDVGCGEG---SFLAQMVNEKTQAAV-GFDIAKDGVYLATN--QNVpaFWCVADLTKLPFAEASFDTIFNLFS 163
Cdd:PRK11088  83 dEKATALLDIGCGEGyytHALADALPEITTMQLfGLDISKVAIKYAAKryPQV--TFCVASSHRLPFADQSLDAIIRIYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312 164 PSNYGEFNRILKKGGQLIKVVPAADYLKELRAAFYpdDETKQQYSNERVVSKF-FEHyptasRQRVTHVFAIPEENRQDL 242
Cdd:PRK11088 161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIY--DEVRLHAPEAEQLEGFeLQH-----SERLAYPMRLTGSEAVAL 233

                        250       260
                 ....*....|....*....|...
gi 514881312 243 LAMSPLEWGASEERKEKLRQTPL 265
Cdd:PRK11088 234 LQMTPFAWKATPEVKQQLAAKGV 256
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 75-197 4.66e-13

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: 65.02  E-value: 4.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  75 ASGMYAPVLETIKA-ALGDAEYLLDVGCGEGSFLAQMVnEKTQAAVGFDIAKDGVYLA----TNQNVPAFWCVADLTKLP 149
Cdd:COG2226    4 VAARYDGREALLAAlGLRPGARVLDLGCGTGRLALALA-ERGARVTGVDISPEMLELAreraAEAGLNVEFVVGDAEDLP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 514881312 150 FAEASFDTIFNLFS-------PSNYGEFNRILKKGGQLIKVVPAADYLKELRAAF 197
Cdd:COG2226   83 FPDGSFDLVISSFVlhhlpdpERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 97-178 2.79e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.43  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312   97 LDVGCGEGSFLAQMVNEKTQAAVGFDIAKDGVYLA----TNQNVPAFWCVADLTKLPFAEASFDTI-----FNLFSPSN- 166
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERAreraAEAGLNVEFVQGDAEDLPFPDGSFDLVvssgvLHHLPDPDl 81

                          90
                  ....*....|....*
gi 514881312  167 ---YGEFNRILKKGG 178
Cdd:pfam13649  82 eaaLREIARVLKPGG 96
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 96-180 3.49e-05

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: 43.79  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312   96 LLDVGCGEGSFLAQMVN--EKTQAAVGFDIAKDGVYLA---TNQNVPAFWCVADLTKLPFAEASFDTI---FNLFSPSNY 167
Cdd:TIGR01934  43 VLDVACGTGDLAIELAKsaPDRGKVTGVDFSSEMLEVAkkkSELPLNIEFIQADAEALPFEDNSFDAVtiaFGLRNVTDI 122

                          90
                  ....*....|....*..
gi 514881312  168 ----GEFNRILKKGGQL 180
Cdd:TIGR01934 123 qkalREMYRVLKPGGRL 139
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-181 9.74e-04

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: 37.79  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  96 LLDVGCGEGSFLAQMVNEKTQAAVGFDIAKD-----GVYLATNQNVPAFWCVADLTKLPF-AEASFDTIFNLFSPSNY-- 167
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPValelaRKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLve 81

                         90       100
                 ....*....|....*....|
gi 514881312 168 ------GEFNRILKKGGQLI 181
Cdd:cd02440   82 dlarflEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 19-265 8.23e-38

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 134.27  E-value: 8.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  19 FECPLCRQAFFPTENGLVCPNRHRFDLSKKGTLFFLDHQVKADYD----QALFLPRQRMIASGMYAPVLETIKAAL---- 90
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDpgdnKEMMQARRAFLDAGHYQPLRDAVANLLaerl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  91 -GDAEYLLDVGCGEG---SFLAQMVNEKTQAAV-GFDIAKDGVYLATN--QNVpaFWCVADLTKLPFAEASFDTIFNLFS 163
Cdd:PRK11088  83 dEKATALLDIGCGEGyytHALADALPEITTMQLfGLDISKVAIKYAAKryPQV--TFCVASSHRLPFADQSLDAIIRIYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312 164 PSNYGEFNRILKKGGQLIKVVPAADYLKELRAAFYpdDETKQQYSNERVVSKF-FEHyptasRQRVTHVFAIPEENRQDL 242
Cdd:PRK11088 161 PCKAEELARVVKPGGIVITVTPGPRHLFELKGLIY--DEVRLHAPEAEQLEGFeLQH-----SERLAYPMRLTGSEAVAL 233

                        250       260
                 ....*....|....*....|...
gi 514881312 243 LAMSPLEWGASEERKEKLRQTPL 265
Cdd:PRK11088 234 LQMTPFAWKATPEVKQQLAAKGV 256
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 75-197 4.66e-13

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: 65.02  E-value: 4.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  75 ASGMYAPVLETIKA-ALGDAEYLLDVGCGEGSFLAQMVnEKTQAAVGFDIAKDGVYLA----TNQNVPAFWCVADLTKLP 149
Cdd:COG2226    4 VAARYDGREALLAAlGLRPGARVLDLGCGTGRLALALA-ERGARVTGVDISPEMLELAreraAEAGLNVEFVVGDAEDLP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 514881312 150 FAEASFDTIFNLFS-------PSNYGEFNRILKKGGQLIKVVPAADYLKELRAAF 197
Cdd:COG2226   83 FPDGSFDLVISSFVlhhlpdpERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 97-178 2.79e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.43  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312   97 LDVGCGEGSFLAQMVNEKTQAAVGFDIAKDGVYLA----TNQNVPAFWCVADLTKLPFAEASFDTI-----FNLFSPSN- 166
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERAreraAEAGLNVEFVQGDAEDLPFPDGSFDLVvssgvLHHLPDPDl 81

                          90
                  ....*....|....*
gi 514881312  167 ---YGEFNRILKKGG 178
Cdd:pfam13649  82 eaaLREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 97-181 3.28e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 61.14  E-value: 3.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312   97 LDVGCGEGSFLAQMVNEKTQAaVGFDIAKDGVYLAT--NQNVPAFWCVADLTKLPFAEASFDTIFNLFS-------PSNY 167
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARV-TGVDISPEMLELARekAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVlhhvedpERAL 79

                          90
                  ....*....|....
gi 514881312  168 GEFNRILKKGGQLI 181
Cdd:pfam08241  80 REIARVLKPGGILI 93
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 82-181 2.01e-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: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  82 VLETIKAALGDAEYLLDVGCGEGSFLAQMVNEKTQaAVGFDIAKDGVYLATN--QNVPAFWCVADLTKLPFAEASFDTIF 159
Cdd:COG2227   14 LAALLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIAREraAELNVDFVQGDLEDLPLEDGSFDLVI 92

                         90       100
                 ....*....|....*....|....*....
gi 514881312 160 N------LFSPSNY-GEFNRILKKGGQLI 181
Cdd:COG2227   93 CsevlehLPDPAALlRELARLLKPGGLLL 121
PRK08317 PRK08317
hypothetical protein; Provisional
 89-181 5.07e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.55  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  89 ALGDAEYLLDVGCGEGSFLAQMVNE--KTQAAVGFDIAKDGVYLATNQ----NVPAFWCVADLTKLPFAEASFDTIF--N 160
Cdd:PRK08317  16 AVQPGDRVLDVGCGPGNDARELARRvgPEGRVVGIDRSEAMLALAKERaaglGPNVEFVRGDADGLPFPDGSFDAVRsdR 95

                         90       100
                 ....*....|....*....|....*.
gi 514881312 161 LFS-----PSNYGEFNRILKKGGQLI 181
Cdd:PRK08317  96 VLQhledpARALAEIARVLRPGGRVV 121
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 84-180 7.44e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 49.00  E-value: 7.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  84 ETIKAA-LGDAEYLLDVGCGEGSF---LAQMVNEKTQAaVGFDI-------AKDGVYLATNQ-NVPafWCVADLTKLPFA 151
Cdd:PRK00216  42 KTIKWLgVRPGDKVLDLACGTGDLaiaLAKAVGKTGEV-VGLDFsegmlavGREKLRDLGLSgNVE--FVQGDAEALPFP 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 514881312 152 EASFD--TIfnlfspsNYG------------EFNRILKKGGQL 180
Cdd:PRK00216 119 DNSFDavTI-------AFGlrnvpdidkalrEMYRVLKPGGRL 154
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 90-181 1.10e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 47.41  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312   90 LGDAEYLLDVGCGEGSF---LAQMVNEKTQaAVGFDIAKDGVYLATN-------QNVpAFwCVADLTKLP--FAEASFDT 157
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLsfeLAEELGPNAE-VVGIDISEEAIEKAREnaqklgfDNV-EF-EQGDIEELPelLEDDKFDV 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 514881312  158 IF-----NLF--SPSNYGEFNRILKKGGQLI 181
Cdd:pfam13847  78 VIsncvlNHIpdPDKVLQEILRVLKPGGRLI 108
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
95-230 2.10e-06

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 46.78  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  95 YLLDVGCGegsflaqmvNEKTQAAVGFDI-AKDGVYLatnqnvpafwcVADLTK-LPFAEASFDTIF---NL--FSPSNY 167
Cdd:COG4627    5 LKLNIGCG---------PKRLPGWLNVDIvPAPGVDI-----------VGDLTDpLPFPDNSVDAIYsshVLehLDYEEA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514881312 168 ----GEFNRILKKGGQLIKVVP-----AADYLKELRAAFYPddetKQQYSNERVVSKFFEHYPTASRQRVTH 230
Cdd:COG4627   65 plalKECYRVLKPGGILRIVVPdlehvARLYLAEYDAALDV----AELRLAGPIDPLGIILGERLAGLAARH 132
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 97-181 3.18e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 46.83  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  97 LDVGCGEGSFLAQMVNEKTQAAVGFDIAKDGVYLATNQNVPAFWC-----VADLTKL-PFAEASFDTI-----FNLFSPS 165
Cdd:COG0500   31 LDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGnveflVADLAELdPLPAESFDLVvafgvLHHLPPE 110

                         90       100
                 ....*....|....*....|
gi 514881312 166 NYGEF----NRILKKGGQLI 181
Cdd:COG0500  111 EREALlrelARALKPGGVLL 130
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 62-181 4.86e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.69  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  62 YDQ-----ALFLPRQRMIASGMYAPVLETI-------------KAALGDAEYLLDVGCGEGSFLAQMVNEKTQAAVGFDI 123
Cdd:COG2230    3 YDLgndfyRLFLDPTMTYSCAYFEDPDDTLeeaqeakldlilrKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514881312 124 AKDGVYLATNQNV------PAFWCVADLTKLPfAEASFDTIFNL-----FSPSNYGEF----NRILKKGGQLI 181
Cdd:COG2230   83 SPEQLEYARERAAeagladRVEVRLADYRDLP-ADGQFDAIVSIgmfehVGPENYPAYfakvARLLKPGGRLL 154
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 96-180 3.49e-05

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: 43.79  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312   96 LLDVGCGEGSFLAQMVN--EKTQAAVGFDIAKDGVYLA---TNQNVPAFWCVADLTKLPFAEASFDTI---FNLFSPSNY 167
Cdd:TIGR01934  43 VLDVACGTGDLAIELAKsaPDRGKVTGVDFSSEMLEVAkkkSELPLNIEFIQADAEALPFEDNSFDAVtiaFGLRNVTDI 122

                          90
                  ....*....|....*..
gi 514881312  168 ----GEFNRILKKGGQL 180
Cdd:TIGR01934 123 qkalREMYRVLKPGGRL 139
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
97-181 1.09e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.58  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  97 LDVGCGEGSFLAQMVNEKTQAAV-GFDIAKDGVYLATNQNVPAFWCVADLTKLPFAEaSFDTIFnlfspSNY-------- 167
Cdd:COG4106    6 LDLGCGTGRLTALLAERFPGARVtGVDLSPEMLARARARLPNVRFVVADLRDLDPPE-PFDLVV-----SNAalhwlpdh 79

                         90
                 ....*....|....*...
gi 514881312 168 -GEFNRI---LKKGGQLI 181
Cdd:COG4106   80 aALLARLaaaLAPGGVLA 97
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
62-188 1.31e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.91  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  62 YDQALflprqrMIASGMYAP--VLETIKAALGDAEYL--LDVGCGEGSFLAQMVnEKTQAAVGFDIAKDGVYLATNQNVP 137
Cdd:COG4976   18 YDAAL------VEDLGYEAPalLAEELLARLPPGPFGrvLDLGCGTGLLGEALR-PRGYRLTGVDLSEEMLAKAREKGVY 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 514881312 138 AFWCVADLTKLPFAEASFDTIFNLFSPSNYGEFN-------RILKKGGQLIKVVPAAD 188
Cdd:COG4976   91 DRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAavfagvaRALKPGGLFIFSVEDAD 148
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-181 9.74e-04

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: 37.79  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  96 LLDVGCGEGSFLAQMVNEKTQAAVGFDIAKD-----GVYLATNQNVPAFWCVADLTKLPF-AEASFDTIFNLFSPSNY-- 167
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPValelaRKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLve 81

                         90       100
                 ....*....|....*....|
gi 514881312 168 ------GEFNRILKKGGQLI 181
Cdd:cd02440   82 dlarflEEARRLLKPGGVLV 101
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
97-181 2.38e-03

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 38.69  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  97 LDVGCGEGSFLAQMVNEKTQAAVGFD-----------IAKdgvYLatNQNVPAFWCVADLTKLPFAEAsFDTIFNL---- 161
Cdd:PRK15068 127 LDVGCGNGYHMWRMLGAGAKLVVGIDpsqlflcqfeaVRK---LL--GNDQRAHLLPLGIEQLPALKA-FDTVFSMgvly 200

                         90       100       110
                 ....*....|....*....|....*....|.
gi 514881312 162 --FSPsnygefnrI---------LKKGGQLI 181
Cdd:PRK15068 201 hrRSP--------LdhlkqlkdqLVPGGELV 223
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 79-199 2.50e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 37.79  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312   79 YAPVLETIKAALGDAEYLLDVGCGEGSFLAQMVNEKTQaAVGFDIAKDGVYLATNQNVPAfwcVADLTKLPFAEASFDTI 158
Cdd:pfam13489   9 LADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFS-VTGVDPSPIAIERALLNVRFD---QFDEQEAAVPAGKFDVI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 514881312  159 --FNLF-----SPSNYGEFNRILKKGGQLIKVVPAADYLKELRAAFYP 199
Cdd:pfam13489  85 vaREVLehvpdPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWP 132
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 62-202 3.78e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 37.82  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514881312  62 YDQALFLPRQRmiasgmyAPVLETIKAALGDAeYLLDVGCGEGSfLAQMVNEKTQAAVGFDIAKDGVYLATNQNVPAFWC 141
Cdd:PRK10258  20 YEQHAELQRQS-------ADALLAMLPQRKFT-HVLDAGCGPGW-MSRYWRERGSQVTALDLSPPMLAQARQKDAADHYL 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514881312 142 VADLTKLPFAEASFDTIFnlfspSNY------------GEFNRILKKGGQLIKVVPAADYLKELRAAFYPDDE 202
Cdd:PRK10258  91 AGDIESLPLATATFDLAW-----SNLavqwcgnlstalRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDE 158
 
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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