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Conserved domains on  [gi|488288358|ref|WP_002359566|]
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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; ...
 19-280 4.60e-39

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: 137.74  E-value: 4.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  19 FRCPTCHEPMHLEGVGLICQQRHQFDLSKKGTLYFLNhgVQTEY------NKKMFTSRGKMIQSGMYAP----VLNKIMH 88
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLP--VQHKRskdpgdNKEMMQARRAFLDAGHYQPlrdaVANLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  89 YLPQN-KTVVDVGCGEGSFLAELSQAgLSGLKI----GFDLSKEGIYLASNQPIDAFWCVADLTNLPFANEGLDTILNIF 163
Cdd:PRK11088  81 RLDEKaTALLDIGCGEGYYTHALADA-LPEITTmqlfGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358 164 SPSHYQEFRRVLKADGTVIKIIPEENYLKELRAAFYpnDEKKQSYSNQKVVQRFaeELavEVDERITYCFDIPEERRLDL 243
Cdd:PRK11088 160 APCKAEELARVVKPGGIVITVTPGPRHLFELKGLIY--DEVRLHAPEAEQLEGF--EL--QHSERLAYPMRLTGSEAVAL 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488288358 244 LEMSPLEWQVSQEVKAELQQRPLEKITIDVRLLVGRK 280
Cdd:PRK11088 234 LQMTPFAWKATPEVKQQLAAKGVFSCETDFNIRVYRR 270
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 19-280 4.60e-39

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 137.74  E-value: 4.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  19 FRCPTCHEPMHLEGVGLICQQRHQFDLSKKGTLYFLNhgVQTEY------NKKMFTSRGKMIQSGMYAP----VLNKIMH 88
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLP--VQHKRskdpgdNKEMMQARRAFLDAGHYQPlrdaVANLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  89 YLPQN-KTVVDVGCGEGSFLAELSQAgLSGLKI----GFDLSKEGIYLASNQPIDAFWCVADLTNLPFANEGLDTILNIF 163
Cdd:PRK11088  81 RLDEKaTALLDIGCGEGYYTHALADA-LPEITTmqlfGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358 164 SPSHYQEFRRVLKADGTVIKIIPEENYLKELRAAFYpnDEKKQSYSNQKVVQRFaeELavEVDERITYCFDIPEERRLDL 243
Cdd:PRK11088 160 APCKAEELARVVKPGGIVITVTPGPRHLFELKGLIY--DEVRLHAPEAEQLEGF--EL--QHSERLAYPMRLTGSEAVAL 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488288358 244 LEMSPLEWQVSQEVKAELQQRPLEKITIDVRLLVGRK 280
Cdd:PRK11088 234 LQMTPFAWKATPEVKQQLAAKGVFSCETDFNIRVYRR 270
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 90-182 1.10e-15

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: 72.33  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  90 LPQNKTVVDVGCGEGSFLAELSQAGLSGlkIGFDLSKEGIYLA----SNQPIDAFWCVADLTNLPFANEGLDTILNIFSP 165
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAERGARV--TGVDISPEMLELAreraAEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVL 97

                         90       100
                 ....*....|....*....|....
gi 488288358 166 SH-------YQEFRRVLKADGTVI 182
Cdd:COG2226   98 HHlpdperaLAEIARVLKPGGRLV 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 96-179 3.12e-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: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358   96 VVDVGCGEGSFLAELSQAGlsGLKI-GFDLSKEGIYLA----SNQPIDAFWCVADLTNLPFANEGLDTILNIFSPSH--- 167
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG--GARVtGVDLSPEMLERAreraAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpd 78

                          90
                  ....*....|....*...
gi 488288358  168 ------YQEFRRVLKADG 179
Cdd:pfam13649  79 pdleaaLREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 95-182 6.38e-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: 38.57  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  95 TVVDVGCGEGSFLAELSQAGlSGLKIGFDLSKEGI-----YLASNQPIDAFWCVADLTNLPF-ANEGLDTILNIFSPSHY 168
Cdd:cd02440    1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALelarkAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|..
gi 488288358 169 --------QEFRRVLKADGTVI 182
Cdd:cd02440   80 vedlarflEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 19-280 4.60e-39

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 137.74  E-value: 4.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  19 FRCPTCHEPMHLEGVGLICQQRHQFDLSKKGTLYFLNhgVQTEY------NKKMFTSRGKMIQSGMYAP----VLNKIMH 88
Cdd:PRK11088   3 YQCPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLP--VQHKRskdpgdNKEMMQARRAFLDAGHYQPlrdaVANLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  89 YLPQN-KTVVDVGCGEGSFLAELSQAgLSGLKI----GFDLSKEGIYLASNQPIDAFWCVADLTNLPFANEGLDTILNIF 163
Cdd:PRK11088  81 RLDEKaTALLDIGCGEGYYTHALADA-LPEITTmqlfGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358 164 SPSHYQEFRRVLKADGTVIKIIPEENYLKELRAAFYpnDEKKQSYSNQKVVQRFaeELavEVDERITYCFDIPEERRLDL 243
Cdd:PRK11088 160 APCKAEELARVVKPGGIVITVTPGPRHLFELKGLIY--DEVRLHAPEAEQLEGF--EL--QHSERLAYPMRLTGSEAVAL 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488288358 244 LEMSPLEWQVSQEVKAELQQRPLEKITIDVRLLVGRK 280
Cdd:PRK11088 234 LQMTPFAWKATPEVKQQLAAKGVFSCETDFNIRVYRR 270
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 90-182 1.10e-15

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: 72.33  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  90 LPQNKTVVDVGCGEGSFLAELSQAGLSGlkIGFDLSKEGIYLA----SNQPIDAFWCVADLTNLPFANEGLDTILNIFSP 165
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAERGARV--TGVDISPEMLELAreraAEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVL 97

                         90       100
                 ....*....|....*....|....
gi 488288358 166 SH-------YQEFRRVLKADGTVI 182
Cdd:COG2226   98 HHlpdperaLAEIARVLKPGGRLV 121
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 86-182 5.08e-14

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: 67.35  E-value: 5.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  86 IMHYLPQNKTVVDVGCGEGSFLAELSQAGLSGlkIGFDLSKEGIYLASN--QPIDAFWCVADLTNLPFANEGLDTILNIF 163
Cdd:COG2227   18 LARLLPAGGRVLDVGCGTGRLALALARRGADV--TGVDISPEALEIAREraAELNVDFVQGDLEDLPLEDGSFDLVICSE 95

                         90       100
                 ....*....|....*....|....*.
gi 488288358 164 SPSHY-------QEFRRVLKADGTVI 182
Cdd:COG2227   96 VLEHLpdpaallRELARLLKPGGLLL 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 96-179 3.12e-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: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358   96 VVDVGCGEGSFLAELSQAGlsGLKI-GFDLSKEGIYLA----SNQPIDAFWCVADLTNLPFANEGLDTILNIFSPSH--- 167
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG--GARVtGVDLSPEMLERAreraAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpd 78

                          90
                  ....*....|....*...
gi 488288358  168 ------YQEFRRVLKADG 179
Cdd:pfam13649  79 pdleaaLREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 97-182 3.51e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 58.45  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358   97 VDVGCGEGSFLAELSQAGLSglKIGFDLSKEGIYLAS--NQPIDAFWCVADLTNLPFANEGLDTILNIFSPSH------- 167
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELARekAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHvedpera 78

                          90
                  ....*....|....*
gi 488288358  168 YQEFRRVLKADGTVI 182
Cdd:pfam08241  79 LREIARVLKPGGILI 93
PRK08317 PRK08317
hypothetical protein; Provisional
 95-182 2.07e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.79  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  95 TVVDVGCGEGSFLAELSQA-GLSGLKIGFDLSKEGIYLASNQPID----AFWCVADLTNLPFANEGLDT--ILNIFS--- 164
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALAKERAAGlgpnVEFVRGDADGLPFPDGSFDAvrSDRVLQhle 101

                         90       100
                 ....*....|....*....|
gi 488288358 165 -PSHY-QEFRRVLKADGTVI 182
Cdd:PRK08317 102 dPARAlAEIARVLRPGGRVV 121
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
88-182 1.18e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 50.77  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  88 HYLPQNKTVVDVGCGEGSFLAELSQAGLSglKIGFDLSKEGIYLASNQPIDAFWCVADLTNLPFANEGLDTIL--NIFS- 164
Cdd:COG4976   42 LPPGPFGRVLDLGCGTGLLGEALRPRGYR--LTGVDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFDLIVaaDVLTy 119

                         90       100
                 ....*....|....*....|..
gi 488288358 165 ----PSHYQEFRRVLKADGTVI 182
Cdd:COG4976  120 lgdlAAVFAGVARALKPGGLFI 141
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 79-182 3.71e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.53  E-value: 3.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  79 YAPVLNKIMHYLPQNKTVVDVGCGEGSFLAELSQAGLSGLkIGFDLSKEGIYLASNQPIDAFWC-----VADLTNL-PFA 152
Cdd:COG0500   13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRV-IGIDLSPEAIALARARAAKAGLGnveflVADLAELdPLP 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488288358 153 NEGLDTILNIFSPSH---------YQEFRRVLKADGTVI 182
Cdd:COG0500   92 AESFDLVVAFGVLHHlppeerealLRELARALKPGGVLL 130
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 90-182 4.24e-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: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  90 LPQNKTVVDVGCGEGSFLAELsqAGLSGLKI-GFDLSKEGIYLASNQ------PIDAFWCVADLTNLPfANEGLDTILNI 162
Cdd:COG2230   49 LKPGMRVLDIGCGWGGLALYL--ARRYGVRVtGVTLSPEQLEYARERaaeaglADRVEVRLADYRDLP-ADGQFDAIVSI 125

                         90       100
                 ....*....|....*....|....*....
gi 488288358 163 -----FSPSHYQEF----RRVLKADGTVI 182
Cdd:COG2230  126 gmfehVGPENYPAYfakvARLLKPGGRLL 154
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
92-182 5.18e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 44.04  E-value: 5.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  92 QNKTVVDVGCGEGSFLAELSQAgLSGLKI-GFDLSKEGIYLASNQPIDAFWCVADLTNLPFaNEGLDTILNIFS----PS 166
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAER-FPGARVtGVDLSPEMLARARARLPNVRFVVADLRDLDP-PEPFDLVVSNAAlhwlPD 78

                         90
                 ....*....|....*....
gi 488288358 167 H---YQEFRRVLKADGTVI 182
Cdd:COG4106   79 HaalLARLAAALAPGGVLA 97
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 79-182 1.66e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 43.96  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358   79 YAPVLNKIMHYLPQNKTVVDVGCGEGSFLAELSQAGLSGlkIGFDLSKEGIYLASNQPI------DAFWCVADLTNLPFA 152
Cdd:pfam13489   9 LADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSV--TGVDPSPIAIERALLNVRfdqfdeQEAAVPAGKFDVIVA 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 488288358  153 NEGLDTILNifsPSHY-QEFRRVLKADGTVI 182
Cdd:pfam13489  87 REVLEHVPD---PPALlRQIAALLKPGGLLL 114
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 93-207 2.62e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 43.17  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358   93 NKTVVDVGCGEGSFLAEL-SQAGLSGLKIGFDLSKEGIYLA-----SNQPIDAFWCVADLTNLP--FANEGLDTILNI-- 162
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELaEELGPNAEVVGIDISEEAIEKArenaqKLGFDNVEFEQGDIEELPelLEDDKFDVVISNcv 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 488288358  163 -----FSPSHYQEFRRVLKADGTVikIIPEENYLKELRAAFYPNDEKKQS 207
Cdd:pfam13847  84 lnhipDPDKVLQEILRVLKPGGRL--IISDPDSLAELPAHVKEDSTYYAG 131
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 69-198 4.33e-04

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 40.26  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358   69 SRG--KMIQsgmyapvLNKIMHYLPQNKTVVDVGCGEGSFLAELSQAGlSGLKIGFDLskegiylasnQPIDAfwcvadl 146
Cdd:pfam01728   3 SRAayKLLE-------IDEKFGLLKPGKTVLDLGAAPGGWSQVALQRG-AGKVVGVDL----------GPMQL------- 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288358  147 tNLPFANEGLDTI-LNIFSPSHYQEFRRVLK-------ADG----TVIKIIPEENYLKELRAAF 198
Cdd:pfam01728  58 -WKPRNDPGVTFIqGDIRDPETLDLLEELLGrkvdlvlSDGspfiSGNKVLDHLRSLDLVKAAL 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 95-182 6.38e-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: 38.57  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  95 TVVDVGCGEGSFLAELSQAGlSGLKIGFDLSKEGI-----YLASNQPIDAFWCVADLTNLPF-ANEGLDTILNIFSPSHY 168
Cdd:cd02440    1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALelarkAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|..
gi 488288358 169 --------QEFRRVLKADGTVI 182
Cdd:cd02440   80 vedlarflEEARRLLKPGGVLV 101
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 97-181 5.27e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.81  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358   97 VDVGCGEGSFLAELSQAgLSGLKI-GFDLSKEGIYLASNQ----PIDAFWCVADLTNLPFANEGL--DTILNIFSPSH-- 167
Cdd:pfam08242   1 LEIGCGTGTLLRALLEA-LPGLEYtGLDISPAALEAARERlaalGLLNAVRVELFQLDLGELDPGsfDVVVASNVLHHla 79

                          90
                  ....*....|....*....
gi 488288358  168 -----YQEFRRVLKADGTV 181
Cdd:pfam08242  80 dpravLRNIRRLLKPGGVL 98
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 90-181 5.90e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.44  E-value: 5.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288358  90 LPQNKTVVDVGCGEGSFLAELS-QAGLSGLKIGFDLSKE----------GIYLASNQPidafWCVADLTNLPFANEGLD- 157
Cdd:PRK00216  49 VRPGDKVLDLACGTGDLAIALAkAVGKTGEVVGLDFSEGmlavgreklrDLGLSGNVE----FVQGDAEALPFPDNSFDa 124

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488288358 158 -TI---L-NIfspSHY----QEFRRVLKADGTV 181
Cdd:PRK00216 125 vTIafgLrNV---PDIdkalREMYRVLKPGGRL 154
 
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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