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Conserved domains on  [gi|427994561|gb|AFY73256|]
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methylase involved in ubiquinone/menaquinone biosynthesis [Synechococcus sp. PCC 7502]

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; ...
 11-282 9.81e-66

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: 206.69  E-value: 9.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  11 CPIDGKELTPRNQSLICSKGHNFDIARQGYFNLLMVQHKASRDPGDTKEMVAARSRFLQTGCYEAIAQTIANLTEKHVSN 90
Cdd:PRK11088   5 CPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAERLDE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  91 lsdlNSITILDAGCGEGYYLNWLL-TMAQKwkypEVGILIGMDISKWAVQSAAKRNREITWIVGSNARPPFSPNSINLIL 169
Cdd:PRK11088  85 ----KATALLDIGCGEGYYTHALAdALPEI----TTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAII 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561 170 CAFGfPSFDV-FRRVLKPLGKIIMVDPAPNHLMELRQLIYPELKSKTSTVQTLpskgfNGFNLVESYHLTYKAKVENSQA 248
Cdd:PRK11088 157 RIYA-PCKAEeLARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQL-----EGFELQHSERLAYPMRLTGSEA 230

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 427994561 249 VqDLFLMTPHYFRSPPTAKTTIAALQ----ELEFTVDV 282
Cdd:PRK11088 231 V-ALLQMTPFAWKATPEVKQQLAAKGvfscETDFNIRV 267
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 11-282 9.81e-66

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 206.69  E-value: 9.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  11 CPIDGKELTPRNQSLICSKGHNFDIARQGYFNLLMVQHKASRDPGDTKEMVAARSRFLQTGCYEAIAQTIANLTEKHVSN 90
Cdd:PRK11088   5 CPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAERLDE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  91 lsdlNSITILDAGCGEGYYLNWLL-TMAQKwkypEVGILIGMDISKWAVQSAAKRNREITWIVGSNARPPFSPNSINLIL 169
Cdd:PRK11088  85 ----KATALLDIGCGEGYYTHALAdALPEI----TTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAII 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561 170 CAFGfPSFDV-FRRVLKPLGKIIMVDPAPNHLMELRQLIYPELKSKTSTVQTLpskgfNGFNLVESYHLTYKAKVENSQA 248
Cdd:PRK11088 157 RIYA-PCKAEeLARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQL-----EGFELQHSERLAYPMRLTGSEA 230

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 427994561 249 VqDLFLMTPHYFRSPPTAKTTIAALQ----ELEFTVDV 282
Cdd:PRK11088 231 V-ALLQMTPFAWKATPEVKQQLAAKGvfscETDFNIRV 267
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 73-207 1.51e-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: 77.34  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  73 YEAIAQTIAnLTEKHVSNLSDLNSITILDAGCGEGYYLNWLLTMAqkwkypevGILIGMDISKWAVQSAAKRNRE----I 148
Cdd:COG2226    1 FDRVAARYD-GREALLAALGLRPGARVLDLGCGTGRLALALAERG--------ARVTGVDISPEMLELARERAAEaglnV 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 427994561 149 TWIVGSNARPPFSPNSINLILCAFGF-------PSFDVFRRVLKPLGKIIMVDPAPNHLMELRQLI 207
Cdd:COG2226   72 EFVVGDAEDLPFPDGSFDLVISSFVLhhlpdpeRALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 99-186 2.61e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.81  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561   99 ILDAGCGEGYYLNWLltmAQKWKYpEVgilIGMDISKWAVQSAAKRNRE----ITWIVGSNARPPFSPNSINLILCAFGF 174
Cdd:pfam13649   1 VLDLGCGTGRLTLAL---ARRGGA-RV---TGVDLSPEMLERARERAAEaglnVEFVQGDAEDLPFPDGSFDLVVSSGVL 73

                          90       100
                  ....*....|....*....|.
gi 427994561  175 PSFDV---------FRRVLKP 186
Cdd:pfam13649  74 HHLPDpdleaalreIARVLKP 94
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 86-275 1.21e-06

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: 48.44  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561   86 KHVSNLSDLNSITILDAGCGEGYylnwlLTMAQKWKYPEVGIlIGMDISKWAVQSAAKRNRE-ITWIVGSNARPPFSPNS 164
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGY-----LTRALLKRFPQAEF-IALDISAGMLAQAKTKLSEnVQFICGDAEKLPLEDSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  165 INLILCAFGFPSFDVF-------RRVLKPLGKIIMVDPAPNHLMELRQL---IYPELKSKTSTVQTLPskgfNGFNLVES 234
Cdd:TIGR02072  99 FDLIVSNLALQWCDDLsqalselARVLKPGGLLAFSTFGPGTLHELRQSfgqHGLRYLSLDELKALLK----NSFELLTL 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 427994561  235 YHLTYKAKVENSQAV-QDLFLMTPHYFRSPPTAKTTIAALQE 275
Cdd:TIGR02072 175 EEELITLSFDDPLDVlRHLKKTGANGLSSGRTSRKQLKAFLE 216
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 98-193 2.29e-06

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: 45.50  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  98 TILDAGCGEGYYLNWLLtmaqKWKYPEVgilIGMDISKWAVQSAAKRNRE-----ITWIVGS-NARPPFSPNSINLILCA 171
Cdd:cd02440    1 RVLDLGCGTGALALALA----SGPGARV---TGVDISPVALELARKAAAAlladnVEVLKGDaEELPPEADESFDVIISD 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 427994561 172 FGFPS--------FDVFRRVLKPLGKIIMV 193
Cdd:cd02440   74 PPLHHlvedlarfLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 11-282 9.81e-66

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 206.69  E-value: 9.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  11 CPIDGKELTPRNQSLICSKGHNFDIARQGYFNLLMVQHKASRDPGDTKEMVAARSRFLQTGCYEAIAQTIANLTEKHVSN 90
Cdd:PRK11088   5 CPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAERLDE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  91 lsdlNSITILDAGCGEGYYLNWLL-TMAQKwkypEVGILIGMDISKWAVQSAAKRNREITWIVGSNARPPFSPNSINLIL 169
Cdd:PRK11088  85 ----KATALLDIGCGEGYYTHALAdALPEI----TTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAII 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561 170 CAFGfPSFDV-FRRVLKPLGKIIMVDPAPNHLMELRQLIYPELKSKTSTVQTLpskgfNGFNLVESYHLTYKAKVENSQA 248
Cdd:PRK11088 157 RIYA-PCKAEeLARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEAEQL-----EGFELQHSERLAYPMRLTGSEA 230

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 427994561 249 VqDLFLMTPHYFRSPPTAKTTIAALQ----ELEFTVDV 282
Cdd:PRK11088 231 V-ALLQMTPFAWKATPEVKQQLAAKGvfscETDFNIRV 267
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 73-207 1.51e-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: 77.34  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  73 YEAIAQTIAnLTEKHVSNLSDLNSITILDAGCGEGYYLNWLLTMAqkwkypevGILIGMDISKWAVQSAAKRNRE----I 148
Cdd:COG2226    1 FDRVAARYD-GREALLAALGLRPGARVLDLGCGTGRLALALAERG--------ARVTGVDISPEMLELARERAAEaglnV 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 427994561 149 TWIVGSNARPPFSPNSINLILCAFGF-------PSFDVFRRVLKPLGKIIMVDPAPNHLMELRQLI 207
Cdd:COG2226   72 EFVVGDAEDLPFPDGSFDLVISSFVLhhlpdpeRALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 99-186 2.61e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.81  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561   99 ILDAGCGEGYYLNWLltmAQKWKYpEVgilIGMDISKWAVQSAAKRNRE----ITWIVGSNARPPFSPNSINLILCAFGF 174
Cdd:pfam13649   1 VLDLGCGTGRLTLAL---ARRGGA-RV---TGVDLSPEMLERARERAAEaglnVEFVQGDAEDLPFPDGSFDLVVSSGVL 73

                          90       100
                  ....*....|....*....|.
gi 427994561  175 PSFDV---------FRRVLKP 186
Cdd:pfam13649  74 HHLPDpdleaalreIARVLKP 94
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 100-192 1.63e-10

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 56.90  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  100 LDAGCGEGYYLNWLLTMaqkwkYPEVgilIGMDISKWAVQSAAKRNRE--ITWIVGSNARPPFSPNSINLILCAFGFPSF 177
Cdd:pfam08241   1 LDVGCGTGLLTELLARL-----GARV---TGVDISPEMLELAREKAPRegLTFVVGDAEDLPFPDNSFDLVLSSEVLHHV 72

                          90       100
                  ....*....|....*....|..
gi 427994561  178 D----VFR---RVLKPLGKIIM 192
Cdd:pfam08241  73 EdperALReiaRVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
78-191 3.10e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 58.09  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  78 QTIANLTEKHVSNLSDLNSITILDAGCGEGYYLNWLLTMAQKwkypevgiLIGMDISKWAVQSAAKRNREITWIVGSNAR 157
Cdd:COG4976   29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR--------LTGVDLSEEMLAKAREKGVYDRLLVADLAD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 427994561 158 PPFSPNSINLILCAFGFPSF----DVFR---RVLKPLGKII 191
Cdd:COG4976  101 LAEPDGRFDLIVAADVLTYLgdlaAVFAgvaRALKPGGLFI 141
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 98-195 1.02e-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: 55.41  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  98 TILDAGCGEGYYLNWLltmAQK-WKYpevgilIGMDISKWAVQSAAKRNRE--ITWIVGSNARPPFSPNSINLILCAFGF 174
Cdd:COG2227   27 RVLDVGCGTGRLALAL---ARRgADV------TGVDISPEALEIARERAAElnVDFVQGDLEDLPLEDGSFDLVICSEVL 97

                         90       100
                 ....*....|....*....|....*...
gi 427994561 175 -------PSFDVFRRVLKPLGKIIMVDP 195
Cdd:COG2227   98 ehlpdpaALLRELARLLKPGGLLLLSTP 125
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 86-275 1.21e-06

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: 48.44  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561   86 KHVSNLSDLNSITILDAGCGEGYylnwlLTMAQKWKYPEVGIlIGMDISKWAVQSAAKRNRE-ITWIVGSNARPPFSPNS 164
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGY-----LTRALLKRFPQAEF-IALDISAGMLAQAKTKLSEnVQFICGDAEKLPLEDSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  165 INLILCAFGFPSFDVF-------RRVLKPLGKIIMVDPAPNHLMELRQL---IYPELKSKTSTVQTLPskgfNGFNLVES 234
Cdd:TIGR02072  99 FDLIVSNLALQWCDDLsqalselARVLKPGGLLAFSTFGPGTLHELRQSfgqHGLRYLSLDELKALLK----NSFELLTL 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 427994561  235 YHLTYKAKVENSQAV-QDLFLMTPHYFRSPPTAKTTIAALQE 275
Cdd:TIGR02072 175 EEELITLSFDDPLDVlRHLKKTGANGLSSGRTSRKQLKAFLE 216
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 98-193 2.29e-06

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: 45.50  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  98 TILDAGCGEGYYLNWLLtmaqKWKYPEVgilIGMDISKWAVQSAAKRNRE-----ITWIVGS-NARPPFSPNSINLILCA 171
Cdd:cd02440    1 RVLDLGCGTGALALALA----SGPGARV---TGVDISPVALELARKAAAAlladnVEVLKGDaEELPPEADESFDVIISD 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 427994561 172 FGFPS--------FDVFRRVLKPLGKIIMV 193
Cdd:cd02440   74 PPLHHlvedlarfLEEARRLLKPGGVLVLT 103
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 97-225 2.56e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.26  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561   97 ITILDAGCGEGYYLNWLLTmaqkwKYPEVGILIGMDISKWAVQSAAKRNRE-----ITWIVGS--NARPPFSPNSINLIL 169
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAE-----ELGPNAEVVGIDISEEAIEKARENAQKlgfdnVEFEQGDieELPELLEDDKFDVVI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 427994561  170 C-----AFGFPS--FDVFRRVLKPLGKIIMVDpaPNHLMELRQLIYPELKSKTSTVQTLPSKG 225
Cdd:pfam13847  80 SncvlnHIPDPDkvLQEILRVLKPGGRLIISD--PDSLAELPAHVKEDSTYYAGCVGGAILKK 140
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 96-211 3.83e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 46.45  E-value: 3.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  96 SITILDAGCGEGYYLNWlLTMAQKWKYpevgilIGMDISKWAVQSAAKRNRE-----ITWIVGS-NARPPFSPNSINLIL 169
Cdd:COG0500   27 GGRVLDLGCGTGRNLLA-LAARFGGRV------IGIDLSPEAIALARARAAKaglgnVEFLVADlAELDPLPAESFDLVV 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 427994561 170 CafgfpsFDVF---------------RRVLKPLGKIIMVDPAPNHLMELRQLIYPEL 211
Cdd:COG0500  100 A------FGVLhhlppeereallrelARALKPGGVLLLSASDAAAALSLARLLLLAT 150
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 98-195 1.56e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.15  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  98 TILDAGCGEGYylnWLLTMAQKWKYpEVgilIGMDISKWAVQSAAKRNRE------ITWIVGsNARPPFSPNSINLI--- 168
Cdd:COG2230   54 RVLDIGCGWGG---LALYLARRYGV-RV---TGVTLSPEQLEYARERAAEagladrVEVRLA-DYRDLPADGQFDAIvsi 125

                         90       100       110
                 ....*....|....*....|....*....|...
gi 427994561 169 --LCAFGFPS----FDVFRRVLKPLGKIIMVDP 195
Cdd:COG2230  126 gmFEHVGPENypayFAKVARLLKPGGRLLLHTP 158
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
98-153 1.78e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.89  E-value: 1.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 427994561  98 TILDAGCGEGYYLNWLltmAQKWKYPEVgilIGMDISKWAVQSAAKRNREITWIVG 153
Cdd:COG4106    4 RVLDLGCGTGRLTALL---AERFPGARV---TGVDLSPEMLARARARLPNVRFVVA 53
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 97-189 2.95e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 41.29  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  97 ITILDAGCGEGyylnwllTMAQKW--KYPEVGILIGMDISKWAVQSAAKRNRE------ITWIVGSNARPPFSPNSINLI 168
Cdd:PRK00216  53 DKVLDLACGTG-------DLAIALakAVGKTGEVVGLDFSEGMLAVGREKLRDlglsgnVEFVQGDAEALPFPDNSFDAV 125

                         90       100
                 ....*....|....*....|....*...
gi 427994561 169 LCAFG---FPSFDV----FRRVLKPLGK 189
Cdd:PRK00216 126 TIAFGlrnVPDIDKalreMYRVLKPGGR 153
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 93-144 7.08e-04

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 40.49  E-value: 7.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 427994561   93 DLNSITILDAGCGEGYYLNwlltmaqKWKYPEVGILIGMDISKWAVQSAAKR 144
Cdd:pfam03291  61 NSNKRKVLDLGCGKGGDLE-------KWFKGGISQLIGTDIAEVSIEQCRER 105
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 100-190 3.11e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.19  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561  100 LDAGCGEGYYLNWLLTMAQKWKYpevgilIGMDISKWAVQSAAKRNREITWIVGSNARPP------FSPNSINLILCAFG 173
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEY------TGLDISPAALEAARERLAALGLLNAVRVELFqldlgeLDPGSFDVVVASNV 74

                          90       100
                  ....*....|....*....|....
gi 427994561  174 F-------PSFDVFRRVLKPLGKI 190
Cdd:pfam08242  75 LhhladprAVLRNIRRLLKPGGVL 98
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 88-170 4.14e-03

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 37.18  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427994561   88 VSNLSDLNSITILDAGCGEGYylnwlLTMAQKWKYPEVgILIGMDISKWAVQSA---AKRNR-EITWIVGSNARPPFSPN 163
Cdd:pfam05175  24 LEHLPKDLSGKVLDLGCGAGV-----LGAALAKESPDA-ELTMVDINARALESArenLAANGlENGEVVASDVYSGVEDG 97


                  ....*..
gi 427994561  164 SINLILC 170
Cdd:pfam05175  98 KFDLIIS 104
 
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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