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Conserved domains on  [gi|2273532497|gb|UTO41771|]
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TylF/MycF family methyltransferase [Bacillus cereus]

Protein Classification

TylF/MycF family methyltransferase( domain architecture ID 10529713)

TylF/MycF family methyltransferase similar to Streptomyces fradiae macrocin O-methyltransferase (TylF) and Micromonospora griseorubida mycinamicin III 3''-O-methyltransferase (MycF)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TylF pfam05711
Macrocin-O-methyltransferase (TylF); This family consists of bacterial macrocin ...
 7-280 1.96e-159

Macrocin-O-methyltransferase (TylF); This family consists of bacterial macrocin O-methyltransferase (TylF) proteins. TylF is responsible for the methylation of macrocin to produce tylosin. Tylosin is a macrolide antibiotic used in veterinary medicine to treat infections caused by Gram-positive bacteria and as an animal growth promoter in the swine industry. It is produced by several Streptomyces species. As with other macrolides, the antibiotic activity of tylosin is due to the inhibition of protein biosynthesis by a mechanism that involves the binding of tylosin to the ribosome, preventing the formation of the mRNA-aminoacyl-tRNA-ribosome complex. The structure of one representative sequence from this family, NovP, shows it to be an S-adenosyl-l-methionine-dependent O-methyltransferase that catalyzes the penultimate step in the biosynthesis of the aminocoumarin antibiotic novobiocin. Specifically, it methylates at 4-OH of the noviose moiety, and the resultant methoxy group is important for the potency of the mature antibiotic. It is likely that the key structural features of NovP are common to the rest of the family and include: a helical 'lid' region that gates access to the co-substrate binding pocket and an active centre that contains a 3-Asp putative metal binding site. A further conserved Asp probably acts as the general base that initiates the reaction by de-protonating the 4-OH group of the noviose unit.


:

Pssm-ID: 428598  Cd Length: 255  Bit Score: 443.32  E-value: 1.96e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497   7 VQLYLELLKKTILFEIWLEYEAYLpaslhiskelefepvtvplpLFIKQYAENHNLKIVKPNVSKSERHDGMDWPRAAHS 86
Cdd:pfam05711   1 ASLYLDLLKKVLTGTVYEESELRL--------------------ILYKYHANRAPASARRSTFDAEKRAVGRDWPSLAHT 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497  87 MIGRERMNQLQEAMETVVRENIEGDFIETGVWRGGSCIFMNGFLQANNITDRNVWVADSFEGLPAPNlEQYPKDYGDYLH 166
Cdd:pfam05711  61 MIGRRRLDNLQECVEDVIAEGVPGDLIETGVWRGGACIFMRGILAAHGVRDRTVWVADSFAGLPAPD-PRYPGDAGDKLH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497 167 TF-DYLRVSLEQVQENFKKYDLLNDQVKFLKGWFKDTLPTAPIEKIAIARLDGDMYESTMDGLVNLYDKVSKGGYIIIDD 245
Cdd:pfam05711 140 ELnEVLAVSLEEVRDNFRRYGLLDDQVRFLKGWFKDTLPTAPIEKLAVLRLDGDLYESTMDALEALYPKVSPGGFVIVDD 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2273532497 246 YGL-PPCAEAVTDFRNQRNLKAPITKIDVFGVYWRK 280
Cdd:pfam05711 220 YGAvPGCREAVDDFRAAHGITAPLITIDWTGVYWRK 255
 
Name Accession Description Interval E-value
TylF pfam05711
Macrocin-O-methyltransferase (TylF); This family consists of bacterial macrocin ...
 7-280 1.96e-159

Macrocin-O-methyltransferase (TylF); This family consists of bacterial macrocin O-methyltransferase (TylF) proteins. TylF is responsible for the methylation of macrocin to produce tylosin. Tylosin is a macrolide antibiotic used in veterinary medicine to treat infections caused by Gram-positive bacteria and as an animal growth promoter in the swine industry. It is produced by several Streptomyces species. As with other macrolides, the antibiotic activity of tylosin is due to the inhibition of protein biosynthesis by a mechanism that involves the binding of tylosin to the ribosome, preventing the formation of the mRNA-aminoacyl-tRNA-ribosome complex. The structure of one representative sequence from this family, NovP, shows it to be an S-adenosyl-l-methionine-dependent O-methyltransferase that catalyzes the penultimate step in the biosynthesis of the aminocoumarin antibiotic novobiocin. Specifically, it methylates at 4-OH of the noviose moiety, and the resultant methoxy group is important for the potency of the mature antibiotic. It is likely that the key structural features of NovP are common to the rest of the family and include: a helical 'lid' region that gates access to the co-substrate binding pocket and an active centre that contains a 3-Asp putative metal binding site. A further conserved Asp probably acts as the general base that initiates the reaction by de-protonating the 4-OH group of the noviose unit.


Pssm-ID: 428598  Cd Length: 255  Bit Score: 443.32  E-value: 1.96e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497   7 VQLYLELLKKTILFEIWLEYEAYLpaslhiskelefepvtvplpLFIKQYAENHNLKIVKPNVSKSERHDGMDWPRAAHS 86
Cdd:pfam05711   1 ASLYLDLLKKVLTGTVYEESELRL--------------------ILYKYHANRAPASARRSTFDAEKRAVGRDWPSLAHT 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497  87 MIGRERMNQLQEAMETVVRENIEGDFIETGVWRGGSCIFMNGFLQANNITDRNVWVADSFEGLPAPNlEQYPKDYGDYLH 166
Cdd:pfam05711  61 MIGRRRLDNLQECVEDVIAEGVPGDLIETGVWRGGACIFMRGILAAHGVRDRTVWVADSFAGLPAPD-PRYPGDAGDKLH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497 167 TF-DYLRVSLEQVQENFKKYDLLNDQVKFLKGWFKDTLPTAPIEKIAIARLDGDMYESTMDGLVNLYDKVSKGGYIIIDD 245
Cdd:pfam05711 140 ELnEVLAVSLEEVRDNFRRYGLLDDQVRFLKGWFKDTLPTAPIEKLAVLRLDGDLYESTMDALEALYPKVSPGGFVIVDD 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2273532497 246 YGL-PPCAEAVTDFRNQRNLKAPITKIDVFGVYWRK 280
Cdd:pfam05711 220 YGAvPGCREAVDDFRAAHGITAPLITIDWTGVYWRK 255
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 165-245 3.46e-05

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 43.25  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497 165 LHTFDYLRVSLEQVQENFKKYDLlNDQVKFLKGWFKDTLPTAPIEKIAIARLDGDmYESTMDGLVNLYDKVSKGGYIIID 244
Cdd:COG4122    44 LTTIEIDPERAAIARENFARAGL-ADRIRLILGDALEVLPRLADGPFDLVFIDAD-KSNYPDYLELALPLLRPGGLIVAD 121


                  .
gi 2273532497 245 D 245
Cdd:COG4122   122 N 122
 
Name Accession Description Interval E-value
TylF pfam05711
Macrocin-O-methyltransferase (TylF); This family consists of bacterial macrocin ...
 7-280 1.96e-159

Macrocin-O-methyltransferase (TylF); This family consists of bacterial macrocin O-methyltransferase (TylF) proteins. TylF is responsible for the methylation of macrocin to produce tylosin. Tylosin is a macrolide antibiotic used in veterinary medicine to treat infections caused by Gram-positive bacteria and as an animal growth promoter in the swine industry. It is produced by several Streptomyces species. As with other macrolides, the antibiotic activity of tylosin is due to the inhibition of protein biosynthesis by a mechanism that involves the binding of tylosin to the ribosome, preventing the formation of the mRNA-aminoacyl-tRNA-ribosome complex. The structure of one representative sequence from this family, NovP, shows it to be an S-adenosyl-l-methionine-dependent O-methyltransferase that catalyzes the penultimate step in the biosynthesis of the aminocoumarin antibiotic novobiocin. Specifically, it methylates at 4-OH of the noviose moiety, and the resultant methoxy group is important for the potency of the mature antibiotic. It is likely that the key structural features of NovP are common to the rest of the family and include: a helical 'lid' region that gates access to the co-substrate binding pocket and an active centre that contains a 3-Asp putative metal binding site. A further conserved Asp probably acts as the general base that initiates the reaction by de-protonating the 4-OH group of the noviose unit.


Pssm-ID: 428598  Cd Length: 255  Bit Score: 443.32  E-value: 1.96e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497   7 VQLYLELLKKTILFEIWLEYEAYLpaslhiskelefepvtvplpLFIKQYAENHNLKIVKPNVSKSERHDGMDWPRAAHS 86
Cdd:pfam05711   1 ASLYLDLLKKVLTGTVYEESELRL--------------------ILYKYHANRAPASARRSTFDAEKRAVGRDWPSLAHT 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497  87 MIGRERMNQLQEAMETVVRENIEGDFIETGVWRGGSCIFMNGFLQANNITDRNVWVADSFEGLPAPNlEQYPKDYGDYLH 166
Cdd:pfam05711  61 MIGRRRLDNLQECVEDVIAEGVPGDLIETGVWRGGACIFMRGILAAHGVRDRTVWVADSFAGLPAPD-PRYPGDAGDKLH 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497 167 TF-DYLRVSLEQVQENFKKYDLLNDQVKFLKGWFKDTLPTAPIEKIAIARLDGDMYESTMDGLVNLYDKVSKGGYIIIDD 245
Cdd:pfam05711 140 ELnEVLAVSLEEVRDNFRRYGLLDDQVRFLKGWFKDTLPTAPIEKLAVLRLDGDLYESTMDALEALYPKVSPGGFVIVDD 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2273532497 246 YGL-PPCAEAVTDFRNQRNLKAPITKIDVFGVYWRK 280
Cdd:pfam05711 220 YGAvPGCREAVDDFRAAHGITAPLITIDWTGVYWRK 255
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 113-246 5.63e-08

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 50.00  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497 113 IETGVWRGGSCIFMNGFLQANNITdrnvwvadsfeglpapnleqypkdygdYLHTFDYLRVSlEQVQENFKKyDLLNDQV 192
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAALRDNGLG---------------------------RLTAVDPDPGA-EEAGALLRK-AGLDDRV 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2273532497 193 KFLKGWFKDTLPTAPIEKIAIARLDGDM-YESTMDGLVNLYDKVSKGGYIIIDDY 246
Cdd:pfam13578  52 RLIVGDSREALPSLADGPIDLLFIDGDHtYEAVLNDLELWLPRLAPGGVILFHDI 106
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 165-245 3.46e-05

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 43.25  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273532497 165 LHTFDYLRVSLEQVQENFKKYDLlNDQVKFLKGWFKDTLPTAPIEKIAIARLDGDmYESTMDGLVNLYDKVSKGGYIIID 244
Cdd:COG4122    44 LTTIEIDPERAAIARENFARAGL-ADRIRLILGDALEVLPRLADGPFDLVFIDAD-KSNYPDYLELALPLLRPGGLIVAD 121


                  .
gi 2273532497 245 D 245
Cdd:COG4122   122 N 122
 
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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