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Conserved domains on  [gi|504706646|ref|WP_014893748|]
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MULTISPECIES: O-methyltransferase [Bacillus]

Protein Classification

O-methyltransferase( domain architecture ID 11467877)

O-methyltransferase of the class I-like SAM-binding methyltransferase superfamily, such as catechol O-methyltransferases that can use various catechol-like compounds

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
37-197 6.02e-51

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: 161.89  E-value: 6.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  37 REMGQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEEtNGNVTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAF 116
Cdd:COG4122    2 PEQGRLLYLLARLLGAKRILEIGTGTGYSTLWLARALPD-DGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646 117 LDSQLDHSFDFIFLDSERTQYMWWLEHIKRILQPKSLLVVDNATSH------------ASELAEFINMIEEDEMFETVLL 184
Cdd:COG4122   81 LPRLADGPFDLVFIDADKSNYPDYLELALPLLRPGGLIVADNVLWHgrvadparrdpsTRAIREFNEYLREDPRLESVLL 160
                        170
                 ....*....|...
gi 504706646 185 AFQNGAFVARKKK 197
Cdd:COG4122  161 PIGDGLLLARKRG 173
 
Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
37-197 6.02e-51

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: 161.89  E-value: 6.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  37 REMGQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEEtNGNVTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAF 116
Cdd:COG4122    2 PEQGRLLYLLARLLGAKRILEIGTGTGYSTLWLARALPD-DGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646 117 LDSQLDHSFDFIFLDSERTQYMWWLEHIKRILQPKSLLVVDNATSH------------ASELAEFINMIEEDEMFETVLL 184
Cdd:COG4122   81 LPRLADGPFDLVFIDADKSNYPDYLELALPLLRPGGLIVADNVLWHgrvadparrdpsTRAIREFNEYLREDPRLESVLL 160
                        170
                 ....*....|...
gi 504706646 185 AFQNGAFVARKKK 197
Cdd:COG4122  161 PIGDGLLLARKRG 173
Methyltransf_3 pfam01596
O-methyltransferase; Members of this family are O-methyltransferases. The family includes ...
15-196 2.15e-24

O-methyltransferase; Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase, caffeoyl-CoA O-methyltransferase and a family of bacterial O-methyltransferases that may be involved in antibiotic production.


Pssm-ID: 396257 [Multi-domain]  Cd Length: 203  Bit Score: 94.87  E-value: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   15 EQYGEEHDRNKKTREEKLRN------ISREMGQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEEtNGNVTTVELSSE 88
Cdd:pfam01596   1 ETSAYEHEYLKELREETAKLplapmqVSPDEGQFLGMLVKLTGAKNVLEIGVFTGYSALAMALALPE-DGKITAIDIDPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   89 RVGEALANFEKANLLQRIDVHNQEAGAFLDS----QLDHSFDFIFLDSERTQYMWWLEHIKRILQPKSLLVVDNATSHAS 164
Cdd:pfam01596  80 AYEIAKKFIQKAGVAHKISFILGPALKVLEQltqdKPLPEFDFIFIDADKSNYPNYYERLLELLKVGGLMAIDNTLWHGK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 504706646  165 ------------ELAEFINMIEEDEMFETVLLAFQNGAFVARKK 196
Cdd:pfam01596 160 vtepddqeaktqRLQEFNKDLAQDPRVEISVIPVGDGITLCRKI 203
PLN02589 PLN02589
caffeoyl-CoA O-methyltransferase
5-167 1.55e-15

caffeoyl-CoA O-methyltransferase


Pssm-ID: 166230  Cd Length: 247  Bit Score: 72.33  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   5 DTLDSLLFQLEQYGEEHDRNKKTREEKLR---NI---SREMGQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEEtNG 78
Cdd:PLN02589  27 DALYQYILETSVYPREPESMKELRELTAKhpwNImttSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALALPE-DG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  79 NVTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAFLDSQLDH-----SFDFIFLDSERTQYMWWLEHIKRILQPKSL 153
Cdd:PLN02589 106 KILAMDINRENYELGLPVIQKAGVAHKIDFREGPALPVLDQMIEDgkyhgTFDFIFVDADKDNYINYHKRLIDLVKVGGV 185
                        170
                 ....*....|....
gi 504706646 154 LVVDNATSHASELA 167
Cdd:PLN02589 186 IGYDNTLWNGSVVA 199
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
54-149 1.37e-07

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: 47.81  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  54 NILEIGTSNGYSTLWLANAVeetNGNVTTVELSSERVGEALANfEKANLLQRIDVHNQEAGAFLDsQLDHSFDFIFLDSE 133
Cdd:cd02440    1 RVLDLGCGTGALALALASGP---GARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPP-EADESFDVIISDPP 75
                         90
                 ....*....|....*.
gi 504706646 134 rtqYMWWLEHIKRILQ 149
Cdd:cd02440   76 ---LHHLVEDLARFLE 88
 
Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
37-197 6.02e-51

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: 161.89  E-value: 6.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  37 REMGQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEEtNGNVTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAF 116
Cdd:COG4122    2 PEQGRLLYLLARLLGAKRILEIGTGTGYSTLWLARALPD-DGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646 117 LDSQLDHSFDFIFLDSERTQYMWWLEHIKRILQPKSLLVVDNATSH------------ASELAEFINMIEEDEMFETVLL 184
Cdd:COG4122   81 LPRLADGPFDLVFIDADKSNYPDYLELALPLLRPGGLIVADNVLWHgrvadparrdpsTRAIREFNEYLREDPRLESVLL 160
                        170
                 ....*....|...
gi 504706646 185 AFQNGAFVARKKK 197
Cdd:COG4122  161 PIGDGLLLARKRG 173
Methyltransf_3 pfam01596
O-methyltransferase; Members of this family are O-methyltransferases. The family includes ...
15-196 2.15e-24

O-methyltransferase; Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase, caffeoyl-CoA O-methyltransferase and a family of bacterial O-methyltransferases that may be involved in antibiotic production.


Pssm-ID: 396257 [Multi-domain]  Cd Length: 203  Bit Score: 94.87  E-value: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   15 EQYGEEHDRNKKTREEKLRN------ISREMGQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEEtNGNVTTVELSSE 88
Cdd:pfam01596   1 ETSAYEHEYLKELREETAKLplapmqVSPDEGQFLGMLVKLTGAKNVLEIGVFTGYSALAMALALPE-DGKITAIDIDPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   89 RVGEALANFEKANLLQRIDVHNQEAGAFLDS----QLDHSFDFIFLDSERTQYMWWLEHIKRILQPKSLLVVDNATSHAS 164
Cdd:pfam01596  80 AYEIAKKFIQKAGVAHKISFILGPALKVLEQltqdKPLPEFDFIFIDADKSNYPNYYERLLELLKVGGLMAIDNTLWHGK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 504706646  165 ------------ELAEFINMIEEDEMFETVLLAFQNGAFVARKK 196
Cdd:pfam01596 160 vtepddqeaktqRLQEFNKDLAQDPRVEISVIPVGDGITLCRKI 203
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
56-158 6.58e-16

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 70.03  E-value: 6.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   56 LEIGTSNGYSTLWLANAVEETN-GNVTTVELsSERVGEALANFEKANLLQRIDVHNQEAGAFLDSQLDHSFDFIFLDS-- 132
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAALRDNGlGRLTAVDP-DPGAEEAGALLRKAGLDDRVRLIVGDSREALPSLADGPIDLLFIDGdh 79
                          90       100
                  ....*....|....*....|....*.
gi 504706646  133 ERTQYMWWLEHIKRILQPKSLLVVDN 158
Cdd:pfam13578  80 TYEAVLNDLELWLPRLAPGGVILFHD 105
PLN02589 PLN02589
caffeoyl-CoA O-methyltransferase
5-167 1.55e-15

caffeoyl-CoA O-methyltransferase


Pssm-ID: 166230  Cd Length: 247  Bit Score: 72.33  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   5 DTLDSLLFQLEQYGEEHDRNKKTREEKLR---NI---SREMGQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEEtNG 78
Cdd:PLN02589  27 DALYQYILETSVYPREPESMKELRELTAKhpwNImttSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALALPE-DG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  79 NVTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAFLDSQLDH-----SFDFIFLDSERTQYMWWLEHIKRILQPKSL 153
Cdd:PLN02589 106 KILAMDINRENYELGLPVIQKAGVAHKIDFREGPALPVLDQMIEDgkyhgTFDFIFVDADKDNYINYHKRLIDLVKVGGV 185
                        170
                 ....*....|....
gi 504706646 154 LVVDNATSHASELA 167
Cdd:PLN02589 186 IGYDNTLWNGSVVA 199
PLN02781 PLN02781
Probable caffeoyl-CoA O-methyltransferase
5-158 2.65e-15

Probable caffeoyl-CoA O-methyltransferase


Pssm-ID: 215417  Cd Length: 234  Bit Score: 71.39  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   5 DTLDSLLFQLEQYGEEHDRNKKTRE---EKLRNISrEM------GQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEE 75
Cdd:PLN02781  14 EALKQYIMETSAYPREHELLKELREatvQKYGNLS-EMevpvdeGLFLSMLVKIMNAKNTLEIGVFTGYSLLTTALALPE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  76 tNGNVTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAFLDSQLDHS----FDFIFLDSERTQYMWWLEHIKRILQPK 151
Cdd:PLN02781  93 -DGRITAIDIDKEAYEVGLEFIKKAGVDHKINFIQSDALSALDQLLNNDpkpeFDFAFVDADKPNYVHFHEQLLKLVKVG 171

                 ....*..
gi 504706646 152 SLLVVDN 158
Cdd:PLN02781 172 GIIAFDN 178
PLN02476 PLN02476
O-methyltransferase
25-196 7.16e-12

O-methyltransferase


Pssm-ID: 178094  Cd Length: 278  Bit Score: 62.39  E-value: 7.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  25 KKTREE--KLR----NISREMGQFLSILVKGCSAKNILEIGTSNGYSTLWLANAVEETnGNVTTVELSSERVGEALANFE 98
Cdd:PLN02476  86 RQLREEtsKMRgsqmQVSPDQAQLLAMLVQILGAERCIEVGVYTGYSSLAVALVLPES-GCLVACERDSNSLEVAKRYYE 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  99 KANLLQRIDVHNQEAGAFLDSQL----DHSFDFIFLDSERTQYMWWLEHIKRILQPKSLLVVDNATSHASELAEFIN--- 171
Cdd:PLN02476 165 LAGVSHKVNVKHGLAAESLKSMIqngeGSSYDFAFVDADKRMYQDYFELLLQLVRVGGVIVMDNVLWHGRVADPLVNdak 244
                        170       180       190
                 ....*....|....*....|....*....|....
gi 504706646 172 ---------MIEEDEMFETVLLAFQNGAFVARKK 196
Cdd:PLN02476 245 tisirnfnkKLMDDKRVSISMVPIGDGMTICRKR 278
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
53-183 8.22e-11

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 59.02  E-value: 8.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  53 KNILEIGTSNGYSTLWLANAVEETnGNVTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAFLDsqlDHSFDFIFLDs 132
Cdd:COG2519   93 ARVLEAGTGSGALTLALARAVGPE-GKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGID---EGDVDAVFLD- 167
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504706646 133 ertqyM---W-WLEHIKRILQPKSLLVVDNAT-SHASELAE------FInmieEDEMFETVL 183
Cdd:COG2519  168 -----MpdpWeALEAVAKALKPGGVLVAYVPTvNQVSKLVEalresgFT----DIEAVETLL 220
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
55-150 9.43e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 50.64  E-value: 9.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   55 ILEIGTSNGYSTLWLANAVeetNGNVTTVELSSERVGEALANFEKANLlqRIDVHNQEAGAFldSQLDHSFDFIFLdSER 134
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG---GARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDL--PFPDGSFDLVVS-SGV 72
                          90       100
                  ....*....|....*....|..
gi 504706646  135 TQYMWW------LEHIKRILQP 150
Cdd:pfam13649  73 LHHLPDpdleaaLREIARVLKP 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
54-168 1.05e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 52.61  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  54 NILEIGTSNGYSTLWLANAveeTNGNVTTVELSSERVGEALANFEKANlLQRIDVHNQEAGAFLDSQLDHsFDFIFLD-- 131
Cdd:COG0500   29 RVLDLGCGTGRNLLALAAR---FGGRVIGIDLSPEAIALARARAAKAG-LGNVEFLVADLAELDPLPAES-FDLVVAFgv 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 504706646 132 ------SERTQYmwwLEHIKRILQPKSLLVVDNATSHASELAE 168
Cdd:COG0500  104 lhhlppEEREAL---LRELARALKPGGVLLLSASDAAAALSLA 143
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
55-156 1.20e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.16  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  55 ILEIGTSNGYSTLWLAnavEETNGNVTTVELSSERVGEALANFEKANLLQRIDVHNQEagaFLDSQLDHSFDFIFL---- 130
Cdd:COG2230   55 VLDIGCGWGGLALYLA---RRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLAD---YRDLPADGQFDAIVSigmf 128
                         90       100       110
                 ....*....|....*....|....*....|
gi 504706646 131 ----DSERTQYmwwLEHIKRILQPKSLLVV 156
Cdd:COG2230  129 ehvgPENYPAY---FAKVARLLKPGGRLLL 155
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
54-149 1.37e-07

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: 47.81  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  54 NILEIGTSNGYSTLWLANAVeetNGNVTTVELSSERVGEALANfEKANLLQRIDVHNQEAGAFLDsQLDHSFDFIFLDSE 133
Cdd:cd02440    1 RVLDLGCGTGALALALASGP---GARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPP-EADESFDVIISDPP 75
                         90
                 ....*....|....*.
gi 504706646 134 rtqYMWWLEHIKRILQ 149
Cdd:cd02440   76 ---LHHLVEDLARFLE 88
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
53-170 3.75e-07

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: 47.68  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  53 KNILEIGTSNGYSTLWLAnaveETNGNVTTVELSSERVGEALANFEKANLlqRIDVHNQEAGAF-LDsqlDHSFDFIFL- 130
Cdd:COG2226   24 ARVLDLGCGTGRLALALA----ERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpFP---DGSFDLVISs 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 504706646 131 -------DSERTqymwwLEHIKRILQPK-SLLVVDNATSHASELAEFI 170
Cdd:COG2226   95 fvlhhlpDPERA-----LAEIARVLKPGgRLVVVDFSPPDLAELEELL 137
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
53-156 1.44e-05

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: 42.70  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646  53 KNILEIGTSNGYSTLWLANAVEEtngnVTTVELSSERVGEALANFEKANllqrIDVHNQEAGAFldSQLDHSFDFIFL-- 130
Cdd:COG2227   26 GRVLDVGCGTGRLALALARRGAD----VTGVDISPEALEIARERAAELN----VDFVQGDLEDL--PLEDGSFDLVICse 95
                         90       100       110
                 ....*....|....*....|....*....|..
gi 504706646 131 ------DSERtqymwWLEHIKRILQPKSLLVV 156
Cdd:COG2227   96 vlehlpDPAA-----LLRELARLLKPGGLLLL 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
56-156 2.67e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 38.41  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   56 LEIGTSNGYSTLWLAnaveETNGNVTTVELSSERVGEALANFEKANLLQRIdvhnqeaGAFLDSQL-DHSFDFIFLdser 134
Cdd:pfam08241   1 LDVGCGTGLLTELLA----RLGARVTGVDISPEMLELAREKAPREGLTFVV-------GDAEDLPFpDNSFDLVLS---- 65
                          90       100       110
                  ....*....|....*....|....*....|..
gi 504706646  135 tqyMWWLEH----------IKRILQPKSLLVV 156
Cdd:pfam08241  66 ---SEVLHHvedperalreIARVLKPGGILII 94
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
80-131 3.87e-04

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 39.68  E-value: 3.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504706646  80 VTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAFLDSQLDHSFDFIFLD 131
Cdd:COG0742   67 VVFVEKDRKAAAVIRKNLEKLGLEDRARVIRGDALRFLKRLAGEPFDLVFLD 118
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
51-129 5.59e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 39.36  E-value: 5.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504706646  51 SAKNILEIGTSNGYSTLWLANAVEetNGNVTTVELSSERVGEALANFEKANLLQRIDVHNQEAGAFLDSQLDHSFDFIF 129
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQRSP--GARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDLVV 113
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
54-104 2.19e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 37.69  E-value: 2.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504706646  54 NILEIGTSNGYSTLWLANAVEETnGNVTTVelssERVGEaLANFEKANLLQ 104
Cdd:PRK13942  79 KVLEIGTGSGYHAAVVAEIVGKS-GKVVTI----ERIPE-LAEKAKKTLKK 123
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
51-177 2.24e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.01  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504706646   51 SAKNILEIGTSNGYSTLWLANAVEEtNGNVTTVELSSERVGEALANFEKaNLLQRIDVHNQEAGAFLDSQLDHSFDFIFL 130
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGP-NAEVVGIDISEEAIEKARENAQK-LGFDNVEFEQGDIEELPELLEDDKFDVVIS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504706646  131 --------DSERTqymwwLEHIKRILQPKSLLVVdnatSHASELAEFINMIEEDE 177
Cdd:pfam13847  81 ncvlnhipDPDKV-----LQEILRVLKPGGRLII----SDPDSLAELPAHVKEDS 126
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
54-102 3.09e-03

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 37.11  E-value: 3.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 504706646  54 NILEIGTSNGYSTLWLANAVEEtngnVTTVELSSERVGEALANFEKANL 102
Cdd:PRK00312  81 RVLEIGTGSGYQAAVLAHLVRR----VFSVERIKTLQWEAKRRLKQLGL 125
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
55-102 7.67e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 35.83  E-value: 7.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504706646  55 ILEIGTSNGYSTLWLANAVeetnGNVTTVELSSERVGEALANFEKANL 102
Cdd:COG2518   70 VLEIGTGSGYQAAVLARLA----GRVYSVERDPELAERARERLAALGY 113
 
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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