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Conserved domains on  [gi|1745905482|gb|KAA5399925|]
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methyltransferase domain-containing protein [Phocaeicola dorei]

Protein Classification

RsmD family RNA methyltransferase( domain architecture ID 10002368)

RsmD family RNA methyltransferase similar to 16S rRNA (guanine(966)-N(2))-methyltransferase RsmD, which specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:0003676|GO:0031167|GO:0008168

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 1-178 3.85e-66

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: 200.31  E-value: 3.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   1 MRVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLsNNYFDfenGVTALDLFAGTGSISIELVSRGCDRVISVEKDPQH 80
Cdd:COG0742     1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNIL-GPDIE---GARVLDLFAGSGALGLEALSRGAASVVFVEKDRKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  81 LSFISQVMREVK-TDKCFPIRADVFRFIDK-CSEQFDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKENHFE 158
Cdd:COG0742    77 AAVIRKNLEKLGlEDRARVIRGDALRFLKRlAGEPFDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSKREELP 156

                         170       180
                  ....*....|....*....|...
gi 1745905482 159 DNP---HFIERRVYGSVNFSFFK 178
Cdd:COG0742   157 ELPaglELLKERKYGDTRLSFYR 179
 
Name Accession Description Interval E-value
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 1-178 3.85e-66

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: 200.31  E-value: 3.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   1 MRVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLsNNYFDfenGVTALDLFAGTGSISIELVSRGCDRVISVEKDPQH 80
Cdd:COG0742     1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNIL-GPDIE---GARVLDLFAGSGALGLEALSRGAASVVFVEKDRKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  81 LSFISQVMREVK-TDKCFPIRADVFRFIDK-CSEQFDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKENHFE 158
Cdd:COG0742    77 AAVIRKNLEKLGlEDRARVIRGDALRFLKRlAGEPFDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSKREELP 156

                         170       180
                  ....*....|....*....|...
gi 1745905482 159 DNP---HFIERRVYGSVNFSFFK 178
Cdd:COG0742   157 ELPaglELLKERKYGDTRLSFYR 179
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
1-178 3.34e-41

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 136.99  E-value: 3.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   1 MRVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLSNnyfdFENGVTALDLFAGTGSISIELVSRGCDRVISVEKDPQh 80
Cdd:pfam03602   1 MRIIGGKARGRKLKVPPGPGTRPTTDRVREALFNWLAP----YIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKR- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  81 lsFISQVMREVKTDKCFP--IRADVFRFIDK---CSEQFDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKEN 155
Cdd:pfam03602  76 --AVQILKENLQLLGLPGavLVMDALLALLRlagKGPVFDIVFLDPPYAKGLIEEVLDLLAEKGWLKPNALIYVETEKRG 153

                         170       180
                  ....*....|....*....|....*.
gi 1745905482 156 HFEDNPHFIE---RRVYGSVNFSFFK 178
Cdd:pfam03602 154 ELPEQPGNLElvrEKKYGQTTLAFYQ 179
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
 2-178 5.43e-32

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 113.66  E-value: 5.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   2 RVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLsnnyFDFENGVTALDLFAGTGSISIELVSRGCDRVISVEKDPqhl 81
Cdd:TIGR00095  11 RIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNIL----RPDIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDR--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  82 SFISQVMREVKTDKC-----FPIRADVFRFIDKCSEQ--FDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKE 154
Cdd:TIGR00095  84 KVAQTLKENLSTLKKsgeqaTVLNDAVRALLFLAKKQtpFDIIYLDPPFNRGLLEALLELLGENKWLNPKGLIVVEYDRE 163

                         170       180
                  ....*....|....*....|....*..
gi 1745905482 155 NHFEDNPHFIER---RVYGSVNFSFFK 178
Cdd:TIGR00095 164 NELPTVPETWSLlrqKVYGQSALRLYQ 190
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
 1-161 8.15e-14

16S rRNA m(2)G966-methyltransferase; Provisional


Pssm-ID: 236793  Cd Length: 199  Bit Score: 66.28  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   1 MRVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLSNNYfdfeNGVTALDLFAGTGSISIELVSRGCDRVISVEKDPQH 80
Cdd:PRK10909   13 IRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVI----VDARCLDCFAGSGALGLEALSRYAAGATLLEMDRAV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  81 LSFISQVMREVKTDKCFPIRADVFRFIDKCSEQFDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKENHFEDN 160
Cdd:PRK10909   89 AQQLIKNLATLKAGNARVVNTNALSFLAQPGTPHNVVFVDPPFRKGLLEETINLLEDNGWLADEALIYVESEVENGLPTV 168


                  .
gi 1745905482 161 P 161
Cdd:PRK10909  169 P 169
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-150 3.28e-13

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: 62.83  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  48 TALDLFAGTGSISIELVSRGCDRVISVEKDPQHLSFISQVMREVKTDKCFPIRADVFRFIDKCSEQFDFIFADPPYAlkD 127
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLH--H 78

                          90       100
                  ....*....|....*....|....*
gi 1745905482 128 LESIPTRIFESG--ILKEDGLLVLE 150
Cdd:cd02440    79 LVEDLARFLEEArrLLKPGGVLVLT 103
rADc smart00650
Ribosomal RNA adenine dimethylases;
54-181 1.80e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.49  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   54 AGTGSISIELVSRgCDRVISVEKDPqHLSFISQvMREVKTDKCFPIRADVFRFiDKCSEQFDFIFADPPYalkdleSIPT 133
Cdd:smart00650  22 PGKGALTEELLER-AKRVTAIEIDP-RLAPRLR-EKFAAADNLTVIHGDALKF-DLPKLQPYKVVGNLPY------NIST 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1745905482  134 RI----FESGILKEDGLLVLEhgKEnhfednphFIERRV--YGSVNFSFFKAMV 181
Cdd:smart00650  92 PIlfklLEEPPAFRDAVLMVQ--KE--------VARRLAakPGSKDYGRLSVLL 135
 
Name Accession Description Interval E-value
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 1-178 3.85e-66

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: 200.31  E-value: 3.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   1 MRVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLsNNYFDfenGVTALDLFAGTGSISIELVSRGCDRVISVEKDPQH 80
Cdd:COG0742     1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNIL-GPDIE---GARVLDLFAGSGALGLEALSRGAASVVFVEKDRKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  81 LSFISQVMREVK-TDKCFPIRADVFRFIDK-CSEQFDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKENHFE 158
Cdd:COG0742    77 AAVIRKNLEKLGlEDRARVIRGDALRFLKRlAGEPFDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSKREELP 156

                         170       180
                  ....*....|....*....|...
gi 1745905482 159 DNP---HFIERRVYGSVNFSFFK 178
Cdd:COG0742   157 ELPaglELLKERKYGDTRLSFYR 179
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
1-178 3.34e-41

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 136.99  E-value: 3.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   1 MRVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLSNnyfdFENGVTALDLFAGTGSISIELVSRGCDRVISVEKDPQh 80
Cdd:pfam03602   1 MRIIGGKARGRKLKVPPGPGTRPTTDRVREALFNWLAP----YIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKR- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  81 lsFISQVMREVKTDKCFP--IRADVFRFIDK---CSEQFDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKEN 155
Cdd:pfam03602  76 --AVQILKENLQLLGLPGavLVMDALLALLRlagKGPVFDIVFLDPPYAKGLIEEVLDLLAEKGWLKPNALIYVETEKRG 153

                         170       180
                  ....*....|....*....|....*.
gi 1745905482 156 HFEDNPHFIE---RRVYGSVNFSFFK 178
Cdd:pfam03602 154 ELPEQPGNLElvrEKKYGQTTLAFYQ 179
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
 2-178 5.43e-32

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 113.66  E-value: 5.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   2 RVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLsnnyFDFENGVTALDLFAGTGSISIELVSRGCDRVISVEKDPqhl 81
Cdd:TIGR00095  11 RIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNIL----RPDIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDR--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  82 SFISQVMREVKTDKC-----FPIRADVFRFIDKCSEQ--FDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKE 154
Cdd:TIGR00095  84 KVAQTLKENLSTLKKsgeqaTVLNDAVRALLFLAKKQtpFDIIYLDPPFNRGLLEALLELLGENKWLNPKGLIVVEYDRE 163

                         170       180
                  ....*....|....*....|....*..
gi 1745905482 155 NHFEDNPHFIER---RVYGSVNFSFFK 178
Cdd:TIGR00095 164 NELPTVPETWSLlrqKVYGQSALRLYQ 190
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
 1-161 8.15e-14

16S rRNA m(2)G966-methyltransferase; Provisional


Pssm-ID: 236793  Cd Length: 199  Bit Score: 66.28  E-value: 8.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   1 MRVISGIYKRRRFDVPHTFKARPTTDFAKENLFNVLSNNYfdfeNGVTALDLFAGTGSISIELVSRGCDRVISVEKDPQH 80
Cdd:PRK10909   13 IRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVI----VDARCLDCFAGSGALGLEALSRYAAGATLLEMDRAV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  81 LSFISQVMREVKTDKCFPIRADVFRFIDKCSEQFDFIFADPPYALKDLESIPTRIFESGILKEDGLLVLEHGKENHFEDN 160
Cdd:PRK10909   89 AQQLIKNLATLKAGNARVVNTNALSFLAQPGTPHNVVFVDPPFRKGLLEETINLLEDNGWLADEALIYVESEVENGLPTV 168


                  .
gi 1745905482 161 P 161
Cdd:PRK10909  169 P 169
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-150 3.28e-13

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: 62.83  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  48 TALDLFAGTGSISIELVSRGCDRVISVEKDPQHLSFISQVMREVKTDKCFPIRADVFRFIDKCSEQFDFIFADPPYAlkD 127
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLH--H 78

                          90       100
                  ....*....|....*....|....*
gi 1745905482 128 LESIPTRIFESG--ILKEDGLLVLE 150
Cdd:cd02440    79 LVEDLARFLEEArrLLKPGGVLVLT 103
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
46-122 3.52e-08

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 51.83  E-value: 3.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  46 GVTALDLFAGTGSISIELVSRGCDRVISVEKDPQHLsFISQV---MREVKTDKCFPIRADVFRFIDKC-SEQFDFIFADP 121
Cdd:COG2521   133 GDRVLDTCTGLGYTAIEALKRGAREVITVEKDPNVL-ELAELnpwSRELANERIKIILGDASEVIKTFpDESFDAIIHDP 211


                  .
gi 1745905482 122 P 122
Cdd:COG2521   212 P 212
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 46-149 5.95e-07

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 48.25  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  46 GVTALDLFAGTGSISIELVSRGCDRVISVEKDPQhlsFISQVMREVK----TDKCFPIRADVFRFIDKCS---EQFDFIF 118
Cdd:COG1092   217 GKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSAT---ALEWAKENAAlnglDDRHEFVQADAFDWLRELAregERFDLII 293

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1745905482 119 ADPPyAL----KDLESIP---TRIFESGI--LKEDGLLVL 149
Cdd:COG1092   294 LDPP-AFakskKDLFDAQrdyKDLNRLALklLAPGGILVT 332
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 43-150 5.10e-06

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: 43.85  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  43 FENGVTALDLFAGTGSISIELVSRGCDrVISVEKDPQHLSFISQVMREVKTDkcfPIRADVFRFiDKCSEQFDFIFA--- 119
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAELNVD---FVQGDLEDL-PLEDGSFDLVICsev 96

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1745905482 120 -----DPPYALKDLesiptrifeSGILKEDGLLVLE 150
Cdd:COG2227    97 lehlpDPAALLREL---------ARLLKPGGLLLLS 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 46-150 6.48e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.52  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  46 GVTALDLFAGTGSISIELVSRGCDRVISVEKDPQHLSFISQVMREVKTDKCFPIRADVFRFIDKCSEQFDFIFADppYAL 125
Cdd:COG0500    27 GGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDPLPAESFDLVVAF--GVL 104

                          90       100
                  ....*....|....*....|....*...
gi 1745905482 126 KDLE-SIPTRIFES--GILKEDGLLVLE 150
Cdd:COG0500   105 HHLPpEEREALLRElaRALKPGGVLLLS 132
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
46-122 7.38e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.51  E-value: 7.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1745905482  46 GVTALDLFAGTGSISIELVSRGCDRVISVEKDPQHLSFISQVMREVKTDKCFpIRADVFRFidKCSEQFDFIFADPP 122
Cdd:COG2263    46 GKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLGVRVDF-IRADVTRI--PLGGSVDTVVMNPP 119
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 16-152 7.59e-06

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 45.04  E-value: 7.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  16 PHTFKARPTTDFAKENLFNVLSNNYFDFEngvtALDLFAGTGSISIELVS--RGCDrVISVEKDPQHLSFISQVMREVK- 92
Cdd:TIGR00536  89 EHVLIPRPETEELVEKALASLISQPPILH----ILDLGTGSGCIALALAYefPNAE-VIAVDISPDALAVAEENAEKNQl 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  93 TDKCFPIRADVFRfiDKCSEQFDFIFADPPY--------------------------ALKDLESIPTRIfeSGILKEDGL 146
Cdd:TIGR00536 164 EHRVEFIQSNLFE--PLAGQKIDIIVSNPPYideedladlpnvvrfepllalvggddGLNILRQIIELA--PDYLKPNGF 239


                  ....*.
gi 1745905482 147 LVLEHG 152
Cdd:TIGR00536 240 LVCEIG 245
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
 50-123 2.07e-05

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 42.71  E-value: 2.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1745905482  50 LDLFAGTGSISIELVSRGCdRVISVEKDPQHLsFISQVMREV--KTDKCFPIRADVFRFIDKCSE---QFDFIFADPPY 123
Cdd:pfam09445   5 LDVFCGGGGNTIQFANVFD-SVISIDINLEHL-ACAQHNAEVygVSDRIWLIHGDWFELLAKLKFekiKYDCVFASPPW 81
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 99-122 3.61e-05

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 43.25  E-value: 3.61e-05
                          10        20
                  ....*....|....*....|....
gi 1745905482  99 IRADVFRFIDKCSEQFDFIFADPP 122
Cdd:PRK11783  594 IQADCLAWLKEAREQFDLIFIDPP 617
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 48-122 4.86e-05

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 42.86  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  48 TALDLFAGTGSISIeLVSRGCDRVISVEKDPQ---------HLSFISQVmrevktdkcFPIRADVFRFIDK--CSEQFDF 116
Cdd:COG2265   236 RVLDLYCGVGTFAL-PLARRAKKVIGVEIVPEavedarenaRLNGLKNV---------EFVAGDLEEVLPEllWGGRPDV 305


                  ....*.
gi 1745905482 117 IFADPP 122
Cdd:COG2265   306 VVLDPP 311
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 44-118 1.82e-04

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 39.62  E-value: 1.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1745905482  44 ENGVTALDLFAGTGSISIELVSR-GCDRVISVEKDPQHLSFISQVMREVKTDKCFPIRADVFRFIDKCSEQFDFIF 118
Cdd:TIGR02469  18 RPGDVLWDIGAGTGSVTIEAARLvPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPEAPEALLPDPDAVF 93
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 50-136 3.16e-04

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 40.54  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  50 LDLFAGTGSISIE--LVSRGCdRVISVEKDPQHLSFisqvmrevktdkcfpIRADVFRFidkCSEQFDFIFADPPYALKD 127
Cdd:COG2242   252 WDIGAGSGSVSIEaaRLAPGG-RVYAIERDPERAAL---------------IRANARRF---GVPNVEVVEGEAPEALAD 312


                  ....*....
gi 1745905482 128 LESiPTRIF 136
Cdd:COG2242   313 LPD-PDAVF 320
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
43-122 9.16e-04

23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 39.05  E-value: 9.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  43 FENGVTALDLFAGTGSISIELVSRGCDRVISVEKDPQHLSFISQVMREVKTD--KCFPIRADVFRFIDKC---SEQFDFI 117
Cdd:PRK15128  218 YVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDlsKAEFVRDDVFKLLRTYrdrGEKFDVI 297


                  ....*
gi 1745905482 118 FADPP 122
Cdd:PRK15128  298 VMDPP 302
rADc smart00650
Ribosomal RNA adenine dimethylases;
54-181 1.80e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.49  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482   54 AGTGSISIELVSRgCDRVISVEKDPqHLSFISQvMREVKTDKCFPIRADVFRFiDKCSEQFDFIFADPPYalkdleSIPT 133
Cdd:smart00650  22 PGKGALTEELLER-AKRVTAIEIDP-RLAPRLR-EKFAAADNLTVIHGDALKF-DLPKLQPYKVVGNLPY------NIST 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1745905482  134 RI----FESGILKEDGLLVLEhgKEnhfednphFIERRV--YGSVNFSFFKAMV 181
Cdd:smart00650  92 PIlfklLEEPPAFRDAVLMVQ--KE--------VARRLAakPGSKDYGRLSVLL 135
PHA03411 PHA03411
putative methyltransferase; Provisional
 50-124 2.18e-03

putative methyltransferase; Provisional


Pssm-ID: 177639 [Multi-domain]  Cd Length: 279  Bit Score: 37.77  E-value: 2.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1745905482  50 LDLFAGTGSISIELVSRgC--DRVISVEKDPQHLSFISQVMREVKTdkcfpIRADVFRFidKCSEQFDFIFADPPYA 124
Cdd:PHA03411   69 LDLCAGIGRLSFCMLHR-CkpEKIVCVELNPEFARIGKRLLPEAEW-----ITSDVFEF--ESNEKFDVVISNPPFG 137
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 42-123 3.42e-03

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: 37.05  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  42 DFENGVTALDLFAGTGSISIELVSRGCD-RVISVEKDPQhlsFISQVMREVK----TDKCFPIRADVFRFIDK-CSEQFD 115
Cdd:COG4123    34 PVKKGGRVLDLGTGTGVIALMLAQRSPGaRITGVEIQPE---AAELARRNVAlnglEDRITVIHGDLKEFAAElPPGSFD 110


                  ....*...
gi 1745905482 116 FIFADPPY 123
Cdd:COG4123   111 LVVSNPPY 118
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-158 4.83e-03

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: 35.74  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  46 GVTALDLFAGTGSISIELVSRGCdRVISVEKDPQHLSFISQVMREVKTDKCFpIRADVFR--FIDkcsEQFDFIFA---- 119
Cdd:COG2226    23 GARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGLNVEF-VVGDAEDlpFPD---GSFDLVISsfvl 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1745905482 120 ----DPPYALKDLESiptrifesgILKEDG-LLVLEHGKENHFE 158
Cdd:COG2226    98 hhlpDPERALAEIAR---------VLKPGGrLVVVDFSPPDLAE 132
PRK14968 PRK14968
putative methyltransferase; Provisional
 44-123 5.77e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.03  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745905482  44 ENGVTALDLFAGTGSISIELVSRGCDrVISVEKDPQ--HLSFISQVMREVKTDKCFPIRADVFRFIDKcsEQFDFIFADP 121
Cdd:PRK14968   22 KKGDRVLEVGTGSGIVAIVAAKNGKK-VVGVDINPYavECAKCNAKLNNIRNNGVEVIRSDLFEPFRG--DKFDVILFNP 98


                  ..
gi 1745905482 122 PY 123
Cdd:PRK14968   99 PY 100
BpsA COG1568
Aminopropyltransferase BpsA, N(4)-bis(aminopropyl)spermidine biosynthesis [Secondary ...
 58-129 9.51e-03

Aminopropyltransferase BpsA, N(4)-bis(aminopropyl)spermidine biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441176  Cd Length: 354  Bit Score: 35.71  E-value: 9.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1745905482  58 SISIELvSRGCDRVISVEKDPQHLSFISQVMREVKtdkcFPIRADVFRFIDKCSE----QFDFIFADPPYALKDLE 129
Cdd:COG1568   167 SIALAL-TGLPRRITVVDIDERLLDFINEVAKEEG----LDIEAVHYDLRNPLPEelrgKFDVFFTDPPETLEGLK 237
 
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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