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Conserved domains on  [gi|1279118920|gb|ATW75320|]
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erythromycin resistance protein [Cloning vector pBBR1MCS-Erm]

Protein Classification

rRNA adenine N(6)-methyltransferase family protein( domain architecture ID 10449687)

rRNA adenine N(6)-methyltransferase family protein is a class I SAM-dependent methyltransferase, similar to bacterial rRNA adenine N-6-methyltransferase and fungal mitochondrial transcription factor 1

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047|GO:0003723
PubMed:  12504684|12826405

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
2-242 1.35e-88

Ribosomal RNA adenine dimethylase;


:

Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 262.69  E-value: 1.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   2 NKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIH 81
Cdd:pfam00398   3 KFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  82 QDILQFQFPNK-----QRYKIVGSIPYHLSTQIIKKVVFESHA--SDIYLIVEEGFYKRTLD-----IHRTLGLLLHTQV 149
Cdd:pfam00398  83 QDFLKFEFPSLvthihQEFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLArpgskLYSRLSVLRQAFT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920 150 SIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFVSKWVNREYRQLFTK------NQFHQAMKHAKVNN 222
Cdd:pfam00398 163 DVKLVAKVPPSIFSPPPKVDSALVRLERHDPDpHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGIND 242

                         250       260
                  ....*....|....*....|
gi 1279118920 223 LSTVTYEQVLSIFNSYLLFN 242
Cdd:pfam00398 243 NALVKKLSPEQTLDIFNELA 262
 
Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
2-242 1.35e-88

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 262.69  E-value: 1.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   2 NKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIH 81
Cdd:pfam00398   3 KFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  82 QDILQFQFPNK-----QRYKIVGSIPYHLSTQIIKKVVFESHA--SDIYLIVEEGFYKRTLD-----IHRTLGLLLHTQV 149
Cdd:pfam00398  83 QDFLKFEFPSLvthihQEFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLArpgskLYSRLSVLRQAFT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920 150 SIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFVSKWVNREYRQLFTK------NQFHQAMKHAKVNN 222
Cdd:pfam00398 163 DVKLVAKVPPSIFSPPPKVDSALVRLERHDPDpHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGIND 242

                         250       260
                  ....*....|....*....|
gi 1279118920 223 LSTVTYEQVLSIFNSYLLFN 242
Cdd:pfam00398 243 NALVKKLSPEQTLDIFNELA 262
rADc smart00650
Ribosomal RNA adenine dimethylases;
17-178 5.19e-61

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 189.26  E-value: 5.19e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   17 VLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDILQFQFPNKQRYK 96
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   97 IVGSIPYHLSTQIIKKVVFESHA-SDIYLIVEEGFYKRTL-----DIHRTLGLLLHTQVSIQQLLKLPAECFHPKPKVNS 170
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*...
gi 1279118920  171 VLIKLTRH 178
Cdd:smart00650 161 AVVRLERR 168
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 6-194 6.69e-45

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 151.43  E-value: 6.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   6 KYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDIL 85
Cdd:COG0030    14 RLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  86 QFQFP---NKQRYKIVGSIPYHLSTQIIKKVVFESHA-SDIYLIV----------EEG--FYKRtldihrtLGLLLHTQV 149
Cdd:COG0030    94 KVDLPalaAGEPLKVVGNLPYNISTPILFKLLEARPPiEDAVLMVqkevaerlvaKPGskDYGR-------LSVLVQYYA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1279118920 150 SIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFV 194
Cdd:COG0030   167 DVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPlVPVADEKLFFRVV 212
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
1-195 2.00e-35

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 126.55  E-value: 2.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   1 MNKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLI 80
Cdd:PRK14896    1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  81 HQDILQFQFPNKQryKIVGSIPYHLSTQIIKKVV---FEShasdIYLIVEEGFYKR------TLDIHRtLGLLLHTQVSI 151
Cdd:PRK14896   81 EGDALKVDLPEFN--KVVSNLPYQISSPITFKLLkhgFEP----AVLMYQKEFAERmvakpgTKEYGR-LSVMVQYYADV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1279118920 152 QQLLKLPAECFHPKPKVNSVLIKLTRHTTDVPDKYWKLYTYFVS 195
Cdd:PRK14896  154 EIVEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFVK 197
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 6-178 1.10e-33

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 121.95  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   6 KYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDIL 85
Cdd:TIGR00755   6 SLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  86 QFQFP--NKQRYKIVGSIPYHLSTQIIKKvVFESHAS--DIYLIVEEGFYKR------TLDIHRtLGLLLHTQVSIQQLL 155
Cdd:TIGR00755  86 KFDLNelAKDLTKVVGNLPYNISSPLIFK-LLKEKDAfkLAVLMVQKEVAERlvakpgSKDYGR-LSVLVQYYANVEIVF 163

                         170       180
                  ....*....|....*....|...
gi 1279118920 156 KLPAECFHPKPKVNSVLIKLTRH 178
Cdd:TIGR00755 164 KVPPSAFYPPPKVDSAVVRLVPL 186
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 32-118 1.51e-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: 48.58  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  32 TVYEIGTGKGHLTTKLAKIS-KQVTSIELDSHLFNLSSEK--LKLNTRVTLIHQDILQFQFPNKQRY-KIVGSIPYHLST 107
Cdd:cd02440     1 RVLDLGCGTGALALALASGPgARVTGVDISPVALELARKAaaALLADNVEVLKGDAEELPPEADESFdVIISDPPLHHLV 80

                          90
                  ....*....|.
gi 1279118920 108 QIIKKVVFESH 118
Cdd:cd02440    81 EDLARFLEEAR 91
 
Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
2-242 1.35e-88

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 262.69  E-value: 1.35e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   2 NKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIH 81
Cdd:pfam00398   3 KFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  82 QDILQFQFPNK-----QRYKIVGSIPYHLSTQIIKKVVFESHA--SDIYLIVEEGFYKRTLD-----IHRTLGLLLHTQV 149
Cdd:pfam00398  83 QDFLKFEFPSLvthihQEFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLArpgskLYSRLSVLRQAFT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920 150 SIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFVSKWVNREYRQLFTK------NQFHQAMKHAKVNN 222
Cdd:pfam00398 163 DVKLVAKVPPSIFSPPPKVDSALVRLERHDPDpHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGIND 242

                         250       260
                  ....*....|....*....|
gi 1279118920 223 LSTVTYEQVLSIFNSYLLFN 242
Cdd:pfam00398 243 NALVKKLSPEQTLDIFNELA 262
rADc smart00650
Ribosomal RNA adenine dimethylases;
17-178 5.19e-61

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 189.26  E-value: 5.19e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   17 VLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDILQFQFPNKQRYK 96
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   97 IVGSIPYHLSTQIIKKVVFESHA-SDIYLIVEEGFYKRTL-----DIHRTLGLLLHTQVSIQQLLKLPAECFHPKPKVNS 170
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*...
gi 1279118920  171 VLIKLTRH 178
Cdd:smart00650 161 AVVRLERR 168
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 6-194 6.69e-45

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 151.43  E-value: 6.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   6 KYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDIL 85
Cdd:COG0030    14 RLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  86 QFQFP---NKQRYKIVGSIPYHLSTQIIKKVVFESHA-SDIYLIV----------EEG--FYKRtldihrtLGLLLHTQV 149
Cdd:COG0030    94 KVDLPalaAGEPLKVVGNLPYNISTPILFKLLEARPPiEDAVLMVqkevaerlvaKPGskDYGR-------LSVLVQYYA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1279118920 150 SIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFV 194
Cdd:COG0030   167 DVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPlVPVADEKLFFRVV 212
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
1-195 2.00e-35

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 126.55  E-value: 2.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   1 MNKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLI 80
Cdd:PRK14896    1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  81 HQDILQFQFPNKQryKIVGSIPYHLSTQIIKKVV---FEShasdIYLIVEEGFYKR------TLDIHRtLGLLLHTQVSI 151
Cdd:PRK14896   81 EGDALKVDLPEFN--KVVSNLPYQISSPITFKLLkhgFEP----AVLMYQKEFAERmvakpgTKEYGR-LSVMVQYYADV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1279118920 152 QQLLKLPAECFHPKPKVNSVLIKLTRHTTDVPDKYWKLYTYFVS 195
Cdd:PRK14896  154 EIVEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFVK 197
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 6-178 1.10e-33

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 121.95  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   6 KYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDIL 85
Cdd:TIGR00755   6 SLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  86 QFQFP--NKQRYKIVGSIPYHLSTQIIKKvVFESHAS--DIYLIVEEGFYKR------TLDIHRtLGLLLHTQVSIQQLL 155
Cdd:TIGR00755  86 KFDLNelAKDLTKVVGNLPYNISSPLIFK-LLKEKDAfkLAVLMVQKEVAERlvakpgSKDYGR-LSVLVQYYANVEIVF 163

                         170       180
                  ....*....|....*....|...
gi 1279118920 156 KLPAECFHPKPKVNSVLIKLTRH 178
Cdd:TIGR00755 164 KVPPSAFYPPPKVDSAVVRLVPL 186
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 1-175 3.37e-12

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 64.64  E-value: 3.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920   1 MNKniKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNlsseklKLNTRV--- 77
Cdd:PTZ00338   10 FNK--KFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVA------ELKKRFqns 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  78 ------TLIHQDILQFQFPNKQryKIVGSIPYHLSTQIIKKVVfeSHASDI---YLIVEEGFYKRTL----DIHRTLgLL 144
Cdd:PTZ00338   82 plasklEVIEGDALKTEFPYFD--VCVANVPYQISSPLVFKLL--AHRPLFrcaVLMFQKEFALRLLaqpgDELYCR-LS 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1279118920 145 LHTQV--SIQQLLKLPAECFHPKPKVNSVLIKL 175
Cdd:PTZ00338  157 VNTQLlcRVTHLMKVSKNSFNPPPKVESSVVRI 189
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 24-83 8.48e-08

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 50.86  E-value: 8.48e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279118920  24 QLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKL-KLN-TRVTLIHQD 83
Cdd:COG2518    61 ALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLaALGyDNVTVRVGD 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 32-118 1.51e-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: 48.58  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  32 TVYEIGTGKGHLTTKLAKIS-KQVTSIELDSHLFNLSSEK--LKLNTRVTLIHQDILQFQFPNKQRY-KIVGSIPYHLST 107
Cdd:cd02440     1 RVLDLGCGTGALALALASGPgARVTGVDISPVALELARKAaaALLADNVEVLKGDAEELPPEADESFdVIISDPPLHHLV 80

                          90
                  ....*....|.
gi 1279118920 108 QIIKKVVFESH 118
Cdd:cd02440    81 EDLARFLEEAR 91
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 20-91 2.10e-06

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: 46.14  E-value: 2.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279118920  20 QIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKL-KLNTRVTLIHQDILQFQFPN 91
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAaEAGLNVEFVVGDAEDLPFPD 85
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
28-92 1.71e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.64  E-value: 1.71e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279118920  28 KETDTVYEIGTGKGhLTTKLA--KISKQVTSIELDSHLFNLSSEKLKLN---TRVTLIHQDILQFQFPNK 92
Cdd:COG4076    34 KPGDVVLDIGTGSG-LLSMLAarAGAKKVYAVEVNPDIAAVARRIIAANglsDRITVINADATDLDLPEK 102
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
21-58 1.01e-04

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 42.11  E-value: 1.01e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1279118920  21 IIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIE 58
Cdd:PRK00312   70 MTELLELKPGDRVLEIGTGSGYQAAVLAHLVRRVFSVE 107
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 20-84 2.86e-04

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: 40.91  E-value: 2.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279118920  20 QIIKQLNLKETDTVYEIGTGKGHLTTKLAKI---SKQVTSIELDSHLF-----NLssEKLKLNTRVTLIHQDI 84
Cdd:COG2519    82 YIIARLDIFPGARVLEAGTGSGALTLALARAvgpEGKVYSYERREDFAeiarkNL--ERFGLPDNVELKLGDI 152
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 33-93 4.90e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 38.31  E-value: 4.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1279118920  33 VYEIGTGKGHLTTKLAK-ISKQVTSIELDSHLFNLSSEKLK-LNTRVTLIHQDILQFQFPNKQ 93
Cdd:pfam13649   1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAeAGLNVEFVQGDAEDLPFPDGS 63
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 15-93 8.37e-04

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: 38.46  E-value: 8.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1279118920  15 EKVLNQIIKQLnLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKlNTRVTLIHQDILQFQFPNKQ 93
Cdd:COG2227    11 DRRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA-ELNVDFVQGDLEDLPLEDGS 87
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 26-87 9.75e-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: 9.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1279118920  26 NLKETDTVYEIGTGKGHLTTKLAKISK--QVTSIELDSHLFNLSSEKLKLN---TRVTLIHQDILQF 87
Cdd:COG4123    34 PVKKGGRVLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNgleDRITVIHGDLKEF 100
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 21-92 3.10e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 37.22  E-value: 3.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279118920  21 IIKQLNLKETDTVYEIGTGKGHLTTKLAK-ISKQVTSIELDSHLFNLSSEKLK---LNTRVTLIHQDILQFQFPNK 92
Cdd:COG2230    43 ILRKLGLKPGMRVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAeagLADRVEVRLADYRDLPADGQ 118
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 25-72 4.73e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 37.30  E-value: 4.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1279118920  25 LNLKETDTVYEIGTGKGHLTTKLAKI---SKQVTSIELDSHLFNLSSEKLK 72
Cdd:PRK13942   72 LDLKEGMKVLEIGTGSGYHAAVVAEIvgkSGKVVTIERIPELAEKAKKTLK 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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