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Conserved domains on  [gi|1109557347|gb|APG42598|]
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erythromycin resistance protein ErmR [Cloning vector pTZvec11_(adhA)]

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
SCOP:  3000118

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;
6-246 5.60e-89

Ribosomal RNA adenine dimethylase;


:

Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 263.84  E-value: 5.60e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   6 NKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIH 85
Cdd:pfam00398   3 KFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  86 QDILQFQFPNK-----QRYKIVGSIPYHLSTQIIKKVVFESHA--SDIYLIVEEGFYKRTLD-----IHRTLGLLLHTQV 153
Cdd:pfam00398  83 QDFLKFEFPSLvthihQEFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLArpgskLYSRLSVLRQAFT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347 154 SIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFVSKWVNREYRQLFTK------NQFHQAMKHAKVNN 226
Cdd:pfam00398 163 DVKLVAKVPPSIFSPPPKVDSALVRLERHDPDpHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGIND 242

                         250       260
                  ....*....|....*....|
gi 1109557347 227 LSTVTYEQVLSIFNSYLLFN 246
Cdd:pfam00398 243 NALVKKLSPEQTLDIFNELA 262
 
Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
6-246 5.60e-89

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 263.84  E-value: 5.60e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   6 NKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIH 85
Cdd:pfam00398   3 KFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  86 QDILQFQFPNK-----QRYKIVGSIPYHLSTQIIKKVVFESHA--SDIYLIVEEGFYKRTLD-----IHRTLGLLLHTQV 153
Cdd:pfam00398  83 QDFLKFEFPSLvthihQEFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLArpgskLYSRLSVLRQAFT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347 154 SIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFVSKWVNREYRQLFTK------NQFHQAMKHAKVNN 226
Cdd:pfam00398 163 DVKLVAKVPPSIFSPPPKVDSALVRLERHDPDpHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGIND 242

                         250       260
                  ....*....|....*....|
gi 1109557347 227 LSTVTYEQVLSIFNSYLLFN 246
Cdd:pfam00398 243 NALVKKLSPEQTLDIFNELA 262
rADc smart00650
Ribosomal RNA adenine dimethylases;
21-182 5.89e-61

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 189.26  E-value: 5.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   21 VLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDILQFQFPNKQRYK 100
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  101 IVGSIPYHLSTQIIKKVVFESHA-SDIYLIVEEGFYKRTL-----DIHRTLGLLLHTQVSIQQLLKLPAECFHPKPKVNS 174
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*...
gi 1109557347  175 VLIKLTRH 182
Cdd:smart00650 161 AVVRLERR 168
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 1-198 5.05e-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: 151.82  E-value: 5.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   1 MADPMNKNIK----YSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLK 76
Cdd:COG0030     1 MSKSRRYGLRpkkrLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  77 LNTRVTLIHQDILQFQFP---NKQRYKIVGSIPYHLSTQIIKKVVFESHA-SDIYLIV----------EEG--FYKRtld 140
Cdd:COG0030    81 AYPNLTVIEGDALKVDLPalaAGEPLKVVGNLPYNISTPILFKLLEARPPiEDAVLMVqkevaerlvaKPGskDYGR--- 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1109557347 141 ihrtLGLLLHTQVSIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFV 198
Cdd:COG0030   158 ----LSVLVQYYADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPlVPVADEKLFFRVV 212
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
5-199 2.20e-35

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 126.55  E-value: 2.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   5 MNKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLI 84
Cdd:PRK14896    1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  85 HQDILQFQFPNKQryKIVGSIPYHLSTQIIKKVV---FEShasdIYLIVEEGFYKR------TLDIHRtLGLLLHTQVSI 155
Cdd:PRK14896   81 EGDALKVDLPEFN--KVVSNLPYQISSPITFKLLkhgFEP----AVLMYQKEFAERmvakpgTKEYGR-LSVMVQYYADV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1109557347 156 QQLLKLPAECFHPKPKVNSVLIKLTRHTTDVPDKYWKLYTYFVS 199
Cdd:PRK14896  154 EIVEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFVK 197
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 10-182 8.47e-34

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: 122.34  E-value: 8.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  10 KYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDIL 89
Cdd:TIGR00755   6 SLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  90 QFQFP--NKQRYKIVGSIPYHLSTQIIKKvVFESHAS--DIYLIVEEGFYKR------TLDIHRtLGLLLHTQVSIQQLL 159
Cdd:TIGR00755  86 KFDLNelAKDLTKVVGNLPYNISSPLIFK-LLKEKDAfkLAVLMVQKEVAERlvakpgSKDYGR-LSVLVQYYANVEIVF 163

                         170       180
                  ....*....|....*....|...
gi 1109557347 160 KLPAECFHPKPKVNSVLIKLTRH 182
Cdd:TIGR00755 164 KVPPSAFYPPPKVDSAVVRLVPL 186
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 36-122 1.56e-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: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  36 TVYEIGTGKGHLTTKLAKIS-KQVTSIELDSHLFNLSSEK--LKLNTRVTLIHQDILQFQFPNKQRY-KIVGSIPYHLST 111
Cdd:cd02440     1 RVLDLGCGTGALALALASGPgARVTGVDISPVALELARKAaaALLADNVEVLKGDAEELPPEADESFdVIISDPPLHHLV 80

                          90
                  ....*....|.
gi 1109557347 112 QIIKKVVFESH 122
Cdd:cd02440    81 EDLARFLEEAR 91
 
Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
6-246 5.60e-89

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 263.84  E-value: 5.60e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   6 NKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIH 85
Cdd:pfam00398   3 KFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDENLTVIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  86 QDILQFQFPNK-----QRYKIVGSIPYHLSTQIIKKVVFESHA--SDIYLIVEEGFYKRTLD-----IHRTLGLLLHTQV 153
Cdd:pfam00398  83 QDFLKFEFPSLvthihQEFLVVGNLPYNISTPIVKQLLFESRFgiVDMLLMLQKEFARRLLArpgskLYSRLSVLRQAFT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347 154 SIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFVSKWVNREYRQLFTK------NQFHQAMKHAKVNN 226
Cdd:pfam00398 163 DVKLVAKVPPSIFSPPPKVDSALVRLERHDPDpHPVKDLDVYDSVVRKLFNRKRKTLSTSlkslfpGGQLQAFSSHGIND 242

                         250       260
                  ....*....|....*....|
gi 1109557347 227 LSTVTYEQVLSIFNSYLLFN 246
Cdd:pfam00398 243 NALVKKLSPEQTLDIFNELA 262
rADc smart00650
Ribosomal RNA adenine dimethylases;
21-182 5.89e-61

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 189.26  E-value: 5.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   21 VLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDILQFQFPNKQRYK 100
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  101 IVGSIPYHLSTQIIKKVVFESHA-SDIYLIVEEGFYKRTL-----DIHRTLGLLLHTQVSIQQLLKLPAECFHPKPKVNS 174
Cdd:smart00650  81 VVGNLPYNISTPILFKLLEEPPAfRDAVLMVQKEVARRLAakpgsKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKVDS 160


                   ....*...
gi 1109557347  175 VLIKLTRH 182
Cdd:smart00650 161 AVVRLERR 168
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 1-198 5.05e-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: 151.82  E-value: 5.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   1 MADPMNKNIK----YSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLK 76
Cdd:COG0030     1 MSKSRRYGLRpkkrLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  77 LNTRVTLIHQDILQFQFP---NKQRYKIVGSIPYHLSTQIIKKVVFESHA-SDIYLIV----------EEG--FYKRtld 140
Cdd:COG0030    81 AYPNLTVIEGDALKVDLPalaAGEPLKVVGNLPYNISTPILFKLLEARPPiEDAVLMVqkevaerlvaKPGskDYGR--- 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1109557347 141 ihrtLGLLLHTQVSIQQLLKLPAECFHPKPKVNSVLIKLTRHTTD-VPDKYWKLYTYFV 198
Cdd:COG0030   158 ----LSVLVQYYADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPlVPVADEKLFFRVV 212
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
5-199 2.20e-35

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 126.55  E-value: 2.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   5 MNKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLI 84
Cdd:PRK14896    1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAGNVEII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  85 HQDILQFQFPNKQryKIVGSIPYHLSTQIIKKVV---FEShasdIYLIVEEGFYKR------TLDIHRtLGLLLHTQVSI 155
Cdd:PRK14896   81 EGDALKVDLPEFN--KVVSNLPYQISSPITFKLLkhgFEP----AVLMYQKEFAERmvakpgTKEYGR-LSVMVQYYADV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1109557347 156 QQLLKLPAECFHPKPKVNSVLIKLTRHTTDVPDKYWKLYTYFVS 199
Cdd:PRK14896  154 EIVEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDFFDDFVK 197
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 10-182 8.47e-34

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: 122.34  E-value: 8.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  10 KYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDIL 89
Cdd:TIGR00755   6 SLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDAL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  90 QFQFP--NKQRYKIVGSIPYHLSTQIIKKvVFESHAS--DIYLIVEEGFYKR------TLDIHRtLGLLLHTQVSIQQLL 159
Cdd:TIGR00755  86 KFDLNelAKDLTKVVGNLPYNISSPLIFK-LLKEKDAfkLAVLMVQKEVAERlvakpgSKDYGR-LSVLVQYYANVEIVF 163

                         170       180
                  ....*....|....*....|...
gi 1109557347 160 KLPAECFHPKPKVNSVLIKLTRH 182
Cdd:TIGR00755 164 KVPPSAFYPPPKVDSAVVRLVPL 186
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 4-179 2.59e-12

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 65.02  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347   4 PMNKniKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNlsseklKLNTRV-- 81
Cdd:PTZ00338    9 VFNK--KFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVA------ELKKRFqn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  82 -------TLIHQDILQFQFPNKQryKIVGSIPYHLSTQIIKKVVfeSHASDI---YLIVEEGFYKRTL----DIHRTLgL 147
Cdd:PTZ00338   81 splasklEVIEGDALKTEFPYFD--VCVANVPYQISSPLVFKLL--AHRPLFrcaVLMFQKEFALRLLaqpgDELYCR-L 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1109557347 148 LLHTQV--SIQQLLKLPAECFHPKPKVNSVLIKL 179
Cdd:PTZ00338  156 SVNTQLlcRVTHLMKVSKNSFNPPPKVESSVVRI 189
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 28-87 8.83e-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: 8.83e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109557347  28 QLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKL-KLN-TRVTLIHQD 87
Cdd:COG2518    61 ALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLaALGyDNVTVRVGD 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 36-122 1.56e-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: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  36 TVYEIGTGKGHLTTKLAKIS-KQVTSIELDSHLFNLSSEK--LKLNTRVTLIHQDILQFQFPNKQRY-KIVGSIPYHLST 111
Cdd:cd02440     1 RVLDLGCGTGALALALASGPgARVTGVDISPVALELARKAaaALLADNVEVLKGDAEELPPEADESFdVIISDPPLHHLV 80

                          90
                  ....*....|.
gi 1109557347 112 QIIKKVVFESH 122
Cdd:cd02440    81 EDLARFLEEAR 91
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 24-95 2.16e-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: 2.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109557347  24 QIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKL-KLNTRVTLIHQDILQFQFPN 95
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAaEAGLNVEFVVGDAEDLPFPD 85
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
32-96 1.77e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.64  E-value: 1.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109557347  32 KETDTVYEIGTGKGhLTTKLA--KISKQVTSIELDSHLFNLSSEKLKLN---TRVTLIHQDILQFQFPNK 96
Cdd:COG4076    34 KPGDVVLDIGTGSG-LLSMLAarAGAKKVYAVEVNPDIAAVARRIIAANglsDRITVINADATDLDLPEK 102
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
25-62 1.04e-04

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 42.11  E-value: 1.04e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1109557347  25 IIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIE 62
Cdd:PRK00312   70 MTELLELKPGDRVLEIGTGSGYQAAVLAHLVRRVFSVE 107
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 24-88 2.96e-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: 2.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109557347  24 QIIKQLNLKETDTVYEIGTGKGHLTTKLAKI---SKQVTSIELDSHLF-----NLssEKLKLNTRVTLIHQDI 88
Cdd:COG2519    82 YIIARLDIFPGARVLEAGTGSGALTLALARAvgpEGKVYSYERREDFAeiarkNL--ERFGLPDNVELKLGDI 152
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 37-97 5.01e-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: 5.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109557347  37 VYEIGTGKGHLTTKLAK-ISKQVTSIELDSHLFNLSSEKLK-LNTRVTLIHQDILQFQFPNKQ 97
Cdd:pfam13649   1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAeAGLNVEFVQGDAEDLPFPDGS 63
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 19-97 8.57e-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: 8.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109557347  19 EKVLNQIIKQLnLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKlNTRVTLIHQDILQFQFPNKQ 97
Cdd:COG2227    11 DRRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA-ELNVDFVQGDLEDLPLEDGS 87
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 30-91 1.01e-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: 39.36  E-value: 1.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109557347  30 NLKETDTVYEIGTGKGHLTTKLAKISK--QVTSIELDSHLFNLSSEKLKLN---TRVTLIHQDILQF 91
Cdd:COG4123    34 PVKKGGRVLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNgleDRITVIHGDLKEF 100
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 25-96 3.18e-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: 3.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109557347  25 IIKQLNLKETDTVYEIGTGKGHLTTKLAK-ISKQVTSIELDSHLFNLSSEKLK---LNTRVTLIHQDILQFQFPNK 96
Cdd:COG2230    43 ILRKLGLKPGMRVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAeagLADRVEVRLADYRDLPADGQ 118
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 29-76 4.87e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 37.30  E-value: 4.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1109557347  29 LNLKETDTVYEIGTGKGHLTTKLAKI---SKQVTSIELDSHLFNLSSEKLK 76
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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