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Conserved domains on  [gi|156102204|ref|XP_001616795|]
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dimethyladenosine transferase, putative [Plasmodium vivax]

Protein Classification

rRNA adenine N(6)-methyltransferase family protein( domain architecture ID 10794378)

rRNA adenine N(6)-methyltransferase family protein is a class I SAM-dependent methyltransferase, similar to Schizosaccharomyces pombe dimethyladenosine transferase that specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008173
PubMed:  12826405|12504684

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 71-361 1.42e-176

dimethyladenosine transferase-like protein; Provisional


:

Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 494.14  E-value: 1.42e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  71 KSGNKMNMILYKKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLY 150
Cdd:PTZ00338   1 TGGSKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 151 EG-YNNLEVYEGDAIKTVFPRFDICTANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVK 229
Cdd:PTZ00338  81 SPlASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 230 LFCKVVKICNVDRSSFNPPPKVDSVILKLIPKENNFFINFDEWDNLLRICFSRKRKTLHAIFKRNAVLNMLEHNYKNFCT 309
Cdd:PTZ00338 161 LLCRVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCT 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156102204 310 -FNKIVPVNF-PFKKYCLDTLKELDMTECRSVSLDENDFLKLLLKFNKKGIHFF 361
Cdd:PTZ00338 241 mINKKVPVSLePFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHFV 294
 
Name Accession Description Interval E-value
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 71-361 1.42e-176

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 494.14  E-value: 1.42e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  71 KSGNKMNMILYKKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLY 150
Cdd:PTZ00338   1 TGGSKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 151 EG-YNNLEVYEGDAIKTVFPRFDICTANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVK 229
Cdd:PTZ00338  81 SPlASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 230 LFCKVVKICNVDRSSFNPPPKVDSVILKLIPKENNFFINFDEWDNLLRICFSRKRKTLHAIFKRNAVLNMLEHNYKNFCT 309
Cdd:PTZ00338 161 LLCRVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCT 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156102204 310 -FNKIVPVNF-PFKKYCLDTLKELDMTECRSVSLDENDFLKLLLKFNKKGIHFF 361
Cdd:PTZ00338 241 mINKKVPVSLePFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHFV 294
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 75-293 3.22e-80

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: 248.12  E-value: 3.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  75 KMNMILYKKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYN 154
Cdd:COG0030    6 RYGLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRET--FAAYP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 155 NLEVYEGDAIKTVFPRFDICT-----ANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVK 229
Cdd:COG0030   84 NLTVIEGDALKVDLPALAAGEplkvvGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQ 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156102204 230 LFCKVVKICNVDRSSFNPPPKVDSVILKLIPKENNFF--INFDEWDNLLRICFSRKRKTLHAIFKR 293
Cdd:COG0030  164 YYADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPLVpvADEKLFFRVVKAAFSQRRKTLRNSLKS 229
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 82-293 2.49e-76

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: 237.51  E-value: 2.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204   82 KKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYNNLEVYEG 161
Cdd:TIGR00755   5 KSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKL--LSLYNNLEIIEG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  162 DAIKTVFPRFDI----CTANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVKLFCKVVKI 237
Cdd:TIGR00755  83 DALKFDLNELAKdltkVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156102204  238 CNVDRSSFNPPPKVDSVILKLIPKENNFFI-NFDEWDNLLRICFSRKRKTLHAIFKR 293
Cdd:TIGR00755 163 FKVPPSAFYPPPKVDSAVVRLVPLKRKPSPkDFALFEELLKAAFQQRRKTLRNNLKN 219
rADc smart00650
Ribosomal RNA adenine dimethylases;
94-262 3.54e-65

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 205.82  E-value: 3.54e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204    94 ILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYNNLEVYEGDAIKTVFPR--F 171
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREK--FAAADNLTVIHGDALKFDLPKlqP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204   172 DICTANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVKLFCKVVKICNVDRSSFNPPPKV 251
Cdd:smart00650  79 YKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKV 158

                          170
                   ....*....|.
gi 156102204   252 DSVILKLIPKE 262
Cdd:smart00650 159 DSAVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
82-307 2.78e-56

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 186.03  E-value: 2.78e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204   82 KKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYNNLEVYEG 161
Cdd:pfam00398   6 TSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKK--LSLDENLTVIHQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  162 DAIKTVFP-------RFDICTANIPYKISSPLIFKLI-AHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVKLFCK 233
Cdd:pfam00398  84 DFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVLRQAFTD 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156102204  234 VVKICNVDRSSFNPPPKVDSVILKLIPKENNFF--INFDEWDNLLRICFSRKRKTLHAIFKRNAVLNMLEHNYKNF 307
Cdd:pfam00398 164 VKLVAKVPPSIFSPPPKVDSALVRLERHDPDPHpvKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFSSHG 239
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 110-205 6.18e-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: 64.76  E-value: 6.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 110 VLEIGCGTGNLTVKLLPI-AKKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDAIKTVF---PRFDICTANIPYKISSP 185
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeadESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|..
gi 156102204 186 LIFKLI--AHRPLFKCAVLMFQ 205
Cdd:cd02440   82 DLARFLeeARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 71-361 1.42e-176

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 494.14  E-value: 1.42e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  71 KSGNKMNMILYKKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLY 150
Cdd:PTZ00338   1 TGGSKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 151 EG-YNNLEVYEGDAIKTVFPRFDICTANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVK 229
Cdd:PTZ00338  81 SPlASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 230 LFCKVVKICNVDRSSFNPPPKVDSVILKLIPKENNFFINFDEWDNLLRICFSRKRKTLHAIFKRNAVLNMLEHNYKNFCT 309
Cdd:PTZ00338 161 LLCRVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCT 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 156102204 310 -FNKIVPVNF-PFKKYCLDTLKELDMTECRSVSLDENDFLKLLLKFNKKGIHFF 361
Cdd:PTZ00338 241 mINKKVPVSLePFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHFV 294
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 75-293 3.22e-80

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: 248.12  E-value: 3.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  75 KMNMILYKKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYN 154
Cdd:COG0030    6 RYGLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRET--FAAYP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 155 NLEVYEGDAIKTVFPRFDICT-----ANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVK 229
Cdd:COG0030   84 NLTVIEGDALKVDLPALAAGEplkvvGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQ 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156102204 230 LFCKVVKICNVDRSSFNPPPKVDSVILKLIPKENNFF--INFDEWDNLLRICFSRKRKTLHAIFKR 293
Cdd:COG0030  164 YYADVEILFTVPPEAFYPPPKVDSAVVRLTPRPEPLVpvADEKLFFRVVKAAFSQRRKTLRNSLKS 229
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 82-293 2.49e-76

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: 237.51  E-value: 2.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204   82 KKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYNNLEVYEG 161
Cdd:TIGR00755   5 KSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKL--LSLYNNLEIIEG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  162 DAIKTVFPRFDI----CTANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVKLFCKVVKI 237
Cdd:TIGR00755  83 DALKFDLNELAKdltkVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156102204  238 CNVDRSSFNPPPKVDSVILKLIPKENNFFI-NFDEWDNLLRICFSRKRKTLHAIFKR 293
Cdd:TIGR00755 163 FKVPPSAFYPPPKVDSAVVRLVPLKRKPSPkDFALFEELLKAAFQQRRKTLRNNLKN 219
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
82-298 2.51e-75

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 235.18  E-value: 2.51e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  82 KKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYNNLEVYEG 161
Cdd:PRK14896   5 KKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDD--EIAAGNVEIIEG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 162 DAIKTVFPRFDICTANIPYKISSPLIFKLIAHRplFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVKLFCKVVKICNVD 241
Cdd:PRK14896  83 DALKVDLPEFNKVVSNLPYQISSPITFKLLKHG--FEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEIVEKVP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 156102204 242 RSSFNPPPKVDSVILKLIPKENNFFINFDE-WDNLLRICFSRKRKTLhaifkRNAVLN 298
Cdd:PRK14896 161 PGAFSPKPKVDSAVVRLTPREPKYEVYDEDfFDDFVKALFQHRRKTL-----RNALKN 213
rADc smart00650
Ribosomal RNA adenine dimethylases;
94-262 3.54e-65

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 205.82  E-value: 3.54e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204    94 ILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYNNLEVYEGDAIKTVFPR--F 171
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREK--FAAADNLTVIHGDALKFDLPKlqP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204   172 DICTANIPYKISSPLIFKLIAHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVKLFCKVVKICNVDRSSFNPPPKV 251
Cdd:smart00650  79 YKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPKV 158

                          170
                   ....*....|.
gi 156102204   252 DSVILKLIPKE 262
Cdd:smart00650 159 DSAVVRLERRP 169
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
82-307 2.78e-56

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 186.03  E-value: 2.78e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204   82 KKHGQHLLKNPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRclYEGYNNLEVYEG 161
Cdd:pfam00398   6 TSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKK--LSLDENLTVIHQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  162 DAIKTVFP-------RFDICTANIPYKISSPLIFKLI-AHRPLFKCAVLMFQKEFADRMLANVGDSNYSRLTVNVKLFCK 233
Cdd:pfam00398  84 DFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVLRQAFTD 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156102204  234 VVKICNVDRSSFNPPPKVDSVILKLIPKENNFF--INFDEWDNLLRICFSRKRKTLHAIFKRNAVLNMLEHNYKNF 307
Cdd:pfam00398 164 VKLVAKVPPSIFSPPPKVDSALVRLERHDPDPHpvKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFSSHG 239
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 110-205 6.18e-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: 64.76  E-value: 6.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 110 VLEIGCGTGNLTVKLLPI-AKKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDAIKTVF---PRFDICTANIPYKISSP 185
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeadESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|..
gi 156102204 186 LIFKLI--AHRPLFKCAVLMFQ 205
Cdd:cd02440   82 DLARFLeeARRLLKPGGVLVLT 103
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 84-163 5.29e-12

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 64.34  E-value: 5.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  84 HGQHLLKnPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDA 163
Cdd:COG2518   45 HGQTISQ-PYIVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDG 123
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 96-177 7.81e-12

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: 62.70  E-value: 7.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  96 DKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYEGYnNLEVYEGDAIKTVFP--RFDI 173
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPdgSFDL 90


                 ....
gi 156102204 174 CTAN 177
Cdd:COG2226   91 VISS 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
94-180 1.16e-11

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 63.09  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  94 ILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYegynnLEVYEGDAIKTVFP--RF 171
Cdd:COG4976   34 LAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVY-----DRLLVADLADLAEPdgRF 108

                         90
                 ....*....|.
gi 156102204 172 D--ICTANIPY 180
Cdd:COG4976  109 DliVAADVLTY 119
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 110-177 1.20e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.96  E-value: 1.20e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156102204  110 VLEIGCGTGNLTVKLLPIAK-KVITIDIDARMVSEVKKRCLYEGYnNLEVYEGDAIKTVFP--RFDICTAN 177
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPdgSFDLVVSS 70
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 91-177 2.60e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.85  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  91 NPGILDKILLAAKIKSSDVVLEIGCGTGNLTVKLL-PIAKKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDAIKTV-- 167
Cdd:COG0500   11 LPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDpl 90

                         90
                 ....*....|.
gi 156102204 168 -FPRFDICTAN 177
Cdd:COG0500   91 pAESFDLVVAF 101
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 96-180 5.66e-08

HemK-related putative methylase; 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. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 52.55  E-value: 5.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204   96 DKILLAAKIK--SSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYEGYnNLEVYEGDAIKTVFPRFDI 173
Cdd:TIGR00537   7 DSLLLEANLRelKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNV-GLDVVMTDLFKGVRGKFDV 85


                  ....*..
gi 156102204  174 CTANIPY 180
Cdd:TIGR00537  86 ILFNPPY 92
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
110-177 1.47e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.05  E-value: 1.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156102204 110 VLEIGCGTGNLTVKLL---PIAkKVITIDIDARMVSEVKKRclyegYNNLEVYEGDAIKTVFPR-FDICTAN 177
Cdd:COG4106    5 VLDLGCGTGRLTALLAerfPGA-RVTGVDLSPEMLARARAR-----LPNVRFVVADLRDLDPPEpFDLVVSN 70
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 111-177 1.95e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 48.82  E-value: 1.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156102204  111 LEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYEGYNNLevyEGDAIKTVFP--RFDICTAN 177
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFV---VGDAEDLPFPdnSFDLVLSS 66
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 99-177 2.56e-07

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: 49.25  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  99 LLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRClyeGYNNLEVYEGDAIKTVFP--RFDICTA 176
Cdd:COG2227   17 LLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERA---AELNVDFVQGDLEDLPLEdgSFDLVIC 93


                 .
gi 156102204 177 N 177
Cdd:COG2227   94 S 94
PRK14968 PRK14968
putative methyltransferase; Provisional
 96-180 8.22e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 49.13  E-value: 8.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  96 DKILLA--AKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYEGYNN--LEVYEGDAIKTVFPR- 170
Cdd:PRK14968  11 DSFLLAenAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNngVEVIRSDLFEPFRGDk 90

                         90
                 ....*....|
gi 156102204 171 FDICTANIPY 180
Cdd:PRK14968  91 FDVILFNPPY 100
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 104-177 8.90e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.18  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  104 IKSSDVVLEIGCGTGNLTVKLLPIA---KKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDA--IKTVFP--RFDICTA 176
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIeeLPELLEddKFDVVIS 80


                  .
gi 156102204  177 N 177
Cdd:pfam13847  81 N 81
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
100-174 2.17e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 48.49  E-value: 2.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156102204 100 LAAKIKSSDVVLEIGCGTGNLTVKLLPI-AKKVITIDIDARMVSEVKKRCLYEGYN-NLEVYEGDAIKTVFP-RFDIC 174
Cdd:COG4076   29 IERVVKPGDVVLDIGTGSGLLSMLAARAgAKKVYAVEVNPDIAAVARRIIAANGLSdRITVINADATDLDLPeKADVI 106
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 95-180 4.51e-06

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: 47.45  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  95 LDKILLAA--KIKSSDVVLEIGCGTGnltvkLLPI-------AKKVITIDIDARMVSEVKKRCLYEGYNN-LEVYEGDaI 164
Cdd:COG4123   24 TDAVLLAAfaPVKKGGRVLDLGTGTG-----VIALmlaqrspGARITGVEIQPEAAELARRNVALNGLEDrITVIHGD-L 97

                         90       100
                 ....*....|....*....|.
gi 156102204 165 KTVFP-----RFDICTANIPY 180
Cdd:COG4123   98 KEFAAelppgSFDLVVSNPPY 118
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 102-184 5.32e-06

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 46.48  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 102 AKIKSSDVVLEIGCGTGNLTV--KLLPIakKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDAIKTVFP--RFD-ICTa 176
Cdd:COG1041   22 AGAKEGDTVLDPFCGTGTILIeaGLLGR--RVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDLPLAdeSVDaIVT- 98


                 ....*...
gi 156102204 177 NIPYKISS 184
Cdd:COG1041   99 DPPYGRSS 106
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 111-177 5.45e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.67  E-value: 5.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156102204  111 LEIGCGTGNLTVKLLP--IAKKVITIDIDARMVSEVKKR-CLYEGYN--NLEVYEGDAIKTVFPRFDICTAN 177
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalPGLEYTGLDISPAALEAARERlAALGLLNavRVELFQLDLGELDPGSFDVVVAS 72
PRK08317 PRK08317
hypothetical protein; Provisional
 96-174 7.02e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 46.85  E-value: 7.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  96 DKILLAAKIKSSDVVLEIGCGTGNLtvkLLPIAK------KVITIDIDARMVSEVKKRCLYEGyNNLEVYEGDAIKTVFP 169
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGND---ARELARrvgpegRVVGIDRSEAMLALAKERAAGLG-PNVEFVRGDADGLPFP 84


                 ....*..
gi 156102204 170 --RFDIC 174
Cdd:PRK08317  85 dgSFDAV 91
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
100-163 1.74e-05

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 45.20  E-value: 1.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156102204 100 LAAKI------KSSDVVLEIGCGTGNLT---VKLLPIAKKVITIDIDARMVSEVKKRclyegYNNLEVYEGDA 163
Cdd:COG3963   33 LARAMasevdwSGAGPVVELGPGTGVFTraiLARGVPDARLLAVEINPEFAEHLRRR-----FPRVTVVNGDA 100
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 98-163 5.08e-05

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: 42.70  E-value: 5.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156102204   98 ILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAK--KVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDA 163
Cdd:TIGR02469  11 TLAKLRLRPGDVLWDIGAGTGSVTIEAARLVPngRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDA 78
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 100-177 8.55e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 42.80  E-value: 8.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156102204  100 LAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDAiktvfpRFDICTAN 177
Cdd:pfam13489  16 LLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPAG------KFDVIVAR 87
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
92-163 1.16e-04

precorrin-6Y C5,15-methyltransferase subunit CbiT;


Pssm-ID: 180961  Cd Length: 196  Bit Score: 42.67  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  92 PGI-LDK-----ILLAA-KIKSSDVVLEIGCGTGNLTVK---LLPIAKkVITIDIDARMVSEVKKRCLYEGYNNLEVYEG 161
Cdd:PRK07402  19 PGIpLTKrevrlLLISQlRLEPDSVLWDIGAGTGTIPVEaglLCPKGR-VIAIERDEEVVNLIRRNCDRFGVKNVEVIEG 97


                 ..
gi 156102204 162 DA 163
Cdd:PRK07402  98 SA 99
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 95-172 1.63e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.84  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  95 LDKILLAAKIKSSDVVLEIGCGTGNLtvkLLPIAK----KVITIDIDARMVSEVKKRCLYEGY-NNLEVYEGDAIKTVFP 169
Cdd:COG2230   40 LDLILRKLGLKPGMRVLDIGCGWGGL---ALYLARrygvRVTGVTLSPEQLEYARERAAEAGLaDRVEVRLADYRDLPAD 116


                 ....
gi 156102204 170 -RFD 172
Cdd:COG2230  117 gQFD 120
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 94-163 1.75e-04

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: 43.24  E-value: 1.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  94 ILDKILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDA 163
Cdd:COG2265  221 LYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDL 290
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 99-172 2.52e-04

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 41.71  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  99 LLAAKIKSSDVVLEIGCGTGNLTVK---LLPIAKKVITIDIDARMVSEVKKRCLYEGY-NNLEVYEGDA---IKTVFPRF 171
Cdd:PRK00377  33 LSKLRLRKGDMILDIGCGTGSVTVEaslLVGETGKVYAVDKDEKAINLTRRNAEKFGVlNNIVLIKGEApeiLFTINEKF 112


                 .
gi 156102204 172 D 172
Cdd:PRK00377 113 D 113
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 94-180 3.83e-04

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.07  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  94 ILDKILLAAKIKSSDVVLEIGCGTGNLTV---KLLPIAkKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDAIKTVF-P 169
Cdd:PRK09328  96 LVEWALEALLLKEPLRVLDLGTGSGAIALalaKERPDA-EVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLPgG 174

                         90
                 ....*....|.
gi 156102204 170 RFDICTANIPY 180
Cdd:PRK09328 175 RFDLIVSNPPY 185
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
97-190 6.20e-04

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 40.96  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  97 KILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAKKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDAIKTVFPR--FD-- 172
Cdd:PRK00312  69 RMTELLELKPGDRVLEIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPAYapFDri 148

                         90
                 ....*....|....*...
gi 156102204 173 ICTANIPyKISSPLIFKL 190
Cdd:PRK00312 149 LVTAAAP-EIPRALLEQL 165
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 101-175 1.76e-03

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 39.75  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204 101 AAKIKSSDVVLEIGCGTGNLTVKL---LPIAKKVITIDIDARMVSEVKKRCLYEGY-NNLEVYEGDAIKTVFP--RFDIC 174
Cdd:PRK00216  46 WLGVRPGDKVLDLACGTGDLAIALakaVGKTGEVVGLDFSEGMLAVGREKLRDLGLsGNVEFVQGDAEALPFPdnSFDAV 125


                 .
gi 156102204 175 T 175
Cdd:PRK00216 126 T 126
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
95-187 2.62e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 39.39  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  95 LDKILLAAKikssdVVLEIGCGTGNLTV---KLLpiAKKVITIDID--ARMVSE-------VKKRclyegynnLEVYEGD 162
Cdd:COG2264  142 LEKLLKPGK-----TVLDVGCGSGILAIaaaKLG--AKRVLAVDIDpvAVEAARenaelngVEDR--------IEVVLGD 206

                         90       100
                 ....*....|....*....|....*
gi 156102204 163 AIKTvfPRFDICTANIpykISSPLI 187
Cdd:COG2264  207 LLED--GPYDLVVANI---LANPLI 226
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 110-174 2.96e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 39.05  E-value: 2.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156102204 110 VLEIGCGTGNLTVkllPIAK---KVITIDIDARMVSEVKKRCLYEG-YNNLEVYEGDaIKTVFPRFD--IC 174
Cdd:PRK07580  67 ILDAGCGVGSLSI---PLARrgaKVVASDISPQMVEEARERAPEAGlAGNITFEVGD-LESLLGRFDtvVC 133
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 109-168 3.41e-03

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 38.04  E-value: 3.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156102204  109 VVLEIGCGTGNLTVKLLPI--AKKVITIDIDARMVSEVKKRCLYEGYNNLEVYEGDAIKTVF 168
Cdd:pfam02390   4 VFLEIGCGMGGFLVAMAKAnpDKNFIGIEIRVPGVAKALKKIDALGLQNLRILCGNALDVLP 65
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 98-172 7.07e-03

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: 37.83  E-value: 7.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156102204  98 ILLAAKIKSSDVVLEIGCGTGNLTVKLLPIAK---KVITIDIDARMvSEVKKRCLYEGY--NNLEVYEGDAIKTVFPR-F 171
Cdd:COG2519   83 IIARLDIFPGARVLEAGTGSGALTLALARAVGpegKVYSYERREDF-AEIARKNLERFGlpDNVELKLGDIREGIDEGdV 161


                 .
gi 156102204 172 D 172
Cdd:COG2519  162 D 162
 
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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