|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
24-312 |
6.85e-177 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 490.67 E-value: 6.85e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 24 SAGGLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPV 103
Cdd:PTZ00338 4 SKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 104 ASKLQVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLA 183
Cdd:PTZ00338 84 ASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 184 RVDHLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVHN 263
Cdd:PTZ00338 164 RVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMIN 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 7657198 264 IIIPEDFS-IADKIQQILTSTGFSDKRARSMDIDDFIRLLHGFNAEGIHF 312
Cdd:PTZ00338 244 KKVPVSLEpFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
35-305 |
1.38e-85 |
|
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: 257.54 E-value: 1.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVqgtPVASKLQVLVGDV 114
Cdd:TIGR00755 8 GQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 115 LKTDLPFFD----TCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMK 190
Cdd:TIGR00755 85 LKFDLNELAkdltKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIVFK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 191 VGKNNFRPPPKVESSVVRIEPKNPPP-PINFQEWDGLVRITFVRKNKTLSAAFKSSavqqlleknyrihcsvhniiIPED 269
Cdd:TIGR00755 165 VPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKNL--------------------LSEL 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 7657198 270 FsiadkiqQILTSTGFS-DKRARSMDIDDFIRLLHGF 305
Cdd:TIGR00755 225 V-------ELLEELGIDpDKRVEQLSPEDFLRLANLL 254
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
35-301 |
5.76e-85 |
|
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: 256.59 E-value: 5.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvASKLQVLVGDV 114
Cdd:COG0030 16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAA---YPNLTVIEGDA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 115 LKTDLP-----FFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLM 189
Cdd:COG0030 93 LKVDLPalaagEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYADVEILF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 190 KVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAvqqlleknyrihcsvhniiip 267
Cdd:COG0030 173 TVPPEAFYPPPKVDSAVVRLTPRPEPlvPVADEKLFFRVVKAAFSQRRKTLRNSLKSLF--------------------- 231
|
250 260 270
....*....|....*....|....*....|....*
gi 7657198 268 edfsIADKIQQILTSTGFS-DKRARSMDIDDFIRL 301
Cdd:COG0030 232 ----SKERLEEALEAAGIDpTARAEELSVEEFARL 262
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
44-213 |
3.56e-78 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 235.48 E-value: 3.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 44 IINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvASKLQVLVGDVLKTDLPF-- 121
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 122 FDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPK 201
Cdd:smart00650 78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
170
....*....|..
gi 7657198 202 VESSVVRIEPKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
27-255 |
1.58e-75 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 232.26 E-value: 1.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 27 GLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQgtpVASK 106
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 107 LQVLVGDVLKTDLP-------FFDTCVANLPYQISSPFVFKLL-LHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSIN 178
Cdd:pfam00398 78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7657198 179 TQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNY 255
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFS 236
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
60-160 |
2.56e-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: 48.20 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 60 VLEVGPGTGNMTVKLLE-KAKKVVACELDPRLVAELhKRVQGTPVASKLQVLVGDVLktDLPF-----FDTCVANLPYQI 133
Cdd:cd02440 2 VLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAE--ELPPeadesFDVIISDPPLHH 78
|
90 100
....*....|....*....|....*....
gi 7657198 134 SSPFVFKLL--LHRPFFRCAILMFQREFA 160
Cdd:cd02440 79 LVEDLARFLeeARRLLKPGGVLVLTLVLA 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
24-312 |
6.85e-177 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 490.67 E-value: 6.85e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 24 SAGGLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPV 103
Cdd:PTZ00338 4 SKSGMVFNKKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVAELKKRFQNSPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 104 ASKLQVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLA 183
Cdd:PTZ00338 84 ASKLEVIEGDALKTEFPYFDVCVANVPYQISSPLVFKLLAHRPLFRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQLLC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 184 RVDHLMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNYRIHCSVHN 263
Cdd:PTZ00338 164 RVTHLMKVSKNSFNPPPKVESSVVRIEPKNPPPDVDFEEWDGLLRICFSRKNKTLSAIFKTKSVLQTLEHNYKSWCTMIN 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 7657198 264 IIIPEDFS-IADKIQQILTSTGFSDKRARSMDIDDFIRLLHGFNAEGIHF 312
Cdd:PTZ00338 244 KKVPVSLEpFKEFIAEILEDSGMFEKRSVKLDIDDFLKLLLAFNKKGIHF 293
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
35-305 |
1.38e-85 |
|
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: 257.54 E-value: 1.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVqgtPVASKLQVLVGDV 114
Cdd:TIGR00755 8 GQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 115 LKTDLPFFD----TCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMK 190
Cdd:TIGR00755 85 LKFDLNELAkdltKVVGNLPYNISSPLIFKLLKEKDAFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYANVEIVFK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 191 VGKNNFRPPPKVESSVVRIEPKNPPP-PINFQEWDGLVRITFVRKNKTLSAAFKSSavqqlleknyrihcsvhniiIPED 269
Cdd:TIGR00755 165 VPPSAFYPPPKVDSAVVRLVPLKRKPsPKDFALFEELLKAAFQQRRKTLRNNLKNL--------------------LSEL 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 7657198 270 FsiadkiqQILTSTGFS-DKRARSMDIDDFIRLLHGF 305
Cdd:TIGR00755 225 V-------ELLEELGIDpDKRVEQLSPEDFLRLANLL 254
|
|
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
35-301 |
5.76e-85 |
|
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: 256.59 E-value: 5.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvASKLQVLVGDV 114
Cdd:COG0030 16 GQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAA---YPNLTVIEGDA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 115 LKTDLP-----FFDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLM 189
Cdd:COG0030 93 LKVDLPalaagEPLKVVGNLPYNISTPILFKLLEARPPIEDAVLMVQKEVAERLVAKPGSKDYGRLSVLVQYYADVEILF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 190 KVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAvqqlleknyrihcsvhniiip 267
Cdd:COG0030 173 TVPPEAFYPPPKVDSAVVRLTPRPEPlvPVADEKLFFRVVKAAFSQRRKTLRNSLKSLF--------------------- 231
|
250 260 270
....*....|....*....|....*....|....*
gi 7657198 268 edfsIADKIQQILTSTGFS-DKRARSMDIDDFIRL 301
Cdd:COG0030 232 ----SKERLEEALEAAGIDpTARAEELSVEEFARL 262
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
28-246 |
6.05e-79 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 240.57 E-value: 6.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 28 LMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRvqgTPVASKL 107
Cdd:PRK14896 1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDD---EIAAGNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 108 QVLVGDVLKTDLPFFDTCVANLPYQISSPFVFKLLLHRpfFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDH 187
Cdd:PRK14896 78 EIIEGDALKVDLPEFNKVVSNLPYQISSPITFKLLKHG--FEPAVLMYQKEFAERMVAKPGTKEYGRLSVMVQYYADVEI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 188 LMKVGKNNFRPPPKVESSVVRIEPKNPPPPINFQE-WDGLVRITFVRKNKTLSAAFKSSA 246
Cdd:PRK14896 156 VEKVPPGAFSPKPKVDSAVVRLTPREPKYEVYDEDfFDDFVKALFQHRRKTLRNALKNSA 215
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
44-213 |
3.56e-78 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 235.48 E-value: 3.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 44 IINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvASKLQVLVGDVLKTDLPF-- 121
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKlq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 122 FDTCVANLPYQISSPFVFKLLLHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSINTQLLARVDHLMKVGKNNFRPPPK 201
Cdd:smart00650 78 PYKVVGNLPYNISTPILFKLLEEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSAFRPPPK 157
|
170
....*....|..
gi 7657198 202 VESSVVRIEPKN 213
Cdd:smart00650 158 VDSAVVRLERRP 169
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
27-255 |
1.58e-75 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 232.26 E-value: 1.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 27 GLMFNTGIGQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQgtpVASK 106
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLS---LDEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 107 LQVLVGDVLKTDLP-------FFDTCVANLPYQISSPFVFKLL-LHRPFFRCAILMFQREFALRLVAKPGDKLYCRLSIN 178
Cdd:pfam00398 78 LTVIHQDFLKFEFPslvthihQEFLVVGNLPYNISTPIVKQLLfESRFGIVDMLLMLQKEFARRLLARPGSKLYSRLSVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7657198 179 TQLLARVDHLMKVGKNNFRPPPKVESSVVRIEPKNPP--PPINFQEWDGLVRITFVRKNKTLSAAFKSSAVQQLLEKNY 255
Cdd:pfam00398 158 RQAFTDVKLVAKVPPSIFSPPPKVDSALVRLERHDPDphPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQLQAFS 236
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
48-129 |
1.72e-11 |
|
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: 61.16 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVasKLQVLVGDVlkTDLPF----FD 123
Cdd:COG2226 14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDA--EDLPFpdgsFD 89
|
....*.
gi 7657198 124 TCVANL 129
Cdd:COG2226 90 LVISSF 95
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
60-145 |
1.87e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 51.03 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 60 VLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPVasKLQVLVGDVlkTDLPF----FDTCVANLPYQIS 134
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL--NVEFVQGDA--EDLPFpdgsFDLVVSSGVLHHL 76
|
90
....*....|.
gi 7657198 135 SPFVFKLLLHR 145
Cdd:pfam13649 77 PDPDLEAALRE 87
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
60-160 |
2.56e-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: 48.20 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 60 VLEVGPGTGNMTVKLLE-KAKKVVACELDPRLVAELhKRVQGTPVASKLQVLVGDVLktDLPF-----FDTCVANLPYQI 133
Cdd:cd02440 2 VLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAE--ELPPeadesFDVIISDPPLHH 78
|
90 100
....*....|....*....|....*....
gi 7657198 134 SSPFVFKLL--LHRPFFRCAILMFQREFA 160
Cdd:cd02440 79 LVEDLARFLeeARRLLKPGGVLVLTLVLA 107
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
45-128 |
2.72e-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: 48.86 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 45 INSIIDKAALRPTDVvLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVasklQVLVGDVlkTDLPF--- 121
Cdd:COG2227 14 LAALLARLLPAGGRV-LDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV----DFVQGDL--EDLPLedg 86
|
....*...
gi 7657198 122 -FDTCVAN 128
Cdd:COG2227 87 sFDLVICS 94
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-129 |
3.09e-06 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 44.96 E-value: 3.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657198 61 LEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGtpvaSKLQVLVGDVlkTDLPF----FDTCVANL 129
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPR----EGLTFVVGDA--EDLPFpdnsFDLVLSSE 67
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
35-93 |
4.48e-06 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 46.62 E-value: 4.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 7657198 35 GQHILKnPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAE 93
Cdd:COG2518 46 GQTISQ-PYIVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAER 103
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
51-127 |
6.40e-06 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 46.57 E-value: 6.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7657198 51 KAALRPTDVVLEVGPGTGNMTVKLLEK-AKKVVACELDPRLVAELHKRVQGTPVASKLQVLVGDVLKTDLPF-FDTCVA 127
Cdd:COG4076 30 ERVVKPGDVVLDIGTGSGLLSMLAARAgAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEkADVIIS 108
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
46-131 |
9.38e-06 |
|
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: 45.23 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 46 NSIIDKAALR--PTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVasKLQVLVGDVLKTDLPFFD 123
Cdd:TIGR00537 7 DSLLLEANLRelKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNV--GLDVVMTDLFKGVRGKFD 84
|
....*...
gi 7657198 124 TCVANLPY 131
Cdd:TIGR00537 85 VILFNPPY 92
|
|
| COG3963 |
COG3963 |
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism]; |
39-97 |
1.10e-05 |
|
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
Pssm-ID: 443163 Cd Length: 193 Bit Score: 45.20 E-value: 1.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657198 39 LKNPLIINSII-----------DKAALRPTDVVLEVGPGTGNMTVKLLE---KAKKVVACELDPRLVAELHKR 97
Cdd:COG3963 17 LRNPRTVGAIApssralaramaSEVDWSGAGPVVELGPGTGVFTRAILArgvPDARLLAVEINPEFAEHLRRR 89
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
48-131 |
1.37e-05 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 44.89 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLV--AELHKRVQGTPvASKLQVLVGDVLKtdlPF---- 121
Cdd:PRK14968 15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVecAKCNAKLNNIR-NNGVEVIRSDLFE---PFrgdk 90
|
90
....*....|
gi 7657198 122 FDTCVANLPY 131
Cdd:PRK14968 91 FDVILFNPPY 100
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
48-127 |
1.87e-05 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 44.15 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 48 IIDKAALRPTDVVLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPVASKLQVLVGDVLKTDLP-FFDTC 125
Cdd:COG2230 43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADgQFDAI 122
|
..
gi 7657198 126 VA 127
Cdd:COG2230 123 VS 124
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
35-123 |
4.39e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 43.75 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 35 GQHILKNPLIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAK-KVVACELDPRLVAELHKRVQGTPvASKLQVLVGD 113
Cdd:COG0500 5 YYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGgRVIGIDLSPEAIALARARAAKAG-LGNVEFLVAD 83
|
90
....*....|...
gi 7657198 114 VLKTD---LPFFD 123
Cdd:COG0500 84 LAELDplpAESFD 96
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
52-131 |
1.14e-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: 42.82 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 52 AALRPTDVVLEVGPGTGNMTVKLLEK--AKKVVACELDPRLVAELHKRVQGTPVASKLQVLVGDVLKTDLPF----FDTC 125
Cdd:COG4123 33 APVKKGGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELppgsFDLV 112
|
....*.
gi 7657198 126 VANLPY 131
Cdd:COG4123 113 VSNPPY 118
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
60-127 |
2.22e-04 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 41.75 E-value: 2.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7657198 60 VLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRVQGTPVASKLQVLVGDvLKTDLPFFDTCVA 127
Cdd:PRK07580 67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD-LESLLGRFDTVVC 133
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
56-128 |
2.29e-04 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 39.81 E-value: 2.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7657198 56 PTDVVLEVGPGTGNMTVKLLEKAK--KVVACELDPRLVAELHKRVQGtpvaskLQVLVGDVLKTDLPF-FDTCVAN 128
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARARARLPN------VRFVVADLRDLDPPEpFDLVVSN 70
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
61-128 |
2.17e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 36.96 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657198 61 LEVGPGTGNMTVKLLEKAK--KVVACELDPRLV--AELHKRVQGTPVASKLQVLVGDVLKTDLPFFDTCVAN 128
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPglEYTGLDISPAALeaARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS 72
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
43-123 |
4.27e-03 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 37.67 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657198 43 LIINSIIDKAALRPTDVVLEVGPGTGNMTVKLLEKAKKVVACELDPRLVAELHKRvqgtpvASKLQVLVGDVlkTDLPFF 122
Cdd:COG4976 33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK------GVYDRLLVADL--ADLAEP 104
|
.
gi 7657198 123 D 123
Cdd:COG4976 105 D 105
|
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