|
Name |
Accession |
Description |
Interval |
E-value |
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
5-270 |
4.82e-101 |
|
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: 296.27 E-value: 4.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 5 GHRARKRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRFGVDPRFQ 84
Cdd:COG0030 8 GLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLER-AARVTAVEIDRRLAAILRETFAAYPNLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 85 LLEGDVLALPLLPPAGPAPEKVVANIPYNITGPLLERLVGRLDrplerPYRALVLLVQQEVGERIRARPGSSAYSALSVR 164
Cdd:COG0030 87 VIEGDALKVDLPALAAGEPLKVVGNLPYNISTPILFKLLEARP-----PIEDAVLMVQKEVAERLVAKPGSKDYGRLSVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 165 MQLLARCSTVCPVPPRCFSPPPKVNSELIRLDPLsPEQRLEPALARRTDALLRRCFAARRKMLRNTLAGLLPEVELQQAA 244
Cdd:COG0030 162 VQYYADVEILFTVPPEAFYPPPKVDSAVVRLTPR-PEPLVPVADEKLFFRVVKAAFSQRRKTLRNSLKSLFSKERLEEAL 240
|
250 260
....*....|....*....|....*.
gi 1673828943 245 EAAGITLNQRPQELAPERWLALAAVL 270
Cdd:COG0030 241 EAAGIDPTARAEELSVEEFARLANAL 266
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
6-267 |
1.43e-79 |
|
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: 241.37 E-value: 1.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 6 HRARKRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRFGVDPRFQL 85
Cdd:TIGR00755 1 FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKR-AKKVTAIEIDPRLAERLRKLLSLYNNLEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 86 LEGDVLALPLLPPAGPAPeKVVANIPYNITGPLLERLVGRLDrplerPYRALVLLVQQEVGERIRARPGSSAYSALSVRM 165
Cdd:TIGR00755 80 IEGDALKFDLNELAKDLT-KVVGNLPYNISSPLIFKLLKEKD-----AFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 166 QLLARCSTVCPVPPRCFSPPPKVNSELIRLDPLspEQRLEPALARRTDALLRRCFAARRKMLRNTLAGLLPEVElqQAAE 245
Cdd:TIGR00755 154 QYYANVEIVFKVPPSAFYPPPKVDSAVVRLVPL--KRKPSPKDFALFEELLKAAFQQRRKTLRNNLKNLLSELV--ELLE 229
|
250 260
....*....|....*....|..
gi 1673828943 246 AAGITLNQRPQELAPERWLALA 267
Cdd:TIGR00755 230 ELGIDPDKRVEQLSPEDFLRLA 251
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
6-270 |
1.64e-64 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 202.82 E-value: 1.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 6 HRARKRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRFGVDPRFQL 85
Cdd:PRK14896 1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELDPRLAEFLRDDEIAAGNVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 86 LEGDVLALPLLPPagpapEKVVANIPYNITGPLLERLvgrldrpLERPYRALVLLVQQEVGERIRARPGSSAYSALSVRM 165
Cdd:PRK14896 80 IEGDALKVDLPEF-----NKVVSNLPYQISSPITFKL-------LKHGFEPAVLMYQKEFAERMVAKPGTKEYGRLSVMV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 166 QLLARCSTVCPVPPRCFSPPPKVNSELIRLDPLSPEqrLEPALARRTDALLRRCFAARRKMLRNTLAGL-----LPEVEL 240
Cdd:PRK14896 148 QYYADVEIVEKVPPGAFSPKPKVDSAVVRLTPREPK--YEVYDEDFFDDFVKALFQHRRKTLRNALKNSahisgKEDIKA 225
|
250 260 270
....*....|....*....|....*....|
gi 1673828943 241 QQAAEAAGItLNQRPQELAPERWLALAAVL 270
Cdd:PRK14896 226 VVEALPEEL-LNKRVFQLSPEEIAELANLL 254
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
22-197 |
1.17e-52 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 169.61 E-value: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 22 VLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRFGVDPRFQLLEGDVLALPLLPPAGP 101
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLER-AKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 102 apeKVVANIPYNITGPLLERLVgrldrPLERPYRALVLLVQQEVGERIRARPGSSAYSALSVRMQLLARCSTVCPVPPRC 181
Cdd:smart00650 80 ---KVVGNLPYNISTPILFKLL-----EEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSA 151
|
170
....*....|....*.
gi 1673828943 182 FSPPPKVNSELIRLDP 197
Cdd:smart00650 152 FRPPPKVDSAVVRLER 167
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
5-267 |
4.28e-52 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 171.39 E-value: 4.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 5 GHRARKRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLlASPAASVLAIELDRDLVAGLRQRFGVDPRFQ 84
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVIL-AKRAKQVVAIEIDPRLAKLLQKKLSLDENLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 85 LLEGDVLALPLLPPAGPAPE--KVVANIPYNITGPLLERLvgrLDRPLErPYRALVLLVQQEVGERIRARPGSSAYSALS 162
Cdd:pfam00398 80 VIHQDFLKFEFPSLVTHIHQefLVVGNLPYNISTPIVKQL---LFESRF-GIVDMLLMLQKEFARRLLARPGSKLYSRLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 163 VRMQLLARCSTVCPVPPRCFSPPPKVNSELIRLDPlSPEQRLEPALARRTDALLRRCFAARRKMLRNTLAGLLPEVELqQ 242
Cdd:pfam00398 156 VLRQAFTDVKLVAKVPPSIFSPPPKVDSALVRLER-HDPDPHPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQL-Q 233
|
250 260
....*....|....*....|....*
gi 1673828943 243 AAEAAGITLNQRPQELAPERWLALA 267
Cdd:pfam00398 234 AFSSHGINDNALVKKLSPEQTLDIF 258
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
38-130 |
1.42e-03 |
|
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: 37.41 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 38 LLEVGPGRGALTERLLASPAASVLAIELDRDLVAGLRQRF--GVDPRFQLLEGDVlaLPLLPPAGPAPEKVVANIPYNIT 115
Cdd:cd02440 2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAaaLLADNVEVLKGDA--EELPPEADESFDVIISDPPLHHL 79
|
90
....*....|....*
gi 1673828943 116 GPLLERLVGRLDRPL 130
Cdd:cd02440 80 VEDLARFLEEARRLL 94
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsmA |
COG0030 |
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ... |
5-270 |
4.82e-101 |
|
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: 296.27 E-value: 4.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 5 GHRARKRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRFGVDPRFQ 84
Cdd:COG0030 8 GLRPKKRLGQNFLIDPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLER-AARVTAVEIDRRLAAILRETFAAYPNLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 85 LLEGDVLALPLLPPAGPAPEKVVANIPYNITGPLLERLVGRLDrplerPYRALVLLVQQEVGERIRARPGSSAYSALSVR 164
Cdd:COG0030 87 VIEGDALKVDLPALAAGEPLKVVGNLPYNISTPILFKLLEARP-----PIEDAVLMVQKEVAERLVAKPGSKDYGRLSVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 165 MQLLARCSTVCPVPPRCFSPPPKVNSELIRLDPLsPEQRLEPALARRTDALLRRCFAARRKMLRNTLAGLLPEVELQQAA 244
Cdd:COG0030 162 VQYYADVEILFTVPPEAFYPPPKVDSAVVRLTPR-PEPLVPVADEKLFFRVVKAAFSQRRKTLRNSLKSLFSKERLEEAL 240
|
250 260
....*....|....*....|....*.
gi 1673828943 245 EAAGITLNQRPQELAPERWLALAAVL 270
Cdd:COG0030 241 EAAGIDPTARAEELSVEEFARLANAL 266
|
|
| ksgA |
TIGR00755 |
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ... |
6-267 |
1.43e-79 |
|
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: 241.37 E-value: 1.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 6 HRARKRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRFGVDPRFQL 85
Cdd:TIGR00755 1 FRPRKSLGQNFLVDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKR-AKKVTAIEIDPRLAERLRKLLSLYNNLEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 86 LEGDVLALPLLPPAGPAPeKVVANIPYNITGPLLERLVGRLDrplerPYRALVLLVQQEVGERIRARPGSSAYSALSVRM 165
Cdd:TIGR00755 80 IEGDALKFDLNELAKDLT-KVVGNLPYNISSPLIFKLLKEKD-----AFKLAVLMVQKEVAERLVAKPGSKDYGRLSVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 166 QLLARCSTVCPVPPRCFSPPPKVNSELIRLDPLspEQRLEPALARRTDALLRRCFAARRKMLRNTLAGLLPEVElqQAAE 245
Cdd:TIGR00755 154 QYYANVEIVFKVPPSAFYPPPKVDSAVVRLVPL--KRKPSPKDFALFEELLKAAFQQRRKTLRNNLKNLLSELV--ELLE 229
|
250 260
....*....|....*....|..
gi 1673828943 246 AAGITLNQRPQELAPERWLALA 267
Cdd:TIGR00755 230 ELGIDPDKRVEQLSPEDFLRLA 251
|
|
| ksgA |
PRK14896 |
16S ribosomal RNA methyltransferase A; |
6-270 |
1.64e-64 |
|
16S ribosomal RNA methyltransferase A;
Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 202.82 E-value: 1.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 6 HRARKRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRFGVDPRFQL 85
Cdd:PRK14896 1 IRMNKKLGQHFLIDDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELDPRLAEFLRDDEIAAGNVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 86 LEGDVLALPLLPPagpapEKVVANIPYNITGPLLERLvgrldrpLERPYRALVLLVQQEVGERIRARPGSSAYSALSVRM 165
Cdd:PRK14896 80 IEGDALKVDLPEF-----NKVVSNLPYQISSPITFKL-------LKHGFEPAVLMYQKEFAERMVAKPGTKEYGRLSVMV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 166 QLLARCSTVCPVPPRCFSPPPKVNSELIRLDPLSPEqrLEPALARRTDALLRRCFAARRKMLRNTLAGL-----LPEVEL 240
Cdd:PRK14896 148 QYYADVEIVEKVPPGAFSPKPKVDSAVVRLTPREPK--YEVYDEDFFDDFVKALFQHRRKTLRNALKNSahisgKEDIKA 225
|
250 260 270
....*....|....*....|....*....|
gi 1673828943 241 QQAAEAAGItLNQRPQELAPERWLALAAVL 270
Cdd:PRK14896 226 VVEALPEEL-LNKRVFQLSPEEIAELANLL 254
|
|
| PTZ00338 |
PTZ00338 |
dimethyladenosine transferase-like protein; Provisional |
10-228 |
2.76e-53 |
|
dimethyladenosine transferase-like protein; Provisional
Pssm-ID: 240367 [Multi-domain] Cd Length: 294 Bit Score: 175.19 E-value: 2.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 10 KRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRF---GVDPRFQLL 86
Cdd:PTZ00338 12 KKFGQHILKNPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQL-AKKVIAIEIDPRMVAELKKRFqnsPLASKLEVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 87 EGDVLALPLLPPagpapEKVVANIPYNITGPLLERLVGRldRPLerpYRALVLLVQQEVGERIRARPGSSAYSALSVRMQ 166
Cdd:PTZ00338 91 EGDALKTEFPYF-----DVCVANVPYQISSPLVFKLLAH--RPL---FRCAVLMFQKEFALRLLAQPGDELYCRLSVNTQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1673828943 167 LLARCSTVCPVPPRCFSPPPKVNSELIRLDPLSPeqrLEPALARRTDALLRRCFAARRKMLR 228
Cdd:PTZ00338 161 LLCRVTHLMKVSKNSFNPPPKVESSVVRIEPKNP---PPDVDFEEWDGLLRICFSRKNKTLS 219
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
22-197 |
1.17e-52 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 169.61 E-value: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 22 VLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASpAASVLAIELDRDLVAGLRQRFGVDPRFQLLEGDVLALPLLPPAGP 101
Cdd:smart00650 1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLER-AKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQPY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 102 apeKVVANIPYNITGPLLERLVgrldrPLERPYRALVLLVQQEVGERIRARPGSSAYSALSVRMQLLARCSTVCPVPPRC 181
Cdd:smart00650 80 ---KVVGNLPYNISTPILFKLL-----EEPPAFRDAVLMVQKEVARRLAAKPGSKDYGRLSVLLQPYADVKILFKVPPSA 151
|
170
....*....|....*.
gi 1673828943 182 FSPPPKVNSELIRLDP 197
Cdd:smart00650 152 FRPPPKVDSAVVRLER 167
|
|
| RrnaAD |
pfam00398 |
Ribosomal RNA adenine dimethylase; |
5-267 |
4.28e-52 |
|
Ribosomal RNA adenine dimethylase;
Pssm-ID: 395321 [Multi-domain] Cd Length: 263 Bit Score: 171.39 E-value: 4.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 5 GHRARKRFGQHWLTDAAVLDRIVAAAAIEPGEHLLEVGPGRGALTERLlASPAASVLAIELDRDLVAGLRQRFGVDPRFQ 84
Cdd:pfam00398 1 GNKFRTSYGQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVIL-AKRAKQVVAIEIDPRLAKLLQKKLSLDENLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 85 LLEGDVLALPLLPPAGPAPE--KVVANIPYNITGPLLERLvgrLDRPLErPYRALVLLVQQEVGERIRARPGSSAYSALS 162
Cdd:pfam00398 80 VIHQDFLKFEFPSLVTHIHQefLVVGNLPYNISTPIVKQL---LFESRF-GIVDMLLMLQKEFARRLLARPGSKLYSRLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 163 VRMQLLARCSTVCPVPPRCFSPPPKVNSELIRLDPlSPEQRLEPALARRTDALLRRCFAARRKMLRNTLAGLLPEVELqQ 242
Cdd:pfam00398 156 VLRQAFTDVKLVAKVPPSIFSPPPKVDSALVRLER-HDPDPHPVKDLDVYDSVVRKLFNRKRKTLSTSLKSLFPGGQL-Q 233
|
250 260
....*....|....*....|....*
gi 1673828943 243 AAEAAGITLNQRPQELAPERWLALA 267
Cdd:pfam00398 234 AFSSHGINDNALVKKLSPEQTLDIF 258
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
21-89 |
2.58e-07 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 49.16 E-value: 2.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1673828943 21 AVLDRIVAAAAIEPGEHLLEVGPGRGALTERLLASPAASVLAIELDRDLVAGLRQRF---GVDPRFQLLEGD 89
Cdd:COG2230 38 AKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAaeaGLADRVEVRLAD 109
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
24-90 |
2.20e-05 |
|
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: 43.44 E-value: 2.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1673828943 24 DRIVAAAAIEPGEHLLEVGPGRGALTeRLLASPAASVLAIELDRDLVAGLRQRFG-VDPRFQLLEGDV 90
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLA-LALAERGARVTGVDISPEMLELARERAAeAGLNVEFVVGDA 78
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
39-90 |
1.29e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 37.16 E-value: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1673828943 39 LEVGPGRGALTERLLASPAASVLAIELDRDLVAGLRQRFGVD-PRFQLLEGDV 90
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAgLNVEFVQGDA 54
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
38-130 |
1.42e-03 |
|
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: 37.41 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 38 LLEVGPGRGALTERLLASPAASVLAIELDRDLVAGLRQRF--GVDPRFQLLEGDVlaLPLLPPAGPAPEKVVANIPYNIT 115
Cdd:cd02440 2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAaaLLADNVEVLKGDA--EELPPEADESFDVIISDPPLHHL 79
|
90
....*....|....*
gi 1673828943 116 GPLLERLVGRLDRPL 130
Cdd:cd02440 80 VEDLARFLEEARRLL 94
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
6-90 |
2.21e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 38.48 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 6 HRARKRFGQHW----LTDAAVLDRIVAA--AAIEPGEHLLEVGPGRGALTerLLASP--AASVLAIELDRDLVAGLRQ-- 75
Cdd:COG4076 1 DYLMQFFVPRWhhpmLNDVERNDAFKAAieRVVKPGDVVLDIGTGSGLLS--MLAARagAKKVYAVEVNPDIAAVARRii 78
|
90
....*....|....*.
gi 1673828943 76 -RFGVDPRFQLLEGDV 90
Cdd:COG4076 79 aANGLSDRITVINADA 94
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
26-90 |
5.82e-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: 37.45 E-value: 5.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828943 26 IVAAAAIEPGEHLLEVGPGRGALTERLLAS--PAASVLAIELDRDLVAGLRQ---RFGVDPRFQLLEGDV 90
Cdd:COG2519 83 IIARLDIFPGARVLEAGTGSGALTLALARAvgPEGKVYSYERREDFAEIARKnleRFGLPDNVELKLGDI 152
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
25-77 |
9.32e-03 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 36.60 E-value: 9.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1673828943 25 RIVAAAAIEPGEHLLEVGPGRG---ALTERLlaspAASVLAIELDRDLVAGLRQRF 77
Cdd:COG2518 57 RMLEALDLKPGDRVLEIGTGSGyqaAVLARL----AGRVYSVERDPELAERARERL 108
|
|
|