|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
1-397 |
0e+00 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 586.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 1 MTPSIHLAKARDKSLRRKHPWVFSRGIDKVEGEPQQGETVDVYAQNGQWLAKAAYSPASQIRARVWTFEKEE-INKAFFI 79
Cdd:PRK15128 1 MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDEsIDIAFFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 80 KRFKDAQSLREDIIERDGLTGYRLTAAESDGLPGITIDKYQDFLVCQLLSAGAEFNKSIIVEALVECFPDCNIYERSDVA 159
Cdd:PRK15128 81 RRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 160 VRKKEGLEQTVGVLHGEEPPKSVIIEENGVKISVNIMEGHKTGFYMDQRDSRKESMKYVKGKDVLNCFSYTGGFGLYALK 239
Cdd:PRK15128 161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 240 GDAKRVINADVSQLALDTAKFNAELNEFDISKkrAVFLNADVFKLLREYRDQGTKFDVVIMDPPKFVSSKNNLTSGANGY 319
Cdd:PRK15128 241 GGCSQVVSVDTSQEALDIARQNVELNKLDLSK--AEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGY 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1633070433 320 KDVNMLAMQILKPGGTLLTYSCSGLMGADLFQKIIADAALDAGRTVKFVERFEQAADHLIDTAYPEGFYLKGFACKVL 397
Cdd:PRK15128 319 KDINMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
4-397 |
0e+00 |
|
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440709 [Multi-domain] Cd Length: 392 Bit Score: 532.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 4 SIHLAKARDKSLRRKHPWVFSRGIDKVEGEPQQGETVDVYAQNGQWLAKAAYSPASQIRARVWTFEKEE-INKAFFIKRF 82
Cdd:COG1092 1 KVRLKPGKERRLRRGHPWVFSNEIDRVEGELEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEpIDAAFFANRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 83 KDAQSLREDIIERDGLTGYRLTAAESDGLPGITIDKYQDFLVCQLLSAGAEFNKSIIVEALVECFPDCNIYERSDVAVRK 162
Cdd:COG1092 81 RKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEALVEVLGPEGIYLRSDVRVRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 163 KEGLEQTVGVLHGEEPPkSVIIEENGVKISVNIMEGHKTGFYMDQRDSRKESMKYVKGKDVLNCFSYTGGFGLYALKGDA 242
Cdd:COG1092 161 LEGLPQYEGVLYGEAPE-EVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSVHAAAGGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 243 KRVINADVSQLALDTAKFNAELNEFDiskKRAVFLNADVFKLLREYRDQGTKFDVVIMDPPKFVSSKNNLTSGANGYKDV 322
Cdd:COG1092 240 KSVTSVDLSATALEWAKENAALNGLD---DRHEFVQADAFDWLRELAREGERFDLIILDPPAFAKSKKDLFDAQRDYKDL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1633070433 323 NMLAMQILKPGGTLLTYSCSGLMGADLFQKIIADAALDAGRTVKFVERFEQAADHLIDTAYPEGFYLKGFACKVL 397
Cdd:COG1092 317 NRLALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLRVL 391
|
|
| RlmI_M_like |
cd11572 |
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ... |
76-175 |
2.91e-40 |
|
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or central domain is typically found between an N-terminal PUA domain and a C-terminal SAM-dependent methyltransferase domain, such as in the Escherichia coli ribosomal RNA large subunit methyltransferase RlmI (YccW). It may be involved in binding to the RNA substrate.
Pssm-ID: 211413 [Multi-domain] Cd Length: 99 Bit Score: 138.36 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 76 AFFIKRFKDAQSLREDIIeRDGLTGYRLTAAESDGLPGITIDKYQDFLVCQLLSAGAEFNKSIIVEALVECFPDCNIYER 155
Cdd:cd11572 1 AFFKRRIEKALALRKRLL-LDDTNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKELLGPKGIYER 79
|
90 100
....*....|....*....|
gi 1633070433 156 SDVAVRKKEGLEQTVGVLHG 175
Cdd:cd11572 80 SDAAVRELEGLPEEVGVLYG 99
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
172-372 |
3.77e-26 |
|
S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.
Pssm-ID: 287624 [Multi-domain] Cd Length: 286 Bit Score: 106.50 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 172 VLHGEePPKSVIIEENGVKISVNIMEGHKTGFYMDQRDSRKESMKYVKGKDVLNCFSYTGGFGLYALKGDAKRVINADVS 251
Cdd:pfam10672 77 VLSGE-LLETPVVVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 252 QLALDTAKFNAELNEFDIskKRAVFLNADVFKLLREYRDQGtKFDVVIMDPPKFVSSKNNLTsgaNGYKDVNMLAMQILK 331
Cdd:pfam10672 156 RGSLNKGRDNHRLNGHDL--GRVSFLGHDIFKSWGKIKKLG-PYDLVIIDPPSFQKGSFALT---KDYKKILRRLPELLV 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1633070433 332 PGGTLLTYSCSGLMGADLFQKIIADAAldagRTVKFVERFE 372
Cdd:pfam10672 230 EGGTVLACVNSPAVGPDFLIEEMAEEA----PSLHFVERLD 266
|
|
| PUA |
smart00359 |
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
21-67 |
3.91e-07 |
|
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 47.25 E-value: 3.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1633070433 21 WVFSRGIDKVEGEPQQGETVDVYAQNGQWLAKAAYSPASQIRARVWT 67
Cdd:smart00359 18 SLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKG 64
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
218-371 |
8.05e-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: 46.00 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 218 VKGKDVLNCFSYTGgFGLYALKGDAKRVINADVSQLALDTAKFNAELNEFDISkkravFLNADVFKLLREyrdqgtKFDV 297
Cdd:TIGR00537 18 LKPDDVLEIGAGTG-LVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLD-----VVMTDLFKGVRG------KFDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 298 VIMDPPkFVSSKNNLTSGA------NGYKDVNMLAMQ-------ILKPGGTLLTYSCSGLMGADLFQKIIA---DAALDA 361
Cdd:TIGR00537 86 ILFNPP-YLPLEDDLRRGDwldvaiDGGKDGRKVIDRfldelpeILKEGGRVQLIQSSLNGEPDTFDKLDErgfRYEIVA 164
|
170
....*....|
gi 1633070433 362 GRTVKFVERF 371
Cdd:TIGR00537 165 ERGLFFEELF 174
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
1-397 |
0e+00 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 586.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 1 MTPSIHLAKARDKSLRRKHPWVFSRGIDKVEGEPQQGETVDVYAQNGQWLAKAAYSPASQIRARVWTFEKEE-INKAFFI 79
Cdd:PRK15128 1 MTVRLVLAKGREKSLLRRHPWVFSGAVARMEGKASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDEsIDIAFFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 80 KRFKDAQSLREDIIERDGLTGYRLTAAESDGLPGITIDKYQDFLVCQLLSAGAEFNKSIIVEALVECFPDCNIYERSDVA 159
Cdd:PRK15128 81 RRLQQAQKWRDWLAQKDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPECAIYDRSDVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 160 VRKKEGLEQTVGVLHGEEPPKSVIIEENGVKISVNIMEGHKTGFYMDQRDSRKESMKYVKGKDVLNCFSYTGGFGLYALK 239
Cdd:PRK15128 161 VRKKEGMELTQGPVTGELPPALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 240 GDAKRVINADVSQLALDTAKFNAELNEFDISKkrAVFLNADVFKLLREYRDQGTKFDVVIMDPPKFVSSKNNLTSGANGY 319
Cdd:PRK15128 241 GGCSQVVSVDTSQEALDIARQNVELNKLDLSK--AEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGY 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1633070433 320 KDVNMLAMQILKPGGTLLTYSCSGLMGADLFQKIIADAALDAGRTVKFVERFEQAADHLIDTAYPEGFYLKGFACKVL 397
Cdd:PRK15128 319 KDINMLAIQLLNPGGILLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLKGFACRVM 396
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
4-397 |
0e+00 |
|
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440709 [Multi-domain] Cd Length: 392 Bit Score: 532.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 4 SIHLAKARDKSLRRKHPWVFSRGIDKVEGEPQQGETVDVYAQNGQWLAKAAYSPASQIRARVWTFEKEE-INKAFFIKRF 82
Cdd:COG1092 1 KVRLKPGKERRLRRGHPWVFSNEIDRVEGELEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEpIDAAFFANRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 83 KDAQSLREDIIERDGLTGYRLTAAESDGLPGITIDKYQDFLVCQLLSAGAEFNKSIIVEALVECFPDCNIYERSDVAVRK 162
Cdd:COG1092 81 RKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEALVEVLGPEGIYLRSDVRVRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 163 KEGLEQTVGVLHGEEPPkSVIIEENGVKISVNIMEGHKTGFYMDQRDSRKESMKYVKGKDVLNCFSYTGGFGLYALKGDA 242
Cdd:COG1092 161 LEGLPQYEGVLYGEAPE-EVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSVHAAAGGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 243 KRVINADVSQLALDTAKFNAELNEFDiskKRAVFLNADVFKLLREYRDQGTKFDVVIMDPPKFVSSKNNLTSGANGYKDV 322
Cdd:COG1092 240 KSVTSVDLSATALEWAKENAALNGLD---DRHEFVQADAFDWLRELAREGERFDLIILDPPAFAKSKKDLFDAQRDYKDL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1633070433 323 NMLAMQILKPGGTLLTYSCSGLMGADLFQKIIADAALDAGRTVKFVERFEQAADHLIDTAYPEGFYLKGFACKVL 397
Cdd:COG1092 317 NRLALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLRVL 391
|
|
| RlmI_M_like |
cd11572 |
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ... |
76-175 |
2.91e-40 |
|
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or central domain is typically found between an N-terminal PUA domain and a C-terminal SAM-dependent methyltransferase domain, such as in the Escherichia coli ribosomal RNA large subunit methyltransferase RlmI (YccW). It may be involved in binding to the RNA substrate.
Pssm-ID: 211413 [Multi-domain] Cd Length: 99 Bit Score: 138.36 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 76 AFFIKRFKDAQSLREDIIeRDGLTGYRLTAAESDGLPGITIDKYQDFLVCQLLSAGAEFNKSIIVEALVECFPDCNIYER 155
Cdd:cd11572 1 AFFKRRIEKALALRKRLL-LDDTNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKELLGPKGIYER 79
|
90 100
....*....|....*....|
gi 1633070433 156 SDVAVRKKEGLEQTVGVLHG 175
Cdd:cd11572 80 SDAAVRELEGLPEEVGVLYG 99
|
|
| PUA_RlmI |
cd21153 |
PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related proteins; The ... |
3-72 |
1.05e-27 |
|
PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this subfamily contain PUA domains that co-occur N-terminal to SAM-dependent methyltransferase domains and include Escherichia coli RlmI (rRNA large subunit methyltransferase gene I, also called YccW) and Thermus thermophilus methyltransferase RlmO, which are 5-methylcytosine methyltransferases (m5C MTases) that play a role in modifying 23S rRNA. This subfamily also includes Pyrococcus horikoshii PH1915 that may play a role as a 5-methyluridine MTase, and/or perform similar roles.
Pssm-ID: 409295 [Multi-domain] Cd Length: 70 Bit Score: 104.20 E-value: 1.05e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 3 PSIHLAKARDKSLRRKHPWVFSRGIDKVEGEPQQGETVDVYAQNGQWLAKAAYSPASQIRARVWTFEKEE 72
Cdd:cd21153 1 PRIVLKKGKEKSLRRGHPWIFSGAIDRIEGKPEPGDLVDVYDHKGKFLGTGLYNPHSQIRVRVLSFDKEE 70
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
172-372 |
3.77e-26 |
|
S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.
Pssm-ID: 287624 [Multi-domain] Cd Length: 286 Bit Score: 106.50 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 172 VLHGEePPKSVIIEENGVKISVNIMEGHKTGFYMDQRDSRKESMKYVKGKDVLNCFSYTGGFGLYALKGDAKRVINADVS 251
Cdd:pfam10672 77 VLSGE-LLETPVVVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 252 QLALDTAKFNAELNEFDIskKRAVFLNADVFKLLREYRDQGtKFDVVIMDPPKFVSSKNNLTsgaNGYKDVNMLAMQILK 331
Cdd:pfam10672 156 RGSLNKGRDNHRLNGHDL--GRVSFLGHDIFKSWGKIKKLG-PYDLVIIDPPSFQKGSFALT---KDYKKILRRLPELLV 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1633070433 332 PGGTLLTYSCSGLMGADLFQKIIADAAldagRTVKFVERFE 372
Cdd:pfam10672 230 EGGTVLACVNSPAVGPDFLIEEMAEEA----PSLHFVERLD 266
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
94-336 |
7.25e-24 |
|
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;
Pssm-ID: 236981 [Multi-domain] Cd Length: 702 Bit Score: 103.73 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 94 ERDGLTGYRLTAAEsdgLP--GITIDKYQDFLVCQllsagaEFN--KSI-----------IVEALVECFpdcNIyERSDV 158
Cdd:PRK11783 411 KQEGIECYRLYDAD---LPeyNVAVDRYGDWVVVQ------EYAapKTIdeekarqrlfdALAATPEVL---GI-PPNKV 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 159 A--VRKK-------EGLEQTvgvlhGEEppksVIIEENGVKISVNIMEGHKTGFYMDQRDSRKESMKYVKGKDVLNCFSY 229
Cdd:PRK11783 478 VlkTRERqkgknqyQKLAEK-----GEF----LEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAY 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 230 TGGFGLYALKGDAKRVINADVSQLALDTAKFNAELNEFDISKKRavFLNADVFKLLREYRDQgtkFDVVIMDPPKFVSSK 309
Cdd:PRK11783 549 TGTASVHAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQHR--LIQADCLAWLKEAREQ---FDLIFIDPPTFSNSK 623
|
250 260 270
....*....|....*....|....*....|....
gi 1633070433 310 NnltsgANGYKDVN------M-LAMQILKPGGTL 336
Cdd:PRK11783 624 R-----MEDSFDVQrdhvalIkDAKRLLRPGGTL 652
|
|
| PUA_3 |
pfam17785 |
PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent ... |
5-68 |
2.66e-21 |
|
PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent methyltransferases.
Pssm-ID: 436043 [Multi-domain] Cd Length: 64 Bit Score: 86.38 E-value: 2.66e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1633070433 5 IHLAKARDKSLRRKHPWVFSRGIDKVEGEPQQGETVDVYAQNGQWLAKAAYSPASQIRARVWTF 68
Cdd:pfam17785 1 VTLKKKAEKRLKRGHPWIYSNEIERVEGDLEEGDLVRVVDSDGRFLGTGYYNPQSKIAVRVLSR 64
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
219-303 |
1.91e-09 |
|
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: 58.65 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 219 KGKDVLNCFSYTGGFGLYaLKGDAKRVINADVSQLALDTAKFNAELNEFDiskkRAVFLNADVFKLLREyRDQGTKFDVV 298
Cdd:COG2265 233 GGERVLDLYCGVGTFALP-LARRAKKVIGVEIVPEAVEDARENARLNGLK----NVEFVAGDLEEVLPE-LLWGGRPDVV 306
|
....*
gi 1633070433 299 IMDPP 303
Cdd:COG2265 307 VLDPP 311
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
213-303 |
2.98e-08 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 53.36 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 213 ESMKYVKGKDVLNCFSYTGGFGLYALKgDAKRVINADVSQLALDTAKFNAELNefDISKKRAVFLNADVFKLLReyrdqG 292
Cdd:PRK14968 17 ENAVDKKGDRVLEVGTGSGIVAIVAAK-NGKKVVGVDINPYAVECAKCNAKLN--NIRNNGVEVIRSDLFEPFR-----G 88
|
90
....*....|.
gi 1633070433 293 TKFDVVIMDPP 303
Cdd:PRK14968 89 DKFDVILFNPP 99
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
222-338 |
2.39e-07 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 48.58 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 222 DVLNCFSYTGGFGLYALKGDAKRVINADVSQLALDTAKFNAELNEFDiskkRAVFLNADVFKLLrEYRDQgtKFDVVIMD 301
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLAD----NVEVLKGDAEELP-PEADE--SFDVIISD 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 1633070433 302 PPkfvssknnLTSGANGYKDVNMLAMQILKPGGTLLT 338
Cdd:cd02440 74 PP--------LHHLVEDLARFLEEARRLLKPGGVLVL 102
|
|
| PUA |
smart00359 |
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
21-67 |
3.91e-07 |
|
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 47.25 E-value: 3.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1633070433 21 WVFSRGIDKVEGEPQQGETVDVYAQNGQWLAKAAYSPASQIRARVWT 67
Cdd:smart00359 18 SLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKG 64
|
|
| Cons_hypoth95 |
pfam03602 |
Conserved hypothetical protein 95; |
215-303 |
2.33e-06 |
|
Conserved hypothetical protein 95;
Pssm-ID: 427391 [Multi-domain] Cd Length: 179 Bit Score: 47.62 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 215 MKYVKGKDVLNCFSYTGGFGLYALKGDAKRVINADVSQLALDTAKFNAELnefdiSKKRAVFLNADVFKLLREYRDQGTK 294
Cdd:pfam03602 37 APYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQL-----LGLPGAVLVMDALLALLRLAGKGPV 111
|
....*....
gi 1633070433 295 FDVVIMDPP 303
Cdd:pfam03602 112 FDIVFLDPP 120
|
|
| COG2521 |
COG2521 |
Predicted archaeal methyltransferase [General function prediction only]; |
219-339 |
3.66e-06 |
|
Predicted archaeal methyltransferase [General function prediction only];
Pssm-ID: 442011 [Multi-domain] Cd Length: 285 Bit Score: 47.98 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 219 KGKDVLNCFSYTGGFGLYALKGDAKRVI----NADVSQLAldtakfnaELN--EFDISKKRAVFLNADVFKLLREYRDQg 292
Cdd:COG2521 132 RGDRVLDTCTGLGYTAIEALKRGAREVItvekDPNVLELA--------ELNpwSRELANERIKIILGDASEVIKTFPDE- 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1633070433 293 tKFDVVIMDPPKFvSSKNNLTSGANgYKDvnmLAmQILKPGGTLLTY 339
Cdd:COG2521 203 -SFDAIIHDPPRF-SLAGELYSLEF-YRE---LY-RVLKPGGRLFHY 242
|
|
| RsmD |
COG0742 |
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
217-303 |
3.96e-06 |
|
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 440505 [Multi-domain] Cd Length: 183 Bit Score: 47.00 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 217 YVKGKDVLNCFSYTGGFGLYAL-KGdAKRVINADVSQLALDTAKFNAE-LNEFDiskkRAVFLNADVFKLLReyRDQGTK 294
Cdd:COG0742 39 DIEGARVLDLFAGSGALGLEALsRG-AASVVFVEKDRKAAAVIRKNLEkLGLED----RARVIRGDALRFLK--RLAGEP 111
|
....*....
gi 1633070433 295 FDVVIMDPP 303
Cdd:COG0742 112 FDLVFLDPP 120
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
218-371 |
8.05e-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: 46.00 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 218 VKGKDVLNCFSYTGgFGLYALKGDAKRVINADVSQLALDTAKFNAELNEFDISkkravFLNADVFKLLREyrdqgtKFDV 297
Cdd:TIGR00537 18 LKPDDVLEIGAGTG-LVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLD-----VVMTDLFKGVRG------KFDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 298 VIMDPPkFVSSKNNLTSGA------NGYKDVNMLAMQ-------ILKPGGTLLTYSCSGLMGADLFQKIIA---DAALDA 361
Cdd:TIGR00537 86 ILFNPP-YLPLEDDLRRGDwldvaiDGGKDGRKVIDRfldelpeILKEGGRVQLIQSSLNGEPDTFDKLDErgfRYEIVA 164
|
170
....*....|
gi 1633070433 362 GRTVKFVERF 371
Cdd:TIGR00537 165 ERGLFFEELF 174
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
244-337 |
4.46e-05 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 44.76 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 244 RVINADVSQLALDTAKFNAELNEFDiskKRAVFLNADVFKLLREYRdqgtKFDVVIMDPPkFVSS--------------- 308
Cdd:COG2890 138 RVTAVDISPDALAVARRNAERLGLE---DRVRFLQGDLFEPLPGDG----RFDLIVSNPP-YIPEdeiallppevrdhep 209
|
90 100 110
....*....|....*....|....*....|..
gi 1633070433 309 KNNLTSGANGYKDVNMLAMQI---LKPGGTLL 337
Cdd:COG2890 210 RLALDGGEDGLDFYRRIIAQAprlLKPGGWLL 241
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
237-337 |
1.09e-04 |
|
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 42.87 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 237 ALKGDAKRVINADVSQLALDTAKFNAELNEFDiskkRAVFLNADVFKLLREyrdqgTKFDVVIMDPPkfvssknnLTSGA 316
Cdd:COG2813 68 AKRNPEARVTLVDVNARAVELARANAAANGLE----NVEVLWSDGLSGVPD-----GSFDLILSNPP--------FHAGR 130
|
90 100
....*....|....*....|....*
gi 1633070433 317 NGYKDV--NML--AMQILKPGGTLL 337
Cdd:COG2813 131 AVDKEVahALIadAARHLRPGGELW 155
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
219-344 |
2.62e-04 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 40.86 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 219 KGKDVLNCFSYTGGFG--LYALKGDAKRVINADVSQLALDTAKFNAELNEFDiskkRAVFLNADVFKLLREYRDQgtKFD 296
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSfeLAEELGPNAEVVGIDISEEAIEKARENAQKLGFD----NVEFEQGDIEELPELLEDD--KFD 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1633070433 297 VVImdppkfvsSKNNLTSGANGyKDVNMLAMQILKPGGTLLTYSCSGL 344
Cdd:pfam13847 77 VVI--------SNCVLNHIPDP-DKVLQEILRVLKPGGRLIISDPDSL 115
|
|
| PRK04338 |
PRK04338 |
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional |
182-302 |
9.71e-04 |
|
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
Pssm-ID: 235286 Cd Length: 382 Bit Score: 41.05 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 182 VIIEENGVKISV-----NIMEGHKTG-----FY---MD-QRDSRKESMKYVKGKD----VLNCFSYTGGFGL-YALKGDA 242
Cdd:PRK04338 2 MIITEGKVKIEVpdpstYSKDGKFPPswapvFYnprMElNRDISVLVLRAFGPKLpresVLDALSASGIRGIrYALETGV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 243 KRVINADVSQLALDTAKFNAELNEFDiskKRAVFlNADVFKLLREYRdqgtKFDVVIMDP 302
Cdd:PRK04338 82 EKVTLNDINPDAVELIKKNLELNGLE---NEKVF-NKDANALLHEER----KFDVVDIDP 133
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
230-303 |
2.09e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 39.12 E-value: 2.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1633070433 230 TGGFGLYALKGDAKRVINADVSQLALDTAKFNAElnefdISKKRAVFLNADVFKLlreyrDQGTKFDVVIMDPP 303
Cdd:COG2263 56 TGMLAIGAALLGAKKVVGVDIDPEALEIARENAE-----RLGVRVDFIRADVTRI-----PLGGSVDTVVMNPP 119
|
|
| PrmA |
pfam06325 |
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
237-345 |
3.95e-03 |
|
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.
Pssm-ID: 428888 [Multi-domain] Cd Length: 294 Bit Score: 38.79 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 237 ALKGDAKRVINADVSQLALDTAKFNAELNEfdISKKRAVFLNADVFKLlreyrdqgtKFDVVImdppkfvssknnltsgA 316
Cdd:pfam06325 179 ALKLGAKKVVGVDIDPVAVRAAKENAELNG--VEARLEVYLPGDLPKE---------KADVVV----------------A 231
|
90 100 110
....*....|....*....|....*....|...
gi 1633070433 317 NGYKDV-NMLAMQI---LKPGGTLLTyscSGLM 345
Cdd:pfam06325 232 NILADPlIELAPDIyalVKPGGYLIL---SGIL 261
|
|
| hydroxyacyl_CoA_DH |
cd08254 |
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ... |
230-337 |
5.07e-03 |
|
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.
Pssm-ID: 176216 [Multi-domain] Cd Length: 338 Bit Score: 38.77 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 230 TGGFGLYAL---KGDAKRVINADVSQLALDTAK-FNAelnefdiskkRAVFLNADVFKLLREYRDQGTKFDVvIMDppkF 305
Cdd:cd08254 174 LGGLGLNAVqiaKAMGAAVIAVDIKEEKLELAKeLGA----------DEVLNSLDDSPKDKKAAGLGGGFDV-IFD---F 239
|
90 100 110
....*....|....*....|....*....|..
gi 1633070433 306 VssknnltsganGYKDVNMLAMQILKPGGTLL 337
Cdd:cd08254 240 V-----------GTQPTFEDAQKAVKPGGRIV 260
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
237-373 |
7.50e-03 |
|
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 37.85 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 237 ALKGdAKRVINADVSQLALDTAKFNAELNefDISKKRAVFLnADVFKllreyrdqGTKFDVVImdppkfvssknnltsgA 316
Cdd:COG2264 167 AKLG-AKRVLAVDIDPVAVEAARENAELN--GVEDRIEVVL-GDLLE--------DGPYDLVV----------------A 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1633070433 317 NGYKDVNM-LA---MQILKPGGTLLtysCSGLMGADLfqKIIADAALDAGrtVKFVERFEQ 373
Cdd:COG2264 219 NILANPLIeLApdlAALLKPGGYLI---LSGILEEQA--DEVLAAYEAAG--FELVERRER 272
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
231-337 |
7.88e-03 |
|
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: 36.15 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633070433 231 GGFGLYALKGDAKRVINADVSQLALDTAKFNAElnefdisKKRAVFLNADVFKLlrEYRDQgtKFDVVIM--------DP 302
Cdd:COG2227 35 TGRLALALARRGADVTGVDISPEALEIARERAA-------ELNVDFVQGDLEDL--PLEDG--SFDLVICsevlehlpDP 103
|
90 100 110
....*....|....*....|....*....|....*
gi 1633070433 303 PKFVSSknnltsgangykdvnmlAMQILKPGGTLL 337
Cdd:COG2227 104 AALLRE-----------------LARLLKPGGLLL 121
|
|
| |
