|
Name |
Accession |
Description |
Interval |
E-value |
| rsmC |
PRK09489 |
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC; |
1-342 |
0e+00 |
|
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
Pssm-ID: 181902 [Multi-domain] Cd Length: 342 Bit Score: 704.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 1 MSAFTPASEVLLRHSDDFESARVLFAGDLQDDLPARLDTAASRAHTQQFHHWQVLNRQMGDTVRFSLVAEAADVAECDTL 80
Cdd:PRK09489 1 MSALTPASEVLLRHSDDFEQRRVLFAGDLQDDLPAQLDAASVRVHTQQFHHWQVLSRQMGDNARFSLVATAEDVADCDTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 81 IYYWPKNKPEAQFQLMNLLSLLPVGSDIFVVGENRSGVRSAEQMLAEYAPLNKVDSARRCGLYHGRLEKQPAFDADAFWG 160
Cdd:PRK09489 81 IYYWPKNKQEAQFQLMNLLSLLPVGTDIFVVGENRSGVRSAEKMLADYAPLNKIDSARRCGLYHGRLEKQPVFDADKFWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 161 EYTLDNLTIKTLPGVFSRDGLDVGSQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATL 240
Cdd:PRK09489 161 EYQVDGLTVKTLPGVFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 241 AANGLAGDVFASNVFSEVNGRFDMIISNPPFHDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAFLPYPQVLDETFGFH 320
Cdd:PRK09489 241 AANGLEGEVFASNVFSDIKGRFDMIISNPPFHDGIQTSLDAAQTLIRGAVRHLNSGGELRIVANAFLPYPDLLDETFGSH 320
|
330 340
....*....|....*....|..
gi 556293901 321 EVIAQTGRFKVYRTIMTRQAKK 342
Cdd:PRK09489 321 EVLAQTGRFKVYRAIMTRQAKK 342
|
|
| MTS_N |
pfam08468 |
Methyltransferase small domain N-terminal; This domain is found to the N-terminus of the ... |
8-162 |
6.81e-75 |
|
Methyltransferase small domain N-terminal; This domain is found to the N-terminus of the methyltransferase small domain (pfam05175) in bacterial proteins.
Pssm-ID: 430013 Cd Length: 157 Bit Score: 227.85 E-value: 6.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 8 SEVLLRHSDDFESARVLFAGDLQDDLPARLDTAASRAH--TQQFHHWQVLNRQMGDT-VRFSLVAEAAdvAECDTLIYYW 84
Cdd:pfam08468 1 SQVLLRHLDLFEGKSVLLAGDLADDLPAQLAAAASSVHvlTWDYHHAQQLSAKLGNNaVHFGLQLPAD--AQFDTVILYW 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556293901 85 PKNKPEAQFQLMNLLSLLPVGSDIFVVGENRSGVRSAEQMLAEYAPLNKVDSARRCGLYHGRLEKQPA-FDADAFWGEY 162
Cdd:pfam08468 79 PKAKQEAQYLLALLLAHLPPGGEIFVVGENRGGVKSAEKLLAPYGQVNKIDSARHCSLYHGQLEKPPApFDLEDWWKRY 157
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
151-335 |
1.66e-67 |
|
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: 210.05 E-value: 1.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 151 PAFDADAFWgEYTLDN--LTIKTLPGVFSRDGLDVGSQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTLCDV 228
Cdd:COG2813 3 AASDWPRTI-TVRLAGrdLTFVTLPGVFSRDRLDIGTRLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 229 SAPAVEASRATLAANGLA-GDVFASNVFSEV-NGRFDMIISNPPFHDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAF 306
Cdd:COG2813 82 NARAVELARANAAANGLEnVEVLWSDGLSGVpDGSFDLILSNPPFHAGRAVDKEVAHALIADAARHLRPGGELWLVANRH 161
|
170 180
....*....|....*....|....*....
gi 556293901 307 LPYPQVLDETFGFHEVIAQTGRFKVYRTI 335
Cdd:COG2813 162 LPYERKLEELFGNVEVLARNKGFKVLRAV 190
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
199-299 |
2.48e-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: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 199 KVLDVGCGAGVLAAALASHsPKVRLTLCDVSAPAVEASRATLAANGLAGDVF----ASNVFSEVNGRFDMIISNPPFHDg 274
Cdd:cd02440 1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLADNVEVlkgdAEELPPEADESFDVIISDPPLHH- 78
|
90 100
....*....|....*....|....*
gi 556293901 275 lqtSLEAAQALIRGAVRHLNSGGEL 299
Cdd:cd02440 79 ---LVEDLARFLEEARRLLKPGGVL 100
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
185-329 |
1.59e-05 |
|
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: 44.85 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 185 SQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTlcDVSAPAVEASRATLAANGLAGDVFASNVFSEVNGRFDM 264
Cdd:TIGR00537 8 SLLLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTT--DINPFAVKELRENAKLNNVGLDVVMTDLFKGVRGKFDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 265 IISNPPF----------------HDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAFLPYPQVLD--ETFGF-HEVIAQ 325
Cdd:TIGR00537 86 ILFNPPYlpleddlrrgdwldvaIDGGKDGRKVIDRFLDELPEILKEGGRVQLIQSSLNGEPDTFDklDERGFrYEIVAE 165
|
....
gi 556293901 326 TGRF 329
Cdd:TIGR00537 166 RGLF 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rsmC |
PRK09489 |
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC; |
1-342 |
0e+00 |
|
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
Pssm-ID: 181902 [Multi-domain] Cd Length: 342 Bit Score: 704.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 1 MSAFTPASEVLLRHSDDFESARVLFAGDLQDDLPARLDTAASRAHTQQFHHWQVLNRQMGDTVRFSLVAEAADVAECDTL 80
Cdd:PRK09489 1 MSALTPASEVLLRHSDDFEQRRVLFAGDLQDDLPAQLDAASVRVHTQQFHHWQVLSRQMGDNARFSLVATAEDVADCDTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 81 IYYWPKNKPEAQFQLMNLLSLLPVGSDIFVVGENRSGVRSAEQMLAEYAPLNKVDSARRCGLYHGRLEKQPAFDADAFWG 160
Cdd:PRK09489 81 IYYWPKNKQEAQFQLMNLLSLLPVGTDIFVVGENRSGVRSAEKMLADYAPLNKIDSARRCGLYHGRLEKQPVFDADKFWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 161 EYTLDNLTIKTLPGVFSRDGLDVGSQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATL 240
Cdd:PRK09489 161 EYQVDGLTVKTLPGVFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 241 AANGLAGDVFASNVFSEVNGRFDMIISNPPFHDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAFLPYPQVLDETFGFH 320
Cdd:PRK09489 241 AANGLEGEVFASNVFSDIKGRFDMIISNPPFHDGIQTSLDAAQTLIRGAVRHLNSGGELRIVANAFLPYPDLLDETFGSH 320
|
330 340
....*....|....*....|..
gi 556293901 321 EVIAQTGRFKVYRTIMTRQAKK 342
Cdd:PRK09489 321 EVLAQTGRFKVYRAIMTRQAKK 342
|
|
| MTS_N |
pfam08468 |
Methyltransferase small domain N-terminal; This domain is found to the N-terminus of the ... |
8-162 |
6.81e-75 |
|
Methyltransferase small domain N-terminal; This domain is found to the N-terminus of the methyltransferase small domain (pfam05175) in bacterial proteins.
Pssm-ID: 430013 Cd Length: 157 Bit Score: 227.85 E-value: 6.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 8 SEVLLRHSDDFESARVLFAGDLQDDLPARLDTAASRAH--TQQFHHWQVLNRQMGDT-VRFSLVAEAAdvAECDTLIYYW 84
Cdd:pfam08468 1 SQVLLRHLDLFEGKSVLLAGDLADDLPAQLAAAASSVHvlTWDYHHAQQLSAKLGNNaVHFGLQLPAD--AQFDTVILYW 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556293901 85 PKNKPEAQFQLMNLLSLLPVGSDIFVVGENRSGVRSAEQMLAEYAPLNKVDSARRCGLYHGRLEKQPA-FDADAFWGEY 162
Cdd:pfam08468 79 PKAKQEAQYLLALLLAHLPPGGEIFVVGENRGGVKSAEKLLAPYGQVNKIDSARHCSLYHGQLEKPPApFDLEDWWKRY 157
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
166-333 |
1.12e-74 |
|
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.
Pssm-ID: 428349 [Multi-domain] Cd Length: 170 Bit Score: 227.86 E-value: 1.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 166 NLTIKTLPGVFSRDGLDVGSQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATLAANGL 245
Cdd:pfam05175 1 ELTFKTLPGVFSHGRLDIGSRLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 246 -AGDVFASNVFSEV-NGRFDMIISNPPFHDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAFLPYPQVLDETFGFHEVI 323
Cdd:pfam05175 81 eNGEVVASDVYSGVeDGKFDLIISNPPFHAGLATTYNVAQRFIADAKRHLRPGGELWIVANRFLGYPPLLEELFGNVEVV 160
|
170
....*....|
gi 556293901 324 AQTGRFKVYR 333
Cdd:pfam05175 161 AKTNGFKVLK 170
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
151-335 |
1.66e-67 |
|
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: 210.05 E-value: 1.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 151 PAFDADAFWgEYTLDN--LTIKTLPGVFSRDGLDVGSQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTLCDV 228
Cdd:COG2813 3 AASDWPRTI-TVRLAGrdLTFVTLPGVFSRDRLDIGTRLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 229 SAPAVEASRATLAANGLA-GDVFASNVFSEV-NGRFDMIISNPPFHDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAF 306
Cdd:COG2813 82 NARAVELARANAAANGLEnVEVLWSDGLSGVpDGSFDLILSNPPFHAGRAVDKEVAHALIADAARHLRPGGELWLVANRH 161
|
170 180
....*....|....*....|....*....
gi 556293901 307 LPYPQVLDETFGFHEVIAQTGRFKVYRTI 335
Cdd:COG2813 162 LPYERKLEELFGNVEVLARNKGFKVLRAV 190
|
|
| PRK15001 |
PRK15001 |
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG; |
168-335 |
1.40e-17 |
|
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
Pssm-ID: 184963 [Multi-domain] Cd Length: 378 Bit Score: 82.77 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 168 TIKTLPGVFSRDGLDVGSQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATLAANGLAG 247
Cdd:PRK15001 200 TIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 248 ----DVFASNVFSEVNG-RFDMIISNPPFHDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAFLPYPQVLDETFGFHEV 322
Cdd:PRK15001 280 ldrcEFMINNALSGVEPfRFNAVLCNPPFHQQHALTDNVAWEMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTT 359
|
170
....*....|...
gi 556293901 323 IAQTGRFKVYRTI 335
Cdd:PRK15001 360 IATNNKFVVLKAV 372
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
186-299 |
1.94e-09 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 57.85 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 186 QLLLSTLEPHTKGKVLDVGCgagvlaaalaSHSPKVRLTLCDVSAPAVEASRATLAANGLAGDV--FASNVFSEV--NGR 261
Cdd:COG2890 102 ELALALLPAGAPPRVLDLGTgsgaialalaKERPDARVTAVDISPDALAVARRNAERLGLEDRVrfLQGDLFEPLpgDGR 181
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556293901 262 FDMIISNPP---------------FH----------DGlqtsLEAAQALIRGAVRHLNSGGEL 299
Cdd:COG2890 182 FDLIVSNPPyipedeiallppevrDHeprlaldggeDG----LDFYRRIIAQAPRLLKPGGWL 240
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
187-302 |
1.41e-08 |
|
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: 54.77 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 187 LLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATLAANGLAGDVFASN------VFSEVNG 260
Cdd:COG4123 28 LLAAFAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHgdlkefAAELPPG 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 556293901 261 RFDMIISNPPFHD---GLQTSLEA-AQA----------LIRGAVRHLNSGGELRIV 302
Cdd:COG4123 108 SFDLVVSNPPYFKagsGRKSPDEArAIArhedaltledLIRAAARLLKPGGRFALI 163
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
189-299 |
3.28e-08 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 54.01 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 189 LSTLEPHTKGKVLDVGCgagvlaaalaSHSPKVRLTLCDVSAPAVE-ASRATLAANGLAGDVFASNVFSEV-NGRFDMII 266
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTgsgaialalaKERPDAEVTAVDISPEALAvARRNAKHGLGARVEFLQGDWFEPLpGGRFDLIV 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 556293901 267 SNPP---------------FH------DGLQTSLEAAQALIRGAVRHLNSGGEL 299
Cdd:PRK09328 181 SNPPyipeadihllqpevrDHephlalFGGEDGLDFYRRIIEQAPRYLKPGGWL 234
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
199-299 |
2.48e-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: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 199 KVLDVGCGAGVLAAALASHsPKVRLTLCDVSAPAVEASRATLAANGLAGDVF----ASNVFSEVNGRFDMIISNPPFHDg 274
Cdd:cd02440 1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLADNVEVlkgdAEELPPEADESFDVIISDPPLHH- 78
|
90 100
....*....|....*....|....*
gi 556293901 275 lqtSLEAAQALIRGAVRHLNSGGEL 299
Cdd:cd02440 79 ---LVEDLARFLEEARRLLKPGGVL 100
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
200-297 |
2.15e-06 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 45.63 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 200 VLDVGC---GAGVLAAALASHspkvRLTLCDVSAPAVEASRATLAANGLAGDVFASNV--FSEVNGRFDMIISNPPFHdg 274
Cdd:pfam13649 1 VLDLGCgtgRLTLALARRGGA----RVTGVDLSPEMLERARERAAEAGLNVEFVQGDAedLPFPDGSFDLVVSSGVLH-- 74
|
90 100
....*....|....*....|...
gi 556293901 275 lQTSLEAAQALIRGAVRHLNSGG 297
Cdd:pfam13649 75 -HLPDPDLEAALREIARVLKPGG 96
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
185-329 |
1.59e-05 |
|
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: 44.85 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 185 SQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTlcDVSAPAVEASRATLAANGLAGDVFASNVFSEVNGRFDM 264
Cdd:TIGR00537 8 SLLLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTT--DINPFAVKELRENAKLNNVGLDVVMTDLFKGVRGKFDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 265 IISNPPF----------------HDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAFLPYPQVLD--ETFGF-HEVIAQ 325
Cdd:TIGR00537 86 ILFNPPYlpleddlrrgdwldvaIDGGKDGRKVIDRFLDELPEILKEGGRVQLIQSSLNGEPDTFDklDERGFrYEIVAE 165
|
....
gi 556293901 326 TGRF 329
Cdd:TIGR00537 166 RGLF 169
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
227-299 |
5.23e-05 |
|
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: 44.79 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 227 DVSAPAVEASRATLAANGLAGDV--FASNVF------SEVNGRFDMIISNPP--------FHDGLQtsleAAQALIRGAV 290
Cdd:COG1092 246 DLSATALEWAKENAALNGLDDRHefVQADAFdwlrelAREGERFDLIILDPPafakskkdLFDAQR----DYKDLNRLAL 321
|
....*....
gi 556293901 291 RHLNSGGEL 299
Cdd:COG1092 322 KLLAPGGIL 330
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
201-299 |
5.59e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 41.58 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 201 LDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATLAANGLAG----DVFASNVFSEVNGRFDMIISNPPFHdglq 276
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNavrvELFQLDLGELDPGSFDVVVASNVLH---- 76
|
90 100
....*....|....*....|...
gi 556293901 277 tSLEAAQALIRGAVRHLNSGGEL 299
Cdd:pfam08242 77 -HLADPRAVLRNIRRLLKPGGVL 98
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
198-299 |
1.50e-04 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 40.19 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 198 GKVLDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATLA-ANGLAGDVFAsnvfSEVNGRFDMIISNPPFHDglq 276
Cdd:COG4106 3 RRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPnVRFVVADLRD----LDPPEPFDLVVSNAALHW--- 75
|
90 100
....*....|....*....|...
gi 556293901 277 tsLEAAQALIRGAVRHLNSGGEL 299
Cdd:COG4106 76 --LPDHAALLARLAAALAPGGVL 96
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
188-319 |
4.29e-04 |
|
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: 39.98 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 188 LLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVrlTLCDVSAPAVEASRATLAANGLAGDVFASNV----FSevNGRFD 263
Cdd:COG2226 14 LLAALGLRPGARVLDLGCGTGRLALALAERGARV--TGVDISPEMLELARERAAEAGLNVEFVVGDAedlpFP--DGSFD 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 556293901 264 MIISNPPFHDglqtsLEAAQALIRGAVRHLNSGGELrIVANAFLPYPQVLDETF---GF 319
Cdd:COG2226 90 LVISSFVLHH-----LPDPERALAEIARVLKPGGRL-VVVDFSPPDLAELEELLaeaGF 142
|
|
| PRK11727 |
PRK11727 |
23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF; |
227-284 |
9.67e-04 |
|
23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;
Pssm-ID: 236964 Cd Length: 321 Bit Score: 40.62 E-value: 9.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556293901 227 DVSAPAVEASRATLAAN-GLAGDVF------ASNVFS---EVNGRFDMIISNPPFHDglqtSLEAAQA 284
Cdd:PRK11727 145 DIDPQALASAQAIISANpGLNGAIRlrlqkdSKAIFKgiiHKNERFDATLCNPPFHA----SAAEARA 208
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
187-309 |
1.92e-03 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 38.74 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 187 LLLSTLEPHtkGKVLDVGCGAGVLAAALASHsPKVRLTLCDVSAPAVEASRATLAANGLA------GDVFASNVFSEvnG 260
Cdd:COG0500 19 ALLERLPKG--GRVLDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARARAAKAGLGnveflvADLAELDPLPA--E 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 556293901 261 RFDMIISNPPFHDglqTSLEAAQALIRGAVRHLNSGGELRIVANAFLPY 309
Cdd:COG0500 94 SFDLVVAFGVLHH---LPPEEREALLRELARALKPGGVLLLSASDAAAA 139
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
186-273 |
2.38e-03 |
|
HemK family putative methylases; 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. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]
Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 39.26 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 186 QLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATLAANGLAGDVF--ASNVFSEVNG-RF 262
Cdd:TIGR00536 104 KALASLISQPPILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEfiQSNLFEPLAGqKI 183
|
90
....*....|.
gi 556293901 263 DMIISNPPFHD 273
Cdd:TIGR00536 184 DIIVSNPPYID 194
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
185-325 |
3.62e-03 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 37.96 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 185 SQLLLSTLEPHTKGKVLDVGCGAGVLAAALASHSPKVrlTLCDVSAPAVEASRATLAANGLAG---DVFASNVFSEVNGR 261
Cdd:PRK14968 12 SFLLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKV--VGVDINPYAVECAKCNAKLNNIRNngvEVIRSDLFEPFRGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 262 -FDMIISNPPF----------------HDGLQTSLEAAQALIRGAVRHLNSGGELRIVANAFLPYPQVLD--ETFGF-HE 321
Cdd:PRK14968 90 kFDVILFNPPYlpteeeeewddwlnyaLSGGKDGREVIDRFLDEVGRYLKPGGRILLLQSSLTGEDEVLEylEKLGFeAE 169
|
....
gi 556293901 322 VIAQ 325
Cdd:PRK14968 170 VVAE 173
|
|
| PRK14966 |
PRK14966 |
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ... |
198-327 |
4.80e-03 |
|
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional
Pssm-ID: 184930 [Multi-domain] Cd Length: 423 Bit Score: 38.52 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 198 GKVLDVGCGAGVLAAALASHSPKVRLTLCDVSAPAVEASRATLAANGLA-----GDVFASNVFSEvnGRFDMIISNPPFH 272
Cdd:PRK14966 253 GRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAADLGARvefahGSWFDTDMPSE--GKWDIIVSNPPYI 330
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556293901 273 DGLQTSLeaAQALIR--------------GAVRHLNSGGELRIVANAFLPYPQVLDETFGFHEVIAQTG 327
Cdd:PRK14966 331 ENGDKHL--LQGDLRfepqialtdfsdglSCIRTLAQGAPDRLAEGGFLLLEHGFDQGAAVRGVLAENG 397
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
197-299 |
6.84e-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: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293901 197 KGKVLDVGCGAGVLAAALASHSPKVrlTLCDVSAPAVEASRATLAANGL---AGDVFAsnvFSEVNGRFDMIISNPPFHD 273
Cdd:COG2227 25 GGRVLDVGCGTGRLALALARRGADV--TGVDISPEALEIARERAAELNVdfvQGDLED---LPLEDGSFDLVICSEVLEH 99
|
90 100
....*....|....*....|....*.
gi 556293901 274 glqtsLEAAQALIRGAVRHLNSGGEL 299
Cdd:COG2227 100 -----LPDPAALLRELARLLKPGGLL 120
|
|
| |
