|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
46-324 |
1.98e-74 |
|
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 439914 [Multi-domain] Cd Length: 441 Bit Score: 237.98 E-value: 1.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 46 LSHPPLftTVRVNTHLGSVEhvrgllleELQKQFGGSSIPVLQHPALPDVLLIPMTGPrgigirmtepIYLSPSFDNvls 125
Cdd:COG0144 172 NEPPPL--DLRVNTLKASRE--------ELLARLAEEGIEAEPTPLSPDGLRLEGPGP----------VTALPGFRE--- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 126 GYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFD 205
Cdd:COG0144 229 GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 206 ATKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVY 282
Cdd:COG0144 309 ARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVY 376
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1046865904 283 STCTVTLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMLGAG 324
Cdd:COG0144 377 STCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
34-304 |
1.75e-66 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 217.35 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 34 EAERNFETLLLRlshPPlfTTVRVNTHLGSVEHvrglLLEELQKQFggssIPVLQHPALPDVLLIPmtgpRGigirmteP 113
Cdd:PRK14902 165 KAEKILESLNEP---PK--ASIRVNTLKISVEE----LIEKLEEEG----YEVEESLLSPEALVIE----KG-------N 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 114 IYLSPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASL 193
Cdd:PRK14902 221 IAGTDLFKD---GLITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 194 LGLHSIRAFCFDATKalklevmdgvdgAPPFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVA 270
Cdd:PRK14902 298 LGLTNIETKALDARK------------VHEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESV 365
|
250 260 270
....*....|....*....|....*....|....
gi 1046865904 271 VRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFP 304
Cdd:PRK14902 366 AQYLKKGGILVYSTCTIEKEENEEVIEAFLEEHP 399
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
139-333 |
4.32e-53 |
|
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.
Pssm-ID: 426109 [Multi-domain] Cd Length: 199 Bit Score: 174.92 E-value: 4.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 139 AHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKalklevmdgv 218
Cdd:pfam01189 1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 219 dgaPPFLP--ESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENE 293
Cdd:pfam01189 71 ---PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1046865904 294 EQVAWALRTFPCLQLQPqepqIGGEGMLGAGLSLEQLKQL 333
Cdd:pfam01189 148 AVIEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL 183
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
124-377 |
2.26e-48 |
|
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 188051 [Multi-domain] Cd Length: 264 Bit Score: 164.95 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 124 LSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFC 203
Cdd:TIGR00446 49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 204 FDATKalklevmdgvdgAPPFLPEsFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVL 280
Cdd:TIGR00446 129 ADGRK------------FGAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 281 VYSTCTVTLAENEEQVAWALRTFPCLQLqpqEPQIGGEgMLGAGLSLEQLKQLQRFDPcvvplesmdtnslgdarredvi 360
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDE-FFGINIGKGEVKGALRVFP---------------------- 249
|
250
....*....|....*..
gi 1046865904 361 wlANKDCIGFFIAKFLK 377
Cdd:TIGR00446 250 --QNYDCEGFFVAKLRK 264
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
149-283 |
1.49e-09 |
|
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: 55.13 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 149 KILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgaPPFLPES 228
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1046865904 229 FDRILLDAPCSGLgqrpnmactwtlkevtsyQPLQRKLLNVAVRLLKPGGVLVYS 283
Cdd:cd02440 67 FDVIISDPPLHHL------------------VEDLARFLEEARRLLKPGGVLVLT 103
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
46-324 |
1.98e-74 |
|
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 439914 [Multi-domain] Cd Length: 441 Bit Score: 237.98 E-value: 1.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 46 LSHPPLftTVRVNTHLGSVEhvrgllleELQKQFGGSSIPVLQHPALPDVLLIPMTGPrgigirmtepIYLSPSFDNvls 125
Cdd:COG0144 172 NEPPPL--DLRVNTLKASRE--------ELLARLAEEGIEAEPTPLSPDGLRLEGPGP----------VTALPGFRE--- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 126 GYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFD 205
Cdd:COG0144 229 GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 206 ATKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVY 282
Cdd:COG0144 309 ARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVY 376
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1046865904 283 STCTVTLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMLGAG 324
Cdd:COG0144 377 STCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
34-304 |
1.75e-66 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 217.35 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 34 EAERNFETLLLRlshPPlfTTVRVNTHLGSVEHvrglLLEELQKQFggssIPVLQHPALPDVLLIPmtgpRGigirmteP 113
Cdd:PRK14902 165 KAEKILESLNEP---PK--ASIRVNTLKISVEE----LIEKLEEEG----YEVEESLLSPEALVIE----KG-------N 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 114 IYLSPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASL 193
Cdd:PRK14902 221 IAGTDLFKD---GLITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 194 LGLHSIRAFCFDATKalklevmdgvdgAPPFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVA 270
Cdd:PRK14902 298 LGLTNIETKALDARK------------VHEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESV 365
|
250 260 270
....*....|....*....|....*....|....
gi 1046865904 271 VRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFP 304
Cdd:PRK14902 366 AQYLKKGGILVYSTCTIEKEENEEVIEAFLEEHP 399
|
|
| PRK14901 |
PRK14901 |
16S rRNA methyltransferase B; Provisional |
72-326 |
3.89e-61 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237856 [Multi-domain] Cd Length: 434 Bit Score: 203.24 E-value: 3.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 72 LEELQKQFGGSSIPVLQHPALPDVLLIpmTGPRGigirmtePIYLSPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKIL 151
Cdd:PRK14901 190 LEEVQAALAEAGITATPIPGLPQGLRL--TGNPG-------SIRQLPGYEE---GWWTVQDRSAQLVAPLLDPQPGEVIL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 152 DLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALklevmdgvdGAPPFLPESFDR 231
Cdd:PRK14901 258 DACAAPGGKTTHIAELMGDQGEIWAVDRSASRLKKLQENAQRLGLKSIKILAADSRNLL---------ELKPQWRGYFDR 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 232 ILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQL 308
Cdd:PRK14901 329 ILLDAPCSGLGtlhRHPDARWRQTPEKIQELAPLQAELLESLAPLLKPGGTLVYATCTLHPAENEAQIEQFLARHPDWKL 408
|
250 260
....*....|....*....|...
gi 1046865904 309 QPQEPQI-----GGEGMLGAGLS 326
Cdd:PRK14901 409 EPPKQKIwphrqDGDGFFMAVLR 431
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
139-333 |
4.32e-53 |
|
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.
Pssm-ID: 426109 [Multi-domain] Cd Length: 199 Bit Score: 174.92 E-value: 4.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 139 AHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKalklevmdgv 218
Cdd:pfam01189 1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 219 dgaPPFLP--ESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENE 293
Cdd:pfam01189 71 ---PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1046865904 294 EQVAWALRTFPCLQLQPqepqIGGEGMLGAGLSLEQLKQL 333
Cdd:pfam01189 148 AVIEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL 183
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
124-377 |
2.26e-48 |
|
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 188051 [Multi-domain] Cd Length: 264 Bit Score: 164.95 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 124 LSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFC 203
Cdd:TIGR00446 49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 204 FDATKalklevmdgvdgAPPFLPEsFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVL 280
Cdd:TIGR00446 129 ADGRK------------FGAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 281 VYSTCTVTLAENEEQVAWALRTFPCLQLqpqEPQIGGEgMLGAGLSLEQLKQLQRFDPcvvplesmdtnslgdarredvi 360
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDE-FFGINIGKGEVKGALRVFP---------------------- 249
|
250
....*....|....*..
gi 1046865904 361 wlANKDCIGFFIAKFLK 377
Cdd:TIGR00446 250 --QNYDCEGFFVAKLRK 264
|
|
| PRK14904 |
PRK14904 |
16S rRNA methyltransferase B; Provisional |
114-310 |
2.74e-45 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237858 [Multi-domain] Cd Length: 445 Bit Score: 161.77 E-value: 2.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 114 IYLSPSFDN----VLSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQ 189
Cdd:PRK14904 214 FFLSKDFSLfepfLKLGLVSVQNPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYPQKLEKIRS 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 190 NASLLGLHSIRAFCFDATKalklevmdgvdgappFLPE-SFDRILLDAPCSG---LGQRPNMACTWTLKEVTSYQPLQRK 265
Cdd:PRK14904 294 HASALGITIIETIEGDARS---------------FSPEeQPDAILLDAPCTGtgvLGRRAELRWKLTPEKLAELVGLQAE 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1046865904 266 LLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQLQP 310
Cdd:PRK14904 359 LLDHAASLLKPGGVLVYATCSIEPEENELQIEAFLQRHPEFSAEP 403
|
|
| rsmB |
TIGR00563 |
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ... |
33-317 |
9.56e-44 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. The reading frame was originally interpreted as two reading frames, fmu and fmv. The recombinant protein from E. coli was shown to methylate only C967 of small subunit (16S) ribosomal RNA and to produce only m5C at that position. The seed alignment is built from bacterial sequences only. Eukaryotic homologs include Nop2, a protein required for processing pre-rRNA, that is likely also a rRNA methyltransferase, although the fine specificity may differ. Cutoff scores are set to avoid treating archaeal and eukaroytic homologs automatically as functionally equivalent, although they may have very similar roles. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273141 [Multi-domain] Cd Length: 426 Bit Score: 156.95 E-value: 9.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 33 QEAERNFETLLLR--LSHPPLftTVRVNTHLGSVEHVRGLLLEElqkqfGGSSIPVLQHPALPDvLLIPMtgprgigirm 110
Cdd:TIGR00563 146 QKAYPGQWQSICEanNQRPPM--WLRINRTKHSRDEWLALLAEA-----GMKGFPHDLAPDAVR-LETPA---------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 111 tePIYLSPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRdQGEVIALDKILTKVTKLKQN 190
Cdd:TIGR00563 208 --AVHALPGFEE---GWVTVQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELAP-QAQVVALDIHEHRLKRVYEN 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 191 ASLLGLhsirafcfdatkALKLEVMDGVDGAPPFLPES--FDRILLDAPCSGLG---QRPNMacTWTLKEVTSYQ--PLQ 263
Cdd:TIGR00563 282 LKRLGL------------TIKAETKDGDGRGPSQWAENeqFDRILLDAPCSATGvirRHPDI--KWLRKPRDIAElaELQ 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046865904 264 RKLLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQL----QPQEPQIGG 317
Cdd:TIGR00563 348 SEILDAIWPLLKTGGTLVYATCSVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
|
|
| PRK10901 |
PRK10901 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
47-311 |
7.11e-43 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 236790 [Multi-domain] Cd Length: 427 Bit Score: 154.58 E-value: 7.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 47 SHPPLftTVRVNTHLGSVEHVRGLLleelqKQFGGSSIPvlqHPALPDvllipmtgprgiGIRMTEPI---YLsPSFDnv 123
Cdd:PRK10901 168 QRPPM--WLRVNRRHHSRDAYLALL-----AEAGIEAFP---HAVGPD------------AIRLETPVpvhQL-PGFA-- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 124 lSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALmRDQGEVIALDKILTKVTKLKQNASLLGLHSiRAFC 203
Cdd:PRK10901 223 -EGWVSVQDAAAQLAATLLAPQNGERVLDACAAPGGKTAHILEL-APQAQVVALDIDAQRLERVRENLQRLGLKA-TVIV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 204 FDATKALKLevmdgVDGAPpflpesFDRILLDAPCSGLG-----------QRPNmactwtlkEVTSYQPLQRKLLNVAVR 272
Cdd:PRK10901 300 GDARDPAQW-----WDGQP------FDRILLDAPCSATGvirrhpdikwlRRPE--------DIAALAALQSEILDALWP 360
|
250 260 270
....*....|....*....|....*....|....*....
gi 1046865904 273 LLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQLQPQ 311
Cdd:PRK10901 361 LLKPGGTLLYATCSILPEENEQQIKAFLARHPDAELLDT 399
|
|
| PRK14903 |
PRK14903 |
16S rRNA methyltransferase B; Provisional |
43-302 |
6.32e-34 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 184896 [Multi-domain] Cd Length: 431 Bit Score: 130.38 E-value: 6.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 43 LLRLSHPPLFTTVRVNTHLGSVEHVRGLLLEELQKQFGGSSIPVlqhpalpdVLLIpmtgpRGIGIRMTEpiylspsFDN 122
Cdd:PRK14903 154 IMEWNQEPLPTMLRVNSLAITREEVIKILAEEGTEAVPGKHSPF--------SLIV-----RKLGVNMND-------SRV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 123 VLSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAF 202
Cdd:PRK14903 214 IKDGLATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEKHAKRLKLSSIEIK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 203 CFDATKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGV 279
Cdd:PRK14903 294 IADAERLTE------------YVQDTFDRILVDAPCTSLGtarNHPEVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGI 361
|
250 260
....*....|....*....|....
gi 1046865904 280 LVYSTCTVTLAENEEQV-AWALRT 302
Cdd:PRK14903 362 LLYSTCTVTKEENTEVVkRFVYEQ 385
|
|
| yebU |
PRK11933 |
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed |
124-304 |
1.64e-32 |
|
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
Pssm-ID: 183387 [Multi-domain] Cd Length: 470 Bit Score: 127.33 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 124 LSGYIFLQN----LPstVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSI 199
Cdd:PRK11933 89 LSGLFYIQEassmLP--VAALFADDNAPQRVLDMAAAPGSKTTQIAALMNNQGAIVANEYSASRVKVLHANISRCGVSNV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 200 RAFCFDATkalklevmdgVDGAppFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKP 276
Cdd:PRK11933 167 ALTHFDGR----------VFGA--ALPETFDAILLDAPCSGEGtvrKDPDALKNWSPESNLEIAATQRELIESAFHALKP 234
|
170 180
....*....|....*....|....*...
gi 1046865904 277 GGVLVYSTCTVTLAENEEQVAWALRTFP 304
Cdd:PRK11933 235 GGTLVYSTCTLNREENQAVCLWLKETYP 262
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
149-283 |
1.49e-09 |
|
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: 55.13 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 149 KILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgaPPFLPES 228
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1046865904 229 FDRILLDAPCSGLgqrpnmactwtlkevtsyQPLQRKLLNVAVRLLKPGGVLVYS 283
Cdd:cd02440 67 FDVIISDPPLHHL------------------VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
120-281 |
4.09e-09 |
|
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: 54.61 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 120 FDNVLSGYIFLQNLpstvvAHVLDPQPGEKILDLCAAPGgktTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHsI 199
Cdd:COG2226 1 FDRVAARYDGREAL-----LAALGLRPGARVLDLGCGTG---RLALALAERGARVTGVDISPEMLELARERAAEAGLN-V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 200 RAFCFDATkalklevmdgvdgAPPFLPESFDRILldapcsglgqrpnmaCTWTLKEVTSyqplQRKLLNVAVRLLKPGGV 279
Cdd:COG2226 72 EFVVGDAE-------------DLPFPDGSFDLVI---------------SSFVLHHLPD----PERALAEIARVLKPGGR 119
|
..
gi 1046865904 280 LV 281
Cdd:COG2226 120 LV 121
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
146-320 |
1.85e-06 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 47.41 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 146 PGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALKLevmdgvdgappFL 225
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPEL-----------LE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 226 PESFDRILLDapcsglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCtVTLAENEEQVawaLRTFPC 305
Cdd:pfam13847 72 DDKFDVVISN-------------------CVLNHIPDPDKVLQEILRVLKPGGRLIISDP-DSLAELPAHV---KEDSTY 128
|
170
....*....|....*
gi 1046865904 306 LQLQPQEPQIGGEGM 320
Cdd:pfam13847 129 YAGCVGGAILKKKLY 143
|
|
| Trm5 |
COG2520 |
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
146-282 |
1.64e-05 |
|
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442010 [Multi-domain] Cd Length: 333 Bit Score: 46.39 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 146 PGEKILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGL-HSIRAFCFDATKalklevmdgvdgAPPF 224
Cdd:COG2520 180 PGERVLDMFAGVGPFSIPIAK--RSGAKVVAIDINPDAVEYLKENIRLNKVeDRVTPILGDARE------------VAPE 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046865904 225 LPESFDRILLDAPCSGLgqrpnmactwtlkevtsyqplqrKLLNVAVRLLKPGGVLVY 282
Cdd:COG2520 246 LEGKADRIIMNLPHSAD-----------------------EFLDAALRALKPGGVIHY 280
|
|
| FtsJ |
pfam01728 |
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
146-281 |
5.39e-05 |
|
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 43.35 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 146 PGEKILDLCAAPGGKTThiAALMRDQGEVIALDKILTKVTKLKQNAsllGLHSIRAFCFDATKALKLEvmdgvdgapPFL 225
Cdd:pfam01728 21 PGKTVLDLGAAPGGWSQ--VALQRGAGKVVGVDLGPMQLWKPRNDP---GVTFIQGDIRDPETLDLLE---------ELL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046865904 226 PESFDRILLDApcsglgqRPNMACTWTLKEVTSYQpLQRKLLNVAVRLLKPGGVLV 281
Cdd:pfam01728 87 GRKVDLVLSDG-------SPFISGNKVLDHLRSLD-LVKAALEVALELLRKGGNFV 134
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
145-284 |
6.75e-05 |
|
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 43.01 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 145 QPGEKILDLCAapGGKTTHIAALMRDqGEVIALDkILTK-VTKLKQNASLLGLHSIRAFCFDATKalklevmdgvdgaPP 223
Cdd:COG1041 25 KEGDTVLDPFC--GTGTILIEAGLLG-RRVIGSD-IDPKmVEGARENLEHYGYEDADVIRGDARD-------------LP 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046865904 224 FLPESFDRILLDAPcsgLGQRPnmacTWTLKEVTSyqpLQRKLLNVAVRLLKPGGVLVYST 284
Cdd:COG1041 88 LADESVDAIVTDPP---YGRSS----KISGEELLE---LYEKALEEAARVLKPGGRVVIVT 138
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
147-301 |
6.90e-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: 44.40 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 147 GEKILDLCAAPGGKTthIAALMRDQGEVIALDKILTKVTKLKQNASLLGL----HSIRAFCFDATKALKLEvmdgvdgap 222
Cdd:COG1092 217 GKRVLNLFSYTGGFS--VHAAAGGAKSVTSVDLSATALEWAKENAALNGLddrhEFVQADAFDWLRELARE--------- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 223 pflPESFDRILLDAPC-----SGL--GQRpnmactwtlkevtSYqplqRKLLNVAVRLLKPGGVLVYSTCT--VTLAENE 293
Cdd:COG1092 286 ---GERFDLIILDPPAfakskKDLfdAQR-------------DY----KDLNRLALKLLAPGGILVTSSCSrhFSLDLFL 345
|
....*...
gi 1046865904 294 EQVAWALR 301
Cdd:COG1092 346 EILARAAR 353
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
150-278 |
7.62e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 41.40 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 150 ILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHsIRAFCFDATkalklevmdgvdgAPPFLPESF 229
Cdd:pfam13649 1 VLDLGCGTGRLTLALAR--RGGARVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAE-------------DLPFPDGSF 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1046865904 230 DRILldapcsglgqrpnmaCTWTLKEVTsyQPLQRKLLNVAVRLLKPGG 278
Cdd:pfam13649 65 DLVV---------------SSGVLHHLP--DPDLEAALREIARVLKPGG 96
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
56-286 |
1.70e-04 |
|
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: 42.84 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 56 RVNTHLGSVEHvrglllEEL-QKQFG-------GSSIPVLQhPALPDvllIPMTGPRGigirmTEPIYlsPSfDnvlSGY 127
Cdd:COG2519 24 KFHTHKGIIDH------DDLiGKPEGsvvttskGKEFLVLR-PTLYD---YVLSMKRG-----TQIIY--PK-D---AGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 128 IflqnlpstvvAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHsirafcfdat 207
Cdd:COG2519 83 I----------IARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLP---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 208 KALKLEVMDGVDGAPPflpESFDRILLD--APcsglgqrpnmactWtlkevtsyqplqrKLLNVAVRLLKPGGVLV-YST 284
Cdd:COG2519 143 DNVELKLGDIREGIDE---GDVDAVFLDmpDP-------------W-------------EALEAVAKALKPGGVLVaYVP 193
|
..
gi 1046865904 285 CT 286
Cdd:COG2519 194 TV 195
|
|
| PRK14967 |
PRK14967 |
putative methyltransferase; Provisional |
146-330 |
1.89e-04 |
|
putative methyltransferase; Provisional
Pssm-ID: 184931 [Multi-domain] Cd Length: 223 Bit Score: 42.35 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 146 PGEKILDLCAAPGGKTTHIAALmrDQGEVIALDKILTKVTKLKQNASLLGLHsIRAFCFDATKALKLEVMDGVDGAPPFL 225
Cdd:PRK14967 36 PGRRVLDLCTGSGALAVAAAAA--GAGSVTAVDISRRAVRSARLNALLAGVD-VDVRRGDWARAVEFRPFDVVVSNPPYV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 226 PESFDRilldAPCSGLGQrpnmacTWtlkevtSYQPLQRKLLN----VAVRLLKPGGVL--VYSTC---TVTLAENEEQ- 295
Cdd:PRK14967 113 PAPPDA----PPSRGPAR------AW------DAGPDGRAVLDrlcdAAPALLAPGGSLllVQSELsgvERTLTRLSEAg 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1046865904 296 -----VAWALRTF-PClqLQPQEPQIGGEGMLGAGLSLEQL 330
Cdd:PRK14967 177 ldaevVASQWIPFgPV--LRARAAWLERRGLLPPGQREEEL 215
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
146-284 |
1.91e-04 |
|
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: 40.77 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 146 PGEKILDLCAAPGgkttHIAALMRDQG-EVIALDKILTKVTKLKQNASLLGlhsIRAFCFDATKAlklevmdgvdgapPF 224
Cdd:COG2227 24 AGGRVLDVGCGTG----RLALALARRGaDVTGVDISPEALEIARERAAELN---VDFVQGDLEDL-------------PL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 225 LPESFDRILldapCSglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLVYST 284
Cdd:COG2227 84 EDGSFDLVI----CS---------------EVLEHLPDPAALLRELARLLKPGGLLLLST 124
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
142-281 |
1.96e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 42.62 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 142 LDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKiltkvtklkqNASLLGLHSIRAfcfdATKALKLEVMDGVDGA 221
Cdd:PRK08317 15 LAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDR----------SEAMLALAKERA----AGLGPNVEFVRGDADG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 222 PPFLPESFDRILLDapcsglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLV 281
Cdd:PRK08317 81 LPFPDGSFDAVRSD-------------------RVLQHLEDPARALAEIARVLRPGGRVV 121
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
138-283 |
3.47e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 41.44 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 138 VAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQgeVIALDKILTKVTKLKQNASLLGLHSIRafcfdatkalkLEVMDg 217
Cdd:COG0500 18 LALLERLPKGGRVLDLGCGTGRNLLALAARFGGR--VIGIDLSPEAIALARARAAKAGLGNVE-----------FLVAD- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046865904 218 VDGAPPFLPESFDRILLdapcsglgqrpNMACTWTLKEVtsyqplQRKLLNVAVRLLKPGGVLVYS 283
Cdd:COG0500 84 LAELDPLPAESFDLVVA-----------FGVLHHLPPEE------REALLRELARALKPGGVLLLS 132
|
|
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
142-240 |
6.68e-04 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 41.68 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 142 LDPQPGEKILDLCAAPGGKTTHIAalmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALKLEvmdgvdga 221
Cdd:PRK13168 293 LDPQPGDRVLDLFCGLGNFTLPLA---RQAAEVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQ-------- 361
|
90
....*....|....*....
gi 1046865904 222 pPFLPESFDRILLDAPCSG 240
Cdd:PRK13168 362 -PWALGGFDKVLLDPPRAG 379
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
144-281 |
1.38e-03 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 39.73 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046865904 144 PQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgapP 223
Cdd:pfam01209 40 VKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEEL-------------P 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1046865904 224 FLPESFDRILLdapcsGLGqrpnmactwtLKEVTSYQplqrKLLNVAVRLLKPGGVLV 281
Cdd:pfam01209 107 FEDDSFDIVTI-----SFG----------LRNFPDYL----KVLKEAFRVLKPGGRVV 145
|
|
| RlmE |
COG0293 |
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
146-178 |
1.75e-03 |
|
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 39.28 E-value: 1.75e-03
10 20 30
....*....|....*....|....*....|...
gi 1046865904 146 PGEKILDLCAAPGGKTTHIAALMRDQGEVIALD 178
Cdd:COG0293 50 PGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82
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