|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
46-323 |
4.11e-75 |
|
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: 239.52 E-value: 4.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 46 LSHPPLftTVRVNTHLGSVEHVrgllLEELQKFGgssIPVLQHPALPDVLLIPMTGPrgigirmtepIYLSPSFDNvlsG 125
Cdd:COG0144 172 NEPPPL--DLRVNTLKASREEL----LARLAEEG---IEAEPTPLSPDGLRLEGPGP----------VTALPGFRE---G 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 126 YIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDA 205
Cdd:COG0144 230 LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 206 TKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYS 282
Cdd:COG0144 310 RELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVYS 377
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958709381 283 TCTVTLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMLGAG 323
Cdd:COG0144 378 TCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
34-303 |
1.07e-66 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 217.74 E-value: 1.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 34 EAERNFETLLLRlshPPlfTTVRVNTHLGSVEHvrglLLEELQKFGgssIPVLQHPALPDVLLIPmtgpRGigirmtePI 113
Cdd:PRK14902 165 KAEKILESLNEP---PK--ASIRVNTLKISVEE----LIEKLEEEG---YEVEESLLSPEALVIE----KG-------NI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 114 YLSPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLL 193
Cdd:PRK14902 222 AGTDLFKD---GLITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 194 GLHSIRAFCFDATKalklevmdgvdgAPPFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAV 270
Cdd:PRK14902 299 GLTNIETKALDARK------------VHEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVA 366
|
250 260 270
....*....|....*....|....*....|...
gi 1958709381 271 RLLKPGGVLVYSTCTVTLAENEEQVAWALRTFP 303
Cdd:PRK14902 367 QYLKKGGILVYSTCTIEKEENEEVIEAFLEEHP 399
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
138-332 |
3.95e-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: 3.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 138 AHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKalklevmdgv 217
Cdd:pfam01189 1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 218 dgaPPFLP--ESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENE 292
Cdd:pfam01189 71 ---PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958709381 293 EQVAWALRTFPCLQLQPqepqIGGEGMLGAGLSLEQLKQL 332
Cdd:pfam01189 148 AVIEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL 183
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
123-376 |
2.38e-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: 2.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 123 LSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFC 202
Cdd:TIGR00446 49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 203 FDATKalklevmdgvdgAPPFLPEsFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVL 279
Cdd:TIGR00446 129 ADGRK------------FGAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 280 VYSTCTVTLAENEEQVAWALRTFPCLQLqpqEPQIGGEgMLGAGLSLEQLKQLQRFDPcvvplesmdtnslgdarredvi 359
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDE-FFGINIGKGEVKGALRVFP---------------------- 249
|
250
....*....|....*..
gi 1958709381 360 wlANKDCIGFFIAKFLK 376
Cdd:TIGR00446 250 --QNYDCEGFFVAKLRK 264
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
148-282 |
1.65e-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: 54.74 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 148 KILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgaPPFLPES 227
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958709381 228 FDRILLDAPCSGLgqrpnmactwtlkevtsyQPLQRKLLNVAVRLLKPGGVLVYS 282
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 ... |
46-323 |
4.11e-75 |
|
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: 239.52 E-value: 4.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 46 LSHPPLftTVRVNTHLGSVEHVrgllLEELQKFGgssIPVLQHPALPDVLLIPMTGPrgigirmtepIYLSPSFDNvlsG 125
Cdd:COG0144 172 NEPPPL--DLRVNTLKASREEL----LARLAEEG---IEAEPTPLSPDGLRLEGPGP----------VTALPGFRE---G 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 126 YIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDA 205
Cdd:COG0144 230 LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 206 TKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYS 282
Cdd:COG0144 310 RELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVYS 377
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958709381 283 TCTVTLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMLGAG 323
Cdd:COG0144 378 TCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
34-303 |
1.07e-66 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 217.74 E-value: 1.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 34 EAERNFETLLLRlshPPlfTTVRVNTHLGSVEHvrglLLEELQKFGgssIPVLQHPALPDVLLIPmtgpRGigirmtePI 113
Cdd:PRK14902 165 KAEKILESLNEP---PK--ASIRVNTLKISVEE----LIEKLEEEG---YEVEESLLSPEALVIE----KG-------NI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 114 YLSPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLL 193
Cdd:PRK14902 222 AGTDLFKD---GLITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 194 GLHSIRAFCFDATKalklevmdgvdgAPPFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAV 270
Cdd:PRK14902 299 GLTNIETKALDARK------------VHEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVA 366
|
250 260 270
....*....|....*....|....*....|...
gi 1958709381 271 RLLKPGGVLVYSTCTVTLAENEEQVAWALRTFP 303
Cdd:PRK14902 367 QYLKKGGILVYSTCTIEKEENEEVIEAFLEEHP 399
|
|
| PRK14901 |
PRK14901 |
16S rRNA methyltransferase B; Provisional |
56-325 |
1.67e-60 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237856 [Multi-domain] Cd Length: 434 Bit Score: 201.31 E-value: 1.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 56 RVNTHLGSVEHVRglllEELQKFGGSSIPVlqhPALPDVLLIpmTGPRGigirmtePIYLSPSFDNvlsGYIFLQNLPST 135
Cdd:PRK14901 182 RINPLRTSLEEVQ----AALAEAGITATPI---PGLPQGLRL--TGNPG-------SIRQLPGYEE---GWWTVQDRSAQ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 136 VVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALklevmd 215
Cdd:PRK14901 243 LVAPLLDPQPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSASRLKKLQENAQRLGLKSIKILAADSRNLL------ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 216 gvdGAPPFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENE 292
Cdd:PRK14901 317 ---ELKPQWRGYFDRILLDAPCSGLGtlhRHPDARWRQTPEKIQELAPLQAELLESLAPLLKPGGTLVYATCTLHPAENE 393
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958709381 293 EQVAWALRTFPCLQLQPQEPQI-----GGEGMLGAGLS 325
Cdd:PRK14901 394 AQIEQFLARHPDWKLEPPKQKIwphrqDGDGFFMAVLR 431
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
138-332 |
3.95e-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: 3.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 138 AHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKalklevmdgv 217
Cdd:pfam01189 1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 218 dgaPPFLP--ESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENE 292
Cdd:pfam01189 71 ---PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958709381 293 EQVAWALRTFPCLQLQPqepqIGGEGMLGAGLSLEQLKQL 332
Cdd:pfam01189 148 AVIEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL 183
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
123-376 |
2.38e-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: 2.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 123 LSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFC 202
Cdd:TIGR00446 49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 203 FDATKalklevmdgvdgAPPFLPEsFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVL 279
Cdd:TIGR00446 129 ADGRK------------FGAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 280 VYSTCTVTLAENEEQVAWALRTFPCLQLqpqEPQIGGEgMLGAGLSLEQLKQLQRFDPcvvplesmdtnslgdarredvi 359
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDE-FFGINIGKGEVKGALRVFP---------------------- 249
|
250
....*....|....*..
gi 1958709381 360 wlANKDCIGFFIAKFLK 376
Cdd:TIGR00446 250 --QNYDCEGFFVAKLRK 264
|
|
| PRK14904 |
PRK14904 |
16S rRNA methyltransferase B; Provisional |
113-309 |
2.68e-45 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237858 [Multi-domain] Cd Length: 445 Bit Score: 161.77 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 113 IYLSPSFDN----VLSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQ 188
Cdd:PRK14904 214 FFLSKDFSLfepfLKLGLVSVQNPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYPQKLEKIRS 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 189 NASLLGLHSIRAFCFDATKalklevmdgvdgappFLPE-SFDRILLDAPCSG---LGQRPNMACTWTLKEVTSYQPLQRK 264
Cdd:PRK14904 294 HASALGITIIETIEGDARS---------------FSPEeQPDAILLDAPCTGtgvLGRRAELRWKLTPEKLAELVGLQAE 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958709381 265 LLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQLQP 309
Cdd:PRK14904 359 LLDHAASLLKPGGVLVYATCSIEPEENELQIEAFLQRHPEFSAEP 403
|
|
| rsmB |
TIGR00563 |
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ... |
33-316 |
5.39e-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: 157.72 E-value: 5.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 33 QEAERNFETLLLR--LSHPPLftTVRVNthlgSVEHVRGLLLEELQKFGGSSIPVLQHPALPDvLLIPMtgprgigirmt 110
Cdd:TIGR00563 146 QKAYPGQWQSICEanNQRPPM--WLRIN----RTKHSRDEWLALLAEAGMKGFPHDLAPDAVR-LETPA----------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 111 ePIYLSPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRdQGEVIALDKILTKVTKLKQNA 190
Cdd:TIGR00563 208 -AVHALPGFEE---GWVTVQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELAP-QAQVVALDIHEHRLKRVYENL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 191 SLLGLhsirafcfdatkALKLEVMDGVDGAPPFLPES--FDRILLDAPCSGLG---QRPNMacTWTLKEVTSYQ--PLQR 263
Cdd:TIGR00563 283 KRLGL------------TIKAETKDGDGRGPSQWAENeqFDRILLDAPCSATGvirRHPDI--KWLRKPRDIAElaELQS 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958709381 264 KLLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQL----QPQEPQIGG 316
Cdd:TIGR00563 349 EILDAIWPLLKTGGTLVYATCSVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
|
|
| PRK10901 |
PRK10901 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
47-310 |
1.02e-43 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 236790 [Multi-domain] Cd Length: 427 Bit Score: 156.89 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 47 SHPPLftTVRVNTHLGSVEHVrgllLEELQKFGGSSIPvlqHPALPDvllipmtgprgiGIRMTEPI---YLsPSFDnvl 123
Cdd:PRK10901 168 QRPPM--WLRVNRRHHSRDAY----LALLAEAGIEAFP---HAVGPD------------AIRLETPVpvhQL-PGFA--- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 124 SGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALmRDQGEVIALDKILTKVTKLKQNASLLGLHSiRAFCF 203
Cdd:PRK10901 223 EGWVSVQDAAAQLAATLLAPQNGERVLDACAAPGGKTAHILEL-APQAQVVALDIDAQRLERVRENLQRLGLKA-TVIVG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 204 DATKALKLevmdgVDGAPpflpesFDRILLDAPCSGLG-----------QRPNmactwtlkEVTSYQPLQRKLLNVAVRL 272
Cdd:PRK10901 301 DARDPAQW-----WDGQP------FDRILLDAPCSATGvirrhpdikwlRRPE--------DIAALAALQSEILDALWPL 361
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958709381 273 LKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQLQPQ 310
Cdd:PRK10901 362 LKPGGTLLYATCSILPEENEQQIKAFLARHPDAELLDT 399
|
|
| PRK14903 |
PRK14903 |
16S rRNA methyltransferase B; Provisional |
43-301 |
1.17e-33 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 184896 [Multi-domain] Cd Length: 431 Bit Score: 129.61 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 43 LLRLSHPPLFTTVRVNthlgSVEHVRGLLLEELQKFGGSSIPVlqhPALPDVLLIpmtgpRGIGIRMTEpiylspsFDNV 122
Cdd:PRK14903 154 IMEWNQEPLPTMLRVN----SLAITREEVIKILAEEGTEAVPG---KHSPFSLIV-----RKLGVNMND-------SRVI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 123 LSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFC 202
Cdd:PRK14903 215 KDGLATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEKHAKRLKLSSIEIKI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 203 FDATKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVL 279
Cdd:PRK14903 295 ADAERLTE------------YVQDTFDRILVDAPCTSLGtarNHPEVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGIL 362
|
250 260
....*....|....*....|...
gi 1958709381 280 VYSTCTVTLAENEEQV-AWALRT 301
Cdd:PRK14903 363 LYSTCTVTKEENTEVVkRFVYEQ 385
|
|
| yebU |
PRK11933 |
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed |
123-303 |
1.59e-32 |
|
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
Pssm-ID: 183387 [Multi-domain] Cd Length: 470 Bit Score: 127.33 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 123 LSGYIFLQN----LPstVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSI 198
Cdd:PRK11933 89 LSGLFYIQEassmLP--VAALFADDNAPQRVLDMAAAPGSKTTQIAALMNNQGAIVANEYSASRVKVLHANISRCGVSNV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 199 RAFCFDATkalklevmdgVDGAppFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKP 275
Cdd:PRK11933 167 ALTHFDGR----------VFGA--ALPETFDAILLDAPCSGEGtvrKDPDALKNWSPESNLEIAATQRELIESAFHALKP 234
|
170 180
....*....|....*....|....*...
gi 1958709381 276 GGVLVYSTCTVTLAENEEQVAWALRTFP 303
Cdd:PRK11933 235 GGTLVYSTCTLNREENQAVCLWLKETYP 262
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
148-282 |
1.65e-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: 54.74 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 148 KILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgaPPFLPES 227
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958709381 228 FDRILLDAPCSGLgqrpnmactwtlkevtsyQPLQRKLLNVAVRLLKPGGVLVYS 282
Cdd:cd02440 67 FDVIISDPPLHHL------------------VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
119-280 |
4.20e-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: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 119 FDNVLSGYIFLQNLpstvvAHVLDPQPGEKILDLCAAPGgktTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHsI 198
Cdd:COG2226 1 FDRVAARYDGREAL-----LAALGLRPGARVLDLGCGTG---RLALALAERGARVTGVDISPEMLELARERAAEAGLN-V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 199 RAFCFDATkalklevmdgvdgAPPFLPESFDRILldapcsglgqrpnmaCTWTLKEVTSyqplQRKLLNVAVRLLKPGGV 278
Cdd:COG2226 72 EFVVGDAE-------------DLPFPDGSFDLVI---------------SSFVLHHLPD----PERALAEIARVLKPGGR 119
|
..
gi 1958709381 279 LV 280
Cdd:COG2226 120 LV 121
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
145-319 |
1.83e-06 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 47.41 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 145 PGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALKLevmdgvdgappFL 224
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPEL-----------LE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 225 PESFDRILLDapcsglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCtVTLAENEEQVawaLRTFPC 304
Cdd:pfam13847 72 DDKFDVVISN-------------------CVLNHIPDPDKVLQEILRVLKPGGRLIISDP-DSLAELPAHV---KEDSTY 128
|
170
....*....|....*
gi 1958709381 305 LQLQPQEPQIGGEGM 319
Cdd:pfam13847 129 YAGCVGGAILKKKLY 143
|
|
| Trm5 |
COG2520 |
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
145-281 |
1.63e-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: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 145 PGEKILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGL-HSIRAFCFDATKalklevmdgvdgAPPF 223
Cdd:COG2520 180 PGERVLDMFAGVGPFSIPIAK--RSGAKVVAIDINPDAVEYLKENIRLNKVeDRVTPILGDARE------------VAPE 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958709381 224 LPESFDRILLDAPCSGLgqrpnmactwtlkevtsyqplqrKLLNVAVRLLKPGGVLVY 281
Cdd:COG2520 246 LEGKADRIIMNLPHSAD-----------------------EFLDAALRALKPGGVIHY 280
|
|
| FtsJ |
pfam01728 |
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
145-280 |
5.37e-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: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 145 PGEKILDLCAAPGGKTThiAALMRDQGEVIALDKILTKVTKLKQNAsllGLHSIRAFCFDATKALKLEvmdgvdgapPFL 224
Cdd:pfam01728 21 PGKTVLDLGAAPGGWSQ--VALQRGAGKVVGVDLGPMQLWKPRNDP---GVTFIQGDIRDPETLDLLE---------ELL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958709381 225 PESFDRILLDApcsglgqRPNMACTWTLKEVTSYQpLQRKLLNVAVRLLKPGGVLV 280
Cdd:pfam01728 87 GRKVDLVLSDG-------SPFISGNKVLDHLRSLD-LVKAALEVALELLRKGGNFV 134
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
144-283 |
6.73e-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: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 144 QPGEKILDLCAapGGKTTHIAALMRDqGEVIALDkILTK-VTKLKQNASLLGLHSIRAFCFDATKalklevmdgvdgaPP 222
Cdd:COG1041 25 KEGDTVLDPFC--GTGTILIEAGLLG-RRVIGSD-IDPKmVEGARENLEHYGYEDADVIRGDARD-------------LP 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958709381 223 FLPESFDRILLDAPcsgLGQRPnmacTWTLKEVTSyqpLQRKLLNVAVRLLKPGGVLVYST 283
Cdd:COG1041 88 LADESVDAIVTDPP---YGRSS----KISGEELLE---LYEKALEEAARVLKPGGRVVIVT 138
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
146-300 |
6.81e-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: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 146 GEKILDLCAAPGGKTthIAALMRDQGEVIALDKILTKVTKLKQNASLLGL----HSIRAFCFDATKALKLEvmdgvdgap 221
Cdd:COG1092 217 GKRVLNLFSYTGGFS--VHAAAGGAKSVTSVDLSATALEWAKENAALNGLddrhEFVQADAFDWLRELARE--------- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 222 pflPESFDRILLDAPC-----SGL--GQRpnmactwtlkevtSYqplqRKLLNVAVRLLKPGGVLVYSTCT--VTLAENE 292
Cdd:COG1092 286 ---GERFDLIILDPPAfakskKDLfdAQR-------------DY----KDLNRLALKLLAPGGILVTSSCSrhFSLDLFL 345
|
....*...
gi 1958709381 293 EQVAWALR 300
Cdd:COG1092 346 EILARAAR 353
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
149-277 |
7.60e-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: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 149 ILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHsIRAFCFDATkalklevmdgvdgAPPFLPESF 228
Cdd:pfam13649 1 VLDLGCGTGRLTLALAR--RGGARVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAE-------------DLPFPDGSF 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958709381 229 DRILldapcsglgqrpnmaCTWTLKEVTsyQPLQRKLLNVAVRLLKPGG 277
Cdd:pfam13649 65 DLVV---------------SSGVLHHLP--DPDLEAALREIARVLKPGG 96
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
141-280 |
1.95e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 42.62 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 141 LDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKiltkvtklkqNASLLGLHSIRAfcfdATKALKLEVMDGVDGA 220
Cdd:PRK08317 15 LAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDR----------SEAMLALAKERA----AGLGPNVEFVRGDADG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 221 PPFLPESFDRILLDapcsglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLV 280
Cdd:PRK08317 81 LPFPDGSFDAVRSD-------------------RVLQHLEDPARALAEIARVLRPGGRVV 121
|
|
| PRK14967 |
PRK14967 |
putative methyltransferase; Provisional |
145-329 |
1.99e-04 |
|
putative methyltransferase; Provisional
Pssm-ID: 184931 [Multi-domain] Cd Length: 223 Bit Score: 42.35 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 145 PGEKILDLCAAPGGKTTHIAALmrDQGEVIALDKILTKVTKLKQNASLLGLHsIRAFCFDATKALKLEVMDGVDGAPPFL 224
Cdd:PRK14967 36 PGRRVLDLCTGSGALAVAAAAA--GAGSVTAVDISRRAVRSARLNALLAGVD-VDVRRGDWARAVEFRPFDVVVSNPPYV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 225 PESFDRilldAPCSGLGQrpnmacTWtlkevtSYQPLQRKLLN----VAVRLLKPGGVL--VYSTC---TVTLAENEEQ- 294
Cdd:PRK14967 113 PAPPDA----PPSRGPAR------AW------DAGPDGRAVLDrlcdAAPALLAPGGSLllVQSELsgvERTLTRLSEAg 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958709381 295 -----VAWALRTF-PClqLQPQEPQIGGEGMLGAGLSLEQL 329
Cdd:PRK14967 177 ldaevVASQWIPFgPV--LRARAAWLERRGLLPPGQREEEL 215
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
145-283 |
2.16e-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: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 145 PGEKILDLCAAPGgkttHIAALMRDQG-EVIALDKILTKVTKLKQNASLLGlhsIRAFCFDATKAlklevmdgvdgapPF 223
Cdd:COG2227 24 AGGRVLDVGCGTG----RLALALARRGaDVTGVDISPEALEIARERAAELN---VDFVQGDLEDL-------------PL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 224 LPESFDRILldapCSglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLVYST 283
Cdd:COG2227 84 EDGSFDLVI----CS---------------EVLEHLPDPAALLRELARLLKPGGLLLLST 124
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
137-282 |
3.62e-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: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 137 VAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQgeVIALDKILTKVTKLKQNASLLGLHSIRafcfdatkalkLEVMDg 216
Cdd:COG0500 18 LALLERLPKGGRVLDLGCGTGRNLLALAARFGGR--VIGIDLSPEAIALARARAAKAGLGNVE-----------FLVAD- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958709381 217 VDGAPPFLPESFDRILLdapcsglgqrpNMACTWTLKEVtsyqplQRKLLNVAVRLLKPGGVLVYS 282
Cdd:COG0500 84 LAELDPLPAESFDLVVA-----------FGVLHHLPPEE------REALLRELARALKPGGVLLLS 132
|
|
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
141-239 |
6.65e-04 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 41.68 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958709381 141 LDPQPGEKILDLCAAPGGKTTHIAalmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALKLEvmdgvdga 220
Cdd:PRK13168 293 LDPQPGDRVLDLFCGLGNFTLPLA---RQAAEVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQ-------- 361
|
90
....*....|....*....
gi 1958709381 221 pPFLPESFDRILLDAPCSG 239
Cdd:PRK13168 362 -PWALGGFDKVLLDPPRAG 379
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
143-280 |
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 1958709381 143 PQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgapP 222
Cdd:pfam01209 40 VKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEEL-------------P 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958709381 223 FLPESFDRILLdapcsGLGqrpnmactwtLKEVTSYQplqrKLLNVAVRLLKPGGVLV 280
Cdd:pfam01209 107 FEDDSFDIVTI-----SFG----------LRNFPDYL----KVLKEAFRVLKPGGRVV 145
|
|
| RlmE |
COG0293 |
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
145-177 |
1.74e-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: 1.74e-03
10 20 30
....*....|....*....|....*....|...
gi 1958709381 145 PGEKILDLCAAPGGKTTHIAALMRDQGEVIALD 177
Cdd:COG0293 50 PGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82
|
|
|