|
Name |
Accession |
Description |
Interval |
E-value |
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
7-335 |
7.46e-83 |
|
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: 256.26 E-value: 7.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 7 LANALEKRQDLLaqvKADNTDCFRVFHGTVEGVNGLNIDRYGDAWLIQTFhqTLG-EDELQQIQASLVQLADLPIVYnDR 85
Cdd:COG1092 80 LRKALALRRKLA---KREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEY--SAGmERRRDEILEALVEVLGPEGIY-LR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 86 SNKNSRVLNSMDAETEAFAQSAQ---VMQENGIKFTTKLrHEGQDPLLFLDMRVGREFVKANSHNKTVLNLFSYTCGIGT 162
Cdd:COG1092 154 SDVRVRQLEGLPQYEGVLYGEAPeevEVEENGLKFLVDL-TDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 163 AAAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQVCEFIQSDAFPALRQLAglkvggRRNQklpaypklsatQFDLVFLD 242
Cdd:COG1092 233 HAAAGGAKSVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDWLRELA------REGE-----------RFDLIILD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 243 PPRFAKSPFGTVDLINDYQSLFKPALLTTKKGGTIVCCNNVAKVERDTWFNALVRCVEKQGRSVTNHTWLNCHEDFP--- 319
Cdd:COG1092 296 PPAFAKSKKDLFDAQRDYKDLNRLALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPvlp 375
|
330
....*....|....*.
gi 752774872 320 SFDGNHPLKMVALTID 335
Cdd:COG1092 376 AFPEGEYLKGLLLRVL 391
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
30-330 |
1.06e-33 |
|
S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.
Pssm-ID: 287624 [Multi-domain] Cd Length: 286 Bit Score: 125.38 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 30 RVFHGT---VEGVNGLNIDrYGDAWLIQTFHQTLGEDELQQIQASLVQLADLPIvYNDRSNKnSRVLNSM---DAETEAF 103
Cdd:pfam10672 2 RLFHGRgrcWPGLEQLTCD-WLQGQLLVNLFKEVDPAFLQALKRGLEQLTTAPA-WAAKQGR-HLVLQHRyadGAPSEVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 104 A---QSAQVMQENGIKFTTKLrHEGQDPLLFLDMRVGREFVKANSHNKTVLNLFSYTCGIGTAAAVGGAKRVVNIDFSSF 180
Cdd:pfam10672 79 SgelLETPVVVENGLKYQLDI-GRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 181 ALAAGKKNAELN--DVTQVcEFIQSDAFpalRQLAGLKVGGrrnqklpaypklsatQFDLVFLDPPRFAKSPFGtvdLIN 258
Cdd:pfam10672 158 SLNKGRDNHRLNghDLGRV-SFLGHDIF---KSWGKIKKLG---------------PYDLVIIDPPSFQKGSFA---LTK 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752774872 259 DYQSLFK--PALLTtkKGGTIVCCNNVAKVERDTwfnaLVRCVEKQGRSVTNHTWLNCHEDFPSFDGNHPLKMV 330
Cdd:pfam10672 216 DYKKILRrlPELLV--EGGTVLACVNSPAVGPDF----LIEEMAEEAPSLHFVERLDNPPEFPDVDPAAGLKVL 283
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
7-310 |
1.43e-20 |
|
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;
Pssm-ID: 236981 [Multi-domain] Cd Length: 702 Bit Score: 92.56 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 7 LANALEK-RQDLLAQVKADNTDCFRVFHGTVEGVNgLNIDRYGDAWLIQTFH--QTLGEDELQQ-----IQASLVQLaDL 78
Cdd:PRK11783 395 FANRLRKnLKKLKKWAKQEGIECYRLYDADLPEYN-VAVDRYGDWVVVQEYAapKTIDEEKARQrlfdaLAATPEVL-GI 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 79 P---IVYNDRS-NKNSRVLNSMDAETEAFaqsaqVMQENGIKFTTKLrhegQDPL---LFLDMRVGREFVKANSHNKTVL 151
Cdd:PRK11783 473 PpnkVVLKTRErQKGKNQYQKLAEKGEFL-----EVTEYGAKLLVNL----TDYLdtgLFLDHRPTRRMIGQMAKGKDFL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 152 NLFSYTcgiGTA---AAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQV-CEFIQSDAFPALRQlaglkvgGRRnqklpa 227
Cdd:PRK11783 544 NLFAYT---GTAsvhAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRqHRLIQADCLAWLKE-------ARE------ 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 228 ypklsatQFDLVFLDPPRFA--KSPFGTVDLINDYQSLFKPALLTTKKGGTIVCCNNVAKVERDtwFNALvrcvEKQGRS 305
Cdd:PRK11783 608 -------QFDLIFIDPPTFSnsKRMEDSFDVQRDHVALIKDAKRLLRPGGTLYFSNNKRGFKMD--EEGL----AKLGLK 674
|
....*
gi 752774872 306 VTNHT 310
Cdd:PRK11783 675 AEEIT 679
|
|
| RlmI_M_like |
cd11572 |
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ... |
7-93 |
1.21e-09 |
|
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or central domain is typically found between an N-terminal PUA domain and a C-terminal SAM-dependent methyltransferase domain, such as in the Escherichia coli ribosomal RNA large subunit methyltransferase RlmI (YccW). It may be involved in binding to the RNA substrate.
Pssm-ID: 211413 [Multi-domain] Cd Length: 99 Bit Score: 54.78 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 7 LANALEKRQDLLAqvkaDNTDCFRVFHGtvE--GVNGLNIDRYGDAWLIQTFhqTLG-EDELQQIQASLVQLADLPIVYn 83
Cdd:cd11572 7 IEKALALRKRLLL----DDTNAYRLVHG--EgdGLPGLIVDRYGDVLVVQIL--SAGmERLKELIVEALKELLGPKGIY- 77
|
90
....*....|
gi 752774872 84 DRSNKNSRVL 93
Cdd:cd11572 78 ERSDAAVREL 87
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
7-335 |
7.46e-83 |
|
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: 256.26 E-value: 7.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 7 LANALEKRQDLLaqvKADNTDCFRVFHGTVEGVNGLNIDRYGDAWLIQTFhqTLG-EDELQQIQASLVQLADLPIVYnDR 85
Cdd:COG1092 80 LRKALALRRKLA---KREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEY--SAGmERRRDEILEALVEVLGPEGIY-LR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 86 SNKNSRVLNSMDAETEAFAQSAQ---VMQENGIKFTTKLrHEGQDPLLFLDMRVGREFVKANSHNKTVLNLFSYTCGIGT 162
Cdd:COG1092 154 SDVRVRQLEGLPQYEGVLYGEAPeevEVEENGLKFLVDL-TDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 163 AAAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQVCEFIQSDAFPALRQLAglkvggRRNQklpaypklsatQFDLVFLD 242
Cdd:COG1092 233 HAAAGGAKSVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDWLRELA------REGE-----------RFDLIILD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 243 PPRFAKSPFGTVDLINDYQSLFKPALLTTKKGGTIVCCNNVAKVERDTWFNALVRCVEKQGRSVTNHTWLNCHEDFP--- 319
Cdd:COG1092 296 PPAFAKSKKDLFDAQRDYKDLNRLALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPvlp 375
|
330
....*....|....*.
gi 752774872 320 SFDGNHPLKMVALTID 335
Cdd:COG1092 376 AFPEGEYLKGLLLRVL 391
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
30-330 |
1.06e-33 |
|
S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.
Pssm-ID: 287624 [Multi-domain] Cd Length: 286 Bit Score: 125.38 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 30 RVFHGT---VEGVNGLNIDrYGDAWLIQTFHQTLGEDELQQIQASLVQLADLPIvYNDRSNKnSRVLNSM---DAETEAF 103
Cdd:pfam10672 2 RLFHGRgrcWPGLEQLTCD-WLQGQLLVNLFKEVDPAFLQALKRGLEQLTTAPA-WAAKQGR-HLVLQHRyadGAPSEVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 104 A---QSAQVMQENGIKFTTKLrHEGQDPLLFLDMRVGREFVKANSHNKTVLNLFSYTCGIGTAAAVGGAKRVVNIDFSSF 180
Cdd:pfam10672 79 SgelLETPVVVENGLKYQLDI-GRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 181 ALAAGKKNAELN--DVTQVcEFIQSDAFpalRQLAGLKVGGrrnqklpaypklsatQFDLVFLDPPRFAKSPFGtvdLIN 258
Cdd:pfam10672 158 SLNKGRDNHRLNghDLGRV-SFLGHDIF---KSWGKIKKLG---------------PYDLVIIDPPSFQKGSFA---LTK 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752774872 259 DYQSLFK--PALLTtkKGGTIVCCNNVAKVERDTwfnaLVRCVEKQGRSVTNHTWLNCHEDFPSFDGNHPLKMV 330
Cdd:pfam10672 216 DYKKILRrlPELLV--EGGTVLACVNSPAVGPDF----LIEEMAEEAPSLHFVERLDNPPEFPDVDPAAGLKVL 283
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
7-310 |
1.43e-20 |
|
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;
Pssm-ID: 236981 [Multi-domain] Cd Length: 702 Bit Score: 92.56 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 7 LANALEK-RQDLLAQVKADNTDCFRVFHGTVEGVNgLNIDRYGDAWLIQTFH--QTLGEDELQQ-----IQASLVQLaDL 78
Cdd:PRK11783 395 FANRLRKnLKKLKKWAKQEGIECYRLYDADLPEYN-VAVDRYGDWVVVQEYAapKTIDEEKARQrlfdaLAATPEVL-GI 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 79 P---IVYNDRS-NKNSRVLNSMDAETEAFaqsaqVMQENGIKFTTKLrhegQDPL---LFLDMRVGREFVKANSHNKTVL 151
Cdd:PRK11783 473 PpnkVVLKTRErQKGKNQYQKLAEKGEFL-----EVTEYGAKLLVNL----TDYLdtgLFLDHRPTRRMIGQMAKGKDFL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 152 NLFSYTcgiGTA---AAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQV-CEFIQSDAFPALRQlaglkvgGRRnqklpa 227
Cdd:PRK11783 544 NLFAYT---GTAsvhAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRqHRLIQADCLAWLKE-------ARE------ 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 228 ypklsatQFDLVFLDPPRFA--KSPFGTVDLINDYQSLFKPALLTTKKGGTIVCCNNVAKVERDtwFNALvrcvEKQGRS 305
Cdd:PRK11783 608 -------QFDLIFIDPPTFSnsKRMEDSFDVQRDHVALIKDAKRLLRPGGTLYFSNNKRGFKMD--EEGL----AKLGLK 674
|
....*
gi 752774872 306 VTNHT 310
Cdd:PRK11783 675 AEEIT 679
|
|
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
15-246 |
5.50e-19 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 86.81 E-value: 5.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 15 QDLLAQvkADNTDCFRVFHGTVEGVNGLNIDRYGDAWLIQTFHQTlGEDELQQIQASLVQLADLPIVYnDRSNKNSRVLN 94
Cdd:PRK15128 90 RDWLAQ--KDGLDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAG-AEYQRAALISALQTLYPECAIY-DRSDVAVRKKE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 95 SMDAE----TEAFAQSAQVMQENGIKFTTKLRHeGQDPLLFLDMRVGREFVKANSHNKTVLNLFSYTCGIGTAAAVGGAK 170
Cdd:PRK15128 166 GMELTqgpvTGELPPALLPIEEHGMKLLVDIQG-GHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALMGGCS 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752774872 171 RVVNIDFSSFALAAGKKNAELN--DVTQVcEFIQSDAFPALRQLaglkvggrRNQklpaypklsATQFDLVFLDPPRF 246
Cdd:PRK15128 245 QVVSVDTSQEALDIARQNVELNklDLSKA-EFVRDDVFKLLRTY--------RDR---------GEKFDVIVMDPPKF 304
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
138-245 |
4.67e-12 |
|
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441866 [Multi-domain] Cd Length: 377 Bit Score: 66.35 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 138 REFVKANShNKTVLNLFsytCGIGT--AAAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQVcEFIQSDAFpalRQLAGL 215
Cdd:COG2265 226 LEWLDLTG-GERVLDLY---CGVGTfaLPLARRAKKVIGVEIVPEAVEDARENARLNGLKNV-EFVAGDLE---EVLPEL 297
|
90 100 110
....*....|....*....|....*....|
gi 752774872 216 KVGGRrnqklpaypklsatqFDLVFLDPPR 245
Cdd:COG2265 298 LWGGR---------------PDVVVLDPPR 312
|
|
| RsmD |
COG0742 |
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
146-279 |
1.62e-10 |
|
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 440505 [Multi-domain] Cd Length: 183 Bit Score: 59.32 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 146 HNKTVLNLFSytcGIGtaaAVG------GAKRVVNIDFSSFALAAGKKNAELNDVTQVCEFIQSDAFPALRQLAGlkvgg 219
Cdd:COG0742 41 EGARVLDLFA---GSG---ALGlealsrGAASVVFVEKDRKAAAVIRKNLEKLGLEDRARVIRGDALRFLKRLAG----- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 752774872 220 rrnqklpaypklsaTQFDLVFLDPPrFAKspfgtvDLIND-YQSLFKPALLttKKGGTIVC 279
Cdd:COG0742 110 --------------EPFDLVFLDPP-YAK------GLLEKaLELLAENGLL--APGGLIVV 147
|
|
| RlmI_M_like |
cd11572 |
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ... |
7-93 |
1.21e-09 |
|
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or central domain is typically found between an N-terminal PUA domain and a C-terminal SAM-dependent methyltransferase domain, such as in the Escherichia coli ribosomal RNA large subunit methyltransferase RlmI (YccW). It may be involved in binding to the RNA substrate.
Pssm-ID: 211413 [Multi-domain] Cd Length: 99 Bit Score: 54.78 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 7 LANALEKRQDLLAqvkaDNTDCFRVFHGtvE--GVNGLNIDRYGDAWLIQTFhqTLG-EDELQQIQASLVQLADLPIVYn 83
Cdd:cd11572 7 IEKALALRKRLLL----DDTNAYRLVHG--EgdGLPGLIVDRYGDVLVVQIL--SAGmERLKELIVEALKELLGPKGIY- 77
|
90
....*....|
gi 752774872 84 DRSNKNSRVL 93
Cdd:cd11572 78 ERSDAAVREL 87
|
|
| Cons_hypoth95 |
pfam03602 |
Conserved hypothetical protein 95; |
146-279 |
7.27e-08 |
|
Conserved hypothetical protein 95;
Pssm-ID: 427391 [Multi-domain] Cd Length: 179 Bit Score: 51.47 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 146 HNKTVLNLFSYTCGIGTAAAVGGAKRVVNIDfssfalaagkKNAElndvtqvcefiqsdAFPALRQ-LAGLKVGGR--RN 222
Cdd:pfam03602 41 EGARVLDLFAGSGALGLEALSRGAKRVTLVE----------KDKR--------------AVQILKEnLQLLGLPGAvlVM 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 752774872 223 QKLPAYPKLSAT--QFDLVFLDPprfaksPFGTVDLINDYQSLFKPALLttKKGGTIVC 279
Cdd:pfam03602 97 DALLALLRLAGKgpVFDIVFLDP------PYAKGLIEEVLDLLAEKGWL--KPNALIYV 147
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
149-280 |
2.34e-05 |
|
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: 42.80 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 149 TVLNLFSYTCGIGTAAAVGGAKRVVNIDFSSFALAAGKKNAeLNDVTQVCEFIQSDAFpalrqlaglkvggrrnqKLPAY 228
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAA-AALLADNVEVLKGDAE-----------------ELPPE 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 752774872 229 PKlsaTQFDLVFLDPPRFAKSPfgtvdlinDYQSLFKPALLTTKKGGTIVCC 280
Cdd:cd02440 63 AD---ESFDVIISDPPLHHLVE--------DLARFLEEARRLLKPGGVLVLT 103
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
163-207 |
7.85e-04 |
|
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 40.54 E-value: 7.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 752774872 163 AAAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQVCEFIQSDAFP 207
Cdd:COG2264 165 AAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLE 209
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
158-244 |
1.04e-03 |
|
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: 39.40 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 158 CGIG----TAAAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQVcEFIQSDAFPAlrqlaglkvggrrnqklpaypkLSA 233
Cdd:COG2813 58 CGYGviglALAKRNPEARVTLVDVNARAVELARANAAANGLENV-EVLWSDGLSG----------------------VPD 114
|
90
....*....|.
gi 752774872 234 TQFDLVFLDPP 244
Cdd:COG2813 115 GSFDLILSNPP 125
|
|
| Trm5 |
COG2520 |
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
134-214 |
1.20e-03 |
|
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: 40.23 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 134 MRVGREfVKANshnKTVLNLFsytCGIGT---AAAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQVCEFIQSDAFPALR 210
Cdd:COG2520 172 LRIAEL-VKPG---ERVLDMF---AGVGPfsiPIAKRSGAKVVAIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVAP 244
|
....
gi 752774872 211 QLAG 214
Cdd:COG2520 245 ELEG 248
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
147-281 |
1.86e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 38.17 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752774872 147 NKTVLNLFSYTCGIGTAAA--VGGAKRVVNIDFSSFALAAGKKNAELNDVTQVcEFIQSDAFPALRQLAGLKvggrrnqk 224
Cdd:pfam13847 4 GMRVLDLGCGTGHLSFELAeeLGPNAEVVGIDISEEAIEKARENAQKLGFDNV-EFEQGDIEELPELLEDDK-------- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 752774872 225 lpaypklsatqFDLVFLdpprfakspFGTVDLINDYQSLFKPALLTTKKGGTIVCCN 281
Cdd:pfam13847 75 -----------FDVVIS---------NCVLNHIPDPDKVLQEILRVLKPGGRLIISD 111
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
159-209 |
6.42e-03 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 37.82 E-value: 6.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 752774872 159 GIGTAAAVGGAkRVVNIDFSSFALAAGKKNAELNDVTQVCEFIQSDAFPAL 209
Cdd:COG2890 127 ALALAKERPDA-RVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFEPL 176
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
158-210 |
8.57e-03 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 36.80 E-value: 8.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 752774872 158 CGIGTAAAVGGAKRVVNIDFSSFALAAGKKNAELNDVTQVC-EFIQSDAFPALR 210
Cdd:PRK14968 34 SGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGvEVIRSDLFEPFR 87
|
|
| |
