|
Name |
Accession |
Description |
Interval |
E-value |
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
3-392 |
8.56e-126 |
|
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: 367.97 E-value: 8.56e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 3 KISLKQTFAEQVKKGYPLISKDAVSRVNG-VQEGELIEWVDERGSFLGKGYYGVQNKGIGWVLSFDANEKIDQAFFVSKL 81
Cdd:COG1092 1 KVRLKPGKERRLRRGHPWVFSNEIDRVEGeLEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEPIDAAFFANRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 82 EQASKSRTHLFRDAQTTAFRVFNGEGDGIGGITIDYYDGFYLIQWYSEGVYTLKEDVLAAIEQVYPDyKGIYEK-----K 156
Cdd:COG1092 81 RKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEALVEVLGP-EGIYLRsdvrvR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 157 RFDTSGQYIEdddFVKGEKGEfPLIVKENGMNVAVYLNDGAMTGIFLDQRHVRKAIRdRYAKGKTVLNTFSYTGAFSVAA 236
Cdd:COG1092 160 QLEGLPQYEG---VLYGEAPE-EVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVA-ELAKGKRVLNLFSYTGGFSVHA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 237 ALGGASRTTSVDVANRSLKKTSEQFEVNGIDvDGQDIKVMDVFKYFPFAAKKGWSYDVVILDPPSFARTKKHTFSAAKDY 316
Cdd:COG1092 235 AAGGAKSVTSVDLSATALEWAKENAALNGLD-DRHEFVQADAFDWLRELAREGERFDLIILDPPAFAKSKKDLFDAQRDY 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573276 317 KKLLKEAIQITAENGVIVASTNSSAFGMKKFKGFIAQAFKESGKTYRILEEYTLPEDFRTTKNYPEGNYLKVVFIQ 392
Cdd:COG1092 314 KDLNRLALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLR 389
|
|
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
18-387 |
3.05e-69 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 223.17 E-value: 3.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 18 YPLISKDAVSRVNG-VQEGELIEWVDERGSFLGKGYYGVQNKGIGWVLSFDANEKIDQAFFVSKLEQASKSRTHLFRDAQ 96
Cdd:PRK15128 19 HPWVFSGAVARMEGkASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDESIDIAFFTRRLQQAQKWRDWLAQKDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 97 TTAFRVFNGEGDGIGGITIDYYDGFYLIQWYSEGVYTLKEDVLAAIEQVYPDYkGIYEkkRFDTSGQYIEDDDFVKGE-K 175
Cdd:PRK15128 99 LDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPEC-AIYD--RSDVAVRKKEGMELTQGPvT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 176 GEFP---LIVKENGMNVAVYLNDGAMTGIFLDQRHVRKAIRdRYAKGKTVLNTFSYTGAFSVAAALGGASRTTSVDVANR 252
Cdd:PRK15128 176 GELPpalLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATR-RYVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSQE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 253 SLKKTSEQFEVNGIDVDGQDIKVMDVFKYFPFAAKKGWSYDVVILDPPSFARTKKHTFSAAKDYKKLLKEAIQITAENGV 332
Cdd:PRK15128 255 ALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKDINMLAIQLLNPGGI 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 518573276 333 IVASTNSSAFGMKKFKGFIAQAFKESGKTYRILEEYTLPEDFRTTKNYPEGNYLK 387
Cdd:PRK15128 335 LLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLK 389
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
101-374 |
1.17e-34 |
|
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: 129.61 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 101 RVFNGEG---DGIGGITIDYYDGFYLIQWYSEgvytLKEDVLAAIEQVYPDY--KGIYEKKRFDT---SGQYIED--DDF 170
Cdd:pfam10672 2 RLFHGRGrcwPGLEQLTCDWLQGQLLVNLFKE----VDPAFLQALKRGLEQLttAPAWAAKQGRHlvlQHRYADGapSEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 171 VKGEKGEFPLIVkENGMNVAVYLNDGAMTGIFLDQRHVRKAIRDRyAKGKTVLNTFSYTGAFSVAAALGGASRTTSVDVA 250
Cdd:pfam10672 78 LSGELLETPVVV-ENGLKYQLDIGRNQNFGLFLDMRLGRRWVQEN-AKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 251 NRSLKKTSEQFEVNGIDVDGQDIKVMDVFKYFPfAAKKGWSYDVVILDPPSFartKKHTFSAAKDYKKLLKEAIQITAEN 330
Cdd:pfam10672 156 RGSLNKGRDNHRLNGHDLGRVSFLGHDIFKSWG-KIKKLGPYDLVIIDPPSF---QKGSFALTKDYKKILRRLPELLVEG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518573276 331 GVIVASTNSSAFGmkkfKGFIAQAFKESGKTYRILEEYTLPEDF 374
Cdd:pfam10672 232 GTVLACVNSPAVG----PDFLIEEMAEEAPSLHFVERLDNPPEF 271
|
|
| RlmI_M_like |
cd11572 |
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ... |
75-173 |
1.38e-28 |
|
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: 107.16 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 75 AFFVSKLEQASKSRTHLFRDAqTTAFRVFNGEGDGIGGITIDYYDGFYLIQWYSEGVYTLKEDVLAAIEQVYPDyKGIYE 154
Cdd:cd11572 1 AFFKRRIEKALALRKRLLLDD-TNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKELLGP-KGIYE 78
|
90 100
....*....|....*....|.
gi 518573276 155 KKRFDT--SGQYIEDDDFVKG 173
Cdd:cd11572 79 RSDAAVreLEGLPEEVGVLYG 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
3-392 |
8.56e-126 |
|
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: 367.97 E-value: 8.56e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 3 KISLKQTFAEQVKKGYPLISKDAVSRVNG-VQEGELIEWVDERGSFLGKGYYGVQNKGIGWVLSFDANEKIDQAFFVSKL 81
Cdd:COG1092 1 KVRLKPGKERRLRRGHPWVFSNEIDRVEGeLEPGDLVEVEDADGRFLGRGYYNPHSQIAVRLLSRDPDEPIDAAFFANRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 82 EQASKSRTHLFRDAQTTAFRVFNGEGDGIGGITIDYYDGFYLIQWYSEGVYTLKEDVLAAIEQVYPDyKGIYEK-----K 156
Cdd:COG1092 81 RKALALRRKLAKREGTNAYRLVHGEADGLPGLIVDRYGDVLVVQEYSAGMERRRDEILEALVEVLGP-EGIYLRsdvrvR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 157 RFDTSGQYIEdddFVKGEKGEfPLIVKENGMNVAVYLNDGAMTGIFLDQRHVRKAIRdRYAKGKTVLNTFSYTGAFSVAA 236
Cdd:COG1092 160 QLEGLPQYEG---VLYGEAPE-EVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVA-ELAKGKRVLNLFSYTGGFSVHA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 237 ALGGASRTTSVDVANRSLKKTSEQFEVNGIDvDGQDIKVMDVFKYFPFAAKKGWSYDVVILDPPSFARTKKHTFSAAKDY 316
Cdd:COG1092 235 AAGGAKSVTSVDLSATALEWAKENAALNGLD-DRHEFVQADAFDWLRELAREGERFDLIILDPPAFAKSKKDLFDAQRDY 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573276 317 KKLLKEAIQITAENGVIVASTNSSAFGMKKFKGFIAQAFKESGKTYRILEEYTLPEDFRTTKNYPEGNYLKVVFIQ 392
Cdd:COG1092 314 KDLNRLALKLLAPGGILVTSSCSRHFSLDLFLEILARAARDAGRRVRIIERLTQPPDHPVLPAFPEGEYLKGLLLR 389
|
|
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
18-387 |
3.05e-69 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 223.17 E-value: 3.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 18 YPLISKDAVSRVNG-VQEGELIEWVDERGSFLGKGYYGVQNKGIGWVLSFDANEKIDQAFFVSKLEQASKSRTHLFRDAQ 96
Cdd:PRK15128 19 HPWVFSGAVARMEGkASLGETIDIVDHQGKWLARGAYSPASQIRARVWTFDPDESIDIAFFTRRLQQAQKWRDWLAQKDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 97 TTAFRVFNGEGDGIGGITIDYYDGFYLIQWYSEGVYTLKEDVLAAIEQVYPDYkGIYEkkRFDTSGQYIEDDDFVKGE-K 175
Cdd:PRK15128 99 LDSYRLIAGESDGLPGITIDRFGNFLVLQLLSAGAEYQRAALISALQTLYPEC-AIYD--RSDVAVRKKEGMELTQGPvT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 176 GEFP---LIVKENGMNVAVYLNDGAMTGIFLDQRHVRKAIRdRYAKGKTVLNTFSYTGAFSVAAALGGASRTTSVDVANR 252
Cdd:PRK15128 176 GELPpalLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATR-RYVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSQE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 253 SLKKTSEQFEVNGIDVDGQDIKVMDVFKYFPFAAKKGWSYDVVILDPPSFARTKKHTFSAAKDYKKLLKEAIQITAENGV 332
Cdd:PRK15128 255 ALDIARQNVELNKLDLSKAEFVRDDVFKLLRTYRDRGEKFDVIVMDPPKFVENKSQLMGACRGYKDINMLAIQLLNPGGI 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 518573276 333 IVASTNSSAFGMKKFKGFIAQAFKESGKTYRILEEYTLPEDFRTTKNYPEGNYLK 387
Cdd:PRK15128 335 LLTFSCSGLMTSDLFQKIIADAAIDAGRDVQFIEQFRQAADHPVIATYPEGLYLK 389
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
101-374 |
1.17e-34 |
|
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: 129.61 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 101 RVFNGEG---DGIGGITIDYYDGFYLIQWYSEgvytLKEDVLAAIEQVYPDY--KGIYEKKRFDT---SGQYIED--DDF 170
Cdd:pfam10672 2 RLFHGRGrcwPGLEQLTCDWLQGQLLVNLFKE----VDPAFLQALKRGLEQLttAPAWAAKQGRHlvlQHRYADGapSEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 171 VKGEKGEFPLIVkENGMNVAVYLNDGAMTGIFLDQRHVRKAIRDRyAKGKTVLNTFSYTGAFSVAAALGGASRTTSVDVA 250
Cdd:pfam10672 78 LSGELLETPVVV-ENGLKYQLDIGRNQNFGLFLDMRLGRRWVQEN-AKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 251 NRSLKKTSEQFEVNGIDVDGQDIKVMDVFKYFPfAAKKGWSYDVVILDPPSFartKKHTFSAAKDYKKLLKEAIQITAEN 330
Cdd:pfam10672 156 RGSLNKGRDNHRLNGHDLGRVSFLGHDIFKSWG-KIKKLGPYDLVIIDPPSF---QKGSFALTKDYKKILRRLPELLVEG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518573276 331 GVIVASTNSSAFGmkkfKGFIAQAFKESGKTYRILEEYTLPEDF 374
Cdd:pfam10672 232 GTVLACVNSPAVG----PDFLIEEMAEEAPSLHFVERLDNPPEF 271
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
137-375 |
1.74e-31 |
|
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: 126.07 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 137 DVLAAIEQVYP-DYKGIYEKKRFDTSG--QYiedddfVK-GEKGEFpLIVKENGMNVAVYLNDGAMTGIFLDQRHVRKAI 212
Cdd:PRK11783 461 DALAATPEVLGiPPNKVVLKTRERQKGknQY------QKlAEKGEF-LEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMI 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 213 RDRyAKGKTVLNTFSYTGAFSVAAALGGASRTTSVDVANRSLKKTSEQFEVNGIDVDGQDIKVMDVFKyfpfaakkgW-- 290
Cdd:PRK11783 534 GQM-AKGKDFLNLFAYTGTASVHAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLA---------Wlk 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 291 ----SYDVVILDPPSFARTKK--HTFSAAKDYKKLLKEAIQITAENGVIVASTNssafgmkkFKGFI--AQAFKESGktY 362
Cdd:PRK11783 604 eareQFDLIFIDPPTFSNSKRmeDSFDVQRDHVALIKDAKRLLRPGGTLYFSNN--------KRGFKmdEEGLAKLG--L 673
|
250
....*....|....*
gi 518573276 363 RILE--EYTLPEDFR 375
Cdd:PRK11783 674 KAEEitAKTLPPDFA 688
|
|
| RlmI_M_like |
cd11572 |
Middle domain of the SAM-dependent methyltransferase RlmI and related proteins; This middle or ... |
75-173 |
1.38e-28 |
|
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: 107.16 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 75 AFFVSKLEQASKSRTHLFRDAqTTAFRVFNGEGDGIGGITIDYYDGFYLIQWYSEGVYTLKEDVLAAIEQVYPDyKGIYE 154
Cdd:cd11572 1 AFFKRRIEKALALRKRLLLDD-TNAYRLVHGEGDGLPGLIVDRYGDVLVVQILSAGMERLKELIVEALKELLGP-KGIYE 78
|
90 100
....*....|....*....|.
gi 518573276 155 KKRFDT--SGQYIEDDDFVKG 173
Cdd:cd11572 79 RSDAAVreLEGLPEEVGVLYG 99
|
|
| PUA_3 |
pfam17785 |
PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent ... |
4-66 |
5.53e-18 |
|
PUA-like domain; This PUA-like domain is found at the N-terminus of SAM-dependent methyltransferases.
Pssm-ID: 436043 [Multi-domain] Cd Length: 64 Bit Score: 77.52 E-value: 5.53e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518573276 4 ISLKQTFAEQVKKGYPLISKDAVSRVNG-VQEGELIEWVDERGSFLGKGYYGVQNKGIGWVLSF 66
Cdd:pfam17785 1 VTLKKKAEKRLKRGHPWIYSNEIERVEGdLEEGDLVRVVDSDGRFLGTGYYNPQSKIAVRVLSR 64
|
|
| PUA_RlmI |
cd21153 |
PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related proteins; The ... |
2-70 |
2.49e-12 |
|
PUA RNA-binding domain of the SAM-dependent methyltransferase RlmI and related proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this subfamily contain PUA domains that co-occur N-terminal to SAM-dependent methyltransferase domains and include Escherichia coli RlmI (rRNA large subunit methyltransferase gene I, also called YccW) and Thermus thermophilus methyltransferase RlmO, which are 5-methylcytosine methyltransferases (m5C MTases) that play a role in modifying 23S rRNA. This subfamily also includes Pyrococcus horikoshii PH1915 that may play a role as a 5-methyluridine MTase, and/or perform similar roles.
Pssm-ID: 409295 [Multi-domain] Cd Length: 70 Bit Score: 61.83 E-value: 2.49e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 2 KKISLKQTFAEQVKKGYPLISKDAVSRVNG-VQEGELIEWVDERGSFLGKGYYGVQNKGIGWVLSFDANE 70
Cdd:cd21153 1 PRIVLKKGKEKSLRRGHPWIFSGAIDRIEGkPEPGDLVDVYDHKGKFLGTGLYNPHSQIRVRVLSFDKEE 70
|
|
| PRK14967 |
PRK14967 |
putative methyltransferase; Provisional |
219-300 |
1.01e-05 |
|
putative methyltransferase; Provisional
Pssm-ID: 184931 [Multi-domain] Cd Length: 223 Bit Score: 46.20 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 219 GKTVLNTFSYTGAFSVAAALGGASRTTSVDVANRSLKKTSEQFEVNGIDVdgqdikvmDVFKYFPFAAKKGWSYDVVILD 298
Cdd:PRK14967 37 GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDV--------DVRRGDWARAVEFRPFDVVVSN 108
|
..
gi 518573276 299 PP 300
Cdd:PRK14967 109 PP 110
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
218-371 |
2.47e-05 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 44.89 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 218 KGKTVLNTFSYTGAFSVAAALGGASRTTSVDVANRSLKKTSEQFEVNGIDVdgqDIKVMDVFKyFPFAAkkgwSYDVVIL 297
Cdd:COG2263 45 EGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLGVRV---DFIRADVTR-IPLGG----SVDTVVM 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573276 298 DPPsfartkkhtFSAAKDY--KKLLKEAIQITAengVIVASTNSSAfgmkkfKGFIAQAFKESGKTYRILEEYTLP 371
Cdd:COG2263 117 NPP---------FGAQRRHadRPFLEKALEIAA---VIYSIHNAGS------LDFVERFAADRGGEITHVFRAEFP 174
|
|
| Cons_hypoth95 |
pfam03602 |
Conserved hypothetical protein 95; |
208-333 |
6.40e-05 |
|
Conserved hypothetical protein 95;
Pssm-ID: 427391 [Multi-domain] Cd Length: 179 Bit Score: 43.38 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 208 VRKA---IRDRYAKGKTVLNTFSYTGAFSVAAALGGASRTTSVDV---ANRSLKKTSEQFEVNGIDVdgqdikVMDVFKY 281
Cdd:pfam03602 28 VREAlfnWLAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKdkrAVQILKENLQLLGLPGAVL------VMDALLA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 518573276 282 FPFAAKKGWSYDVVILDPPsFArtkkhtfsaakdyKKLLKEAIQITAENGVI 333
Cdd:pfam03602 102 LLRLAGKGPVFDIVFLDPP-YA-------------KGLIEEVLDLLAEKGWL 139
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
218-350 |
8.61e-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: 42.63 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 218 KGKTVLNTFSYTGAFSVAAALGGAsRTTSVDVANRSLKKTSEQFEVNGIDVdgQDIKVMDVFKyFPFAAKkgwSYDVVIL 297
Cdd:COG1041 26 EGDTVLDPFCGTGTILIEAGLLGR-RVIGSDIDPKMVEGARENLEHYGYED--ADVIRGDARD-LPLADE---SVDAIVT 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 518573276 298 DPP--SFARTKKHTFSAAkdYKKLLKEAIQITAENGVIVASTNSSAFGMKKFKGF 350
Cdd:COG1041 99 DPPygRSSKISGEELLEL--YEKALEEAARVLKPGGRVVIVTPRDIDELLEEAGF 151
|
|
| RsmD |
COG0742 |
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
219-366 |
3.28e-04 |
|
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: 41.22 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 219 GKTVLNTFSYTGAfsvaaaLG------GASRTTSVD---VANRSLKKTSEQFEVNGidvdgqDIKV--MDVFKYFPFAAK 287
Cdd:COG0742 42 GARVLDLFAGSGA------LGlealsrGAASVVFVEkdrKAAAVIRKNLEKLGLED------RARVirGDALRFLKRLAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 288 KgwSYDVVILDPPsFARtkkhtfsaaKDYKKLLK--EAIQITAENGVIVASTNSSAFGMKKFKGFIAQAFKESGKT-YRI 364
Cdd:COG0742 110 E--PFDLVFLDPP-YAK---------GLLEKALEllAENGLLAPGGLIVVEHSKREELPELPAGLELLKERKYGDTrLSF 177
|
..
gi 518573276 365 LE 366
Cdd:COG0742 178 YR 179
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
221-336 |
4.50e-04 |
|
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: 39.34 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 221 TVLNTFSYTGAFSVAAALGGASRTTSVDV---ANRSLKKTSEQFEVNGIDVdgqdiKVMDVFKyFPFAAKKgwSYDVVIL 297
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDIspvALELARKAAAALLADNVEV-----LKGDAEE-LPPEADE--SFDVIIS 72
|
90 100 110
....*....|....*....|....*....|....*....
gi 518573276 298 DPPsfartkkhTFSAAKDYKKLLKEAIQITAENGVIVAS 336
Cdd:cd02440 73 DPP--------LHHLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
206-300 |
2.77e-03 |
|
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: 39.39 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573276 206 RHVRKAIRDRyaKGKTVLNTFSYTGAFSVAAAlGGASRTTSVDVANRSLKKTSEQFEVNGID-VDgqdIKVMDVFKYFPf 284
Cdd:COG2265 223 AAALEWLDLT--GGERVLDLYCGVGTFALPLA-RRAKKVIGVEIVPEAVEDARENARLNGLKnVE---FVAGDLEEVLP- 295
|
90
....*....|....*.
gi 518573276 285 AAKKGWSYDVVILDPP 300
Cdd:COG2265 296 ELLWGGRPDVVVLDPP 311
|
|
| |
