|
Name |
Accession |
Description |
Interval |
E-value |
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
1-704 |
0e+00 |
|
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: 1087.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 1 MQFIALTSIGIENLLVDELTELGAVVSKQTVGSVRFEADSTLAQKVCLSTRYATRVLMLIEEKEgVNDKDSLYKFARFQP 80
Cdd:PRK11783 2 NSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFK-VYSDLDLYLGVQAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 81 WQEWFGPTQTFAVDFNGTNDSLKNTQFSGLVIKDAIVDYFNDLYEQRPNVDKQDANVRVVARLNRHGVALYIDYSGPRLS 160
Cdd:PRK11783 81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 161 ERGYRQGQGKAPIKEHLAAAIIKRSGWLENvNQPLFDPCCGAGTILIEAAGMARNEAPGLFREGFAFERLPSFRAAKFKQ 240
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWPQE-GTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 241 LREELIEQ----ITDPKLWLIGHDYDAQVLDKAIANAERAELGNVIKFKQSDATKLTSVAKL--PGVVISNLPYGERIGS 314
Cdd:PRK11783 240 LLEEAQERaragLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKgpTGLVISNPPYGERLGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 315 MAELVNLHRSMGVGFKKHFNHWKLALLGMDESLFKLLKLVKQKRYKFKNGPLDVELNLYQLDDKQVSLTSddkpalnfEG 394
Cdd:PRK11783 320 EPALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDA--------EG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 395 SMSFANRLKKNKQGLKNWLKQNEVQAYRVYDADIPEYNVAVDIYGDSAVIFEYAAPKEIDEKTSEKRLQDVISLTAQQLN 474
Cdd:PRK11783 392 AQDFANRLRKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 475 IAPENIAVKVRKKQKGEEQYTPMAKQNRTMVVEEFGAKFKVNLFDYLDTGLFLDHRLARRYIQQNAKDKRFLNLFAYTGT 554
Cdd:PRK11783 472 IPPNKVVLKTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 555 ASVHAALGGAKAITTVDLSKTYLKWGQDNFALNDISNTRYRFEQADCLKWLEYAQGQYDLIFLDPPTFSNSKRMKDAFDV 634
Cdd:PRK11783 552 ASVHAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDV 631
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 635 QTDHIKLLTWVKKILSPSGTLIFSNNKRGFVMDEVGLMGLGLKAENISEKTLSPDFKRNKKIHNSWLITH 704
Cdd:PRK11783 632 QRDHVALIKDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITH 701
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
1-373 |
1.06e-141 |
|
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 439886 [Multi-domain] Cd Length: 369 Bit Score: 419.12 E-value: 1.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 1 MQFIALTSIGIENLLVDELTELGAVVSKQTVGSVRFEADSTLAQKVCLSTRYATRVLMLIEEKEgVNDKDSLYKFARFQP 80
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFK-ARTFDDLYEGAKAIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 81 WQEWFGPTQTFAVDFNGTNDSLKNTQFSGLVIKDAIVDYFNDLYEQRPNVDKQDANVRVVARLNRHGVALYIDYSGPRLS 160
Cdd:COG0116 80 WEEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 161 ERGYRQGQGKAPIKEHLAAAIIKRSGWleNVNQPLFDPCCGAGTILIEAAGMARNEAPGLFREgFAFERLPSFRAAKFKQ 240
Cdd:COG0116 160 KRGYREAQGEAPLKETLAAALLLLSGW--DGDRPLVDPMCGSGTILIEAALIAANIAPGLNRD-FAFEKWPDFDAELWQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 241 LREELIEQIT-DPKLWLIGHDYDAQVLDKAIANAERAELGNVIKFKQSDATKLTSVAKlPGVVISNLPYGERIGSMAELV 319
Cdd:COG0116 237 LREEAEARIKrDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAE-PGLIITNPPYGERLGEEEELE 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 940388013 320 NLHRSMGVGFKKHFNHWKLALLGMDESLFKLLKLVKQKRYKFKNGPLDVELNLY 373
Cdd:COG0116 316 ALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
3-156 |
1.14e-43 |
|
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 212584 Cd Length: 152 Bit Score: 154.28 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 3 FIALTSIGIENLLVDELTELGAVVSKQTVGSVRFEADSTLAQKVCLSTRYATRVLMLIEEKEgVNDKDSLYKFARFQPWQ 82
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFE-AEDFDDLYELAKAIDWE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388013 83 EWFGPTQTFAVDFNGTNDSLKNTQFSGLVIKDAIVDYFNDLYEqRPNVDKQDANVRVVARLNRHGVALYIDYSG 156
Cdd:cd11715 80 DYLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKGK-RPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
162-367 |
5.97e-38 |
|
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.
Pssm-ID: 395932 [Multi-domain] Cd Length: 184 Bit Score: 139.41 E-value: 5.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 162 RGYRQGQGKAPIKEHLAAAIIKRSGWLenVNQPLFDPCCGAGTILIEAAGMARNEAPGLFREgfaferlpsfraakfkql 241
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWK--PGDPLLDPMCGSGTILIEAALMGANIAPGKFDA------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 242 reelieqitDPKLWLIGHDYDAQVLDKAIANAERAELGNVIKFKQSDATKLTSVAKLPGVVISNLPYGERIGSMAELVNL 321
Cdd:pfam01170 61 ---------RVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 940388013 322 HRSMGVGFKKHF--NHWKLALLGMDESLFKLLKLVKQKRYKFKNGPLD 367
Cdd:pfam01170 132 YPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIG 179
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
68-153 |
3.16e-10 |
|
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 214952 [Multi-domain] Cd Length: 83 Bit Score: 56.90 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 68 DKDSLYKFARFQ-PWQEWFGPTQTFAVDFNGTNdslKNTQFSGLVIKDAIVDYFNDLYEQRPnVDKQDANVRVVARLNRH 146
Cdd:smart00981 1 DLEDLYETALELiRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKD 76
|
....*..
gi 940388013 147 GVALYID 153
Cdd:smart00981 77 KAYLSID 83
|
|
| TIGR00095 |
TIGR00095 |
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ... |
532-620 |
1.47e-05 |
|
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 188022 [Multi-domain] Cd Length: 190 Bit Score: 46.25 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 532 ARRYIQQNakdkRFLNLFAYTGTASVHAALGGAKAITTVDLSKTYLKWGQDNFALNDISNTRYRFEQADCLKWLEYAQGQ 611
Cdd:TIGR00095 45 LRPDIVGA----HFLDLFAGSGALGLEALSRGAASAVFVEQDRKVAQTLKENLSTLKKSGEQATVLNDAVRALLFLAKKQ 120
|
90
....*....|.
gi 940388013 612 --YDLIFLDPP 620
Cdd:TIGR00095 121 tpFDIIYLDPP 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
1-704 |
0e+00 |
|
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: 1087.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 1 MQFIALTSIGIENLLVDELTELGAVVSKQTVGSVRFEADSTLAQKVCLSTRYATRVLMLIEEKEgVNDKDSLYKFARFQP 80
Cdd:PRK11783 2 NSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFK-VYSDLDLYLGVQAID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 81 WQEWFGPTQTFAVDFNGTNDSLKNTQFSGLVIKDAIVDYFNDLYEQRPNVDKQDANVRVVARLNRHGVALYIDYSGPRLS 160
Cdd:PRK11783 81 WTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 161 ERGYRQGQGKAPIKEHLAAAIIKRSGWLENvNQPLFDPCCGAGTILIEAAGMARNEAPGLFREGFAFERLPSFRAAKFKQ 240
Cdd:PRK11783 161 QRGYRQATGEAPLKENLAAAILLRSGWPQE-GTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALWQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 241 LREELIEQ----ITDPKLWLIGHDYDAQVLDKAIANAERAELGNVIKFKQSDATKLTSVAKL--PGVVISNLPYGERIGS 314
Cdd:PRK11783 240 LLEEAQERaragLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKgpTGLVISNPPYGERLGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 315 MAELVNLHRSMGVGFKKHFNHWKLALLGMDESLFKLLKLVKQKRYKFKNGPLDVELNLYQLDDKQVSLTSddkpalnfEG 394
Cdd:PRK11783 320 EPALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAEESTSSDA--------EG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 395 SMSFANRLKKNKQGLKNWLKQNEVQAYRVYDADIPEYNVAVDIYGDSAVIFEYAAPKEIDEKTSEKRLQDVISLTAQQLN 474
Cdd:PRK11783 392 AQDFANRLRKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQRLFDALAATPEVLG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 475 IAPENIAVKVRKKQKGEEQYTPMAKQNRTMVVEEFGAKFKVNLFDYLDTGLFLDHRLARRYIQQNAKDKRFLNLFAYTGT 554
Cdd:PRK11783 472 IPPNKVVLKTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAKGKDFLNLFAYTGT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 555 ASVHAALGGAKAITTVDLSKTYLKWGQDNFALNDISNTRYRFEQADCLKWLEYAQGQYDLIFLDPPTFSNSKRMKDAFDV 634
Cdd:PRK11783 552 ASVHAALGGAKSTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPTFSNSKRMEDSFDV 631
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 635 QTDHIKLLTWVKKILSPSGTLIFSNNKRGFVMDEVGLMGLGLKAENISEKTLSPDFKRNKKIHNSWLITH 704
Cdd:PRK11783 632 QRDHVALIKDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKLGLKAEEITAKTLPPDFARNPKIHNCWLITH 701
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
1-373 |
1.06e-141 |
|
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 439886 [Multi-domain] Cd Length: 369 Bit Score: 419.12 E-value: 1.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 1 MQFIALTSIGIENLLVDELTELGAVVSKQTVGSVRFEADSTLAQKVCLSTRYATRVLMLIEEKEgVNDKDSLYKFARFQP 80
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFK-ARTFDDLYEGAKAIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 81 WQEWFGPTQTFAVDFNGTNDSLKNTQFSGLVIKDAIVDYFNDLYEQRPNVDKQDANVRVVARLNRHGVALYIDYSGPRLS 160
Cdd:COG0116 80 WEEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 161 ERGYRQGQGKAPIKEHLAAAIIKRSGWleNVNQPLFDPCCGAGTILIEAAGMARNEAPGLFREgFAFERLPSFRAAKFKQ 240
Cdd:COG0116 160 KRGYREAQGEAPLKETLAAALLLLSGW--DGDRPLVDPMCGSGTILIEAALIAANIAPGLNRD-FAFEKWPDFDAELWQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 241 LREELIEQIT-DPKLWLIGHDYDAQVLDKAIANAERAELGNVIKFKQSDATKLTSVAKlPGVVISNLPYGERIGSMAELV 319
Cdd:COG0116 237 LREEAEARIKrDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAE-PGLIITNPPYGERLGEEEELE 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 940388013 320 NLHRSMGVGFKKHFNHWKLALLGMDESLFKLLKLVKQKRYKFKNGPLDVELNLY 373
Cdd:COG0116 316 ALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
398-699 |
1.56e-101 |
|
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: 316.35 E-value: 1.56e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 398 FANRLKKNKQGLKNWLKQNEVQAYRVYDAD---IPeyNVAVDIYGDSAVIFEYAAPKEIdektsekRLQDVISLTAQQLN 474
Cdd:COG1092 76 FANRLRKALALRRKLAKREGTNAYRLVHGEadgLP--GLIVDRYGDVLVVQEYSAGMER-------RRDEILEALVEVLG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 475 iaPENIAVKV---RKKQKGEEQYTPMA--KQNRTMVVEEFGAKFKVNLFDYLDTGLFLDHRLARRYIQQNAKDKRFLNLF 549
Cdd:COG1092 147 --PEGIYLRSdvrVRQLEGLPQYEGVLygEAPEEVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVLNLF 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 550 AYTGTASVHAALGGAKAITTVDLSKTYLKWGQDNFALNDISNtRYRFEQADCLKWLEYAQ---GQYDLIFLDPPTFSNSK 626
Cdd:COG1092 225 SYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGLDD-RHEFVQADAFDWLRELAregERFDLIILDPPAFAKSK 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940388013 627 rmKDAFDVQTDHIKLLTWVKKILSPSGTLIFSNNKRGFVMDEV------GLMGLGLKAENISEKTLSPDFKRNKKIHNS 699
Cdd:COG1092 304 --KDLFDAQRDYKDLNRLALKLLAPGGILVTSSCSRHFSLDLFleilarAARDAGRRVRIIERLTQPPDHPVLPAFPEG 380
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
3-156 |
1.14e-43 |
|
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 212584 Cd Length: 152 Bit Score: 154.28 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 3 FIALTSIGIENLLVDELTELGAVVSKQTVGSVRFEADSTLAQKVCLSTRYATRVLMLIEEKEgVNDKDSLYKFARFQPWQ 82
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFE-AEDFDDLYELAKAIDWE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 940388013 83 EWFGPTQTFAVDFNGTNDSLKNTQFSGLVIKDAIVDYFNDLYEqRPNVDKQDANVRVVARLNRHGVALYIDYSG 156
Cdd:cd11715 80 DYLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKGK-RPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
162-367 |
5.97e-38 |
|
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.
Pssm-ID: 395932 [Multi-domain] Cd Length: 184 Bit Score: 139.41 E-value: 5.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 162 RGYRQGQGKAPIKEHLAAAIIKRSGWLenVNQPLFDPCCGAGTILIEAAGMARNEAPGLFREgfaferlpsfraakfkql 241
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWK--PGDPLLDPMCGSGTILIEAALMGANIAPGKFDA------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 242 reelieqitDPKLWLIGHDYDAQVLDKAIANAERAELGNVIKFKQSDATKLTSVAKLPGVVISNLPYGERIGSMAELVNL 321
Cdd:pfam01170 61 ---------RVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 940388013 322 HRSMGVGFKKHF--NHWKLALLGMDESLFKLLKLVKQKRYKFKNGPLD 367
Cdd:pfam01170 132 YPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIG 179
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
501-656 |
3.57e-29 |
|
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: 117.67 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 501 NRTMVVEEFGAKFKVNLFDYLDTGLFLDHRLARRYIQQNAKDKRFLNLFAYTGTASVHAALGGAKAITTVDLSKTYLKWG 580
Cdd:pfam10672 83 LETPVVVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARGSLNKG 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940388013 581 QDNFALNDISNTRYRFEQADCLK-WLEYAQ-GQYDLIFLDPPTFSnskrmKDAFDVQTDHIKLLTWVKKILSPSGTLI 656
Cdd:pfam10672 163 RDNHRLNGHDLGRVSFLGHDIFKsWGKIKKlGPYDLVIIDPPSFQ-----KGSFALTKDYKKILRRLPELLVEGGTVL 235
|
|
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
398-626 |
1.21e-16 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 82.58 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 398 FANRLKKnKQGLKNWL-KQNEVQAYRVYDAD---IPeyNVAVDIYGDSAVIFEYAAPKEIDEKTSEKRLQdvisltaqql 473
Cdd:PRK15128 79 FTRRLQQ-AQKWRDWLaQKDGLDSYRLIAGEsdgLP--GITIDRFGNFLVLQLLSAGAEYQRAALISALQ---------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 474 NIAPE-----NIAVKVRKKQKGEEQYTPMAKQN--RTMVVEEFGAKFKVNLFDYLDTGLFLDHRLARRYIQQNAKDKRFL 546
Cdd:PRK15128 146 TLYPEcaiydRSDVAVRKKEGMELTQGPVTGELppALLPIEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 547 NLFAYTGTASVHAALGGAKAITTVDLSKTYLKWGQDNFALNDISNTRYRFEQADCLKWLE--YAQGQ-YDLIFLDPPTFS 623
Cdd:PRK15128 226 NCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDLSKAEFVRDDVFKLLRtyRDRGEkFDVIVMDPPKFV 305
|
...
gi 940388013 624 NSK 626
Cdd:PRK15128 306 ENK 308
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
173-317 |
2.17e-10 |
|
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: 59.96 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 173 IKEHLAAAIIKRSGWLENVNqpLFDPCCGAGTILIEAAGMARNeapglfregfaferlpsfraakfkqlreelieqitdp 252
Cdd:COG1041 10 LDPRLARALVNLAGAKEGDT--VLDPFCGTGTILIEAGLLGRR------------------------------------- 50
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940388013 253 klwLIGHDYDAQVLDKAIANAERAELGNvIKFKQSDATKLTSVAKLPGVVISNLPYGERIGSMAE 317
Cdd:COG1041 51 ---VIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADESVDAIVTDPPYGRSSKISGE 111
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
68-153 |
3.16e-10 |
|
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 214952 [Multi-domain] Cd Length: 83 Bit Score: 56.90 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 68 DKDSLYKFARFQ-PWQEWFGPTQTFAVDFNGTNdslKNTQFSGLVIKDAIVDYFNDLYEQRPnVDKQDANVRVVARLNRH 146
Cdd:smart00981 1 DLEDLYETALELiRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKD 76
|
....*..
gi 940388013 147 GVALYID 153
Cdd:smart00981 77 KAYLSID 83
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
544-658 |
1.01e-08 |
|
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: 53.59 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 544 RFLNLFAYTGTASVHAALGGAKAITTVDLSKTYLKWGQDNFALNDISNtrYRFEQADCLKWLEYAQGQYDLIFLDPPtfs 623
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN--VEVLKGDAEELPPEADESFDVIISDPP--- 75
|
90 100 110
....*....|....*....|....*....|....*
gi 940388013 624 nskrmkdAFDVQTDHIKLLTWVKKILSPSGTLIFS 658
Cdd:cd02440 76 -------LHHLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
| RsmD |
COG0742 |
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
536-620 |
3.97e-06 |
|
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: 47.77 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 536 IQQNAKDKRFLNLFAYTGtasvhaALG------GAKAITTVDLSK---TYLKwgqDNFALNDISNtRYRFEQADCLKWLE 606
Cdd:COG0742 36 LGPDIEGARVLDLFAGSG------ALGlealsrGAASVVFVEKDRkaaAVIR---KNLEKLGLED-RARVIRGDALRFLK 105
|
90
....*....|....*
gi 940388013 607 -YAQGQYDLIFLDPP 620
Cdd:COG0742 106 rLAGEPFDLVFLDPP 120
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
528-658 |
4.83e-06 |
|
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: 46.16 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 528 DHRLARRYIQQNAKDKRFLNLFAYTGTASVHAALGGAKaITTVDLSKTYLKWGQDNFALNDIsntryRFEQADCLKwLEY 607
Cdd:COG2227 11 DRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAELNV-----DFVQGDLED-LPL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 940388013 608 AQGQYDLIFldpptfsnskrmkdAFDVQ---TDHIKLLTWVKKILSPSGTLIFS 658
Cdd:COG2227 84 EDGSFDLVI--------------CSEVLehlPDPAALLRELARLLKPGGLLLLS 123
|
|
| Cons_hypoth95 |
pfam03602 |
Conserved hypothetical protein 95; |
536-620 |
7.02e-06 |
|
Conserved hypothetical protein 95;
Pssm-ID: 427391 [Multi-domain] Cd Length: 179 Bit Score: 46.85 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 536 IQQNAKDKRFLNLFAYTGTASVHAALGGAKAITTVDLSKTYLKWGQDNFALNDISNTRYRFEQADCLKWLEYAQGQYDLI 615
Cdd:pfam03602 36 LAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDALLALLRLAGKGPVFDIV 115
|
....*
gi 940388013 616 FLDPP 620
Cdd:pfam03602 116 FLDPP 120
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
43-139 |
8.85e-06 |
|
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 460749 Cd Length: 143 Bit Score: 45.89 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 43 AQKVCLSTRYATRVLMLIEEKEGVNDKDSLYKFARFQPWQEWFGPTQTFAVDFNGTNdslKNTQFSGLVIKDAIVDYFND 122
Cdd:pfam02926 37 RELLKEALEKAPGIERFPVAETCEADLEDILELAKEIIKDKFKKEGETFAVRVKRRG---KNHEFTSLEINREVGKAIVE 113
|
90
....*....|....*..
gi 940388013 123 LYEQRPNVDKQDANVRV 139
Cdd:pfam02926 114 KTGLKVDLENPDIVVHV 130
|
|
| TIGR00095 |
TIGR00095 |
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ... |
532-620 |
1.47e-05 |
|
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 188022 [Multi-domain] Cd Length: 190 Bit Score: 46.25 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 532 ARRYIQQNakdkRFLNLFAYTGTASVHAALGGAKAITTVDLSKTYLKWGQDNFALNDISNTRYRFEQADCLKWLEYAQGQ 611
Cdd:TIGR00095 45 LRPDIVGA----HFLDLFAGSGALGLEALSRGAASAVFVEQDRKVAQTLKENLSTLKKSGEQATVLNDAVRALLFLAKKQ 120
|
90
....*....|.
gi 940388013 612 --YDLIFLDPP 620
Cdd:TIGR00095 121 tpFDIIYLDPP 131
|
|
| THUMP |
cd11688 |
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ... |
3-139 |
1.40e-04 |
|
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 212583 Cd Length: 148 Bit Score: 42.48 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 3 FIALTSIGIENLLVDELTELGAV------VSKQTVGSVRFEADSTLAQKVCLSTRYATRVLMLIEeKEGVNDKDSLYKFA 76
Cdd:cd11688 1 VFATTGKGLEEILAAELYELLEVrgfdaeIQVVPHGRVHFKTDTDEAVYQLVMWSRLISRIMPPL-GECKADLEDLYETA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940388013 77 RFQPWQEWFGPTQTFAVDFNGTNDSLKNTQFSGLVIKDAIVDYFNdlyeqrPNVDKQDANVRV 139
Cdd:cd11688 80 LEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFN------PEVDLDNPDIVV 136
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
552-674 |
7.51e-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: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 552 TGTASVH-AALGGAKaITTVDLSKTYLKWGQDNFALNDISNtrYRFEQADCLKWLEYAQGQYDLIFldpptfsnskrmkd 630
Cdd:COG0500 37 TGRNLLAlAARFGGR-VIGIDLSPEAIALARARAAKAGLGN--VEFLVADLAELDPLPAESFDLVV-------------- 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 940388013 631 AFDVQTDH-----IKLLTWVKKILSPSGTLIFSNNKRGFVMDEVGLMGL 674
Cdd:COG0500 100 AFGVLHHLppeerEALLRELARALKPGGVLLLSASDAAAALSLARLLLL 148
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
522-659 |
9.23e-04 |
|
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443298 Cd Length: 173 Bit Score: 40.55 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 522 DTGLFLdHRLARryiQQNAKdkRFLNLFAYTGTASVHAALG---GAKaITTVDLSKTYLKWGQDNFALNDISNtRYRFEQ 598
Cdd:COG4122 3 EQGRLL-YLLAR---LLGAK--RILEIGTGTGYSTLWLARAlpdDGR-LTTIEIDPERAAIARENFARAGLAD-RIRLIL 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940388013 599 ADCLKWLE-YAQGQYDLIFLDpptfSNSKRMKDAFDvqtdhiklltWVKKILSPSGTLIFSN 659
Cdd:COG4122 75 GDALEVLPrLADGPFDLVFID----ADKSNYPDYLE----------LALPLLRPGGLIVADN 122
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
552-616 |
1.24e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 38.70 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940388013 552 TGTASVH-AALGGAKaITTVDLSKTYLKWGQDNFALNDIsntRYRFEQADCLKwLEYAQGQYDLIF 616
Cdd:pfam13649 8 TGRLTLAlARRGGAR-VTGVDLSPEMLERARERAAEAGL---NVEFVQGDAED-LPFPDGSFDLVV 68
|
|
| Trm5 |
COG2520 |
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
436-623 |
3.78e-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: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 436 DIYGDSAVIfeyaapkEIDEKTSEKRLQDVISLTAQQLNIapENIAVKVRKKqKGEE---QYTPMAKQNRTMVVE-EFGA 511
Cdd:COG2520 83 DIIGDIAII-------KIPDELEEYKEEIAEAILESHPNV--KTVLAKASGV-EGEFrvpELELLAGEGRTETIHrENGC 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940388013 512 KFKVNLfdyldTGLFLDHRLA--RRYIQQNAKD-KRFLNLFAYTGTASVHAALGGAKAITTVDLSKTYLKWGQDNFALND 588
Cdd:COG2520 153 RFKLDV-----AKVYFSPRLAteRLRIAELVKPgERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKENIRLNK 227
|
170 180 190
....*....|....*....|....*....|....*
gi 940388013 589 ISNtRYRFEQADCLKWLEYAQGQYDLIFLDPPTFS 623
Cdd:COG2520 228 VED-RVTPILGDAREVAPELEGKADRIIMNLPHSA 261
|
|
| |
