|
Name |
Accession |
Description |
Interval |
E-value |
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
4-717 |
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: 1042.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 4 FTFFVSCAKGIELLLKDELERLGISS-QEKLAGVEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQQDLYEFISSINW 82
Cdd:PRK11783 2 NSLFASCAKGLEELLKDELEALGASEcKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAIDW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 83 MDYFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDQFRNVINQRPNIDTENPDNVIKLHLHKQFVNVFLCLNIDSLHK 162
Cdd:PRK11783 82 TEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLHQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 163 RSYRQFQGQAPLKESLAAAILIKAGWLEElkkhQPILIDPMCGSGTILIEAALMAKNIAPVLLNKEFKIFNSKFHNQELW 242
Cdd:PRK11783 162 RGYRQATGEAPLKENLAAAILLRSGWPQE----GTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 243 DNLLEIAKNSQKVTNA----IICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFE--SEGLIVTNPPYGERL 316
Cdd:PRK11783 238 QELLEEAQERARAGLAelpsKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPkgPTGLVISNPPYGERL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 317 ygDQLDELLDIFNGFGDRLSQDFYGWKVAVLTSFADSIKEMQLRTTERNKFYNGAIETILYQFKINEhakfkhetqlekn 396
Cdd:PRK11783 318 --GEEPALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAE------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 397 iriaEASAQKSDEHIDFANKLKKNLKSLKPWLKQTGLECYRLYDADIPTFAVAVDVYSEHIFLQEYRADATIDQNIAKQR 476
Cdd:PRK11783 383 ----ESTSSDAEGAQDFANRLRKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 477 FYQAIYQIHKTLDIKYENIHTRVRQRQKGKEQYQKENDKNKFHIINEFDAKFYVNFDDYLDTGIFLDHRKIRQLVAKAAK 556
Cdd:PRK11783 459 LFDALAATPEVLGIPPNKVVLKTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAK 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 557 NKTLLNLFSYTCTASVHAALKGAK-TTSVDMSNTYLEWGKNNFTLNNIDAKKHSFIQADCISWLKTNKDKFDVIFLDPPT 635
Cdd:PRK11783 539 GKDFLNLFAYTGTASVHAALGGAKsTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPT 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 636 FSNSKRMDDILDIQRDHELLINLAMDSLKKDGILYFSNNYRRFKMSPQILEK--FNCENIDKICLSRDFLSNKNIHNCWE 713
Cdd:PRK11783 619 FSNSKRMEDSFDVQRDHVALIKDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKlgLKAEEITAKTLPPDFARNPKIHNCWL 698
|
....
gi 489106589 714 IKYK 717
Cdd:PRK11783 699 ITHA 702
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
4-379 |
5.51e-153 |
|
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: 448.40 E-value: 5.51e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 4 FTFFVSCAKGIELLLKDELERLGISS-QEKLAGVEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQQDLYEFISSINW 82
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDvKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 83 MDYFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDQFRNVINQRPNIDTENPDNVIKLHLHKQFVNVFLCLNIDSLHK 162
Cdd:COG0116 81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 163 RSYRQFQGQAPLKESLAAAILIKAGWleelKKHQPiLIDPMCGSGTILIEAALMAKNIAPvLLNKEFKIFNSKFHNQELW 242
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGW----DGDRP-LVDPMCGSGTILIEAALIAANIAP-GLNRDFAFEKWPDFDAELW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 243 DNLLEIAKNS-QKVTNAIICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESeGLIVTNPPYGERLyGDQl 321
Cdd:COG0116 235 QELREEAEARiKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEP-GLIITNPPYGERL-GEE- 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489106589 322 DELLDIFNGFGDRLSQDFYGWKVAVLTSFADSIKEMQLRTTERNKFYNGAIETILYQF 379
Cdd:COG0116 312 EELEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
6-389 |
6.40e-44 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 162.15 E-value: 6.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 6 FFVSCAKGIELLLKDELERLGISSQEKLAG---VEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQ-QDLYEFISSIN 81
Cdd:NF040721 3 FYATLSPGLEKISAEEIEELGGKIKEIREGkgrVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSlEDIYKRVYSID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 82 WmDYFAVDKTFKI--IISGKHyDFNnTMFVSQKTKDAIVDQFRNVINQRPNIDTENPDNVIKLHLHKqfvNVFLcLNID- 158
Cdd:NF040721 83 F-SFIKPEQSFAIrpLRVGEH-DFT-SIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIF---DELL-VGIDt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 159 ----SLHKRSYRQFQGQAPLKESLAAAILIKAGWleelkKHQPILIDPMCGSGTILIEAALMAKNIAPVLLNKEF---KI 231
Cdd:NF040721 156 tgdeGLHKRGYRVYQHPAHLNPTIASSLIYLSGW-----KDEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFafkKI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 232 FNSKFHNQELWDNLLEIAknsqkvtnaiicGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESEGLIVTNPP 311
Cdd:NF040721 231 FGHELLEKIKKDVELKIY------------GIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPP 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489106589 312 YGERLYGDQLDEllDIFNGFGDRLSQDFYGWKVAVLTsfadsikemqlrTTERNKFYNGAIETilyQFKINEHAKFKH 389
Cdd:NF040721 299 YGLRIGKKRIIK--KLYNNFLRSAKKILHKRSRIVVI------------TAEKKIFEEAAAKN---GFEIIEEFNVMY 359
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
6-155 |
1.85e-42 |
|
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: 150.81 E-value: 1.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 6 FFVSCAKGIELLLKDELERLGISSQEKL-AGVEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQQDLYEFISSINWMD 84
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEDVEVGpGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489106589 85 YFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDQFRNViNQRPNIDTENPDNVIKLHLHKQFVNVFLCL 155
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDL 150
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
163-378 |
5.16e-39 |
|
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: 142.49 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 163 RSYRQFQGQAPLKESLAAAILIKAGWLEElkkhQPILiDPMCGSGTILIEAALMAKNIAPVLLnkefkifnskfhnqelw 242
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPG----DPLL-DPMCGSGTILIEAALMGANIAPGKF----------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 243 dnlleiaknsQKVTNAIICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESEGLIVTNPPYGERLygDQLD 322
Cdd:pfam01170 59 ----------DARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRL--GSKG 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489106589 323 ELLDIFNGFGDRLSQDF--YGWKVAVLTSFADSIKEMQLRTTERNKFYNGAIETILYQ 378
Cdd:pfam01170 127 ALEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
71-153 |
4.43e-11 |
|
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: 59.21 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 71 QDLYE-FISSINWMDYFAVDKTFKIIISGKHYDFNntmFVSQKTKDAIVDQFRNVINQRPnIDTENPDNVIKLHLHKQFV 149
Cdd:smart00981 3 EDLYEtALELIRWEKIFKEGKTFAVRAKRRGKNHE---FTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKDKA 78
|
....
gi 489106589 150 NVFL 153
Cdd:smart00981 79 YLSI 82
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
556-651 |
3.64e-03 |
|
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 129628 [Multi-domain] Cd Length: 179 Bit Score: 39.07 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 556 KNKTLLNLFSYTCTASVHAALKGAKTTSVDMSNTYLEWGKNNFTLNNIDAkkhSFIQADCiswLKTNKDKFDVIFLDPPT 635
Cdd:TIGR00537 19 KPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGL---DVVMTDL---FKGVRGKFDVILFNPPY 92
|
90
....*....|....*...
gi 489106589 636 F--SNSKRMDDILDIQRD 651
Cdd:TIGR00537 93 LplEDDLRRGDWLDVAID 110
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
4-717 |
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: 1042.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 4 FTFFVSCAKGIELLLKDELERLGISS-QEKLAGVEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQQDLYEFISSINW 82
Cdd:PRK11783 2 NSLFASCAKGLEELLKDELEALGASEcKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAIDW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 83 MDYFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDQFRNVINQRPNIDTENPDNVIKLHLHKQFVNVFLCLNIDSLHK 162
Cdd:PRK11783 82 TEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLHQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 163 RSYRQFQGQAPLKESLAAAILIKAGWLEElkkhQPILIDPMCGSGTILIEAALMAKNIAPVLLNKEFKIFNSKFHNQELW 242
Cdd:PRK11783 162 RGYRQATGEAPLKENLAAAILLRSGWPQE----GTPLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHDEALW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 243 DNLLEIAKNSQKVTNA----IICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFE--SEGLIVTNPPYGERL 316
Cdd:PRK11783 238 QELLEEAQERARAGLAelpsKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPkgPTGLVISNPPYGERL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 317 ygDQLDELLDIFNGFGDRLSQDFYGWKVAVLTSFADSIKEMQLRTTERNKFYNGAIETILYQFKINEhakfkhetqlekn 396
Cdd:PRK11783 318 --GEEPALIALYSQLGRRLKQQFGGWNAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTIAE------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 397 iriaEASAQKSDEHIDFANKLKKNLKSLKPWLKQTGLECYRLYDADIPTFAVAVDVYSEHIFLQEYRADATIDQNIAKQR 476
Cdd:PRK11783 383 ----ESTSSDAEGAQDFANRLRKNLKKLKKWAKQEGIECYRLYDADLPEYNVAVDRYGDWVVVQEYAAPKTIDEEKARQR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 477 FYQAIYQIHKTLDIKYENIHTRVRQRQKGKEQYQKENDKNKFHIINEFDAKFYVNFDDYLDTGIFLDHRKIRQLVAKAAK 556
Cdd:PRK11783 459 LFDALAATPEVLGIPPNKVVLKTRERQKGKNQYQKLAEKGEFLEVTEYGAKLLVNLTDYLDTGLFLDHRPTRRMIGQMAK 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 557 NKTLLNLFSYTCTASVHAALKGAK-TTSVDMSNTYLEWGKNNFTLNNIDAKKHSFIQADCISWLKTNKDKFDVIFLDPPT 635
Cdd:PRK11783 539 GKDFLNLFAYTGTASVHAALGGAKsTTTVDMSNTYLEWAERNFALNGLSGRQHRLIQADCLAWLKEAREQFDLIFIDPPT 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 636 FSNSKRMDDILDIQRDHELLINLAMDSLKKDGILYFSNNYRRFKMSPQILEK--FNCENIDKICLSRDFLSNKNIHNCWE 713
Cdd:PRK11783 619 FSNSKRMEDSFDVQRDHVALIKDAKRLLRPGGTLYFSNNKRGFKMDEEGLAKlgLKAEEITAKTLPPDFARNPKIHNCWL 698
|
....
gi 489106589 714 IKYK 717
Cdd:PRK11783 699 ITHA 702
|
|
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
4-379 |
5.51e-153 |
|
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: 448.40 E-value: 5.51e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 4 FTFFVSCAKGIELLLKDELERLGISS-QEKLAGVEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQQDLYEFISSINW 82
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDvKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 83 MDYFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDQFRNVINQRPNIDTENPDNVIKLHLHKQFVNVFLCLNIDSLHK 162
Cdd:COG0116 81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 163 RSYRQFQGQAPLKESLAAAILIKAGWleelKKHQPiLIDPMCGSGTILIEAALMAKNIAPvLLNKEFKIFNSKFHNQELW 242
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGW----DGDRP-LVDPMCGSGTILIEAALIAANIAP-GLNRDFAFEKWPDFDAELW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 243 DNLLEIAKNS-QKVTNAIICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESeGLIVTNPPYGERLyGDQl 321
Cdd:COG0116 235 QELREEAEARiKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEP-GLIITNPPYGERL-GEE- 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489106589 322 DELLDIFNGFGDRLSQDFYGWKVAVLTSFADSIKEMQLRTTERNKFYNGAIETILYQF 379
Cdd:COG0116 312 EELEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
426-715 |
1.38e-92 |
|
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: 293.63 E-value: 1.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 426 PWLKQTGLECYRLYDAD---IPtfAVAVDVYSEHIFLQEYRADATIdqniAKQRFYQAIyqiHKTLDIK--YENIHTRVR 500
Cdd:COG1092 89 KLAKREGTNAYRLVHGEadgLP--GLIVDRYGDVLVVQEYSAGMER----RRDEILEAL---VEVLGPEgiYLRSDVRVR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 501 QrQKGKEQYQK--ENDKNKFHIINEFDAKFYVNFDDYLDTGIFLDHRKIRQLVAKAAKNKTLLNLFSYTCTASVHAALKG 578
Cdd:COG1092 160 Q-LEGLPQYEGvlYGEAPEEVEVEENGLKFLVDLTDGQKTGLFLDQRENRARVAELAKGKRVLNLFSYTGGFSVHAAAGG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 579 AK-TTSVDMSNTYLEWGKNNFTLNNIDAkKHSFIQADCISWLKT---NKDKFDVIFLDPPTFSNSKRmdDILDIQRDHEL 654
Cdd:COG1092 239 AKsVTSVDLSATALEWAKENAALNGLDD-RHEFVQADAFDWLRElarEGERFDLIILDPPAFAKSKK--DLFDAQRDYKD 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489106589 655 LINLAMDSLKKDGILYFSNNYRRFKMS--PQILE------KFNCENIDKICLSRDFLSNKNIHNCWEIK 715
Cdd:COG1092 316 LNRLALKLLAPGGILVTSSCSRHFSLDlfLEILAraardaGRRVRIIERLTQPPDHPVLPAFPEGEYLK 384
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
6-389 |
6.40e-44 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 162.15 E-value: 6.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 6 FFVSCAKGIELLLKDELERLGISSQEKLAG---VEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQ-QDLYEFISSIN 81
Cdd:NF040721 3 FYATLSPGLEKISAEEIEELGGKIKEIREGkgrVFFEGDLELIPKLNYLSRTLERIVILLHREKFEGSlEDIYKRVYSID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 82 WmDYFAVDKTFKI--IISGKHyDFNnTMFVSQKTKDAIVDQFRNVINQRPNIDTENPDNVIKLHLHKqfvNVFLcLNID- 158
Cdd:NF040721 83 F-SFIKPEQSFAIrpLRVGEH-DFT-SIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIF---DELL-VGIDt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 159 ----SLHKRSYRQFQGQAPLKESLAAAILIKAGWleelkKHQPILIDPMCGSGTILIEAALMAKNIAPVLLNKEF---KI 231
Cdd:NF040721 156 tgdeGLHKRGYRVYQHPAHLNPTIASSLIYLSGW-----KDEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFafkKI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 232 FNSKFHNQELWDNLLEIAknsqkvtnaiicGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESEGLIVTNPP 311
Cdd:NF040721 231 FGHELLEKIKKDVELKIY------------GIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPP 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489106589 312 YGERLYGDQLDEllDIFNGFGDRLSQDFYGWKVAVLTsfadsikemqlrTTERNKFYNGAIETilyQFKINEHAKFKH 389
Cdd:NF040721 299 YGLRIGKKRIIK--KLYNNFLRSAKKILHKRSRIVVI------------TAEKKIFEEAAAKN---GFEIIEEFNVMY 359
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
6-155 |
1.85e-42 |
|
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: 150.81 E-value: 1.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 6 FFVSCAKGIELLLKDELERLGISSQEKL-AGVEFEGSIKDAYKVCIYSYLASQVMLKVATDKVINQQDLYEFISSINWMD 84
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEDVEVGpGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489106589 85 YFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDQFRNViNQRPNIDTENPDNVIKLHLHKQFVNVFLCL 155
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDL 150
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
163-378 |
5.16e-39 |
|
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: 142.49 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 163 RSYRQFQGQAPLKESLAAAILIKAGWLEElkkhQPILiDPMCGSGTILIEAALMAKNIAPVLLnkefkifnskfhnqelw 242
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPG----DPLL-DPMCGSGTILIEAALMGANIAPGKF----------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 243 dnlleiaknsQKVTNAIICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESEGLIVTNPPYGERLygDQLD 322
Cdd:pfam01170 59 ----------DARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRL--GSKG 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489106589 323 ELLDIFNGFGDRLSQDF--YGWKVAVLTSFADSIKEMQLRTTERNKFYNGAIETILYQ 378
Cdd:pfam01170 127 ALEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| Methyltrans_SAM |
pfam10672 |
S-adenosylmethionine-dependent methyltransferase; Members of this family are ... |
520-636 |
7.67e-17 |
|
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: 81.46 E-value: 7.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 520 IINEFDAKFYVNFDDYLDTGIFLDHRKIRQLVAKAAKNKTLLNLFSYTCTASVHAALKGA-KTTSVDMSNTYLEWGKNNF 598
Cdd:pfam10672 87 VVVENGLKYQLDIGRNQNFGLFLDMRLGRRWVQENAKGKNVLNLFAYTCGFSVAAIAGGAsQVVNVDMARGSLNKGRDNH 166
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489106589 599 TLNNIDAKKHSFIQADCI-SWLKTNK-DKFDVIFLDPPTF 636
Cdd:pfam10672 167 RLNGHDLGRVSFLGHDIFkSWGKIKKlGPYDLVIIDPPSF 206
|
|
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
521-669 |
8.50e-17 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 82.96 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 521 INEFDAKFYVNFDDYLDTGIFLDHRKIRQLVAKAAKNKTLLNLFSYTCTASVHAALKGAK-TTSVDMSNTYLEWGKNNFT 599
Cdd:PRK15128 185 IEEHGMKLLVDIQGGHKTGYYLDQRDSRLATRRYVENKRVLNCFSYTGGFAVSALMGGCSqVVSVDTSQEALDIARQNVE 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489106589 600 LNNIDAKKHSFIQADCISWLKTNKD---KFDVIFLDPPTFSNSKrmDDILDIQRDHELLINLAMDSLKKDGIL 669
Cdd:PRK15128 265 LNKLDLSKAEFVRDDVFKLLRTYRDrgeKFDVIVMDPPKFVENK--SQLMGACRGYKDINMLAIQLLNPGGIL 335
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
199-331 |
5.20e-15 |
|
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: 73.44 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 199 LIDPMCGSGTILIEAALMAKNIApvllnkefkifnskfhnqelwdnlleiaknsqkvtnaiicGFDIDNNVLDKAQRNIY 278
Cdd:COG1041 30 VLDPFCGTGTILIEAGLLGRRVI----------------------------------------GSDIDPKMVEGARENLE 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489106589 279 QAGVEDVvTVKRQDIRDLENEFESEGLIVTNPPYGeRLYGDQLDELLDIFNGF 331
Cdd:COG1041 70 HYGYEDA-DVIRGDARDLPLADESVDAIVTDPPYG-RSSKISGEELLELYEKA 120
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
71-153 |
4.43e-11 |
|
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: 59.21 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 71 QDLYE-FISSINWMDYFAVDKTFKIIISGKHYDFNntmFVSQKTKDAIVDQFRNVINQRPnIDTENPDNVIKLHLHKQFV 149
Cdd:smart00981 3 EDLYEtALELIRWEKIFKEGKTFAVRAKRRGKNHE---FTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKDKA 78
|
....
gi 489106589 150 NVFL 153
Cdd:smart00981 79 YLSI 82
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
252-312 |
7.00e-10 |
|
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443299 [Multi-domain] Cd Length: 238 Bit Score: 59.77 E-value: 7.00e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489106589 252 SQKVTNAIICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENEFESEG--LIVTNPPY 312
Cdd:COG4123 56 AQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSfdLVVSNPPY 118
|
|
| THUMP |
cd11688 |
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ... |
6-151 |
2.17e-06 |
|
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: 47.87 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 6 FFVSCAKGIELLLKDELERLGISSQEKL-------AGVEFEG-SIKDAYKVCIYSYLASQVMLKVATDKViNQQDLYEFI 77
Cdd:cd11688 1 VFATTGKGLEEILAAELYELLEVRGFDAeiqvvphGRVHFKTdTDEAVYQLVMWSRLISRIMPPLGECKA-DLEDLYETA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489106589 78 SSINWMDYFAVDKTFKIIISGKHYDFNNTMFVSQKTKDAIVDqfrnviNQRPNIDTENPDNVIKLHLHKQFVNV 151
Cdd:cd11688 80 LEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVD------AFNPEVDLDNPDIVVNVEVHKEIASI 147
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
559-672 |
2.76e-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: 43.57 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 559 TLLNLFSYT-CTASVHAALKGAKTTSVDMS---NTYLEWGKNNFTLNNIDakkhsFIQADCISWLKTNKDKFDVIFLDPP 634
Cdd:cd02440 1 RVLDLGCGTgALALALASGPGARVTGVDISpvaLELARKAAAALLADNVE-----VLKGDAEELPPEADESFDVIISDPP 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 489106589 635 TFSNSKRMDDILDIQRDHellinlamdsLKKDGILYFS 672
Cdd:cd02440 76 LHHLVEDLARFLEEARRL----------LKPGGVLVLT 103
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
257-312 |
2.46e-04 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 43.60 E-value: 2.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489106589 257 NAIICGFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDlenEFESEG---LIVTNPPY 312
Cdd:COG2890 136 DARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFE---PLPGDGrfdLIVSNPPY 191
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
571-634 |
5.73e-04 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 41.42 E-value: 5.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489106589 571 SVHAALKGAKTTSVDMSNTYLEWGKNNFTLNNIDAKKHSFIQADCISWLKtnKDKFDVIFLDPP 634
Cdd:PRK14968 38 AIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLFEPFR--GDKFDVILFNPP 99
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
548-634 |
3.13e-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: 40.54 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 548 RQLVAKA------AKNKTLLNLFSYTCTASVHAALKGAKTTSVDMSNTYLEWGKNNFTLNNIDakKHSFIQADCISWLKT 621
Cdd:COG2265 219 EALYAAAlewldlTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLK--NVEFVAGDLEEVLPE 296
|
90
....*....|....*
gi 489106589 622 --NKDKFDVIFLDPP 634
Cdd:COG2265 297 llWGGRPDVVVLDPP 311
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
50-155 |
3.15e-03 |
|
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: 38.57 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 50 IYSYLASQVMLKVATDKVINQQDLYEFISSINWMDYFAVDKTFKIII--SGKHYDFNntmfvSQKTKDAIVDQFRNVINQ 127
Cdd:pfam02926 43 ALEKAPGIERFPVAETCEADLEDILELAKEIIKDKFKKEGETFAVRVkrRGKNHEFT-----SLEINREVGKAIVEKTGL 117
|
90 100
....*....|....*....|....*...
gi 489106589 128 RpnIDTENPDNVIKLHLHKQFVNVFLCL 155
Cdd:pfam02926 118 K--VDLENPDIVVHVEIIKDKAYISIDR 143
|
|
| hemK_rel_arch |
TIGR00537 |
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
556-651 |
3.64e-03 |
|
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 129628 [Multi-domain] Cd Length: 179 Bit Score: 39.07 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 556 KNKTLLNLFSYTCTASVHAALKGAKTTSVDMSNTYLEWGKNNFTLNNIDAkkhSFIQADCiswLKTNKDKFDVIFLDPPT 635
Cdd:TIGR00537 19 KPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGL---DVVMTDL---FKGVRGKFDVILFNPPY 92
|
90
....*....|....*...
gi 489106589 636 F--SNSKRMDDILDIQRD 651
Cdd:TIGR00537 93 LplEDDLRRGDWLDVAID 110
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
262-299 |
4.41e-03 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 38.37 E-value: 4.41e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489106589 262 GFDIDNNVLDKAQRNIYQAGVEDVVTVKRQDIRDLENE 299
Cdd:COG2230 79 GVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAD 116
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
569-672 |
5.54e-03 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 38.74 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489106589 569 TASVHAALKGAKTTSVDMSNTYLEWGKNNFT---LNNIDakkhsFIQADCISWLKTNKDKFDVIFldpptfsnskrMDDI 645
Cdd:COG0500 40 NLLALAARFGGRVIGIDLSPEAIALARARAAkagLGNVE-----FLVADLAELDPLPAESFDLVV-----------AFGV 103
|
90 100 110
....*....|....*....|....*....|
gi 489106589 646 L---DIQRDHELLINLAmDSLKKDGILYFS 672
Cdd:COG0500 104 LhhlPPEEREALLRELA-RALKPGGVLLLS 132
|
|
| |
