|
Name |
Accession |
Description |
Interval |
E-value |
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
1-373 |
7.51e-99 |
|
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: 297.78 E-value: 7.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 1 MRFFATTFSGLEDIAAAELSSLLGGEAEADVGKVFFTASLEECLKVNYAAQTVNRVFLLLLREHAETLDEIERLAASVDF 80
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 81 GEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRASTGVRLRVDLNNPDIEVYGILRNTELLLGVNTTGESLHR 160
Cdd:COG0116 81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 161 RFYRRGFHRAALSPTVANTLVRLSGWRRHMVLLDPFTGSGTIPLETALYGLGISPGARREnLRFEKIPVFKSIDSARIRE 240
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNRD-FAFEKWPDFDAELWQELRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 241 ELLKREDP-GTVEAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLVeyVDREVDKVVCNPPFGVRL-RLREPEKF 318
Cdd:COG0116 240 EAEARIKRdPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLE--PPAEPGLIITNPPYGERLgEEEELEAL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 315425042 319 YTEAFTAIAQACPHASLTVIVNKPvtvlkALEKS-GYIPLSVRKVLLGDLSSYIFH 373
Cdd:COG0116 318 YRELGDVLKQRFKGWSAYILTSDP-----ELEKAiGLKASKRRKLYNGGLECRLLQ 368
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
1-372 |
5.22e-88 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 270.39 E-value: 5.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 1 MRFFATTFSGLEDIAAAELSSLLGGEAEADVGK--VFFTASLEECLKVNYAAQTVNRVFLLLLREHAE-TLDEIERLAAS 77
Cdd:NF040721 1 MEFYATLSPGLEKISAEEIEELGGKIKEIREGKgrVFFEGDLELIPKLNYLSRTLERIVILLHREKFEgSLEDIYKRVYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 78 VDFgEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRASTGVRLRVDLNNPDIEVYGILRNTELLLGVNTTG-E 156
Cdd:NF040721 81 IDF-SFIKPEQSFAIRPLRVGEHDFTSIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGdE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 157 SLHRRFYRRGFHRAALSPTVANTLVRLSGWRRHMVLLDPFTGSGTIPLETALYGLGISPGARRENLRFEKIpvFKsidsa 236
Cdd:NF040721 160 GLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKI--FG----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 237 riREELLKREDPGTVEAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLVEYVDrEVDKVVCNPPFGVRL-RLREP 315
Cdd:NF040721 233 --HELLEKIKKDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFD-SVDVIVTNPPYGLRIgKKRII 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 315425042 316 EKFYTEAFTAIAQACP-HASLTVIVNKPVTVLKALEKSGYIPLSVRKVLLGDLSSYIF 372
Cdd:NF040721 310 KKLYNNFLRSAKKILHkRSRIVVITAEKKIFEEAAAKNGFEIIEEFNVMYGGLLTKVF 367
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
1-310 |
4.59e-44 |
|
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: 161.89 E-value: 4.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 1 MRFFATTFSGLEDIAAAELSSLLGGEAEADVGKVFFTASLEECLKVNYAAQTVNRVFLLLLREHAETLDEIERLAASVDF 80
Cdd:PRK11783 2 NSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAIDW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 81 GEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRASTGVRLRVDLNNPDIEVYGILRNTELLLGVNTTGESLHR 160
Cdd:PRK11783 82 TEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLHQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 161 RFYRRGFHRAALSPTVANTLVRLSGWRRHMV-LLDPFTGSGTIPLETALYGLGISPGARRENLRFEKIPVF------KSI 233
Cdd:PRK11783 162 RGYRQATGEAPLKENLAAAILLRSGWPQEGTpLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHdealwqELL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315425042 234 DSARIREELLKREDPGTVeaIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLvEYVDREVDK--VVCNPPFGVRL 310
Cdd:PRK11783 242 EEAQERARAGLAELPSKF--YGSDIDPRVIQAARKNARRAGVAELITFEVKDVADL-KNPLPKGPTglVISNPPYGERL 317
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
3-155 |
5.06e-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: 144.26 E-value: 5.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 3 FFATTFSGLEDIAAAELSSLLGGEAEADVGKVFFTASLEECLKVNYAAQTVNRVFLLLLREHAETLDEIERLAASVDFGE 82
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315425042 83 FIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRAStGVRLRVDLNNPDIEVYGILRNTELLLGVNTTG 155
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
161-321 |
6.77e-21 |
|
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: 88.95 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 161 RFYRRGFHRAALSPTVANTLVRLSGWRRHMVLLDPFTGSGTIPLETALYGLGISPGARRENLRFekipvfksidsarire 240
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 241 ellkredpgtvEAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVfRLVEYVDREVDKVVCNPPFGVRL-RLREPEKFY 319
Cdd:pfam01170 65 -----------PLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADA-ADLPLLEGSVDVIVTNPPYGIRLgSKGALEALY 132
|
..
gi 315425042 320 TE 321
Cdd:pfam01170 133 PE 134
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
67-152 |
3.32e-12 |
|
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: 61.52 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 67 TLDEIERLA-ASVDFGEFIDREQSFAVRAERVG-LHVFTSLDIAAAVGKAVIDSYrastgVRLRVDLNNPDIEVYGILRN 144
Cdd:smart00981 1 DLEDLYETAlELIRWEKIFKEGKTFAVRAKRRGkNHEFTSLEVKRAIGDKLLEKT-----GGRKVDLKNPDVVIRVELRK 75
|
....*...
gi 315425042 145 TELLLGVN 152
Cdd:smart00981 76 DKAYLSID 83
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
252-306 |
1.46e-03 |
|
HemK family putative methylases; 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. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]
Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 315425042 252 EAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLVEYVdrEVDKVVCNPPF 306
Cdd:TIGR00536 140 EVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQ--KIDIIVSNPPY 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
1-373 |
7.51e-99 |
|
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: 297.78 E-value: 7.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 1 MRFFATTFSGLEDIAAAELSSLLGGEAEADVGKVFFTASLEECLKVNYAAQTVNRVFLLLLREHAETLDEIERLAASVDF 80
Cdd:COG0116 1 FELFATCARGLEALLADELKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 81 GEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRASTGVRLRVDLNNPDIEVYGILRNTELLLGVNTTGESLHR 160
Cdd:COG0116 81 EEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 161 RFYRRGFHRAALSPTVANTLVRLSGWRRHMVLLDPFTGSGTIPLETALYGLGISPGARREnLRFEKIPVFKSIDSARIRE 240
Cdd:COG0116 161 RGYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNRD-FAFEKWPDFDAELWQELRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 241 ELLKREDP-GTVEAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLVeyVDREVDKVVCNPPFGVRL-RLREPEKF 318
Cdd:COG0116 240 EAEARIKRdPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLE--PPAEPGLIITNPPYGERLgEEEELEAL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 315425042 319 YTEAFTAIAQACPHASLTVIVNKPvtvlkALEKS-GYIPLSVRKVLLGDLSSYIFH 373
Cdd:COG0116 318 YRELGDVLKQRFKGWSAYILTSDP-----ELEKAiGLKASKRRKLYNGGLECRLLQ 368
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
1-372 |
5.22e-88 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 270.39 E-value: 5.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 1 MRFFATTFSGLEDIAAAELSSLLGGEAEADVGK--VFFTASLEECLKVNYAAQTVNRVFLLLLREHAE-TLDEIERLAAS 77
Cdd:NF040721 1 MEFYATLSPGLEKISAEEIEELGGKIKEIREGKgrVFFEGDLELIPKLNYLSRTLERIVILLHREKFEgSLEDIYKRVYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 78 VDFgEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRASTGVRLRVDLNNPDIEVYGILRNTELLLGVNTTG-E 156
Cdd:NF040721 81 IDF-SFIKPEQSFAIRPLRVGEHDFTSIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDTTGdE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 157 SLHRRFYRRGFHRAALSPTVANTLVRLSGWRRHMVLLDPFTGSGTIPLETALYGLGISPGARRENLRFEKIpvFKsidsa 236
Cdd:NF040721 160 GLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGKFREDFAFKKI--FG----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 237 riREELLKREDPGTVEAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLVEYVDrEVDKVVCNPPFGVRL-RLREP 315
Cdd:NF040721 233 --HELLEKIKKDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFD-SVDVIVTNPPYGLRIgKKRII 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 315425042 316 EKFYTEAFTAIAQACP-HASLTVIVNKPVTVLKALEKSGYIPLSVRKVLLGDLSSYIF 372
Cdd:NF040721 310 KKLYNNFLRSAKKILHkRSRIVVITAEKKIFEEAAAKNGFEIIEEFNVMYGGLLTKVF 367
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
1-310 |
4.59e-44 |
|
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: 161.89 E-value: 4.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 1 MRFFATTFSGLEDIAAAELSSLLGGEAEADVGKVFFTASLEECLKVNYAAQTVNRVFLLLLREHAETLDEIERLAASVDF 80
Cdd:PRK11783 2 NSLFASCAKGLEELLKDELEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAIDW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 81 GEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRASTGVRLRVDLNNPDIEVYGILRNTELLLGVNTTGESLHR 160
Cdd:PRK11783 82 TEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLHQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 161 RFYRRGFHRAALSPTVANTLVRLSGWRRHMV-LLDPFTGSGTIPLETALYGLGISPGARRENLRFEKIPVF------KSI 233
Cdd:PRK11783 162 RGYRQATGEAPLKENLAAAILLRSGWPQEGTpLLDPMCGSGTLLIEAAMMAADIAPGLHRERWGFSGWLGHdealwqELL 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315425042 234 DSARIREELLKREDPGTVeaIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLvEYVDREVDK--VVCNPPFGVRL 310
Cdd:PRK11783 242 EEAQERARAGLAELPSKF--YGSDIDPRVIQAARKNARRAGVAELITFEVKDVADL-KNPLPKGPTglVISNPPYGERL 317
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
3-155 |
5.06e-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: 144.26 E-value: 5.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 3 FFATTFSGLEDIAAAELSSLLGGEAEADVGKVFFTASLEECLKVNYAAQTVNRVFLLLLREHAETLDEIERLAASVDFGE 82
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315425042 83 FIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRAStGVRLRVDLNNPDIEVYGILRNTELLLGVNTTG 155
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
161-321 |
6.77e-21 |
|
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: 88.95 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 161 RFYRRGFHRAALSPTVANTLVRLSGWRRHMVLLDPFTGSGTIPLETALYGLGISPGARRENLRFekipvfksidsarire 240
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 241 ellkredpgtvEAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVfRLVEYVDREVDKVVCNPPFGVRL-RLREPEKFY 319
Cdd:pfam01170 65 -----------PLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADA-ADLPLLEGSVDVIVTNPPYGIRLgSKGALEALY 132
|
..
gi 315425042 320 TE 321
Cdd:pfam01170 133 PE 134
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
167-359 |
1.45e-17 |
|
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: 79.22 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 167 FHRAALSPTVANTLVRLSGWRRHMVLLDPFTGSGTIPLETALYGLgispgarrenlrfekipvfksidsarireellkre 246
Cdd:COG1041 5 FYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGR----------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 247 dpgtvEAIGIDVSPKSLNLALDSLETFGREtGVRFVQGDVFRLvEYVDREVDKVVCNPPFG--VRLRLREPEKFYTEAFT 324
Cdd:COG1041 50 -----RVIGSDIDPKMVEGARENLEHYGYE-DADVIRGDARDL-PLADESVDAIVTDPPYGrsSKISGEELLELYEKALE 122
|
170 180 190
....*....|....*....|....*....|....*
gi 315425042 325 AIAQACPHASLTVIVNkPVTVLKALEKSGYIPLSV 359
Cdd:COG1041 123 EAARVLKPGGRVVIVT-PRDIDELLEEAGFKVLER 156
|
|
| THUMP_SPOUT |
cd11718 |
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are ... |
3-139 |
2.77e-12 |
|
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are characterized by containing an N-terminal THUMP domain and a C-terminal SPOUT RNA methyltransferase domain. No functional information is available 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: 212587 Cd Length: 145 Bit Score: 63.84 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 3 FFATTFSGLEDIAAAELSSLLGGeAEADV------GKVFFTASLEECLKVNYAAQTVNRVFLLLlREHAETLDEIERLAA 76
Cdd:cd11718 1 ILVKTQLGMERIAASYIKEIDPD-AKVEPapmgflGLVLVESDEDKKDELALRVPEVERVIPVD-AEVKADLDEIVRVAE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315425042 77 SVdfGEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVidsyRASTGVrlRVDLNNPDIEVY 139
Cdd:cd11718 79 EI--AKHISEGETFAVRTTRRGKHDFTSIDVNVVLGAAV----KELTGA--EVDLNNPDKVVY 133
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
67-152 |
3.32e-12 |
|
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: 61.52 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 67 TLDEIERLA-ASVDFGEFIDREQSFAVRAERVG-LHVFTSLDIAAAVGKAVIDSYrastgVRLRVDLNNPDIEVYGILRN 144
Cdd:smart00981 1 DLEDLYETAlELIRWEKIFKEGKTFAVRAKRRGkNHEFTSLEVKRAIGDKLLEKT-----GGRKVDLKNPDVVIRVELRK 75
|
....*...
gi 315425042 145 TELLLGVN 152
Cdd:smart00981 76 DKAYLSID 83
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
65-153 |
1.94e-11 |
|
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: 61.30 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 65 AETLDEIERLAASVDFGEFIDREQSFAVRAERVGL-HVFTSLDIAAAVGKAVIDSYRAstgvrlRVDLNNPDIEVYGILR 143
Cdd:pfam02926 60 EADLEDILELAKEIIKDKFKKEGETFAVRVKRRGKnHEFTSLEINREVGKAIVEKTGL------KVDLENPDIVVHVEII 133
|
90
....*....|
gi 315425042 144 NTELLLGVNT 153
Cdd:pfam02926 134 KDKAYISIDR 143
|
|
| THUMP_ThiI |
cd11716 |
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ... |
67-139 |
1.32e-10 |
|
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. 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: 212585 Cd Length: 166 Bit Score: 59.38 E-value: 1.32e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315425042 67 TLDEIERLAASVdFGEFIDREQSFAVRAERVG-LHVFTSLDIAAAVGKAVIDSYRAstgvrLRVDLNNPDIEVY 139
Cdd:cd11716 80 DLEDIKEAALEL-LKEELKKGKTFKVRAKRADkSFPFTSMEINREVGAALLENTPD-----LKVDLKNPDVTIR 147
|
|
| THUMP |
cd11688 |
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ... |
3-139 |
2.11e-10 |
|
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: 58.65 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 3 FFATTFSGLEDIAAAELSSLLGGEAE------ADVGKVFF-TASLEECLKVNYAAQTVNRVfLLLLREHAETLDEIERLA 75
Cdd:cd11688 1 VFATTGKGLEEILAAELYELLEVRGFdaeiqvVPHGRVHFkTDTDEAVYQLVMWSRLISRI-MPPLGECKADLEDLYETA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315425042 76 ASVDFGEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRAstgvrlRVDLNNPDIEVY 139
Cdd:cd11688 80 LEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFNP------EVDLDNPDIVVN 137
|
|
| ThiI |
COG0301 |
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ... |
67-139 |
5.67e-09 |
|
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440070 [Multi-domain] Cd Length: 382 Bit Score: 57.02 E-value: 5.67e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315425042 67 TLDEIERLAASVdFGEFIDrEQSFAVRAERVGLHV-FTSLDIAAAVGKAVIDSYRAstgvrLRVDLNNPDIEVY 139
Cdd:COG0301 82 DLEDIKEAALEL-AKEELK-GKTFKVRAKRAGKHFpFTSPELEREVGGALLENTPG-----LKVDLKNPDVTIR 148
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
242-351 |
3.75e-06 |
|
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 47.11 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 242 LLKREDPGTVEAIgiDVSPKSLNLALDSLETFGREtGVRFVQGDVFRLVEyvDREVDKVVCNPPF--GVRLRLREPEKFY 319
Cdd:COG2813 67 LAKRNPEARVTLV--DVNARAVELARANAAANGLE-NVEVLWSDGLSGVP--DGSFDLILSNPPFhaGRAVDKEVAHALI 141
|
90 100 110
....*....|....*....|....*....|..
gi 315425042 320 TEAFTAIAqacPHASLTVIVNKPVTVLKALEK 351
Cdd:COG2813 142 ADAARHLR---PGGELWLVANRHLPYERKLEE 170
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
252-309 |
5.53e-06 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 46.82 E-value: 5.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 315425042 252 EAIGIDVSPKSLNLALDSLETFGREtgVRFVQGDVFRLveYVDREVDKVVCNPPFGVR 309
Cdd:COG2263 70 KVVGVDIDPEALEIARENAERLGVR--VDFIRADVTRI--PLGGSVDTVVMNPPFGAQ 123
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
252-306 |
1.20e-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: 43.96 E-value: 1.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 315425042 252 EAIGIDVSPKSLNLALDSLETFGREtGVRFVQGDVFRLVEYVDREVDKVVCNPPF 306
Cdd:cd02440 23 RVTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELPPEADESFDVIISDPPL 76
|
|
| Tan1 |
COG1818 |
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ... |
68-139 |
1.71e-05 |
|
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure and biogenesis]; tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441423 Cd Length: 162 Bit Score: 44.49 E-value: 1.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315425042 68 LDEIERLAASVdFGEFIDREQSFAVRAERVGLHVFTSLDIAAAVGKAVIDSyrastgvrLRVDLNNPDIEVY 139
Cdd:COG1818 80 LEEIVEAAKEL-AKKKIPEGETFAVRCEKRGKSKLSSREVIRAIGEAIKRG--------AKVDLENPDWVVL 142
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
243-305 |
8.16e-05 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 43.99 E-value: 8.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315425042 243 LKREDPGtVEAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLVEyVDREVDKVVCNPP 305
Cdd:COG2890 130 LAKERPD-ARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFEPLP-GDGRFDLIVSNPP 190
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
240-323 |
6.56e-04 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 38.70 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 240 EELLKRedpGTVEAIGIDVSPKSLNLALDSLETFGREtgVRFVQGDVFRLvEYVDREVDKVVCNPPFGVrLRLREPEKFY 319
Cdd:pfam13649 13 LALARR---GGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDL-PFPDGSFDLVVSSGVLHH-LPDPDLEAAL 85
|
....
gi 315425042 320 TEAF 323
Cdd:pfam13649 86 REIA 89
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
252-306 |
1.46e-03 |
|
HemK family putative methylases; 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. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]
Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 315425042 252 EAIGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLVEYVdrEVDKVVCNPPF 306
Cdd:TIGR00536 140 EVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQ--KIDIIVSNPPY 192
|
|
| Methyltransf_15 |
pfam09445 |
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ... |
254-307 |
6.80e-03 |
|
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.
Pssm-ID: 370496 Cd Length: 165 Bit Score: 36.93 E-value: 6.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 315425042 254 IGIDVSPKSLNLALDSLETFGRETGVRFVQGDVFRLVEYVDREVDK---VVCNPPFG 307
Cdd:pfam09445 26 ISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKFEKIKydcVFASPPWG 82
|
|
| THUMP_THUMPD1_like |
cd11717 |
THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins ... |
67-140 |
7.66e-03 |
|
THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins including THUMP domain-containing protein 1 and Saccharomyces cerevisiae Tan1. Tan1 is non essential and has been shown to be required for the formation of the modified nucleoside N(4)-acetylcytidine (ac(4)C) in tRNA. To date, there is no functional information available about THUMPD1. 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: 212586 Cd Length: 158 Bit Score: 36.79 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315425042 67 TLDEIERLAASVDFGEFIDREQ--SFAVRAERVGLHVFTSLDIAAAVGKAVIDSYRastgvrlrVDLNNPD----IEVYG 140
Cdd:cd11717 78 SLEEIEKLAKELLKKHFPTAEPpkTFAVECKSRNNNKLSRDEVIKAVAELVPEIHK--------VDLKNPDkvilVEVIK 149
|
|
| |
