|
Name |
Accession |
Description |
Interval |
E-value |
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
5-370 |
0e+00 |
|
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: 586.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 5 TLIATAAMGIEALVAREVRDLGYE-CQVENSKVTFEADEKAICRTNLWLRTADRVKIKVGEFKATTFDELFEKTKALNWG 83
Cdd:COG0116 2 ELFATCARGLEALLADELKELGAEdVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 84 DYIPENGEFPVIGKSLKSELFSVSDCQRIVKKAVVEKLKTTYKRTTWFEEDGPLFRIEIAMLKDIATLTIDASGVGLHKR 163
Cdd:COG0116 82 EYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHKR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 164 GYRVDQGEAPLKETLAASLIKLTNWKPDRPFVDPFCGSGTIPIEAALIGQNIAPGFNRGFASDEWGWVGKQNWREARQEA 243
Cdd:COG0116 162 GYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNRDFAFEKWPDFDAELWQELREEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 244 EDLANYDQPLQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFTTKEDYGYVVTNPPYGERLSEKALVEQLYKEM 323
Cdd:COG0116 242 EARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYGERLGEEEELEALYREL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446443379 324 GQVFR-PLDTWSAYVLTSYEAFEKCYGKDASKKRKLFNGFIRTDYYQY 370
Cdd:COG0116 322 GDVLKqRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
5-361 |
5.22e-87 |
|
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: 277.45 E-value: 5.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 5 TLIATAAMGIEALVAREVRDLG-YECQVENSKVTFEADEKAICRTNLWLRTADRVKIKVGEFKATTFDELFEKTKALNWG 83
Cdd:PRK11783 3 SLFASCAKGLEELLKDELEALGaSECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAIDWT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 84 DYIPENGEFPVIgkslkselFSVSDC---------QRiVKKAVVEKLKTTYKRTTWFEEDGPLFRIEIAMLKDIATLTID 154
Cdd:PRK11783 83 EHFSPDKTFAVD--------FSGTNDeirntqfgaLK-VKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 155 ASGVGLHKRGYRVDQGEAPLKETLAASLIKLTNW-KPDRPFVDPFCGSGTIPIEAALIGQNIAPGFNRgfasDEWG---W 230
Cdd:PRK11783 154 LSGESLHQRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHR----ERWGfsgW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 231 VG--KQNWREARQEAEDLANY---DQPLQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFT---TKEDYGYVVT 302
Cdd:PRK11783 230 LGhdEALWQELLEEAQERARAglaELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKnplPKGPTGLVIS 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 303 NPPYGERLSEKALVEQLYKEMGQVFR-PLDTWSAYVLTSYEAFEKCYGKDASKKRKLFNG 361
Cdd:PRK11783 310 NPPYGERLGEEPALIALYSQLGRRLKqQFGGWNAALFSSSPELLSCLGLRADKQYKLKNG 369
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
163-369 |
8.96e-68 |
|
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: 211.83 E-value: 8.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 163 RGYRVDQGEAPLKETLAASLIKLTNWKPDRPFVDPFCGSGTIPIEAALIGQNIAPGFNRgfasdewgwvgkqnwrearqe 242
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFD--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 243 aedlANYDQPlqIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFTTKED-YGYVVTNPPYGERLSEKALVEQLYK 321
Cdd:pfam01170 60 ----ARVRAP--LYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGsVDVIVTNPPYGIRLGSKGALEALYP 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446443379 322 EMGQVFRPL---DTWSAYVLTSYEAFEKCYGKDASKKRKLFNGFIRTDYYQ 369
Cdd:pfam01170 134 EFLREAKRVlrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
6-322 |
1.00e-53 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 181.80 E-value: 1.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 6 LIATAAMGIEALVAREVRDLG---YECQVENSKVTFEADEKAICRTNLWLRTADRVKIKVGEFKAT-TFDELFEKTKALN 81
Cdd:NF040721 3 FYATLSPGLEKISAEEIEELGgkiKEIREGKGRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEgSLEDIYKRVYSID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 82 WgDYIPENGEFPVIGKSLKSELFSVSDCQRIVKKAVVEKLKTTYKRTTWFEEDGP--LFRIEIamLKDIATLTIDASG-V 158
Cdd:NF040721 83 F-SFIKPEQSFAIRPLRVGEHDFTSIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPdvIVRVEL--IFDELLVGIDTTGdE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 159 GLHKRGYRVDQGEAPLKETLAASLIKLTNWKPDRPFVDPFCGSGTIPIEAALIGQNIAPG-FNRGFA-SDEWGwvgkqnw 236
Cdd:NF040721 160 GLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGkFREDFAfKKIFG------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 237 rearQEAEDLANYDQPLQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQmqvKDFTTKEDY----GYVVTNPPYGERLSE 312
Cdd:NF040721 233 ----HELLEKIKKDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQ---GDATKLDKYfdsvDVIVTNPPYGLRIGK 305
|
330
....*....|
gi 446443379 313 KALVEQLYKE 322
Cdd:NF040721 306 KRIIKKLYNN 315
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
6-157 |
1.25e-48 |
|
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: 161.59 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 6 LIATAAMGIEALVAREVRDLGYE-CQVENSKVTFEADEKAICRTNLWLRTADRVKIKVGEFKATTFDELFEKTKALNWGD 84
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEdVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446443379 85 YIPENGEFPVIGKSLKSELFSVSDCQRIVKKAVVEKLKTTYKRtTWFEEDGPLFRIEIAMLKDIATLTIDASG 157
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKGKR-PSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
246-306 |
4.69e-06 |
|
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: 47.73 E-value: 4.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446443379 246 LANYDQPLQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFTTKEDYGYVVTNPPY 306
Cdd:TIGR00536 132 LAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKIDIIVSNPPY 192
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
69-154 |
1.30e-05 |
|
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: 43.03 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 69 TFDELFEKTKAL-NWGDYIPENGEFPVIGKSLKselFSVSDCQRIVKKAVVEKLKTTY-KRTTWFEEdgPLFRIEIAMLK 146
Cdd:smart00981 1 DLEDLYETALELiRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKLLEKTgGRKVDLKN--PDVVIRVELRK 75
|
....*...
gi 446443379 147 DIATLTID 154
Cdd:smart00981 76 DKAYLSID 83
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
5-370 |
0e+00 |
|
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: 586.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 5 TLIATAAMGIEALVAREVRDLGYE-CQVENSKVTFEADEKAICRTNLWLRTADRVKIKVGEFKATTFDELFEKTKALNWG 83
Cdd:COG0116 2 ELFATCARGLEALLADELKELGAEdVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAIPWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 84 DYIPENGEFPVIGKSLKSELFSVSDCQRIVKKAVVEKLKTTYKRTTWFEEDGPLFRIEIAMLKDIATLTIDASGVGLHKR 163
Cdd:COG0116 82 EYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHKR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 164 GYRVDQGEAPLKETLAASLIKLTNWKPDRPFVDPFCGSGTIPIEAALIGQNIAPGFNRGFASDEWGWVGKQNWREARQEA 243
Cdd:COG0116 162 GYREAQGEAPLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNRDFAFEKWPDFDAELWQELREEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 244 EDLANYDQPLQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFTTKEDYGYVVTNPPYGERLSEKALVEQLYKEM 323
Cdd:COG0116 242 EARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYGERLGEEEELEALYREL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446443379 324 GQVFR-PLDTWSAYVLTSYEAFEKCYGKDASKKRKLFNGFIRTDYYQY 370
Cdd:COG0116 322 GDVLKqRFKGWSAYILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
5-361 |
5.22e-87 |
|
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: 277.45 E-value: 5.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 5 TLIATAAMGIEALVAREVRDLG-YECQVENSKVTFEADEKAICRTNLWLRTADRVKIKVGEFKATTFDELFEKTKALNWG 83
Cdd:PRK11783 3 SLFASCAKGLEELLKDELEALGaSECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAIDWT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 84 DYIPENGEFPVIgkslkselFSVSDC---------QRiVKKAVVEKLKTTYKRTTWFEEDGPLFRIEIAMLKDIATLTID 154
Cdd:PRK11783 83 EHFSPDKTFAVD--------FSGTNDeirntqfgaLK-VKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 155 ASGVGLHKRGYRVDQGEAPLKETLAASLIKLTNW-KPDRPFVDPFCGSGTIPIEAALIGQNIAPGFNRgfasDEWG---W 230
Cdd:PRK11783 154 LSGESLHQRGYRQATGEAPLKENLAAAILLRSGWpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGLHR----ERWGfsgW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 231 VG--KQNWREARQEAEDLANY---DQPLQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFT---TKEDYGYVVT 302
Cdd:PRK11783 230 LGhdEALWQELLEEAQERARAglaELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKnplPKGPTGLVIS 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 303 NPPYGERLSEKALVEQLYKEMGQVFR-PLDTWSAYVLTSYEAFEKCYGKDASKKRKLFNG 361
Cdd:PRK11783 310 NPPYGERLGEEPALIALYSQLGRRLKqQFGGWNAALFSSSPELLSCLGLRADKQYKLKNG 369
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
163-369 |
8.96e-68 |
|
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: 211.83 E-value: 8.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 163 RGYRVDQGEAPLKETLAASLIKLTNWKPDRPFVDPFCGSGTIPIEAALIGQNIAPGFNRgfasdewgwvgkqnwrearqe 242
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFD--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 243 aedlANYDQPlqIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFTTKED-YGYVVTNPPYGERLSEKALVEQLYK 321
Cdd:pfam01170 60 ----ARVRAP--LYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGsVDVIVTNPPYGIRLGSKGALEALYP 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446443379 322 EMGQVFRPL---DTWSAYVLTSYEAFEKCYGKDASKKRKLFNGFIRTDYYQ 369
Cdd:pfam01170 134 EFLREAKRVlrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
6-322 |
1.00e-53 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 181.80 E-value: 1.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 6 LIATAAMGIEALVAREVRDLG---YECQVENSKVTFEADEKAICRTNLWLRTADRVKIKVGEFKAT-TFDELFEKTKALN 81
Cdd:NF040721 3 FYATLSPGLEKISAEEIEELGgkiKEIREGKGRVFFEGDLELIPKLNYLSRTLERIVILLHREKFEgSLEDIYKRVYSID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 82 WgDYIPENGEFPVIGKSLKSELFSVSDCQRIVKKAVVEKLKTTYKRTTWFEEDGP--LFRIEIamLKDIATLTIDASG-V 158
Cdd:NF040721 83 F-SFIKPEQSFAIRPLRVGEHDFTSIDIGRVAGEAVIDSYLRDKGVRLKVNLDEPdvIVRVEL--IFDELLVGIDTTGdE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 159 GLHKRGYRVDQGEAPLKETLAASLIKLTNWKPDRPFVDPFCGSGTIPIEAALIGQNIAPG-FNRGFA-SDEWGwvgkqnw 236
Cdd:NF040721 160 GLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPPGkFREDFAfKKIFG------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 237 rearQEAEDLANYDQPLQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQmqvKDFTTKEDY----GYVVTNPPYGERLSE 312
Cdd:NF040721 233 ----HELLEKIKKDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQ---GDATKLDKYfdsvDVIVTNPPYGLRIGK 305
|
330
....*....|
gi 446443379 313 KALVEQLYKE 322
Cdd:NF040721 306 KRIIKKLYNN 315
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
6-157 |
1.25e-48 |
|
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: 161.59 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 6 LIATAAMGIEALVAREVRDLGYE-CQVENSKVTFEADEKAICRTNLWLRTADRVKIKVGEFKATTFDELFEKTKALNWGD 84
Cdd:cd11715 1 FFATCPPGLEELLAAELKALGAEdVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446443379 85 YIPENGEFPVIGKSLKSELFSVSDCQRIVKKAVVEKLKTTYKRtTWFEEDGPLFRIEIAMLKDIATLTIDASG 157
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKGKR-PSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
174-328 |
1.49e-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: 73.83 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 174 LKETLAASLIKLTNWKPDRPFVDPFCGSGTIPIEAALIGqniapgfnrgfasdewgwvgkqnwrearqeaedlanydqpL 253
Cdd:COG1041 10 LDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLG----------------------------------------R 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446443379 254 QIIGSDIDHRMIRVAQDNAEEVGLGDlITFKQMQVKDFTTKED-YGYVVTNPPYGerLSEKALVEQLYKEMGQVFR 328
Cdd:COG1041 50 RVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADEsVDAIVTDPPYG--RSSKISGEELLELYEKALE 122
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
19-124 |
4.97e-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: 60.14 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 19 AREVRDLGYECQVENSKVTFEADEKAICRTNLWLRTADRvkIKVGEFKATTFDELFEKTKALNWGDYIPENGEFPVIGKS 98
Cdd:pfam02926 14 VEVVRSGRGRILVVLKGENPEEDRELLKEALEKAPGIER--FPVAETCEADLEDILELAKEIIKDKFKKEGETFAVRVKR 91
|
90 100
....*....|....*....|....*..
gi 446443379 99 L-KSELFSVSDCQRIVKKAVVEKLKTT 124
Cdd:pfam02926 92 RgKNHEFTSLEINREVGKAIVEKTGLK 118
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
246-306 |
4.69e-06 |
|
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: 47.73 E-value: 4.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446443379 246 LANYDQPLQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFTTKEDYGYVVTNPPY 306
Cdd:TIGR00536 132 LAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKIDIIVSNPPY 192
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
69-154 |
1.30e-05 |
|
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: 43.03 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 69 TFDELFEKTKAL-NWGDYIPENGEFPVIGKSLKselFSVSDCQRIVKKAVVEKLKTTY-KRTTWFEEdgPLFRIEIAMLK 146
Cdd:smart00981 1 DLEDLYETALELiRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKLLEKTgGRKVDLKN--PDVVIRVELRK 75
|
....*...
gi 446443379 147 DIATLTID 154
Cdd:smart00981 76 DKAYLSID 83
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
178-307 |
8.48e-05 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 42.97 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 178 LAASLIKLTNWKPD---RPFVDPFCGSGTIPIEAALIGqniapgfnrgfasdewgwvgkqnwrearqeAEDLanydqplq 254
Cdd:COG2263 30 LAAELLHLAYLRGDiegKTVLDLGCGTGMLAIGAALLG------------------------------AKKV-------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446443379 255 iIGSDIDHRMIRVAQDNAEEvgLGDLITFKQMQVKDFTTKEDYGYVVTNPPYG 307
Cdd:COG2263 72 -VGVDIDPEALEIARENAER--LGVRVDFIRADVTRIPLGGSVDTVVMNPPFG 121
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
253-306 |
1.60e-04 |
|
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: 42.82 E-value: 1.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446443379 253 LQIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQVKDFT---TKEDYGYVVTNPPY 306
Cdd:COG4123 62 ARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAaelPPGSFDLVVSNPPY 118
|
|
| HsdM |
COG0286 |
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms]; |
182-321 |
3.40e-04 |
|
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
Pssm-ID: 440055 [Multi-domain] Cd Length: 243 Bit Score: 41.71 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 182 LIKLTNWKPDRPFVDPFCGSGTIPIEAAligqniapgfnrgfasdewgwvgkqnwREARQEAEDLANydqPLQIIGSDID 261
Cdd:COG0286 35 MVELLDPKPGETVYDPACGSGGFLVEAA---------------------------EYLKEHGGDERK---KLSLYGQEIN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446443379 262 HRMIRVAQ-------DNAEEVGLGDLITfkqmqvKDFTTKEDYGYVVTNPPYGERLSEKALVEQLYK 321
Cdd:COG0286 85 PTTYRLAKmnlllhgIGDPNIELGDTLS------NDGDELEKFDVVLANPPFGGKWKKEELKDDLLG 145
|
|
| COG1743 |
COG1743 |
Adenine-specific DNA methylase, contains a Zn-ribbon domain [Replication, recombination and ... |
158-246 |
5.60e-04 |
|
Adenine-specific DNA methylase, contains a Zn-ribbon domain [Replication, recombination and repair];
Pssm-ID: 441349 [Multi-domain] Cd Length: 871 Bit Score: 42.24 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443379 158 VGLHKRGYRVDQGEAPLKETLAA--SLIKLTNWKPDRPFVDPFCGSGTIPIEAA----------------LIGQ---NIA 216
Cdd:COG1743 75 LGIGPERELVAWENSPNEEVLEEarAEIREAWGGELPTVLDPFAGGGSIPLEALrlglevvasdlnpvavLILKatlEYP 154
|
90 100 110
....*....|....*....|....*....|...
gi 446443379 217 PGFNRGFASD--EWG-WVGKqnwrEARQEAEDL 246
Cdd:COG1743 155 PKFGEGLAEDvrRWGeWIRE----EAEKRIGEL 183
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
254-306 |
9.46e-04 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 40.52 E-value: 9.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446443379 254 QIIGSDIDHRMIRVAQDNAEEVGLGDLITFKQMQV-KDFTTKEDYGYVVTNPPY 306
Cdd:COG2890 138 RVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLfEPLPGDGRFDLIVSNPPY 191
|
|
| |
