|
Name |
Accession |
Description |
Interval |
E-value |
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
33-387 |
1.76e-157 |
|
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: 447.63 E-value: 1.76e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 33 TAVKTLHRAVRFRTNQAGFYRVHLQARLPFRFLRELSHFPCRNREQLHSGVQAAaDWHHWLPPSRSFRVEATGSMPGLSH 112
Cdd:COG0116 25 EDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAI-PWEEYLPPDGTFAVDATSVKSKLFH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 113 SHYSALAVKNALVDWQREHWGERSSIDLDNPDLVLHLHLGGADASLYLDGSGESLHRRGYRPAMGLAPLKENLAAGLIAL 192
Cdd:COG0116 104 SQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHKRGYREAQGEAPLKETLAAALLLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 193 TGWDGSLPLVDPLCGSGTLLIEAAAMALGRAPGLELaqagRFALQRWPDFEALLWRDELAVATAlgrskLIDGSPMAPIF 272
Cdd:COG0116 184 SGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR----DFAFEKWPDFDAELWQELREEAEA-----RIKRDPPLPIF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 273 GFDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDFQPPQQAGLIVCNPPYGVRLGNEENLEQLFFDLGQMLKQRCSGWQL 352
Cdd:COG0116 255 GSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYGERLGEEEELEALYRELGDVLKQRFKGWSA 334
|
330 340 350
....*....|....*....|....*....|....*
gi 2720532957 353 WLLSGDPASTAAMRLKARRRIPISNGGIDCRWLNY 387
Cdd:COG0116 335 YILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
35-389 |
1.30e-117 |
|
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: 357.19 E-value: 1.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 35 VKTLHRAVRFRTNQAGFYRVHLQARLPFRFLRELSHFPCRNREQLHSGVQAAaDWHHWLPPSRSFRVEATGSMPGLSHSH 114
Cdd:PRK11783 28 CKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAI-DWTEHFSPDKTFAVDFSGTNDEIRNTQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 115 YSALAVKNALVDWQREHWGERSSIDLDNPDLVLHLHLGGADASLYLDGSGESLHRRGYRPAMGLAPLKENLAAGLIALTG 194
Cdd:PRK11783 107 FGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGEAPLKENLAAAILLRSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 195 W-DGSLPLVDPLCGSGTLLIEAAAMALGRAPGLelaQAGRFALQRWPDFEALLWRDELAVATALGRSKLIDgsPMAPIFG 273
Cdd:PRK11783 187 WpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGL---HRERWGFSGWLGHDEALWQELLEEAQERARAGLAE--LPSKFYG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 274 FDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDFQPP---QQAGLIVCNPPYGVRLGNEENLEQLFFDLGQMLKQRCSGW 350
Cdd:PRK11783 262 SDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPlpkGPTGLVISNPPYGERLGEEPALIALYSQLGRRLKQQFGGW 341
|
330 340 350
....*....|....*....|....*....|....*....
gi 2720532957 351 QLWLLSGDPASTAAMRLKARRRIPISNGGIDCRWLNYEI 389
Cdd:PRK11783 342 NAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTI 380
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
170-386 |
1.51e-43 |
|
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: 149.81 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 170 RGYRPAMGLAPLKENLAAGLIALTGWDGSLPLVDPLCGSGTLLIEAAAMALGRAPGLELAQagrfalqrwpdfeallwrd 249
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDAR------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 250 elavatalgrsklidgsPMAPIFGFDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDFQPPQQA-GLIVCNPPYGVRLGN 328
Cdd:pfam01170 62 -----------------VRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSvDVIVTNPPYGIRLGS 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 329 EENLEQLFFDLGQMLKQRC--SGWQLWLLSGDPASTAAMRLKARRRIPISNGGIDCRWLN 386
Cdd:pfam01170 125 KGALEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
12-164 |
6.32e-31 |
|
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: 115.37 E-value: 6.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 12 IAVVPPGLELAAAAELTALDCTAVKTLHRAVRFRTNQAGFYRVHLQARLPFRFLRELSHFPCRNREQLHSGVQaAADWHH 91
Cdd:cd11715 2 FATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAK-AIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2720532957 92 WLPPSRSFRVEATGSMPGLSHSHYSALAVKNALVDWQREHwGERSSIDLDNPDLVLHLHLGGADASLYLDGSG 164
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
88-336 |
8.29e-28 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 112.46 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 88 DWHhWLPPSRSFRVEAT--GSmpglsHSHYS---ALAVKNALVDWQREHWGERSSIDLDNPDLVLHLHLGGADASLYLDG 162
Cdd:NF040721 82 DFS-FIKPEQSFAIRPLrvGE-----HDFTSidiGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 163 SG-ESLHRRGYRPAMGLAPLKENLAAGLIALTGWDGSLPLVDPLCGSGTLLIEAAAMALGRAPglelaqaGRFalqrwpd 241
Cdd:NF040721 156 TGdEGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPP-------GKF------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 242 feallwRDELAVATALGRSKL--IDGSPMAPIFGFDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDF-QPPQQAGLIVC 318
Cdd:NF040721 222 ------REDFAFKKIFGHELLekIKKDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLdKYFDSVDVIVT 295
|
250
....*....|....*...
gi 2720532957 319 NPPYGVRLGNEENLEQLF 336
Cdd:NF040721 296 NPPYGLRIGKKRIIKKLY 313
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
75-161 |
1.51e-15 |
|
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: 71.15 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 75 NREQLHSGVQAAADWHHWLPPSRSFRVEATGSmpgLSHSHYSALAVKNALVDWQREHWGERsSIDLDNPDLVLHLHLGGA 154
Cdd:smart00981 1 DLEDLYETALELIRWEKIFKEGKTFAVRAKRR---GKNHEFTSLEVKRAIGDKLLEKTGGR-KVDLKNPDVVIRVELRKD 76
|
....*..
gi 2720532957 155 DASLYLD 161
Cdd:smart00981 77 KAYLSID 83
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
240-333 |
4.97e-06 |
|
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]
Pssm-ID: 274634 [Multi-domain] Cd Length: 250 Bit Score: 47.46 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 240 PDFEALLwrdELAVATALGRSKLID---GS-----------PMAPIFGFDNNAAVVEQAKQNAAAAGVSPwLQFELADFR 305
Cdd:TIGR03534 71 PETEELV---EAALERLKKGPRVLDlgtGSgaialalakerPDARVTAVDISPEALAVARKNARRLGLEN-VEFLQGDWF 146
|
90 100
....*....|....*....|....*...
gi 2720532957 306 DFQPPQQAGLIVCNPPYgVRLGNEENLE 333
Cdd:TIGR03534 147 EPLPSGKFDLIVSNPPY-IPEADIHLLD 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RlmL |
COG0116 |
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ... |
33-387 |
1.76e-157 |
|
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: 447.63 E-value: 1.76e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 33 TAVKTLHRAVRFRTNQAGFYRVHLQARLPFRFLRELSHFPCRNREQLHSGVQAAaDWHHWLPPSRSFRVEATGSMPGLSH 112
Cdd:COG0116 25 EDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKAI-PWEEYLPPDGTFAVDATSVKSKLFH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 113 SHYSALAVKNALVDWQREHWGERSSIDLDNPDLVLHLHLGGADASLYLDGSGESLHRRGYRPAMGLAPLKENLAAGLIAL 192
Cdd:COG0116 104 SQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGESLHKRGYREAQGEAPLKETLAAALLLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 193 TGWDGSLPLVDPLCGSGTLLIEAAAMALGRAPGLELaqagRFALQRWPDFEALLWRDELAVATAlgrskLIDGSPMAPIF 272
Cdd:COG0116 184 SGWDGDRPLVDPMCGSGTILIEAALIAANIAPGLNR----DFAFEKWPDFDAELWQELREEAEA-----RIKRDPPLPIF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 273 GFDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDFQPPQQAGLIVCNPPYGVRLGNEENLEQLFFDLGQMLKQRCSGWQL 352
Cdd:COG0116 255 GSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYGERLGEEEELEALYRELGDVLKQRFKGWSA 334
|
330 340 350
....*....|....*....|....*....|....*
gi 2720532957 353 WLLSGDPASTAAMRLKARRRIPISNGGIDCRWLNY 387
Cdd:COG0116 335 YILTSDPELEKAIGLKASKRRKLYNGGLECRLLQY 369
|
|
| rlmL |
PRK11783 |
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ... |
35-389 |
1.30e-117 |
|
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: 357.19 E-value: 1.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 35 VKTLHRAVRFRTNQAGFYRVHLQARLPFRFLRELSHFPCRNREQLHSGVQAAaDWHHWLPPSRSFRVEATGSMPGLSHSH 114
Cdd:PRK11783 28 CKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQAI-DWTEHFSPDKTFAVDFSGTNDEIRNTQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 115 YSALAVKNALVDWQREHWGERSSIDLDNPDLVLHLHLGGADASLYLDGSGESLHRRGYRPAMGLAPLKENLAAGLIALTG 194
Cdd:PRK11783 107 FGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGEAPLKENLAAAILLRSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 195 W-DGSLPLVDPLCGSGTLLIEAAAMALGRAPGLelaQAGRFALQRWPDFEALLWRDELAVATALGRSKLIDgsPMAPIFG 273
Cdd:PRK11783 187 WpQEGTPLLDPMCGSGTLLIEAAMMAADIAPGL---HRERWGFSGWLGHDEALWQELLEEAQERARAGLAE--LPSKFYG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 274 FDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDFQPP---QQAGLIVCNPPYGVRLGNEENLEQLFFDLGQMLKQRCSGW 350
Cdd:PRK11783 262 SDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPlpkGPTGLVISNPPYGERLGEEPALIALYSQLGRRLKQQFGGW 341
|
330 340 350
....*....|....*....|....*....|....*....
gi 2720532957 351 QLWLLSGDPASTAAMRLKARRRIPISNGGIDCRWLNYEI 389
Cdd:PRK11783 342 NAALFSSSPELLSCLGLRADKQYKLKNGALECVLKNYTI 380
|
|
| UPF0020 |
pfam01170 |
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
170-386 |
1.51e-43 |
|
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: 149.81 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 170 RGYRPAMGLAPLKENLAAGLIALTGWDGSLPLVDPLCGSGTLLIEAAAMALGRAPGLELAQagrfalqrwpdfeallwrd 249
Cdd:pfam01170 1 RGYRPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDAR------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 250 elavatalgrsklidgsPMAPIFGFDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDFQPPQQA-GLIVCNPPYGVRLGN 328
Cdd:pfam01170 62 -----------------VRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSvDVIVTNPPYGIRLGS 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 329 EENLEQLFFDLGQMLKQRC--SGWQLWLLSGDPASTAAMRLKARRRIPISNGGIDCRWLN 386
Cdd:pfam01170 125 KGALEALYPEFLREAKRVLrgGGWLVLLTAENKDFEKAARERAWRKKKEFNVHIGGTRVI 184
|
|
| THUMP_AdoMetMT |
cd11715 |
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
12-164 |
6.32e-31 |
|
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: 115.37 E-value: 6.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 12 IAVVPPGLELAAAAELTALDCTAVKTLHRAVRFRTNQAGFYRVHLQARLPFRFLRELSHFPCRNREQLHSGVQaAADWHH 91
Cdd:cd11715 2 FATCPPGLEELLAAELKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAK-AIDWED 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2720532957 92 WLPPSRSFRVEATGSMPGLSHSHYSALAVKNALVDWQREHwGERSSIDLDNPDLVLHLHLGGADASLYLDGSG 164
Cdd:cd11715 81 YLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
|
|
| Trm14_Arch |
NF040721 |
tRNA (guanine(6)-N2)-methyltransferase; |
88-336 |
8.29e-28 |
|
tRNA (guanine(6)-N2)-methyltransferase;
Pssm-ID: 468685 [Multi-domain] Cd Length: 370 Bit Score: 112.46 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 88 DWHhWLPPSRSFRVEAT--GSmpglsHSHYS---ALAVKNALVDWQREHWGERSSIDLDNPDLVLHLHLGGADASLYLDG 162
Cdd:NF040721 82 DFS-FIKPEQSFAIRPLrvGE-----HDFTSidiGRVAGEAVIDSYLRDKGVRLKVNLDEPDVIVRVELIFDELLVGIDT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 163 SG-ESLHRRGYRPAMGLAPLKENLAAGLIALTGWDGSLPLVDPLCGSGTLLIEAAAMALGRAPglelaqaGRFalqrwpd 241
Cdd:NF040721 156 TGdEGLHKRGYRVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAALIKRNIPP-------GKF------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 242 feallwRDELAVATALGRSKL--IDGSPMAPIFGFDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDF-QPPQQAGLIVC 318
Cdd:NF040721 222 ------REDFAFKKIFGHELLekIKKDVELKIYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLdKYFDSVDVIVT 295
|
250
....*....|....*...
gi 2720532957 319 NPPYGVRLGNEENLEQLF 336
Cdd:NF040721 296 NPPYGLRIGKKRIIKKLY 313
|
|
| THUMP |
smart00981 |
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
75-161 |
1.51e-15 |
|
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: 71.15 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 75 NREQLHSGVQAAADWHHWLPPSRSFRVEATGSmpgLSHSHYSALAVKNALVDWQREHWGERsSIDLDNPDLVLHLHLGGA 154
Cdd:smart00981 1 DLEDLYETALELIRWEKIFKEGKTFAVRAKRR---GKNHEFTSLEVKRAIGDKLLEKTGGR-KVDLKNPDVVIRVELRKD 76
|
....*..
gi 2720532957 155 DASLYLD 161
Cdd:smart00981 77 KAYLSID 83
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
266-322 |
8.86e-08 |
|
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: 52.45 E-value: 8.86e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 266 SPMAPIFGFDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDFQPPQQAG---LIVCNPPY 322
Cdd:COG4123 59 SPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGsfdLVVSNPPY 118
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
262-319 |
1.70e-06 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 45.97 E-value: 1.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2720532957 262 LIDGSPMAPIFGFDNNAAVVEQAKQNAaaagvsPWLQFELADFRDFQPPQQAGLIVCN 319
Cdd:COG4106 19 LAERFPGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEPFDLVVSN 70
|
|
| RF_mod_PrmC |
TIGR03534 |
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ... |
240-333 |
4.97e-06 |
|
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]
Pssm-ID: 274634 [Multi-domain] Cd Length: 250 Bit Score: 47.46 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 240 PDFEALLwrdELAVATALGRSKLID---GS-----------PMAPIFGFDNNAAVVEQAKQNAAAAGVSPwLQFELADFR 305
Cdd:TIGR03534 71 PETEELV---EAALERLKKGPRVLDlgtGSgaialalakerPDARVTAVDISPEALAVARKNARRLGLEN-VEFLQGDWF 146
|
90 100
....*....|....*....|....*...
gi 2720532957 306 DFQPPQQAGLIVCNPPYgVRLGNEENLE 333
Cdd:TIGR03534 147 EPLPSGKFDLIVSNPPY-IPEADIHLLD 173
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
185-336 |
5.94e-06 |
|
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: 46.10 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 185 LAAGLIALTGWDGSLPLVDPLCGSGTLLIEAAAMAlgrapglelaqagrfalqrwpdfeallwrdelavatalgrsklid 264
Cdd:COG1041 14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLG--------------------------------------------- 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2720532957 265 gspmAPIFGFDNNAAVVEQAKQNAAAAGVSPWlQFELADFRDF-QPPQQAGLIVCNPPYGVRL-GNEENLEQLF 336
Cdd:COG1041 49 ----RRVIGSDIDPKMVEGARENLEHYGYEDA-DVIRGDARDLpLADESVDAIVTDPPYGRSSkISGEELLELY 117
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
251-322 |
1.81e-05 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 45.91 E-value: 1.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2720532957 251 LAVATALgrsklidgsPMAPIFGFDNNAAVVEQAKQNAAAAGVSPWLQFELAD-FRDFQPPQQAGLIVCNPPY 322
Cdd:COG2890 128 LALAKER---------PDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDlFEPLPGDGRFDLIVSNPPY 191
|
|
| THUMP |
pfam02926 |
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
86-161 |
2.59e-05 |
|
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: 43.58 E-value: 2.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2720532957 86 AADWHHWLPPSRSFRVEATGsmPGLSHsHYSALAVKNALVDWQREHWGERssIDLDNPDLVLHLHLGGADASLYLD 161
Cdd:pfam02926 72 EIIKDKFKKEGETFAVRVKR--RGKNH-EFTSLEINREVGKAIVEKTGLK--VDLENPDIVVHVEIIKDKAYISID 142
|
|
| HsdM |
COG0286 |
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms]; |
203-355 |
1.15e-04 |
|
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
Pssm-ID: 440055 [Multi-domain] Cd Length: 243 Bit Score: 43.25 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 203 DPLCGSGTLLIEAAamalgrapglelaqagRFALQRWPDFEALLWrdelavatalgrsklidgspmapIFGFDNNAAVVE 282
Cdd:COG0286 49 DPACGSGGFLVEAA----------------EYLKEHGGDERKKLS-----------------------LYGQEINPTTYR 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2720532957 283 QAKQNAAAAGVSPwLQFELADF--RDFQPPQQAGLIVCNPPYGVRLGNEENLEQLFFDLGQMLKQRCSGWQLWLL 355
Cdd:COG0286 90 LAKMNLLLHGIGD-PNIELGDTlsNDGDELEKFDVVLANPPFGGKWKKEELKDDLLGRFGYGLPPKSNADLLFLQ 163
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
271-318 |
1.99e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 41.45 E-value: 1.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2720532957 271 IFGFDNNAAVVEQAKQNAAAAGVSPWLQFELADFRDFQPPQQAGLIVC 318
Cdd:COG2230 77 VTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVS 124
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
266-354 |
2.57e-04 |
|
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: 41.71 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 266 SPMAPIFGFDNNAAVVEQAKQNAAAAGVSPwLQFELADFRDFQPPQQAGLIVCNPPYgvRLGNEEN---LEQLFFDLGQM 342
Cdd:COG2813 71 NPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSGVPDGSFDLILSNPPF--HAGRAVDkevAHALIADAARH 147
|
90
....*....|..
gi 2720532957 343 LKqrcSGWQLWL 354
Cdd:COG2813 148 LR---PGGELWL 156
|
|
| THUMP |
cd11688 |
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ... |
58-159 |
4.84e-04 |
|
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.
Pssm-ID: 212583 Cd Length: 148 Bit Score: 40.16 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 58 ARLPFRFLRELshFPCR-NREQLHSGVQAAAdWHHWLPPSRSFRVEATGSMPGLSHSHYSALAVKNALVDwqrehwGERS 136
Cdd:cd11688 55 SRLISRIMPPL--GECKaDLEDLYETALEIN-EPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVD------AFNP 125
|
90 100
....*....|....*....|...
gi 2720532957 137 SIDLDNPDLVLHLHLGGADASLY 159
Cdd:cd11688 126 EVDLDNPDIVVNVEVHKEIASIA 148
|
|
| PRK01683 |
PRK01683 |
trans-aconitate 2-methyltransferase; Provisional |
267-319 |
1.27e-03 |
|
trans-aconitate 2-methyltransferase; Provisional
Pssm-ID: 234970 Cd Length: 258 Bit Score: 40.31 E-value: 1.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2720532957 267 PMAPIFGFDNNAAVVEQAKQNAaaagvsPWLQFELADFRDFQPPQQAGLIVCN 319
Cdd:PRK01683 54 PAARITGIDSSPAMLAEARSRL------PDCQFVEADIASWQPPQALDLIFAN 100
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
267-322 |
1.28e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 40.15 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2720532957 267 PMAPIFGFDNNAAVVEQAKQNAAAaGVSPWLQFELADFRDFQPPQQAGLIVCNPPY 322
Cdd:PRK09328 131 PDAEVTAVDISPEALAVARRNAKH-GLGARVEFLQGDWFEPLPGGRFDLIVSNPPY 185
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
266-354 |
5.43e-03 |
|
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.
Pssm-ID: 428349 [Multi-domain] Cd Length: 170 Bit Score: 37.57 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720532957 266 SPMAPIFGFDNNAAVVEQAKQNAAAAGVsPWLQFELADFRDFQPPQQAGLIVCNPPYGVRLGNEENL-EQLFFDLGQMLK 344
Cdd:pfam05175 53 SPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYSGVEDGKFDLIISNPPFHAGLATTYNVaQRFIADAKRHLR 131
|
90
....*....|
gi 2720532957 345 qrcSGWQLWL 354
Cdd:pfam05175 132 ---PGGELWI 138
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
251-325 |
5.47e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 37.58 E-value: 5.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2720532957 251 LAVATAL-GRSKLIdgspmapifGFDNNAAVVEQAKQNAAAAGVSpwLQFELADFRDFQPPQQAGLIVCNPPYGVR 325
Cdd:COG2263 59 LAIGAALlGAKKVV---------GVDIDPEALEIARENAERLGVR--VDFIRADVTRIPLGGSVDTVVMNPPFGAQ 123
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
267-319 |
8.20e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 36.63 E-value: 8.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2720532957 267 PMAPIFGFDNNAAVVEQAKQNAAAAGVSPwLQFELADFRDFQ---PPQQAGLIVCN 319
Cdd:pfam13847 27 PNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELPellEDDKFDVVISN 81
|
|
| |
