|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
58-328 |
1.63e-67 |
|
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 439914 [Multi-domain] Cd Length: 441 Bit Score: 217.95 E-value: 1.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 58 GIRMTEPVYLS--PSFDSvlpRYLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKV 135
Cdd:COG0144 211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 136 EKIKQNALLLGLNSIRAFCFDGTKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQP 212
Cdd:COG0144 288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 213 LQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGlsCEQLkqlqrfdpsav 292
Cdd:COG0144 356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG--YLRL----------- 422
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034567161 293 pLPDT-DMDslrearredmlrlankdsiGFFIAKFVK 328
Cdd:COG0144 423 -LPHRhGTD-------------------GFFIARLRK 439
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
78-330 |
2.26e-63 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 207.34 E-value: 2.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 78 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 157
Cdd:PRK14902 231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 158 TKAvkldmvedtegePPFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 234
Cdd:PRK14902 311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 235 TCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrl 313
Cdd:PRK14902 379 TCTIEKEENEEVIEAFLEEHPEFELVPLQHEKPDELVYEVKDGYLQI------------LPNDyGTD------------- 433
|
250
....*....|....*..
gi 1034567161 314 ankdsiGFFIAKFVKCK 330
Cdd:PRK14902 434 ------GFFIAKLRKKG 444
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
92-326 |
4.80e-52 |
|
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.
Pssm-ID: 426109 [Multi-domain] Cd Length: 199 Bit Score: 170.68 E-value: 4.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 92 VLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKavkldmvedteg 171
Cdd:pfam01189 3 LLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 172 ePPFLP--ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQ 246
Cdd:pfam01189 71 -PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 247 VAWALTKFPCLQLQPqepqIGGEGMRGAGLSCEQLKQLqrfdpsavpLPDTDmdslrearredmlrlaNKDsiGFFIAKF 326
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL---------LPHTH----------------NGD--GFFIAKL 198
|
|
| rsmB |
TIGR00563 |
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ... |
81-268 |
1.28e-41 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. The reading frame was originally interpreted as two reading frames, fmu and fmv. The recombinant protein from E. coli was shown to methylate only C967 of small subunit (16S) ribosomal RNA and to produce only m5C at that position. The seed alignment is built from bacterial sequences only. Eukaryotic homologs include Nop2, a protein required for processing pre-rRNA, that is likely also a rRNA methyltransferase, although the fine specificity may differ. Cutoff scores are set to avoid treating archaeal and eukaroytic homologs automatically as functionally equivalent, although they may have very similar roles. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273141 [Multi-domain] Cd Length: 426 Bit Score: 149.63 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 81 LQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMhDQGEVIALDKIFNKVEKIKQNALLLGLnSIRAFCFDGTKA 160
Cdd:TIGR00563 222 VQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELA-PQAQVVALDIHEHRLKRVYENLKRLGL-TIKAETKDGDGR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 161 vkldmvedteGEPPFLP-ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTC 236
Cdd:TIGR00563 300 ----------GPSQWAEnEQFDRILLDAPCSATGvirRHPDIKWLRKPRDIAELAELQSEILDAIWPLLKTGGTLVYATC 369
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034567161 237 TITLAENEEQVAWALTKFPCLQL----QPQEPQIGG 268
Cdd:TIGR00563 370 SVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
|
|
| PUA_NSun6-like |
cd21150 |
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ... |
1-65 |
3.91e-25 |
|
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this subfamily contain PUA domains that co-occur with SAM-dependent methyltransferase domains and may play roles as cytosine-C(5)-methyltransferases specific for tRNAs or rRNAs. Nsun6 binding to its tRNA substrates requires the presence of a 3'-CCA sequence, which is precisely recognized primarily through interactions with residues from the PUA domain, where the molecular surface of the PUA domain snugly fits onto each nucleotide residue of the CCA end. Human RNA:m5C methyltransferase NSun6 (hNSun6) plays a major role in bone metastasis and could be a valuable therapeutic target for bone metastasis and therapy-resistant tumors.
Pssm-ID: 409292 [Multi-domain] Cd Length: 92 Bit Score: 96.75 E-value: 3.91e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034567161 1 MKAGDVISVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKEIFSGLPELkyviRGMGIRMTEPV 65
Cdd:cd21150 31 LKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKP----SGIAVEMTEPV 92
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
100-234 |
1.41e-09 |
|
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: 54.74 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 100 KILDLCAAPGGKTTHIAAlmHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPES 179
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034567161 180 FDRILLDAPCSgmgqrpnmactwsvkevaSYQPLQRKLFTAAVQLLKPEGVLVYS 234
Cdd:cd02440 67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
58-328 |
1.63e-67 |
|
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 439914 [Multi-domain] Cd Length: 441 Bit Score: 217.95 E-value: 1.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 58 GIRMTEPVYLS--PSFDSvlpRYLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKV 135
Cdd:COG0144 211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 136 EKIKQNALLLGLNSIRAFCFDGTKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQP 212
Cdd:COG0144 288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 213 LQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGlsCEQLkqlqrfdpsav 292
Cdd:COG0144 356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG--YLRL----------- 422
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034567161 293 pLPDT-DMDslrearredmlrlankdsiGFFIAKFVK 328
Cdd:COG0144 423 -LPHRhGTD-------------------GFFIARLRK 439
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
78-330 |
2.26e-63 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 207.34 E-value: 2.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 78 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 157
Cdd:PRK14902 231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 158 TKAvkldmvedtegePPFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 234
Cdd:PRK14902 311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 235 TCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrl 313
Cdd:PRK14902 379 TCTIEKEENEEVIEAFLEEHPEFELVPLQHEKPDELVYEVKDGYLQI------------LPNDyGTD------------- 433
|
250
....*....|....*..
gi 1034567161 314 ankdsiGFFIAKFVKCK 330
Cdd:PRK14902 434 ------GFFIAKLRKKG 444
|
|
| PRK14901 |
PRK14901 |
16S rRNA methyltransferase B; Provisional |
81-266 |
3.76e-60 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237856 [Multi-domain] Cd Length: 434 Bit Score: 198.61 E-value: 3.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 81 LQNLP------------SA-LVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGL 147
Cdd:PRK14901 223 IRQLPgyeegwwtvqdrSAqLVAPLLDPQPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSASRLKKLQENAQRLGL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 148 NSIRAFCFDGTKAVkldmvedteGEPPFLPESFDRILLDAPCSGMG---QRPNMacTWSV--KEVASYQPLQRKLFTAAV 222
Cdd:PRK14901 303 KSIKILAADSRNLL---------ELKPQWRGYFDRILLDAPCSGLGtlhRHPDA--RWRQtpEKIQELAPLQAELLESLA 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034567161 223 QLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQI 266
Cdd:PRK14901 372 PLLKPGGTLVYATCTLHPAENEAQIEQFLARHPDWKLEPPKQKI 415
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
92-326 |
4.80e-52 |
|
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.
Pssm-ID: 426109 [Multi-domain] Cd Length: 199 Bit Score: 170.68 E-value: 4.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 92 VLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKavkldmvedteg 171
Cdd:pfam01189 3 LLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 172 ePPFLP--ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQ 246
Cdd:pfam01189 71 -PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 247 VAWALTKFPCLQLQPqepqIGGEGMRGAGLSCEQLKQLqrfdpsavpLPDTDmdslrearredmlrlaNKDsiGFFIAKF 326
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL---------LPHTH----------------NGD--GFFIAKL 198
|
|
| PRK14904 |
PRK14904 |
16S rRNA methyltransferase B; Provisional |
82-261 |
3.92e-46 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237858 [Multi-domain] Cd Length: 445 Bit Score: 162.15 E-value: 3.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 82 QNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKav 161
Cdd:PRK14904 235 QNPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYPQKLEKIRSHASALGITIIETIEGDARS-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 162 kldmvedtegeppFLPE-SFDRILLDAPCSG---MGQRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCT 237
Cdd:PRK14904 313 -------------FSPEeQPDAILLDAPCTGtgvLGRRAELRWKLTPEKLAELVGLQAELLDHAASLLKPGGVLVYATCS 379
|
170 180
....*....|....*....|....
gi 1034567161 238 ITLAENEEQVAWALTKFPCLQLQP 261
Cdd:PRK14904 380 IEPEENELQIEAFLQRHPEFSAEP 403
|
|
| rsmB |
TIGR00563 |
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ... |
81-268 |
1.28e-41 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. The reading frame was originally interpreted as two reading frames, fmu and fmv. The recombinant protein from E. coli was shown to methylate only C967 of small subunit (16S) ribosomal RNA and to produce only m5C at that position. The seed alignment is built from bacterial sequences only. Eukaryotic homologs include Nop2, a protein required for processing pre-rRNA, that is likely also a rRNA methyltransferase, although the fine specificity may differ. Cutoff scores are set to avoid treating archaeal and eukaroytic homologs automatically as functionally equivalent, although they may have very similar roles. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 273141 [Multi-domain] Cd Length: 426 Bit Score: 149.63 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 81 LQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMhDQGEVIALDKIFNKVEKIKQNALLLGLnSIRAFCFDGTKA 160
Cdd:TIGR00563 222 VQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELA-PQAQVVALDIHEHRLKRVYENLKRLGL-TIKAETKDGDGR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 161 vkldmvedteGEPPFLP-ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTC 236
Cdd:TIGR00563 300 ----------GPSQWAEnEQFDRILLDAPCSATGvirRHPDIKWLRKPRDIAELAELQSEILDAIWPLLKTGGTLVYATC 369
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034567161 237 TITLAENEEQVAWALTKFPCLQL----QPQEPQIGG 268
Cdd:TIGR00563 370 SVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
65-328 |
2.78e-41 |
|
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 188051 [Multi-domain] Cd Length: 264 Bit Score: 144.92 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 65 VYLSPSFDSVLPRYL----FLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQ 140
Cdd:TIGR00446 35 VKESPFSIGSTPEYLfgyyYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALIS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 141 NALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPEsFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKL 217
Cdd:TIGR00446 115 NINRMGVLNTIVINADGRKF------------GAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 218 FTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLqpqEPQIGGEGMrGAGLSCEQLKQLQRFDPSavplpdt 297
Cdd:TIGR00446 182 IDAAIDALKPGGVLVYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDEFF-GINIGKGEVKGALRVFPQ------- 250
|
250 260 270
....*....|....*....|....*....|.
gi 1034567161 298 dmdslrearredmlrlaNKDSIGFFIAKFVK 328
Cdd:TIGR00446 251 -----------------NYDCEGFFVAKLRK 264
|
|
| PRK10901 |
PRK10901 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
88-328 |
5.04e-40 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 236790 [Multi-domain] Cd Length: 427 Bit Score: 145.33 E-value: 5.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 88 LVSHVLNPQPGEKILDLCAAPGGKTTHIAALmHDQGEVIALDKIFNKVEKIKQNALLLGLNSiRAFCFDGTKAvkldmve 167
Cdd:PRK10901 235 LAATLLAPQNGERVLDACAAPGGKTAHILEL-APQAQVVALDIDAQRLERVRENLQRLGLKA-TVIVGDARDP------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 168 DT--EGEPpflpesFDRILLDAPCSGMG-----------QRPNmactwsvkEVASYQPLQRKLFTAAVQLLKPEGVLVYS 234
Cdd:PRK10901 306 AQwwDGQP------FDRILLDAPCSATGvirrhpdikwlRRPE--------DIAALAALQSEILDALWPLLKPGGTLLYA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 235 TCTITLAENEEQVAWALTKFPCLQLQPQ-EPQIGGegmrgaglsceqlKQLqrfdpsavpLP-DTDMDslrearredmlr 312
Cdd:PRK10901 372 TCSILPEENEQQIKAFLARHPDAELLDTgTPQQPG-------------RQL---------LPgEEDGD------------ 417
|
250
....*....|....*.
gi 1034567161 313 lankdsiGFFIAKFVK 328
Cdd:PRK10901 418 -------GFFYALLIK 426
|
|
| yebU |
PRK11933 |
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed |
73-255 |
1.38e-31 |
|
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
Pssm-ID: 183387 [Multi-domain] Cd Length: 470 Bit Score: 123.09 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 73 SVLPrylflqnlPSALVSHvlNPQPgEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRA 152
Cdd:PRK11933 100 SMLP--------VAALFAD--DNAP-QRVLDMAAAPGSKTTQIAALMNNQGAIVANEYSASRVKVLHANISRCGVSNVAL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 153 FCFDGTkavkldmvedTEGEppFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEG 229
Cdd:PRK11933 169 THFDGR----------VFGA--ALPETFDAILLDAPCSGEGtvrKDPDALKNWSPESNLEIAATQRELIESAFHALKPGG 236
|
170 180
....*....|....*....|....*.
gi 1034567161 230 VLVYSTCTITLAENEEQVAWALTKFP 255
Cdd:PRK11933 237 TLVYSTCTLNREENQAVCLWLKETYP 262
|
|
| PRK14903 |
PRK14903 |
16S rRNA methyltransferase B; Provisional |
78-253 |
5.18e-29 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 184896 [Multi-domain] Cd Length: 431 Bit Score: 115.74 E-value: 5.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 78 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 157
Cdd:PRK14903 218 LATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEKHAKRLKLSSIEIKIADA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 158 TKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 234
Cdd:PRK14903 298 ERLTE------------YVQDTFDRILVDAPCTSLGtarNHPEVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYS 365
|
170 180
....*....|....*....|
gi 1034567161 235 TCTITLAENEEQV-AWALTK 253
Cdd:PRK14903 366 TCTVTKEENTEVVkRFVYEQ 385
|
|
| PUA_NSun6-like |
cd21150 |
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ... |
1-65 |
3.91e-25 |
|
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this subfamily contain PUA domains that co-occur with SAM-dependent methyltransferase domains and may play roles as cytosine-C(5)-methyltransferases specific for tRNAs or rRNAs. Nsun6 binding to its tRNA substrates requires the presence of a 3'-CCA sequence, which is precisely recognized primarily through interactions with residues from the PUA domain, where the molecular surface of the PUA domain snugly fits onto each nucleotide residue of the CCA end. Human RNA:m5C methyltransferase NSun6 (hNSun6) plays a major role in bone metastasis and could be a valuable therapeutic target for bone metastasis and therapy-resistant tumors.
Pssm-ID: 409292 [Multi-domain] Cd Length: 92 Bit Score: 96.75 E-value: 3.91e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034567161 1 MKAGDVISVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKEIFSGLPELkyviRGMGIRMTEPV 65
Cdd:cd21150 31 LKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKP----SGIAVEMTEPV 92
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
100-234 |
1.41e-09 |
|
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: 54.74 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 100 KILDLCAAPGGKTTHIAAlmHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPES 179
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034567161 180 FDRILLDAPCSgmgqrpnmactwsvkevaSYQPLQRKLFTAAVQLLKPEGVLVYS 234
Cdd:cd02440 67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
71-232 |
3.01e-06 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 46.14 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 71 FDSVLPRYlflqNLPSALVSHvLNPQPGEKILDLCAAPGgktTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNsI 150
Cdd:COG2226 1 FDRVAARY----DGREALLAA-LGLRPGARVLDLGCGTG---RLALALAERGARVTGVDISPEMLELARERAAEAGLN-V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 151 RAFCFDGTkavkldmvedtegEPPFLPESFDRILldapcsgmgqrpnmaCTWSVKEVASyqplQRKLFTAAVQLLKPEGV 230
Cdd:COG2226 72 EFVVGDAE-------------DLPFPDGSFDLVI---------------SSFVLHHLPD----PERALAEIARVLKPGGR 119
|
..
gi 1034567161 231 LV 232
Cdd:COG2226 120 LV 121
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
97-236 |
7.53e-04 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 39.32 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 97 PGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGlnsirafcFDGTKAVKLDMvedTEGEPPFL 176
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLG--------FDNVEFEQGDI---EELPELLE 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 177 PESFDRILLDapcsgmgqrpnmactwsvkEVASYQPLQRKLFTAAVQLLKPEGVLVYSTC 236
Cdd:pfam13847 72 DDKFDVVISN-------------------CVLNHIPDPDKVLQEILRVLKPGGRLIISDP 112
|
|
| FtsJ |
pfam01728 |
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
97-232 |
1.58e-03 |
|
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 38.72 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 97 PGEKILDLCAAPGGKTThiAALMHDQGEVIALDKIFNKVEKIKQNAlllGLNSIRAfcfDGTKAVKLDMVEDTEGEPpfl 176
Cdd:pfam01728 21 PGKTVLDLGAAPGGWSQ--VALQRGAGKVVGVDLGPMQLWKPRNDP---GVTFIQG---DIRDPETLDLLEELLGRK--- 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034567161 177 pesFDRILLDApcsgmgqRPNMACTWSVKEVASYQpLQRKLFTAAVQLLKPEGVLV 232
Cdd:pfam01728 90 ---VDLVLSDG-------SPFISGNKVLDHLRSLD-LVKAALEVALELLRKGGNFV 134
|
|
| RlmE |
COG0293 |
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
97-129 |
1.86e-03 |
|
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 38.90 E-value: 1.86e-03
10 20 30
....*....|....*....|....*....|...
gi 1034567161 97 PGEKILDLCAAPGGKTTHIAALMHDQGEVIALD 129
Cdd:COG0293 50 PGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
72-313 |
2.36e-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: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 72 DSVLPRYLFLQNLPSALvshvlnpQPGEKILDLCAAPGGKTTHIAALMHDQgeVIALDkiFNK--VEKIKQNALLLGLNS 149
Cdd:COG0500 8 DELLPGLAALLALLERL-------PKGGRVLDLGCGTGRNLLALAARFGGR--VIGID--LSPeaIALARARAAKAGLGN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 150 IRafcFdgtkavkldMVEDTEGEPPFLPESFDRILLDApcsgmgqrpnmactwsvkeVASYQPLQR--KLFTAAVQLLKP 227
Cdd:COG0500 77 VE---F---------LVADLAELDPLPAESFDLVVAFG-------------------VLHHLPPEEreALLRELARALKP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 228 EGVLVYStctITLAENEEqvawaltkFPCLQLQPQEPQIGGEGMRGAGLSCEQLKQLQRFDpSAVPLPDTDMDSLREARR 307
Cdd:COG0500 126 GGVLLLS---ASDAAAAL--------SLARLLLLATASLLELLLLLRLLALELYLRALLAA-AATEDLRSDALLESANAL 193
|
....*.
gi 1034567161 308 EDMLRL 313
Cdd:COG0500 194 EYLLSK 199
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
71-183 |
2.47e-03 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 38.98 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 71 FDSVLPRYLFLQNLPSALVSHV--------LNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDkiFN----KV--E 136
Cdd:PRK00216 17 FDSIAPKYDLMNDLLSFGLHRVwrrktikwLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLD--FSegmlAVgrE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034567161 137 KIKQNALLLGLNSIRAfcfdgtKAVKLdmvedtegepPFLPESFDRI 183
Cdd:PRK00216 95 KLRDLGLSGNVEFVQG------DAEAL----------PFPDNSFDAV 125
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
98-253 |
3.75e-03 |
|
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: 38.62 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 98 GEKILDLCAAPGGKTthIAALMHDQGEVIALDkIFNK-VEKIKQNALLLGLNS----IRAFCFDGTKAvkldmvEDTEGE 172
Cdd:COG1092 217 GKRVLNLFSYTGGFS--VHAAAGGAKSVTSVD-LSATaLEWAKENAALNGLDDrhefVQADAFDWLRE------LAREGE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 173 ppflpeSFDRILLDAPcsgmgqrpnmacTW--SVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCT--ITLAENEEQVA 248
Cdd:COG1092 288 ------RFDLIILDPP------------AFakSKKDLFDAQRDYKDLNRLALKLLAPGGILVTSSCSrhFSLDLFLEILA 349
|
....*
gi 1034567161 249 WALTK 253
Cdd:COG1092 350 RAARD 354
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
101-229 |
7.31e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 35.23 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567161 101 ILDLCAAPGGKTTHIAALMHdqGEVIALDKIFNKVEKIKQNALLLGLNsIRAFCFDGTkavkldmvedtegEPPFLPESF 180
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAE-------------DLPFPDGSF 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034567161 181 DRILldapCSGMgqrpnMACTWsvkevasyQPLQRKLFTAAVQLLKPEG 229
Cdd:pfam13649 65 DLVV----SSGV-----LHHLP--------DPDLEAALREIARVLKPGG 96
|
|
| rrmJ |
PRK11188 |
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE; |
96-129 |
8.19e-03 |
|
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
Pssm-ID: 183025 Cd Length: 209 Bit Score: 37.02 E-value: 8.19e-03
10 20 30
....*....|....*....|....*....|....
gi 1034567161 96 QPGEKILDLCAAPGGKTTHIAALMHDQGEVIALD 129
Cdd:PRK11188 50 KPGMTVVDLGAAPGGWSQYAVTQIGDKGRVIACD 83
|
|
|