|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
190-465 |
3.78e-66 |
|
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: 219.11 E-value: 3.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 190 ELKGMGIRmTEPVYLSPsfDSV-LPRYLFLQNLP-------------SALVSHVLNPQPGEKILDLCAAPGGKTTHIAAL 255
Cdd:COG0144 194 RLAEEGIE-AEPTPLSP--DGLrLEGPGPVTALPgfreglfsvqdeaSQLVALLLDPKPGERVLDLCAAPGGKTLHLAEL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 256 MHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QR 332
Cdd:COG0144 271 MGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRH 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 333 PNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAG 412
Cdd:COG0144 339 PDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462517651 413 lsCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrlankdsiGFFIAKFVK 465
Cdd:COG0144 419 --YLRL------------LPHRhGTD-------------------GFFIARLRK 439
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
215-467 |
2.96e-61 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 206.18 E-value: 2.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 215 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 294
Cdd:PRK14902 231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 295 TKAvkldmvedtegePPFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 371
Cdd:PRK14902 311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 372 TCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrl 450
Cdd:PRK14902 379 TCTIEKEENEEVIEAFLEEHPEFELVPLQHEKPDELVYEVKDGYLQI------------LPNDyGTD------------- 433
|
250
....*....|....*..
gi 2462517651 451 ankdsiGFFIAKFVKCK 467
Cdd:PRK14902 434 ------GFFIAKLRKKG 444
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
229-463 |
1.43e-50 |
|
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: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 229 VLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKavkldmvedteg 308
Cdd:pfam01189 3 LLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 309 ePPFLP--ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQ 383
Cdd:pfam01189 71 -PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 384 VAWALTKFPCLQLQPqepqIGGEGMRGAGLSCEQLKQLqrfdpsavpLPDTDmdslrearredmlrlaNKDsiGFFIAKF 463
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL---------LPHTH----------------NGD--GFFIAKL 198
|
|
| PUA_NSun6-like |
cd21150 |
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ... |
113-202 |
3.50e-48 |
|
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: 160.31 E-value: 3.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 113 EAIVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKEIFSGLPEL 191
Cdd:cd21150 2 EVIVDRKCGEAVLRGAHVFAPGVLGAPPGLKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKP 81
|
90
....*....|.
gi 2462517651 192 KGMGIRMTEPV 202
Cdd:cd21150 82 SGIAVEMTEPV 92
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
202-465 |
3.80e-40 |
|
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: 3.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 202 VYLSPSFDSVLPRYL----FLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQ 277
Cdd:TIGR00446 35 VKESPFSIGSTPEYLfgyyYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALIS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 278 NALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPEsFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKL 354
Cdd:TIGR00446 115 NINRMGVLNTIVINADGRKF------------GAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 355 FTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLqpqEPQIGGEGMrGAGLSCEQLKQLQRFDPSavplpdt 434
Cdd:TIGR00446 182 IDAAIDALKPGGVLVYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDEFF-GINIGKGEVKGALRVFPQ------- 250
|
250 260 270
....*....|....*....|....*....|.
gi 2462517651 435 dmdslrearredmlrlaNKDSIGFFIAKFVK 465
Cdd:TIGR00446 251 -----------------NYDCEGFFVAKLRK 264
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
237-371 |
1.99e-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: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 237 KILDLCAAPGGKTTHIAAlmHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPES 316
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462517651 317 FDRILLDAPCSgmgqrpnmactwsvkevaSYQPLQRKLFTAAVQLLKPEGVLVYS 371
Cdd:cd02440 67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
| PUA |
smart00359 |
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
115-202 |
7.25e-06 |
|
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 43.78 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 115 IVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYsDIKGKckkgakefdgtkvFLGNGISELSRKEIFSglPELKGM 194
Cdd:smart00359 4 VVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIV-DEKGE-------------PLGIGLANMSSEEIAR--IKGKGL 67
|
....*...
gi 2462517651 195 GIRMTEPV 202
Cdd:smart00359 68 AVKVRRAV 75
|
|
| Tma20 |
COG2016 |
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ... |
122-184 |
1.60e-04 |
|
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441619 [Multi-domain] Cd Length: 154 Bit Score: 42.08 E-value: 1.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462517651 122 NAVLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKckkgakefdgtkvFLGNGISELSRKEI 184
Cdd:COG2016 84 KFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKHGK-------------PLAVGRALVDGEEM 133
|
|
| PUA |
pfam01472 |
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
115-184 |
4.15e-03 |
|
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes. It is predicted that the PUA domain is an RNA binding domain.
Pssm-ID: 426278 [Multi-domain] Cd Length: 74 Bit Score: 35.92 E-value: 4.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 115 IVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDiKGKckkgakefdgtkvFLGNGISELSRKEI 184
Cdd:pfam01472 4 VVDDGAVKAILNGASLLAPGVVRVDGDFRKGDEVVVVTE-KGE-------------LVAVGLANYSSEEL 59
|
|
| PRK14560 |
PRK14560 |
putative RNA-binding protein; Provisional |
124-184 |
7.26e-03 |
|
putative RNA-binding protein; Provisional
Pssm-ID: 237757 [Multi-domain] Cd Length: 160 Bit Score: 37.14 E-value: 7.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462517651 124 VLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKckkgakefdgtkvFLGNGISELSRKEI 184
Cdd:PRK14560 89 VSNGADVMAPGIVEADEDIKEGDIVFVVEETHGK-------------PLAVGRALMDGDEM 136
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
190-465 |
3.78e-66 |
|
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: 219.11 E-value: 3.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 190 ELKGMGIRmTEPVYLSPsfDSV-LPRYLFLQNLP-------------SALVSHVLNPQPGEKILDLCAAPGGKTTHIAAL 255
Cdd:COG0144 194 RLAEEGIE-AEPTPLSP--DGLrLEGPGPVTALPgfreglfsvqdeaSQLVALLLDPKPGERVLDLCAAPGGKTLHLAEL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 256 MHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QR 332
Cdd:COG0144 271 MGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRH 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 333 PNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAG 412
Cdd:COG0144 339 PDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462517651 413 lsCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrlankdsiGFFIAKFVK 465
Cdd:COG0144 419 --YLRL------------LPHRhGTD-------------------GFFIARLRK 439
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
215-467 |
2.96e-61 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 206.18 E-value: 2.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 215 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 294
Cdd:PRK14902 231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 295 TKAvkldmvedtegePPFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 371
Cdd:PRK14902 311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 372 TCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrl 450
Cdd:PRK14902 379 TCTIEKEENEEVIEAFLEEHPEFELVPLQHEKPDELVYEVKDGYLQI------------LPNDyGTD------------- 433
|
250
....*....|....*..
gi 2462517651 451 ankdsiGFFIAKFVKCK 467
Cdd:PRK14902 434 ------GFFIAKLRKKG 444
|
|
| PRK14901 |
PRK14901 |
16S rRNA methyltransferase B; Provisional |
218-403 |
4.30e-58 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237856 [Multi-domain] Cd Length: 434 Bit Score: 197.46 E-value: 4.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 218 LQNLP------------SA-LVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGL 284
Cdd:PRK14901 223 IRQLPgyeegwwtvqdrSAqLVAPLLDPQPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSASRLKKLQENAQRLGL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 285 NSIRAFCFDGTKAVkldmvedteGEPPFLPESFDRILLDAPCSGMG---QRPNMacTWSV--KEVASYQPLQRKLFTAAV 359
Cdd:PRK14901 303 KSIKILAADSRNLL---------ELKPQWRGYFDRILLDAPCSGLGtlhRHPDA--RWRQtpEKIQELAPLQAELLESLA 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462517651 360 QLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQI 403
Cdd:PRK14901 372 PLLKPGGTLVYATCTLHPAENEAQIEQFLARHPDWKLEPPKQKI 415
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
229-463 |
1.43e-50 |
|
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: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 229 VLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKavkldmvedteg 308
Cdd:pfam01189 3 LLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 309 ePPFLP--ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQ 383
Cdd:pfam01189 71 -PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 384 VAWALTKFPCLQLQPqepqIGGEGMRGAGLSCEQLKQLqrfdpsavpLPDTDmdslrearredmlrlaNKDsiGFFIAKF 463
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL---------LPHTH----------------NGD--GFFIAKL 198
|
|
| PUA_NSun6-like |
cd21150 |
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ... |
113-202 |
3.50e-48 |
|
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: 160.31 E-value: 3.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 113 EAIVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKEIFSGLPEL 191
Cdd:cd21150 2 EVIVDRKCGEAVLRGAHVFAPGVLGAPPGLKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKP 81
|
90
....*....|.
gi 2462517651 192 KGMGIRMTEPV 202
Cdd:cd21150 82 SGIAVEMTEPV 92
|
|
| PRK14904 |
PRK14904 |
16S rRNA methyltransferase B; Provisional |
219-398 |
1.03e-44 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237858 [Multi-domain] Cd Length: 445 Bit Score: 162.15 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 219 QNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKav 298
Cdd:PRK14904 235 QNPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYPQKLEKIRSHASALGITIIETIEGDARS-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 299 kldmvedtegeppFLPE-SFDRILLDAPCSG---MGQRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCT 374
Cdd:PRK14904 313 -------------FSPEeQPDAILLDAPCTGtgvLGRRAELRWKLTPEKLAELVGLQAELLDHAASLLKPGGVLVYATCS 379
|
170 180
....*....|....*....|....
gi 2462517651 375 ITLAENEEQVAWALTKFPCLQLQP 398
Cdd:PRK14904 380 IEPEENELQIEAFLQRHPEFSAEP 403
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
202-465 |
3.80e-40 |
|
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: 3.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 202 VYLSPSFDSVLPRYL----FLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQ 277
Cdd:TIGR00446 35 VKESPFSIGSTPEYLfgyyYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALIS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 278 NALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPEsFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKL 354
Cdd:TIGR00446 115 NINRMGVLNTIVINADGRKF------------GAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 355 FTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLqpqEPQIGGEGMrGAGLSCEQLKQLQRFDPSavplpdt 434
Cdd:TIGR00446 182 IDAAIDALKPGGVLVYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDEFF-GINIGKGEVKGALRVFPQ------- 250
|
250 260 270
....*....|....*....|....*....|.
gi 2462517651 435 dmdslrearredmlrlaNKDSIGFFIAKFVK 465
Cdd:TIGR00446 251 -----------------NYDCEGFFVAKLRK 264
|
|
| rsmB |
TIGR00563 |
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ... |
218-405 |
5.56e-40 |
|
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: 148.86 E-value: 5.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 218 LQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMhDQGEVIALDKIFNKVEKIKQNALLLGLnSIRAFCFDGTKA 297
Cdd:TIGR00563 222 VQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELA-PQAQVVALDIHEHRLKRVYENLKRLGL-TIKAETKDGDGR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 298 vkldmvedteGEPPFLP-ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTC 373
Cdd:TIGR00563 300 ----------GPSQWAEnEQFDRILLDAPCSATGvirRHPDIKWLRKPRDIAELAELQSEILDAIWPLLKTGGTLVYATC 369
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462517651 374 TITLAENEEQVAWALTKFPCLQL----QPQEPQIGG 405
Cdd:TIGR00563 370 SVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
|
|
| PRK10901 |
PRK10901 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
225-465 |
9.70e-39 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 236790 [Multi-domain] Cd Length: 427 Bit Score: 145.33 E-value: 9.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 225 LVSHVLNPQPGEKILDLCAAPGGKTTHIAALmHDQGEVIALDKIFNKVEKIKQNALLLGLNSiRAFCFDGTKAvkldmve 304
Cdd:PRK10901 235 LAATLLAPQNGERVLDACAAPGGKTAHILEL-APQAQVVALDIDAQRLERVRENLQRLGLKA-TVIVGDARDP------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 305 DT--EGEPpflpesFDRILLDAPCSGMG-----------QRPNmactwsvkEVASYQPLQRKLFTAAVQLLKPEGVLVYS 371
Cdd:PRK10901 306 AQwwDGQP------FDRILLDAPCSATGvirrhpdikwlRRPE--------DIAALAALQSEILDALWPLLKPGGTLLYA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 372 TCTITLAENEEQVAWALTKFPCLQLQPQ-EPQIGGegmrgaglsceqlKQLqrfdpsavpLP-DTDMDslrearredmlr 449
Cdd:PRK10901 372 TCSILPEENEQQIKAFLARHPDAELLDTgTPQQPG-------------RQL---------LPgEEDGD------------ 417
|
250
....*....|....*.
gi 2462517651 450 lankdsiGFFIAKFVK 465
Cdd:PRK10901 418 -------GFFYALLIK 426
|
|
| yebU |
PRK11933 |
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed |
210-392 |
1.96e-30 |
|
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
Pssm-ID: 183387 [Multi-domain] Cd Length: 470 Bit Score: 123.09 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 210 SVLPrylflqnlPSALVSHvlNPQPgEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRA 289
Cdd:PRK11933 100 SMLP--------VAALFAD--DNAP-QRVLDMAAAPGSKTTQIAALMNNQGAIVANEYSASRVKVLHANISRCGVSNVAL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 290 FCFDGTkavkldmvedTEGEppFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEG 366
Cdd:PRK11933 169 THFDGR----------VFGA--ALPETFDAILLDAPCSGEGtvrKDPDALKNWSPESNLEIAATQRELIESAFHALKPGG 236
|
170 180
....*....|....*....|....*.
gi 2462517651 367 VLVYSTCTITLAENEEQVAWALTKFP 392
Cdd:PRK11933 237 TLVYSTCTLNREENQAVCLWLKETYP 262
|
|
| PRK14903 |
PRK14903 |
16S rRNA methyltransferase B; Provisional |
215-384 |
5.63e-28 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 184896 [Multi-domain] Cd Length: 431 Bit Score: 115.35 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 215 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 294
Cdd:PRK14903 218 LATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEKHAKRLKLSSIEIKIADA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 295 TKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 371
Cdd:PRK14903 298 ERLTE------------YVQDTFDRILVDAPCTSLGtarNHPEVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYS 365
|
170
....*....|...
gi 2462517651 372 TCTITLAENEEQV 384
Cdd:PRK14903 366 TCTVTKEENTEVV 378
|
|
| PUA |
cd07953 |
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ... |
112-201 |
1.08e-14 |
|
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, and a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was also found in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in regulating the expression of other genes. It has been shown that the PUA domain acts as an RNA binding domain in at least some of the proteins involved in RNA metabolism.
Pssm-ID: 409289 [Multi-domain] Cd Length: 73 Bit Score: 68.86 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 112 CEAIVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDiKGKckkgakefdgtkvFLGNGISELSRKEIfsgLPEL 191
Cdd:cd07953 1 PVVVVDKGAEKAVLNGADLMAPGVVSADGDFKRGDLVRIVSE-GGR-------------PLAIGVAEMSSDEM---KEEL 63
|
90
....*....|
gi 2462517651 192 KGMGIRMTEP 201
Cdd:cd07953 64 KGIAVRVLHF 73
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
237-371 |
1.99e-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: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 237 KILDLCAAPGGKTTHIAAlmHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPES 316
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462517651 317 FDRILLDAPCSgmgqrpnmactwsvkevaSYQPLQRKLFTAAVQLLKPEGVLVYS 371
Cdd:cd02440 67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
208-369 |
3.62e-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: 46.53 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 208 FDSVLPRYlflqNLPSALVSHvLNPQPGEKILDLCAAPGgktTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNsI 287
Cdd:COG2226 1 FDRVAARY----DGREALLAA-LGLRPGARVLDLGCGTG---RLALALAERGARVTGVDISPEMLELARERAAEAGLN-V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 288 RAFCFDGTkavkldmvedtegEPPFLPESFDRILldapcsgmgqrpnmaCTWSVKEVASyqplQRKLFTAAVQLLKPEGV 367
Cdd:COG2226 72 EFVVGDAE-------------DLPFPDGSFDLVI---------------SSFVLHHLPD----PERALAEIARVLKPGGR 119
|
..
gi 2462517651 368 LV 369
Cdd:COG2226 120 LV 121
|
|
| PUA |
smart00359 |
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
115-202 |
7.25e-06 |
|
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 43.78 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 115 IVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYsDIKGKckkgakefdgtkvFLGNGISELSRKEIFSglPELKGM 194
Cdd:smart00359 4 VVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIV-DEKGE-------------PLGIGLANMSSEEIAR--IKGKGL 67
|
....*...
gi 2462517651 195 GIRMTEPV 202
Cdd:smart00359 68 AVKVRRAV 75
|
|
| Tma20 |
COG2016 |
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ... |
122-184 |
1.60e-04 |
|
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441619 [Multi-domain] Cd Length: 154 Bit Score: 42.08 E-value: 1.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462517651 122 NAVLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKckkgakefdgtkvFLGNGISELSRKEI 184
Cdd:COG2016 84 KFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKHGK-------------PLAVGRALVDGEEM 133
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
234-373 |
1.01e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 39.71 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 234 PGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGlnsirafcFDGTKAVKLDMvedTEGEPPFL 313
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLG--------FDNVEFEQGDI---EELPELLE 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 314 PESFDRILLDapcsgmgqrpnmactwsvkEVASYQPLQRKLFTAAVQLLKPEGVLVYSTC 373
Cdd:pfam13847 72 DDKFDVVISN-------------------CVLNHIPDPDKVLQEILRVLKPGGRLIISDP 112
|
|
| FtsJ |
pfam01728 |
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
234-369 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 234 PGEKILDLCAAPGGKTThiAALMHDQGEVIALDKIFNKVEKIKQNAlllGLNSIRAfcfDGTKAVKLDMVEDTEGEPpfl 313
Cdd:pfam01728 21 PGKTVLDLGAAPGGWSQ--VALQRGAGKVVGVDLGPMQLWKPRNDP---GVTFIQG---DIRDPETLDLLEELLGRK--- 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462517651 314 pesFDRILLDApcsgmgqRPNMACTWSVKEVASYQpLQRKLFTAAVQLLKPEGVLV 369
Cdd:pfam01728 90 ---VDLVLSDG-------SPFISGNKVLDHLRSLD-LVKAALEVALELLRKGGNFV 134
|
|
| RlmE |
COG0293 |
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
234-266 |
2.71e-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: 2.71e-03
10 20 30
....*....|....*....|....*....|...
gi 2462517651 234 PGEKILDLCAAPGGKTTHIAALMHDQGEVIALD 266
Cdd:COG0293 50 PGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
209-450 |
3.19e-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: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 209 DSVLPRYLFLQNLPSALvshvlnpQPGEKILDLCAAPGGKTTHIAALMHDQgeVIALDkiFNK--VEKIKQNALLLGLNS 286
Cdd:COG0500 8 DELLPGLAALLALLERL-------PKGGRVLDLGCGTGRNLLALAARFGGR--VIGID--LSPeaIALARARAAKAGLGN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 287 IRafcFdgtkavkldMVEDTEGEPPFLPESFDRILLDApcsgmgqrpnmactwsvkeVASYQPLQR--KLFTAAVQLLKP 364
Cdd:COG0500 77 VE---F---------LVADLAELDPLPAESFDLVVAFG-------------------VLHHLPPEEreALLRELARALKP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 365 EGVLVYStctITLAENEEqvawaltkFPCLQLQPQEPQIGGEGMRGAGLSCEQLKQLQRFDpSAVPLPDTDMDSLREARR 444
Cdd:COG0500 126 GGVLLLS---ASDAAAAL--------SLARLLLLATASLLELLLLLRLLALELYLRALLAA-AATEDLRSDALLESANAL 193
|
....*.
gi 2462517651 445 EDMLRL 450
Cdd:COG0500 194 EYLLSK 199
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
208-320 |
4.00e-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: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 208 FDSVLPRYLFLQNLPSALVSHV--------LNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDkiFN----KV--E 273
Cdd:PRK00216 17 FDSIAPKYDLMNDLLSFGLHRVwrrktikwLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLD--FSegmlAVgrE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462517651 274 KIKQNALLLGLNSIRAfcfdgtKAVKLdmvedtegepPFLPESFDRI 320
Cdd:PRK00216 95 KLRDLGLSGNVEFVQG------DAEAL----------PFPDNSFDAV 125
|
|
| PUA |
pfam01472 |
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
115-184 |
4.15e-03 |
|
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes. It is predicted that the PUA domain is an RNA binding domain.
Pssm-ID: 426278 [Multi-domain] Cd Length: 74 Bit Score: 35.92 E-value: 4.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 115 IVGAQCGNAVLRGAHVYAPGIVSASQFMKAGDVISVYSDiKGKckkgakefdgtkvFLGNGISELSRKEI 184
Cdd:pfam01472 4 VVDDGAVKAILNGASLLAPGVVRVDGDFRKGDEVVVVTE-KGE-------------LVAVGLANYSSEEL 59
|
|
| PUA_MJ1432-like |
cd21154 |
PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA ... |
124-184 |
6.03e-03 |
|
PUA RNA-binding domain of MJ1432, TA1423, PH0734, 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 mostly archaeal family have not been characterized functionally; they may bind to RNA. This family includes Pyrococcus horikoshii PH0734 where the N-terminal domain may modulate the binding target of the C-terminal PUA domain using its characteristic electropositive surface.
Pssm-ID: 409296 [Multi-domain] Cd Length: 84 Bit Score: 35.94 E-value: 6.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462517651 124 VLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKckkgakefdgtkvFLGNGISELSRKEI 184
Cdd:cd21154 15 VANGADVMRPGIVEADEEIKKGDIVVVVDERHGK-------------PLAVGIALMSGEEM 62
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
235-390 |
6.35e-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: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 235 GEKILDLCAAPGGKTthIAALMHDQGEVIALDkIFNK-VEKIKQNALLLGLNS----IRAFCFDGTKAvkldmvEDTEGE 309
Cdd:COG1092 217 GKRVLNLFSYTGGFS--VHAAAGGAKSVTSVD-LSATaLEWAKENAALNGLDDrhefVQADAFDWLRE------LAREGE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517651 310 ppflpeSFDRILLDAPcsgmgqrpnmacTW--SVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCT--ITLAENEEQVA 385
Cdd:COG1092 288 ------RFDLIILDPP------------AFakSKKDLFDAQRDYKDLNRLALKLLAPGGILVTSSCSrhFSLDLFLEILA 349
|
....*
gi 2462517651 386 WALTK 390
Cdd:COG1092 350 RAARD 354
|
|
| PRK14560 |
PRK14560 |
putative RNA-binding protein; Provisional |
124-184 |
7.26e-03 |
|
putative RNA-binding protein; Provisional
Pssm-ID: 237757 [Multi-domain] Cd Length: 160 Bit Score: 37.14 E-value: 7.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462517651 124 VLRGAHVYAPGIVSASQFMKAGDVISVYSDIKGKckkgakefdgtkvFLGNGISELSRKEI 184
Cdd:PRK14560 89 VSNGADVMAPGIVEADEDIKEGDIVFVVEETHGK-------------PLAVGRALMDGDEM 136
|
|
|