|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
194-411 |
1.54e-68 |
|
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: 225.27 E-value: 1.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 194 GIRMTEPIYLS--PSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKV 271
Cdd:COG0144 211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 272 TKLKQNASLLGLHSIRAFCFDATKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQP 348
Cdd:COG0144 288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672082432 349 LQRKLLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMLGAG 411
Cdd:COG0144 356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
204-391 |
2.64e-62 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 209.26 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 204 SPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGL 283
Cdd:PRK14902 224 TDLFKD---GLITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 284 HSIRAFCFDATKalklevmdgvdgAPPFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRL 360
Cdd:PRK14902 301 TNIETKALDARK------------VHEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQY 368
|
170 180 190
....*....|....*....|....*....|.
gi 672082432 361 LKPGGVLVYSTCTVTLAENEEQVAWALRTFP 391
Cdd:PRK14902 369 LKKGGILVYSTCTIEKEENEEVIEAFLEEHP 399
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
226-463 |
1.29e-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: 176.08 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 226 AHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKalklevmdgv 305
Cdd:pfam01189 1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 306 dgaPPFLP--ESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENE 380
Cdd:pfam01189 71 ---PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 381 EQVAWALRTFPCLQLQPqepqIGGEGMLGAGLSLEQLKqlqRFDPcvvPLESMDtnslgdarredviwlankdciGFFIA 460
Cdd:pfam01189 148 AVIEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTL---RLLP---HTHNGD---------------------GFFIA 196
|
...
gi 672082432 461 KFL 463
Cdd:pfam01189 197 KLR 199
|
|
| PUA_NSun6-like |
cd21150 |
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ... |
112-201 |
1.52e-50 |
|
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: 166.85 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 112 EVIVGAQCGNAVLRGAHVYVPGVVSASKFMKAGDVVSVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKDIFNGLPDL 190
Cdd:cd21150 2 EVIVDRKCGEAVLRGAHVFAPGVLGAPPGLKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKP 81
|
90
....*....|.
gi 672082432 191 KGIGIRMTEPI 201
Cdd:cd21150 82 SGIAVEMTEPV 92
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
211-464 |
2.58e-47 |
|
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 188051 [Multi-domain] Cd Length: 264 Bit Score: 164.18 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 211 LSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFC 290
Cdd:TIGR00446 49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 291 FDATKalklevmdgvdgAPPFLPEsFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVL 367
Cdd:TIGR00446 129 ADGRK------------FGAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 368 VYSTCTVTLAENEEQVAWALRTFPCLQLqpqEPQIGGEgMLGAGLSLEQLKQLQRFDPcvvplesmdtnslgdarredvi 447
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDE-FFGINIGKGEVKGALRVFP---------------------- 249
|
250
....*....|....*..
gi 672082432 448 wlANKDCIGFFIAKFLK 464
Cdd:TIGR00446 250 --QNYDCEGFFVAKLRK 264
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
236-370 |
3.72e-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: 53.97 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 236 KILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgaPPFLPES 315
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 672082432 316 FDRILLDAPCSGLgqrpnmactwtlkevtsyQPLQRKLLNVAVRLLKPGGVLVYS 370
Cdd:cd02440 67 FDVIISDPPLHHL------------------VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| PUA |
smart00359 |
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
112-201 |
2.04e-07 |
|
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 48.41 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 112 EVIVGAQCGNAVLRGAHVYVPGVVSASKFMKAGDVVSVYsDIKGKckkgakefdgtkvFLGNGISELSRKDIFNglPDLK 191
Cdd:smart00359 2 KVVVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIV-DEKGE-------------PLGIGLANMSSEEIAR--IKGK 65
|
90
....*....|
gi 672082432 192 GIGIRMTEPI 201
Cdd:smart00359 66 GLAVKVRRAV 75
|
|
| Tma20 |
COG2016 |
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ... |
91-183 |
5.41e-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: 40.54 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 91 LPDVLLIPMTGPRKNIerqqceVIV--GAQcgNAVLRGAHVYVPGVVSASKFMKAGDVVSVYSDIKGKckkgakefdgtk 168
Cdd:COG2016 60 FPTLRGLLKYPPEKPV------VTVdmGAV--KFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKHGK------------ 119
|
90
....*....|....*
gi 672082432 169 vFLGNGISELSRKDI 183
Cdd:COG2016 120 -PLAVGRALVDGEEM 133
|
|
| PUA |
pfam01472 |
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
112-183 |
2.81e-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: 36.31 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672082432 112 EVIVGAQCGNAVLRGAHVYVPGVVSASKFMKAGDVVSVYSDiKGKckkgakefdgtkvFLGNGISELSRKDI 183
Cdd:pfam01472 2 RVVVDDGAVKAILNGASLLAPGVVRVDGDFRKGDEVVVVTE-KGE-------------LVAVGLANYSSEEL 59
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
194-411 |
1.54e-68 |
|
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: 225.27 E-value: 1.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 194 GIRMTEPIYLS--PSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKV 271
Cdd:COG0144 211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 272 TKLKQNASLLGLHSIRAFCFDATKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQP 348
Cdd:COG0144 288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672082432 349 LQRKLLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMLGAG 411
Cdd:COG0144 356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
204-391 |
2.64e-62 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 209.26 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 204 SPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGL 283
Cdd:PRK14902 224 TDLFKD---GLITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 284 HSIRAFCFDATKalklevmdgvdgAPPFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRL 360
Cdd:PRK14902 301 TNIETKALDARK------------VHEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQY 368
|
170 180 190
....*....|....*....|....*....|.
gi 672082432 361 LKPGGVLVYSTCTVTLAENEEQVAWALRTFP 391
Cdd:PRK14902 369 LKKGGILVYSTCTIEKEENEEVIEAFLEEHP 399
|
|
| PRK14901 |
PRK14901 |
16S rRNA methyltransferase B; Provisional |
225-413 |
6.39e-60 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237856 [Multi-domain] Cd Length: 434 Bit Score: 202.47 E-value: 6.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 225 VAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALklevmdg 304
Cdd:PRK14901 244 VAPLLDPQPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSASRLKKLQENAQRLGLKSIKILAADSRNLL------- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 305 vDGAPPFLpESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENEE 381
Cdd:PRK14901 317 -ELKPQWR-GYFDRILLDAPCSGLGtlhRHPDARWRQTPEKIQELAPLQAELLESLAPLLKPGGTLVYATCTLHPAENEA 394
|
170 180 190
....*....|....*....|....*....|....*..
gi 672082432 382 QVAWALRTFPCLQLQPQEPQI-----GGEGMLGAGLS 413
Cdd:PRK14901 395 QIEQFLARHPDWKLEPPKQKIwphrqDGDGFFMAVLR 431
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
226-463 |
1.29e-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: 176.08 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 226 AHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKalklevmdgv 305
Cdd:pfam01189 1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 306 dgaPPFLP--ESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTVTLAENE 380
Cdd:pfam01189 71 ---PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 381 EQVAWALRTFPCLQLQPqepqIGGEGMLGAGLSLEQLKqlqRFDPcvvPLESMDtnslgdarredviwlankdciGFFIA 460
Cdd:pfam01189 148 AVIEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTL---RLLP---HTHNGD---------------------GFFIA 196
|
...
gi 672082432 461 KFL 463
Cdd:pfam01189 197 KLR 199
|
|
| PUA_NSun6-like |
cd21150 |
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ... |
112-201 |
1.52e-50 |
|
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: 166.85 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 112 EVIVGAQCGNAVLRGAHVYVPGVVSASKFMKAGDVVSVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKDIFNGLPDL 190
Cdd:cd21150 2 EVIVDRKCGEAVLRGAHVFAPGVLGAPPGLKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKP 81
|
90
....*....|.
gi 672082432 191 KGIGIRMTEPI 201
Cdd:cd21150 82 SGIAVEMTEPV 92
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
211-464 |
2.58e-47 |
|
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 188051 [Multi-domain] Cd Length: 264 Bit Score: 164.18 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 211 LSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFC 290
Cdd:TIGR00446 49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 291 FDATKalklevmdgvdgAPPFLPEsFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPGGVL 367
Cdd:TIGR00446 129 ADGRK------------FGAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 368 VYSTCTVTLAENEEQVAWALRTFPCLQLqpqEPQIGGEgMLGAGLSLEQLKQLQRFDPcvvplesmdtnslgdarredvi 447
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDE-FFGINIGKGEVKGALRVFP---------------------- 249
|
250
....*....|....*..
gi 672082432 448 wlANKDCIGFFIAKFLK 464
Cdd:TIGR00446 250 --QNYDCEGFFVAKLRK 264
|
|
| PRK14904 |
PRK14904 |
16S rRNA methyltransferase B; Provisional |
201-397 |
3.43e-45 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237858 [Multi-domain] Cd Length: 445 Bit Score: 163.69 E-value: 3.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 201 IYLSPSFDN----VLSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQ 276
Cdd:PRK14904 214 FFLSKDFSLfepfLKLGLVSVQNPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYPQKLEKIRS 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 277 NASLLGLHSIRAFCFDATKalklevmdgvdgappFLPE-SFDRILLDAPCSG---LGQRPNMACTWTLKEVTSYQPLQRK 352
Cdd:PRK14904 294 HASALGITIIETIEGDARS---------------FSPEeQPDAILLDAPCTGtgvLGRRAELRWKLTPEKLAELVGLQAE 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 672082432 353 LLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQLQP 397
Cdd:PRK14904 359 LLDHAASLLKPGGVLVYATCSIEPEENELQIEAFLQRHPEFSAEP 403
|
|
| rsmB |
TIGR00563 |
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ... |
200-404 |
1.64e-42 |
|
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: 155.80 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 200 PIYLSPSFDNvlsGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRdQGEVIALDKILTKVTKLKQNAS 279
Cdd:TIGR00563 208 AVHALPGFEE---GWVTVQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELAP-QAQVVALDIHEHRLKRVYENLK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 280 LLGLhsirafcfdatkALKLEVMDGVDGAPPFLPES--FDRILLDAPCSGLG---QRPNMacTWTLKEVTSYQ--PLQRK 352
Cdd:TIGR00563 284 RLGL------------TIKAETKDGDGRGPSQWAENeqFDRILLDAPCSATGvirRHPDI--KWLRKPRDIAElaELQSE 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 672082432 353 LLNVAVRLLKPGGVLVYSTCTVTLAENEEQVAWALRTFPCLQL----QPQEPQIGG 404
Cdd:TIGR00563 350 ILDAIWPLLKTGGTLVYATCSVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
|
|
| PRK10901 |
PRK10901 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
226-398 |
1.08e-39 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 236790 [Multi-domain] Cd Length: 427 Bit Score: 148.03 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 226 AHVLDPQPGEKILDLCAAPGGKTTHIAALmRDQGEVIALDKILTKVTKLKQNASLLGLHSiRAFCFDATKALKLevmdgV 305
Cdd:PRK10901 237 ATLLAPQNGERVLDACAAPGGKTAHILEL-APQAQVVALDIDAQRLERVRENLQRLGLKA-TVIVGDARDPAQW-----W 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 306 DGAPpflpesFDRILLDAPCSGLG-----------QRPNmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCTV 374
Cdd:PRK10901 310 DGQP------FDRILLDAPCSATGvirrhpdikwlRRPE--------DIAALAALQSEILDALWPLLKPGGTLLYATCSI 375
|
170 180
....*....|....*....|....
gi 672082432 375 TLAENEEQVAWALRTFPCLQLQPQ 398
Cdd:PRK10901 376 LPEENEQQIKAFLARHPDAELLDT 399
|
|
| yebU |
PRK11933 |
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed |
211-391 |
4.93e-32 |
|
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
Pssm-ID: 183387 [Multi-domain] Cd Length: 470 Bit Score: 127.72 E-value: 4.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 211 LSGYIFLQN----LPstVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSI 286
Cdd:PRK11933 89 LSGLFYIQEassmLP--VAALFADDNAPQRVLDMAAAPGSKTTQIAALMNNQGAIVANEYSASRVKVLHANISRCGVSNV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 287 RAFCFDATkalklevmdgVDGAppFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKP 363
Cdd:PRK11933 167 ALTHFDGR----------VFGA--ALPETFDAILLDAPCSGEGtvrKDPDALKNWSPESNLEIAATQRELIESAFHALKP 234
|
170 180
....*....|....*....|....*...
gi 672082432 364 GGVLVYSTCTVTLAENEEQVAWALRTFP 391
Cdd:PRK11933 235 GGTLVYSTCTLNREENQAVCLWLKETYP 262
|
|
| PRK14903 |
PRK14903 |
16S rRNA methyltransferase B; Provisional |
208-389 |
5.93e-32 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 184896 [Multi-domain] Cd Length: 431 Bit Score: 126.91 E-value: 5.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 208 DNVLSGYIFLQNLPSTVVAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIR 287
Cdd:PRK14903 212 RVIKDGLATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEKHAKRLKLSSIE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 288 AFCFDATKALKlevmdgvdgappFLPESFDRILLDAPCSGLG---QRPNMACTWTLKEVTSYQPLQRKLLNVAVRLLKPG 364
Cdd:PRK14903 292 IKIADAERLTE------------YVQDTFDRILVDAPCTSLGtarNHPEVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKG 359
|
170 180
....*....|....*....|....*.
gi 672082432 365 GVLVYSTCTVTLAENEEQV-AWALRT 389
Cdd:PRK14903 360 GILLYSTCTVTKEENTEVVkRFVYEQ 385
|
|
| PUA |
cd07953 |
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ... |
111-200 |
1.22e-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: 68.48 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 111 CEVIVGAQCGNAVLRGAHVYVPGVVSASKFMKAGDVVSVYSDiKGKckkgakefdgtkvFLGNGISELSRKDIfngLPDL 190
Cdd:cd07953 1 PVVVVDKGAEKAVLNGADLMAPGVVSADGDFKRGDLVRIVSE-GGR-------------PLAIGVAEMSSDEM---KEEL 63
|
90
....*....|
gi 672082432 191 KGIGIRMTEP 200
Cdd:cd07953 64 KGIAVRVLHF 73
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
236-370 |
3.72e-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: 53.97 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 236 KILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgaPPFLPES 315
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 672082432 316 FDRILLDAPCSGLgqrpnmactwtlkevtsyQPLQRKLLNVAVRLLKPGGVLVYS 370
Cdd:cd02440 67 FDVIISDPPLHHL------------------VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
207-368 |
4.22e-09 |
|
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: 55.00 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 207 FDNVLSGYIFLQNLpstvvAHVLDPQPGEKILDLCAAPGgktTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHsI 286
Cdd:COG2226 1 FDRVAARYDGREAL-----LAALGLRPGARVLDLGCGTG---RLALALAERGARVTGVDISPEMLELARERAAEAGLN-V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 287 RAFCFDATkalklevmdgvdgAPPFLPESFDRILldapcsglgqrpnmaCTWTLKEVTSyqplQRKLLNVAVRLLKPGGV 366
Cdd:COG2226 72 EFVVGDAE-------------DLPFPDGSFDLVI---------------SSFVLHHLPD----PERALAEIARVLKPGGR 119
|
..
gi 672082432 367 LV 368
Cdd:COG2226 120 LV 121
|
|
| PUA |
smart00359 |
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
112-201 |
2.04e-07 |
|
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 48.41 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 112 EVIVGAQCGNAVLRGAHVYVPGVVSASKFMKAGDVVSVYsDIKGKckkgakefdgtkvFLGNGISELSRKDIFNglPDLK 191
Cdd:smart00359 2 KVVVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIV-DEKGE-------------PLGIGLANMSSEEIAR--IKGK 65
|
90
....*....|
gi 672082432 192 GIGIRMTEPI 201
Cdd:smart00359 66 GLAVKVRRAV 75
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
233-383 |
4.83e-06 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 46.26 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 233 PGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALKLevmdgvdgappFL 312
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPEL-----------LE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672082432 313 PESFDRILLDapcsglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLVYSTCtVTLAENEEQV 383
Cdd:pfam13847 72 DDKFDVVISN-------------------CVLNHIPDPDKVLQEILRVLKPGGRLIISDP-DSLAELPAHV 122
|
|
| Trm5 |
COG2520 |
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
233-369 |
2.26e-05 |
|
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442010 [Multi-domain] Cd Length: 333 Bit Score: 46.39 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 233 PGEKILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGL-HSIRAFCFDATKalklevmdgvdgAPPF 311
Cdd:COG2520 180 PGERVLDMFAGVGPFSIPIAK--RSGAKVVAIDINPDAVEYLKENIRLNKVeDRVTPILGDARE------------VAPE 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 672082432 312 LPESFDRILLDAPCSGLgqrpnmactwtlkevtsyqplqrKLLNVAVRLLKPGGVLVY 369
Cdd:COG2520 246 LEGKADRIIMNLPHSAD-----------------------EFLDAALRALKPGGVIHY 280
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
232-371 |
8.75e-05 |
|
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: 43.01 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 232 QPGEKILDLCAapGGKTTHIAALMRDqGEVIALDkILTK-VTKLKQNASLLGLHSIRAFCFDATKalklevmdgvdgaPP 310
Cdd:COG1041 25 KEGDTVLDPFC--GTGTILIEAGLLG-RRVIGSD-IDPKmVEGARENLEHYGYEDADVIRGDARD-------------LP 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672082432 311 FLPESFDRILLDAPcsgLGQRPnmacTWTLKEVTSyqpLQRKLLNVAVRLLKPGGVLVYST 371
Cdd:COG1041 88 LADESVDAIVTDPP---YGRSS----KISGEELLE---LYEKALEEAARVLKPGGRVVIVT 138
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
234-388 |
1.08e-04 |
|
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: 44.40 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 234 GEKILDLCAAPGGKTthIAALMRDQGEVIALDKILTKVTKLKQNASLLGL----HSIRAFCFDATKALKLEvmdgvdgap 309
Cdd:COG1092 217 GKRVLNLFSYTGGFS--VHAAAGGAKSVTSVDLSATALEWAKENAALNGLddrhEFVQADAFDWLRELARE--------- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 310 pflPESFDRILLDAPC-----SGL--GQRpnmactwtlkevtSYqplqRKLLNVAVRLLKPGGVLVYSTCT--VTLAENE 380
Cdd:COG1092 286 ---GERFDLIILDPPAfakskKDLfdAQR-------------DY----KDLNRLALKLLAPGGILVTSSCSrhFSLDLFL 345
|
....*...
gi 672082432 381 EQVAWALR 388
Cdd:COG1092 346 EILARAAR 353
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
237-365 |
1.14e-04 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 41.01 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 237 ILDLCAAPGGKTTHIAAlmRDQGEVIALDKILTKVTKLKQNASLLGLHsIRAFCFDATkalklevmdgvdgAPPFLPESF 316
Cdd:pfam13649 1 VLDLGCGTGRLTLALAR--RGGARVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAE-------------DLPFPDGSF 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 672082432 317 DRILldapcsglgqrpnmaCTWTLKEVTsyQPLQRKLLNVAVRLLKPGG 365
Cdd:pfam13649 65 DLVV---------------SSGVLHHLP--DPDLEAALREIARVLKPGG 96
|
|
| PRK14967 |
PRK14967 |
putative methyltransferase; Provisional |
233-417 |
1.18e-04 |
|
putative methyltransferase; Provisional
Pssm-ID: 184931 [Multi-domain] Cd Length: 223 Bit Score: 43.50 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 233 PGEKILDLCAAPGGKTTHIAALmrDQGEVIALDKILTKVTKLKQNASLLGLHsIRAFCFDATKALKLEVMDGVDGAPPFL 312
Cdd:PRK14967 36 PGRRVLDLCTGSGALAVAAAAA--GAGSVTAVDISRRAVRSARLNALLAGVD-VDVRRGDWARAVEFRPFDVVVSNPPYV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 313 PESFDRilldAPCSGLGQrpnmacTWtlkevtSYQPLQRKLLN----VAVRLLKPGGVL--VYSTC---TVTLAENEEQ- 382
Cdd:PRK14967 113 PAPPDA----PPSRGPAR------AW------DAGPDGRAVLDrlcdAAPALLAPGGSLllVQSELsgvERTLTRLSEAg 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 672082432 383 -----VAWALRTF-PClqLQPQEPQIGGEGMLGAGLSLEQL 417
Cdd:PRK14967 177 ldaevVASQWIPFgPV--LRARAAWLERRGLLPPGQREEEL 215
|
|
| FtsJ |
pfam01728 |
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
233-368 |
1.30e-04 |
|
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: 42.58 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 233 PGEKILDLCAAPGGKTThiAALMRDQGEVIALDKILTKVTKLKQNAsllGLHSIRAFCFDATKALKLEvmdgvdgapPFL 312
Cdd:pfam01728 21 PGKTVLDLGAAPGGWSQ--VALQRGAGKVVGVDLGPMQLWKPRNDP---GVTFIQGDIRDPETLDLLE---------ELL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 672082432 313 PESFDRILLDApcsglgqRPNMACTWTLKEVTSYQpLQRKLLNVAVRLLKPGGVLV 368
Cdd:pfam01728 87 GRKVDLVLSDG-------SPFISGNKVLDHLRSLD-LVKAALEVALELLRKGGNFV 134
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
233-371 |
2.12e-04 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 41.16 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 233 PGEKILDLCAAPGgkttHIAALMRDQG-EVIALDKILTKVTKLKQNASLLGlhsIRAFCFDATKAlklevmdgvdgapPF 311
Cdd:COG2227 24 AGGRVLDVGCGTG----RLALALARRGaDVTGVDISPEALEIARERAAELN---VDFVQGDLEDL-------------PL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 312 LPESFDRILldapCSglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLVYST 371
Cdd:COG2227 84 EDGSFDLVI----CS---------------EVLEHLPDPAALLRELARLLKPGGLLLLST 124
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
229-368 |
2.60e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 42.62 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 229 LDPQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKiltkvtklkqNASLLGLHSIRAfcfdATKALKLEVMDGVDGA 308
Cdd:PRK08317 15 LAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDR----------SEAMLALAKERA----AGLGPNVEFVRGDADG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 309 PPFLPESFDRILLDapcsglgqrpnmactwtlkEVTSYQPLQRKLLNVAVRLLKPGGVLV 368
Cdd:PRK08317 81 LPFPDGSFDAVRSD-------------------RVLQHLEDPARALAEIARVLRPGGRVV 121
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
225-370 |
2.61e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 42.21 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 225 VAHVLDPQPGEKILDLCAAPGGKTTHIAALMRDQgeVIALDKILTKVTKLKQNASLLGLHSIRafcfdatkalkLEVMDg 304
Cdd:COG0500 18 LALLERLPKGGRVLDLGCGTGRNLLALAARFGGR--VIGIDLSPEAIALARARAAKAGLGNVE-----------FLVAD- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672082432 305 VDGAPPFLPESFDRILLdapcsglgqrpNMACTWTLKEVtsyqplQRKLLNVAVRLLKPGGVLVYS 370
Cdd:COG0500 84 LAELDPLPAESFDLVVA-----------FGVLHHLPPEE------REALLRELARALKPGGVLLLS 132
|
|
| Tma20 |
COG2016 |
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ... |
91-183 |
5.41e-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: 40.54 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 91 LPDVLLIPMTGPRKNIerqqceVIV--GAQcgNAVLRGAHVYVPGVVSASKFMKAGDVVSVYSDIKGKckkgakefdgtk 168
Cdd:COG2016 60 FPTLRGLLKYPPEKPV------VTVdmGAV--KFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKHGK------------ 119
|
90
....*....|....*
gi 672082432 169 vFLGNGISELSRKDI 183
Cdd:COG2016 120 -PLAVGRALVDGEEM 133
|
|
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
229-327 |
7.01e-04 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 42.07 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 229 LDPQPGEKILDLCAAPGGKTTHIAalmRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKALKLEvmdgvdga 308
Cdd:PRK13168 293 LDPQPGDRVLDLFCGLGNFTLPLA---RQAAEVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQ-------- 361
|
90
....*....|....*....
gi 672082432 309 pPFLPESFDRILLDAPCSG 327
Cdd:PRK13168 362 -PWALGGFDKVLLDPPRAG 379
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
231-368 |
1.82e-03 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 39.73 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672082432 231 PQPGEKILDLCAAPGGKTTHIAALMRDQGEVIALDKILTKVTKLKQNASLLGLHSIRAFCFDATKAlklevmdgvdgapP 310
Cdd:pfam01209 40 VKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEEL-------------P 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 672082432 311 FLPESFDRILLdapcsGLGqrpnmactwtLKEVTSYQplqrKLLNVAVRLLKPGGVLV 368
Cdd:pfam01209 107 FEDDSFDIVTI-----SFG----------LRNFPDYL----KVLKEAFRVLKPGGRVV 145
|
|
| RlmE |
COG0293 |
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
233-265 |
2.47e-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: 39.28 E-value: 2.47e-03
10 20 30
....*....|....*....|....*....|...
gi 672082432 233 PGEKILDLCAAPGGKTTHIAALMRDQGEVIALD 265
Cdd:COG0293 50 PGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82
|
|
| PUA |
pfam01472 |
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
112-183 |
2.81e-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: 36.31 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672082432 112 EVIVGAQCGNAVLRGAHVYVPGVVSASKFMKAGDVVSVYSDiKGKckkgakefdgtkvFLGNGISELSRKDI 183
Cdd:pfam01472 2 RVVVDDGAVKAILNGASLLAPGVVRVDGDFRKGDEVVVVTE-KGE-------------LVAVGLANYSSEEL 59
|
|
|