|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
144-414 |
3.19e-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: 217.95 E-value: 3.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 144 GIRMTEPIYLS--PSFDNvlpSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKV 221
Cdd:COG0144 211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 222 NKLKQNASLLGLHSIRAFCFDATKALKldttdgieggppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQP 298
Cdd:COG0144 288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 299 LQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMVGAGltleqlkqLQRFDPSVv 378
Cdd:COG0144 356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG--------YLRLLPHR- 426
|
250 260 270
....*....|....*....|....*....|....*.
gi 260099664 379 plQNMDtdslgearredmiwlankdciGFFIAKFLK 414
Cdd:COG0144 427 --HGTD---------------------GFFIARLRK 439
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
164-414 |
6.06e-62 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 206.57 E-value: 6.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 164 YIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDA 243
Cdd:PRK14902 231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 244 TKAlkldttdgieggPPFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYS 320
Cdd:PRK14902 311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 321 TCTITLAENEEQVAWALRTFPCLQLQPQEPqiggegmvgaGLTLEQLKQLQRFDPSVVPLQNmDTDslgearredmiwla 400
Cdd:PRK14902 379 TCTIEKEENEEVIEAFLEEHPEFELVPLQH----------EKPDELVYEVKDGYLQILPNDY-GTD-------------- 433
|
250
....*....|....
gi 260099664 401 nkdciGFFIAKFLK 414
Cdd:PRK14902 434 -----GFFIAKLRK 442
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
176-413 |
3.06e-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: 173.76 E-value: 3.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 176 AHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKalkldtTDGI 255
Cdd:pfam01189 1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------PDQW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 256 EGGppflpESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQ 332
Cdd:pfam01189 75 LGG-----VLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 333 VAWALRTFPCLQLQPqepqIGGEGMVGAGLTLEQLKQlqrfdpsVVPLQNmdtdslgearredmiwlaNKDciGFFIAKF 412
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLR-------LLPHTH------------------NGD--GFFIAKL 198
|
.
gi 260099664 413 L 413
Cdd:pfam01189 199 R 199
|
|
| PUA_NSun6-like |
cd21150 |
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ... |
62-151 |
3.03e-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: 164.54 E-value: 3.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 62 EVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDINGKCKKGA-KEFDGTKVFLGNGISELSRKDIFNGLPDL 140
Cdd:cd21150 2 EVIVDRKCGEAVLRGAHVFAPGVLGAPPGLKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKP 81
|
90
....*....|.
gi 260099664 141 KGIGIRMTEPI 151
Cdd:cd21150 82 SGIAVEMTEPV 92
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
161-414 |
3.97e-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: 162.64 E-value: 3.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 161 LPSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFC 240
Cdd:TIGR00446 49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 241 FDATKAlkldttdgieggPPFLPEsFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVL 317
Cdd:TIGR00446 129 ADGRKF------------GAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 318 VYSTCTITLAENEEQVAWALRTFPCLQLqpqEPQIGGEGMvGAGLTLEQLKQLQRFDPSvvplqnmdtdslgearredmi 397
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDEFF-GINIGKGEVKGALRVFPQ--------------------- 250
|
250
....*....|....*..
gi 260099664 398 wlaNKDCIGFFIAKFLK 414
Cdd:TIGR00446 251 ---NYDCEGFFVAKLRK 264
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
186-320 |
2.41e-07 |
|
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: 48.97 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 186 KILDMCAAPGGKTTHTAAlmQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKAlkldttdgieggPPFLPES 265
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 260099664 266 FDRIILDAPCSgmgqrpnmactwtlkevtSYQPLQRKLLHVAVQLLKPGGVLVYS 320
Cdd:cd02440 67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
| PUA |
smart00359 |
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
61-151 |
2.79e-07 |
|
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 47.64 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 61 GEVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYsDINGKckkgakefdgtkvFLGNGISELSRKDIFNglPDL 140
Cdd:smart00359 1 GKVVVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIV-DEKGE-------------PLGIGLANMSSEEIAR--IKG 64
|
90
....*....|.
gi 260099664 141 KGIGIRMTEPI 151
Cdd:smart00359 65 KGLAVKVRRAV 75
|
|
| Tma20 |
COG2016 |
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ... |
41-133 |
4.86e-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: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 41 LPDVLLIPMTGPRKNIerqqgeVIV--GAQcgNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDINGKckkgakefdgtk 118
Cdd:COG2016 60 FPTLRGLLKYPPEKPV------VTVdmGAV--KFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKHGK------------ 119
|
90
....*....|....*
gi 260099664 119 vFLGNGISELSRKDI 133
Cdd:COG2016 120 -PLAVGRALVDGEEM 133
|
|
| PUA |
pfam01472 |
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
61-133 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260099664 61 GEVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDiNGKckkgakefdgtkvFLGNGISELSRKDI 133
Cdd:pfam01472 1 GRVVVDDGAVKAILNGASLLAPGVVRVDGDFRKGDEVVVVTE-KGE-------------LVAVGLANYSSEEL 59
|
|
| PRK14560 |
PRK14560 |
putative RNA-binding protein; Provisional |
55-136 |
7.48e-03 |
|
putative RNA-binding protein; Provisional
Pssm-ID: 237757 [Multi-domain] Cd Length: 160 Bit Score: 37.14 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 55 NIERQQGEVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDINGKckkgakefdgtkvFLGNGISELSRKDIF 134
Cdd:PRK14560 71 KLKPEKRRVVVDAGAVKFVSNGADVMAPGIVEADEDIKEGDIVFVVEETHGK-------------PLAVGRALMDGDEMV 137
|
..
gi 260099664 135 NG 136
Cdd:PRK14560 138 EE 139
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| RsmB |
COG0144 |
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ... |
144-414 |
3.19e-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: 217.95 E-value: 3.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 144 GIRMTEPIYLS--PSFDNvlpSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKV 221
Cdd:COG0144 211 GLRLEGPGPVTalPGFRE---GLFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 222 NKLKQNASLLGLHSIRAFCFDATKALKldttdgieggppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQP 298
Cdd:COG0144 288 KRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRHPDIKWRRTPEDIAELAA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 299 LQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQVAWALRTFPCLQLQPQEPQIGGEGMVGAGltleqlkqLQRFDPSVv 378
Cdd:COG0144 356 LQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG--------YLRLLPHR- 426
|
250 260 270
....*....|....*....|....*....|....*.
gi 260099664 379 plQNMDtdslgearredmiwlankdciGFFIAKFLK 414
Cdd:COG0144 427 --HGTD---------------------GFFIARLRK 439
|
|
| PRK14902 |
PRK14902 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
164-414 |
6.06e-62 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 237857 [Multi-domain] Cd Length: 444 Bit Score: 206.57 E-value: 6.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 164 YIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDA 243
Cdd:PRK14902 231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 244 TKAlkldttdgieggPPFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYS 320
Cdd:PRK14902 311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 321 TCTITLAENEEQVAWALRTFPCLQLQPQEPqiggegmvgaGLTLEQLKQLQRFDPSVVPLQNmDTDslgearredmiwla 400
Cdd:PRK14902 379 TCTIEKEENEEVIEAFLEEHPEFELVPLQH----------EKPDELVYEVKDGYLQILPNDY-GTD-------------- 433
|
250
....*....|....
gi 260099664 401 nkdciGFFIAKFLK 414
Cdd:PRK14902 434 -----GFFIAKLRK 442
|
|
| PRK14901 |
PRK14901 |
16S rRNA methyltransferase B; Provisional |
175-352 |
1.24e-58 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237856 [Multi-domain] Cd Length: 434 Bit Score: 197.84 E-value: 1.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 175 VAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIrafcfdatKALKLDTTDG 254
Cdd:PRK14901 244 VAPLLDPQPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSASRLKKLQENAQRLGLKSI--------KILAADSRNL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 255 IEGGPPFLpESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITLAENEE 331
Cdd:PRK14901 316 LELKPQWR-GYFDRILLDAPCSGLGtlhRHPDARWRQTPEKIQELAPLQAELLESLAPLLKPGGTLVYATCTLHPAENEA 394
|
170 180
....*....|....*....|.
gi 260099664 332 QVAWALRTFPCLQLQPQEPQI 352
Cdd:PRK14901 395 QIEQFLARHPDWKLEPPKQKI 415
|
|
| Methyltr_RsmB-F |
pfam01189 |
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ... |
176-413 |
3.06e-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: 173.76 E-value: 3.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 176 AHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKalkldtTDGI 255
Cdd:pfam01189 1 AILLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------PDQW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 256 EGGppflpESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQ 332
Cdd:pfam01189 75 LGG-----VLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 333 VAWALRTFPCLQLQPqepqIGGEGMVGAGLTLEQLKQlqrfdpsVVPLQNmdtdslgearredmiwlaNKDciGFFIAKF 412
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLR-------LLPHTH------------------NGD--GFFIAKL 198
|
.
gi 260099664 413 L 413
Cdd:pfam01189 199 R 199
|
|
| PUA_NSun6-like |
cd21150 |
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ... |
62-151 |
3.03e-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: 164.54 E-value: 3.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 62 EVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDINGKCKKGA-KEFDGTKVFLGNGISELSRKDIFNGLPDL 140
Cdd:cd21150 2 EVIVDRKCGEAVLRGAHVFAPGVLGAPPGLKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKP 81
|
90
....*....|.
gi 260099664 141 KGIGIRMTEPI 151
Cdd:cd21150 82 SGIAVEMTEPV 92
|
|
| nop2p |
TIGR00446 |
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ... |
161-414 |
3.97e-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: 162.64 E-value: 3.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 161 LPSYIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFC 240
Cdd:TIGR00446 49 LFGYYYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALISNINRMGVLNTIVIN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 241 FDATKAlkldttdgieggPPFLPEsFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVL 317
Cdd:TIGR00446 129 ADGRKF------------GAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKELIDAAIDALKPGGVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 318 VYSTCTITLAENEEQVAWALRTFPCLQLqpqEPQIGGEGMvGAGLTLEQLKQLQRFDPSvvplqnmdtdslgearredmi 397
Cdd:TIGR00446 196 VYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDEFF-GINIGKGEVKGALRVFPQ--------------------- 250
|
250
....*....|....*..
gi 260099664 398 wlaNKDCIGFFIAKFLK 414
Cdd:TIGR00446 251 ---NYDCEGFFVAKLRK 264
|
|
| PRK14904 |
PRK14904 |
16S rRNA methyltransferase B; Provisional |
179-364 |
2.30e-45 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 237858 [Multi-domain] Cd Length: 445 Bit Score: 162.92 E-value: 2.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 179 LDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKalkldttdgiegg 258
Cdd:PRK14904 246 LNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYPQKLEKIRSHASALGITIIETIEGDARS------------- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 259 ppFLPE-SFDRIILDAPCSG---MGQRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITLAENEEQVA 334
Cdd:PRK14904 313 --FSPEeQPDAILLDAPCTGtgvLGRRAELRWKLTPEKLAELVGLQAELLDHAASLLKPGGVLVYATCSIEPEENELQIE 390
|
170 180 190
....*....|....*....|....*....|....*
gi 260099664 335 WALRTFPCLQLQPQ-----EPQIGGEGMVGAGLTL 364
Cdd:PRK14904 391 AFLQRHPEFSAEPSpgslpEPFHEVAHPKGAILTL 425
|
|
| rsmB |
TIGR00563 |
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ... |
167-354 |
5.51e-39 |
|
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: 145.01 E-value: 5.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 167 LQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQdKGEVIALDKILTKVNKLKQNASLLGLhsirafcfdatkA 246
Cdd:TIGR00563 222 VQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELAP-QAQVVALDIHEHRLKRVYENLKRLGL------------T 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 247 LKLDTTDGIEGGPPFLPES--FDRIILDAPCSGMG---QRPNMacTWTLKEVTSYQ--PLQRKLLHVAVQLLKPGGVLVY 319
Cdd:TIGR00563 289 IKAETKDGDGRGPSQWAENeqFDRILLDAPCSATGvirRHPDI--KWLRKPRDIAElaELQSEILDAIWPLLKTGGTLVY 366
|
170 180 190
....*....|....*....|....*....|....*....
gi 260099664 320 STCTITLAENEEQVAWALRTFPCLQL----QPQEPQIGG 354
Cdd:TIGR00563 367 ATCSVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
|
|
| PRK10901 |
PRK10901 |
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB; |
176-348 |
1.67e-36 |
|
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
Pssm-ID: 236790 [Multi-domain] Cd Length: 427 Bit Score: 138.40 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 176 AHVLDPQPGEKILDMCAAPGGKTTHTAALmQDKGEVIALDKILTKVNKLKQNASLLGLHSiRAFCFDATkalklDTTDGI 255
Cdd:PRK10901 237 ATLLAPQNGERVLDACAAPGGKTAHILEL-APQAQVVALDIDAQRLERVRENLQRLGLKA-TVIVGDAR-----DPAQWW 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 256 EGGPpflpesFDRIILDAPCSGMG-----------QRPNmactwtlkEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTI 324
Cdd:PRK10901 310 DGQP------FDRILLDAPCSATGvirrhpdikwlRRPE--------DIAALAALQSEILDALWPLLKPGGTLLYATCSI 375
|
170 180
....*....|....*....|....
gi 260099664 325 TLAENEEQVAWALRTFPCLQLQPQ 348
Cdd:PRK10901 376 LPEENEQQIKAFLARHPDAELLDT 399
|
|
| yebU |
PRK11933 |
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed |
170-341 |
3.72e-30 |
|
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
Pssm-ID: 183387 [Multi-domain] Cd Length: 470 Bit Score: 121.55 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 170 LPstVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATkalkl 249
Cdd:PRK11933 102 LP--VAALFADDNAPQRVLDMAAAPGSKTTQIAALMNNQGAIVANEYSASRVKVLHANISRCGVSNVALTHFDGR----- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 250 dttdgIEGGppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTCTITL 326
Cdd:PRK11933 175 -----VFGA--ALPETFDAILLDAPCSGEGtvrKDPDALKNWSPESNLEIAATQRELIESAFHALKPGGTLVYSTCTLNR 247
|
170
....*....|....*
gi 260099664 327 AENEEQVAWALRTFP 341
Cdd:PRK11933 248 EENQAVCLWLKETYP 262
|
|
| PRK14903 |
PRK14903 |
16S rRNA methyltransferase B; Provisional |
164-339 |
3.76e-30 |
|
16S rRNA methyltransferase B; Provisional
Pssm-ID: 184896 [Multi-domain] Cd Length: 431 Bit Score: 120.75 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 164 YIFLQNLPSTVVAHVLDPQPGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDA 243
Cdd:PRK14903 218 LATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEKHAKRLKLSSIEIKIADA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 244 TKALKldttdgieggppFLPESFDRIILDAPCSGMG---QRPNMACTWTLKEVTSYQPLQRKLLHVAVQLLKPGGVLVYS 320
Cdd:PRK14903 298 ERLTE------------YVQDTFDRILVDAPCTSLGtarNHPEVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYS 365
|
170 180
....*....|....*....|
gi 260099664 321 TCTITLAENEEQV-AWALRT 339
Cdd:PRK14903 366 TCTVTKEENTEVVkRFVYEQ 385
|
|
| PUA |
cd07953 |
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ... |
61-150 |
6.40e-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: 66.55 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 61 GEVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDiNGKckkgakefdgtkvFLGNGISELSRKDIfngLPDL 140
Cdd:cd07953 1 PVVVVDKGAEKAVLNGADLMAPGVVSADGDFKRGDLVRIVSE-GGR-------------PLAIGVAEMSSDEM---KEEL 63
|
90
....*....|
gi 260099664 141 KGIGIRMTEP 150
Cdd:cd07953 64 KGIAVRVLHF 73
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
157-318 |
2.31e-07 |
|
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: 49.99 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 157 FDNVLPSYIFLQNLpstvvAHVLDPQPGEKILDMCAAPGgktTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHsI 236
Cdd:COG2226 1 FDRVAARYDGREAL-----LAALGLRPGARVLDLGCGTG---RLALALAERGARVTGVDISPEMLELARERAAEAGLN-V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 237 RAFCFDATKalkldttdgieggPPFLPESFDRIIldapcsgmgqrpnmaCTWTLKEVTSyqplQRKLLHVAVQLLKPGGV 316
Cdd:COG2226 72 EFVVGDAED-------------LPFPDGSFDLVI---------------SSFVLHHLPD----PERALAEIARVLKPGGR 119
|
..
gi 260099664 317 LV 318
Cdd:COG2226 120 LV 121
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
186-320 |
2.41e-07 |
|
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: 48.97 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 186 KILDMCAAPGGKTTHTAAlmQDKGEVIALDKILTKVNKLKQNASLLGLHSIRAFCFDATKAlkldttdgieggPPFLPES 265
Cdd:cd02440 1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 260099664 266 FDRIILDAPCSgmgqrpnmactwtlkevtSYQPLQRKLLHVAVQLLKPGGVLVYS 320
Cdd:cd02440 67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
| PUA |
smart00359 |
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
61-151 |
2.79e-07 |
|
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 47.64 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 61 GEVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYsDINGKckkgakefdgtkvFLGNGISELSRKDIFNglPDL 140
Cdd:smart00359 1 GKVVVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIV-DEKGE-------------PLGIGLANMSSEEIAR--IKG 64
|
90
....*....|.
gi 260099664 141 KGIGIRMTEPI 151
Cdd:smart00359 65 KGLAVKVRRAV 75
|
|
| Trm5 |
COG2520 |
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
183-319 |
4.23e-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: 45.24 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 183 PGEKILDMCAAPGGKTTHTAALmqDKGEVIALDKILTKVNKLKQNASLLGL-HSIRAFCFDATKAlkldttdgieggPPF 261
Cdd:COG2520 180 PGERVLDMFAGVGPFSIPIAKR--SGAKVVAIDINPDAVEYLKENIRLNKVeDRVTPILGDAREV------------APE 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 260099664 262 LPESFDRIILDAPCSGmgqrpnmactwtlkevtsyqplqRKLLHVAVQLLKPGGVLVY 319
Cdd:COG2520 246 LEGKADRIIMNLPHSA-----------------------DEFLDAALRALKPGGVIHY 280
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
182-321 |
1.56e-04 |
|
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: 42.24 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 182 QPGEKILD-MCaapGGKTT-HTAALMqdKGEVIALDkILTK-VNKLKQNASLLGLHSIRAFCFDATKalkldttdgiegg 258
Cdd:COG1041 25 KEGDTVLDpFC---GTGTIlIEAGLL--GRRVIGSD-IDPKmVEGARENLEHYGYEDADVIRGDARD------------- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260099664 259 PPFLPESFDRIILDAPcsgMGQRPnmacTWTLKEVTSyqpLQRKLLHVAVQLLKPGGVLVYST 321
Cdd:COG1041 86 LPLADESVDAIVTDPP---YGRSS----KISGEELLE---LYEKALEEAARVLKPGGRVVIVT 138
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
225-338 |
2.56e-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: 42.86 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 225 KQNASLLGL----HSIRAFCFDATKALKLDttdgieggppflPESFDRIILDAPcsgmgqrpnmacTWT-----LKEVts 295
Cdd:COG1092 256 KENAALNGLddrhEFVQADAFDWLRELARE------------GERFDLIILDPP------------AFAkskkdLFDA-- 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 260099664 296 yqplQR---KLLHVAVQLLKPGGVLVYSTCT--ITLAENEEQVAWALR 338
Cdd:COG1092 310 ----QRdykDLNRLALKLLAPGGILVTSSCSrhFSLDLFLEILARAAR 353
|
|
| Tma20 |
COG2016 |
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ... |
41-133 |
4.86e-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: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 41 LPDVLLIPMTGPRKNIerqqgeVIV--GAQcgNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDINGKckkgakefdgtk 118
Cdd:COG2016 60 FPTLRGLLKYPPEKPV------VTVdmGAV--KFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKHGK------------ 119
|
90
....*....|....*
gi 260099664 119 vFLGNGISELSRKDI 133
Cdd:COG2016 120 -PLAVGRALVDGEEM 133
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
183-321 |
8.27e-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: 39.23 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 183 PGEKILDMCAAPGgkttHTAALMQDKG-EVIALDKILTKVNKLKQNASLLGlhsIRAFCFDATKAlkldttdgieggpPF 261
Cdd:COG2227 24 AGGRVLDVGCGTG----RLALALARRGaDVTGVDISPEALEIARERAAELN---VDFVQGDLEDL-------------PL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 262 LPESFDRIIldapCSgmgqrpnmactwtlkEVTSYQPLQRKLLHVAVQLLKPGGVLVYST 321
Cdd:COG2227 84 EDGSFDLVI----CS---------------EVLEHLPDPAALLRELARLLKPGGLLLLST 124
|
|
| FtsJ |
pfam01728 |
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
183-318 |
2.09e-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: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 183 PGEKILDMCAAPGGKTthTAALMQDKGEVIALDKILTKVNKLKQNAsllGLHSIRAfcfDATkalKLDTTDGIEggpPFL 262
Cdd:pfam01728 21 PGKTVLDLGAAPGGWS--QVALQRGAGKVVGVDLGPMQLWKPRNDP---GVTFIQG---DIR---DPETLDLLE---ELL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 260099664 263 PESFDRIILDApcsgmgqRPNMACTWTLKEVTSYQpLQRKLLHVAVQLLKPGGVLV 318
Cdd:pfam01728 87 GRKVDLVLSDG-------SPFISGNKVLDHLRSLD-LVKAALEVALELLRKGGNFV 134
|
|
| PUA |
pfam01472 |
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
61-133 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260099664 61 GEVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDiNGKckkgakefdgtkvFLGNGISELSRKDI 133
Cdd:pfam01472 1 GRVVVDDGAVKAILNGASLLAPGVVRVDGDFRKGDEVVVVTE-KGE-------------LVAVGLANYSSEEL 59
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
183-322 |
3.07e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 38.17 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 183 PGEKILDMCAAPGGKTTHTAALMQDKGEVIALDKILTKVNKLKQNASLLGLHSIRafcFDATKALKLDTTdgieggppFL 262
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVE---FEQGDIEELPEL--------LE 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 263 PESFDRIILDapcsgmgqrpnmactwtlkEVTSYQPLQRKLLHVAVQLLKPGGVLVYSTC 322
Cdd:pfam13847 72 DDKFDVVISN-------------------CVLNHIPDPDKVLQEILRVLKPGGRLIISDP 112
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
158-320 |
4.33e-03 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 38.36 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 158 DNVLPSYIFLqnlpstvVAHVLDPQPGEKILDMCAAPGgktTHTAALMQ-DKGEVIALDKILTKVNKLKQNASLLGLHSI 236
Cdd:COG0500 8 DELLPGLAAL-------LALLERLPKGGRVLDLGCGTG---RNLLALAArFGGRVIGIDLSPEAIALARARAAKAGLGNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 237 RAFCFDATKALKLDttdgieggppflPESFDRIILdapcsgmgqrpNMACTWTLKEVtsyqplQRKLLHVAVQLLKPGGV 316
Cdd:COG0500 78 EFLVADLAELDPLP------------AESFDLVVA-----------FGVLHHLPPEE------REALLRELARALKPGGV 128
|
....
gi 260099664 317 LVYS 320
Cdd:COG0500 129 LLLS 132
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
187-315 |
7.28e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 35.62 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 187 ILDMCAAPGgktTHTAALMQDKG-EVIALDKILTKVNKLKQNASLLGLHsIRAFCFDATKalkldttdgieggPPFLPES 265
Cdd:pfam13649 1 VLDLGCGTG---RLTLALARRGGaRVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAED-------------LPFPDGS 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 260099664 266 FDRIIldapcsgmgqrpnmaCTWTLKEVTsyQPLQRKLLHVAVQLLKPGG 315
Cdd:pfam13649 64 FDLVV---------------SSGVLHHLP--DPDLEAALREIARVLKPGG 96
|
|
| PRK14560 |
PRK14560 |
putative RNA-binding protein; Provisional |
55-136 |
7.48e-03 |
|
putative RNA-binding protein; Provisional
Pssm-ID: 237757 [Multi-domain] Cd Length: 160 Bit Score: 37.14 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260099664 55 NIERQQGEVIVGAQCGNAVLRGAHVYVPGIVSASKFMKAGDVISVYSDINGKckkgakefdgtkvFLGNGISELSRKDIF 134
Cdd:PRK14560 71 KLKPEKRRVVVDAGAVKFVSNGADVMAPGIVEADEDIKEGDIVFVVEETHGK-------------PLAVGRALMDGDEMV 137
|
..
gi 260099664 135 NG 136
Cdd:PRK14560 138 EE 139
|
|
|