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Conserved domains on  [gi|1189131251|ref|NP_001338047|]
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tRNA (cytosine(72)-C(5))-methyltransferase NSUN6 isoform 5 [Homo sapiens]

Protein Classification

RsmB/NOP family class I SAM-dependent RNA methyltransferase( domain architecture ID 15340246)

RsmB/NOP family class I SAM-dependent RNA methyltransferase similar to tRNA (cytosine(34)-C(5))-methyltransferase, which methylates cytosine at specific positions of intron-containing tRNA(Leu)(CAA) precursors and tRNA(Gly)(GCC) precursors

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0003723
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 49-324 9.84e-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: 218.34  E-value: 9.84e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  49 ELKGMGIRmTEPVYLSPsfDSV-LPRYLFLQNLP-------------SALVSHVLNPQPGEKILDLCAAPGGKTTHIAAL 114
Cdd:COG0144   194 RLAEEGIE-AEPTPLSP--DGLrLEGPGPVTALPgfreglfsvqdeaSQLVALLLDPKPGERVLDLCAAPGGKTLHLAEL 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 115 MHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QR 191
Cdd:COG0144   271 MGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRH 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 192 PNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAG 271
Cdd:COG0144   339 PDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1189131251 272 lsCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrlankdsiGFFIAKFVK 324
Cdd:COG0144   419 --YLRL------------LPHRhGTD-------------------GFFIARLRK 439
PUA_NSun6-like cd21150
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ...
 1-61 2.54e-27

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: 102.53  E-value: 2.54e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189131251   1 MKAGDVISVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKEIFSGLPELKGMGIRMTEPV 61
Cdd:cd21150    31 LKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKPSGIAVEMTEPV 92
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 49-324 9.84e-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: 218.34  E-value: 9.84e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  49 ELKGMGIRmTEPVYLSPsfDSV-LPRYLFLQNLP-------------SALVSHVLNPQPGEKILDLCAAPGGKTTHIAAL 114
Cdd:COG0144   194 RLAEEGIE-AEPTPLSP--DGLrLEGPGPVTALPgfreglfsvqdeaSQLVALLLDPKPGERVLDLCAAPGGKTLHLAEL 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 115 MHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QR 191
Cdd:COG0144   271 MGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRH 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 192 PNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAG 271
Cdd:COG0144   339 PDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1189131251 272 lsCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrlankdsiGFFIAKFVK 324
Cdd:COG0144   419 --YLRL------------LPHRhGTD-------------------GFFIARLRK 439
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
74-326 1.55e-63

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 207.72  E-value: 1.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  74 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 153
Cdd:PRK14902  231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 154 TKAvkldmvedtegePPFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 230
Cdd:PRK14902  311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 231 TCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrl 309
Cdd:PRK14902  379 TCTIEKEENEEVIEAFLEEHPEFELVPLQHEKPDELVYEVKDGYLQI------------LPNDyGTD------------- 433

                         250
                  ....*....|....*..
gi 1189131251 310 ankdsiGFFIAKFVKCK 326
Cdd:PRK14902  434 ------GFFIAKLRKKG 444
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 88-322 4.28e-52

16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.


Pssm-ID: 426109 [Multi-domain]  Cd Length: 199  Bit Score: 170.68  E-value: 4.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  88 VLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKavkldmvedteg 167
Cdd:pfam01189   3 LLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------------ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 168 ePPFLP--ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQ 242
Cdd:pfam01189  71 -PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 243 VAWALTKFPCLQLQPqepqIGGEGMRGAGLSCEQLKQLqrfdpsavpLPDTDmdslrearredmlrlaNKDsiGFFIAKF 322
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL---------LPHTH----------------NGD--GFFIAKL 198
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 77-264 1.33e-41

16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. The reading frame was originally interpreted as two reading frames, fmu and fmv. The recombinant protein from E. coli was shown to methylate only C967 of small subunit (16S) ribosomal RNA and to produce only m5C at that position. The seed alignment is built from bacterial sequences only. Eukaryotic homologs include Nop2, a protein required for processing pre-rRNA, that is likely also a rRNA methyltransferase, although the fine specificity may differ. Cutoff scores are set to avoid treating archaeal and eukaroytic homologs automatically as functionally equivalent, although they may have very similar roles. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273141 [Multi-domain]  Cd Length: 426  Bit Score: 149.63  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  77 LQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMhDQGEVIALDKIFNKVEKIKQNALLLGLnSIRAFCFDGTKA 156
Cdd:TIGR00563 222 VQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELA-PQAQVVALDIHEHRLKRVYENLKRLGL-TIKAETKDGDGR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 157 vkldmvedteGEPPFLP-ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTC 232
Cdd:TIGR00563 300 ----------GPSQWAEnEQFDRILLDAPCSATGvirRHPDIKWLRKPRDIAELAELQSEILDAIWPLLKTGGTLVYATC 369

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1189131251 233 TITLAENEEQVAWALTKFPCLQL----QPQEPQIGG 264
Cdd:TIGR00563 370 SVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
PUA_NSun6-like cd21150
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ...
 1-61 2.54e-27

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: 102.53  E-value: 2.54e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189131251   1 MKAGDVISVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKEIFSGLPELKGMGIRMTEPV 61
Cdd:cd21150    31 LKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKPSGIAVEMTEPV 92
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-230 1.20e-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: 55.13  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  96 KILDLCAAPGGKTTHIAAlmHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPES 175
Cdd:cd02440     1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1189131251 176 FDRILLDAPCSgmgqrpnmactwsvkevaSYQPLQRKLFTAAVQLLKPEGVLVYS 230
Cdd:cd02440    67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 49-324 9.84e-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: 218.34  E-value: 9.84e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  49 ELKGMGIRmTEPVYLSPsfDSV-LPRYLFLQNLP-------------SALVSHVLNPQPGEKILDLCAAPGGKTTHIAAL 114
Cdd:COG0144   194 RLAEEGIE-AEPTPLSP--DGLrLEGPGPVTALPgfreglfsvqdeaSQLVALLLDPKPGERVLDLCAAPGGKTLHLAEL 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 115 MHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QR 191
Cdd:COG0144   271 MGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADARELLE------------WLPGKFDRVLLDAPCSGTGtlrRH 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 192 PNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAG 271
Cdd:COG0144   339 PDIKWRRTPEDIAELAALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLARHPDFELVPLAELLPGLALTDGG 418

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1189131251 272 lsCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrlankdsiGFFIAKFVK 324
Cdd:COG0144   419 --YLRL------------LPHRhGTD-------------------GFFIARLRK 439
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
74-326 1.55e-63

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 207.72  E-value: 1.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  74 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 153
Cdd:PRK14902  231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTTHIAELLKNTGKVVALDIHEHKLKLIEENAKRLGLTNIETKALDA 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 154 TKAvkldmvedtegePPFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 230
Cdd:PRK14902  311 RKV------------HEKFAEKFDKILVDAPCSGLGvirRKPDIKYNKTKEDIESLQEIQLEILESVAQYLKKGGILVYS 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 231 TCTITLAENEEQVAWALTKFPCLQLQPQEPQIGGEGMRGAGLSCEQLkqlqrfdpsavpLPDT-DMDslrearredmlrl 309
Cdd:PRK14902  379 TCTIEKEENEEVIEAFLEEHPEFELVPLQHEKPDELVYEVKDGYLQI------------LPNDyGTD------------- 433

                         250
                  ....*....|....*..
gi 1189131251 310 ankdsiGFFIAKFVKCK 326
Cdd:PRK14902  434 ------GFFIAKLRKKG 444
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 77-262 4.43e-60

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 198.23  E-value: 4.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  77 LQNLP------------SA-LVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGL 143
Cdd:PRK14901  223 IRQLPgyeegwwtvqdrSAqLVAPLLDPQPGEVILDACAAPGGKTTHIAELMGDQGEIWAVDRSASRLKKLQENAQRLGL 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 144 NSIRAFCFDGTKAVkldmvedteGEPPFLPESFDRILLDAPCSGMG---QRPNMacTWSV--KEVASYQPLQRKLFTAAV 218
Cdd:PRK14901  303 KSIKILAADSRNLL---------ELKPQWRGYFDRILLDAPCSGLGtlhRHPDA--RWRQtpEKIQELAPLQAELLESLA 371

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1189131251 219 QLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLQPQEPQI 262
Cdd:PRK14901  372 PLLKPGGTLVYATCTLHPAENEAQIEQFLARHPDWKLEPPKQKI 415
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 88-322 4.28e-52

16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.


Pssm-ID: 426109 [Multi-domain]  Cd Length: 199  Bit Score: 170.68  E-value: 4.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  88 VLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKavkldmvedteg 167
Cdd:pfam01189   3 LLAPQEGETILDMCAAPGGKTTHIAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ------------ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 168 ePPFLP--ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCTITLAENEEQ 242
Cdd:pfam01189  71 -PDQWLggVLFDRILLDAPCSGTGvirRHPDVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENEAV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 243 VAWALTKFPCLQLQPqepqIGGEGMRGAGLSCEQLKQLqrfdpsavpLPDTDmdslrearredmlrlaNKDsiGFFIAKF 322
Cdd:pfam01189 150 IEYFLQKHPDVELVP----TPLFEPVGLAIGEQPTLRL---------LPHTH----------------NGD--GFFIAKL 198
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 78-257 3.50e-46

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 162.15  E-value: 3.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  78 QNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKav 157
Cdd:PRK14904  235 QNPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAELMQNRGQITAVDRYPQKLEKIRSHASALGITIIETIEGDARS-- 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 158 kldmvedtegeppFLPE-SFDRILLDAPCSG---MGQRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCT 233
Cdd:PRK14904  313 -------------FSPEeQPDAILLDAPCTGtgvLGRRAELRWKLTPEKLAELVGLQAELLDHAASLLKPGGVLVYATCS 379

                         170       180
                  ....*....|....*....|....
gi 1189131251 234 ITLAENEEQVAWALTKFPCLQLQP 257
Cdd:PRK14904  380 IEPEENELQIEAFLQRHPEFSAEP 403
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 77-264 1.33e-41

16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. The reading frame was originally interpreted as two reading frames, fmu and fmv. The recombinant protein from E. coli was shown to methylate only C967 of small subunit (16S) ribosomal RNA and to produce only m5C at that position. The seed alignment is built from bacterial sequences only. Eukaryotic homologs include Nop2, a protein required for processing pre-rRNA, that is likely also a rRNA methyltransferase, although the fine specificity may differ. Cutoff scores are set to avoid treating archaeal and eukaroytic homologs automatically as functionally equivalent, although they may have very similar roles. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273141 [Multi-domain]  Cd Length: 426  Bit Score: 149.63  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  77 LQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMhDQGEVIALDKIFNKVEKIKQNALLLGLnSIRAFCFDGTKA 156
Cdd:TIGR00563 222 VQDASAQWVATWLAPQNEETILDACAAPGGKTTHILELA-PQAQVVALDIHEHRLKRVYENLKRLGL-TIKAETKDGDGR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 157 vkldmvedteGEPPFLP-ESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTC 232
Cdd:TIGR00563 300 ----------GPSQWAEnEQFDRILLDAPCSATGvirRHPDIKWLRKPRDIAELAELQSEILDAIWPLLKTGGTLVYATC 369

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1189131251 233 TITLAENEEQVAWALTKFPCLQL----QPQEPQIGG 264
Cdd:TIGR00563 370 SVLPEENSEQIKAFLQEHPDFPFektgTPEQVRDGG 405
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 61-324 2.16e-41

NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 144.92  E-value: 2.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  61 VYLSPSFDSVLPRYL----FLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQ 136
Cdd:TIGR00446  35 VKESPFSIGSTPEYLfgyyYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQLMKNKGCIVANEISKSRTKALIS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 137 NALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPEsFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKL 213
Cdd:TIGR00446 115 NINRMGVLNTIVINADGRKF------------GAYLLK-FDAILLDAPCSGEGvirKDPSRKRNWSEEDIKYCSLLQKEL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 214 FTAAVQLLKPEGVLVYSTCTITLAENEEQVAWALTKFPCLQLqpqEPQIGGEGMrGAGLSCEQLKQLQRFDPSavplpdt 293
Cdd:TIGR00446 182 IDAAIDALKPGGVLVYSTCSLEVEENEEVIDYILRKRPDVVE---EIIKGDEFF-GINIGKGEVKGALRVFPQ------- 250

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1189131251 294 dmdslrearredmlrlaNKDSIGFFIAKFVK 324
Cdd:TIGR00446 251 -----------------NYDCEGFFVAKLRK 264
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
84-324 4.55e-40

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 145.33  E-value: 4.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  84 LVSHVLNPQPGEKILDLCAAPGGKTTHIAALmHDQGEVIALDKIFNKVEKIKQNALLLGLNSiRAFCFDGTKAvkldmve 163
Cdd:PRK10901  235 LAATLLAPQNGERVLDACAAPGGKTAHILEL-APQAQVVALDIDAQRLERVRENLQRLGLKA-TVIVGDARDP------- 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 164 DT--EGEPpflpesFDRILLDAPCSGMG-----------QRPNmactwsvkEVASYQPLQRKLFTAAVQLLKPEGVLVYS 230
Cdd:PRK10901  306 AQwwDGQP------FDRILLDAPCSATGvirrhpdikwlRRPE--------DIAALAALQSEILDALWPLLKPGGTLLYA 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 231 TCTITLAENEEQVAWALTKFPCLQLQPQ-EPQIGGegmrgaglsceqlKQLqrfdpsavpLP-DTDMDslrearredmlr 308
Cdd:PRK10901  372 TCSILPEENEQQIKAFLARHPDAELLDTgTPQQPG-------------RQL---------LPgEEDGD------------ 417

                         250
                  ....*....|....*.
gi 1189131251 309 lankdsiGFFIAKFVK 324
Cdd:PRK10901  418 -------GFFYALLIK 426
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 69-251 1.64e-31

rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 123.09  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  69 SVLPrylflqnlPSALVSHvlNPQPgEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRA 148
Cdd:PRK11933  100 SMLP--------VAALFAD--DNAP-QRVLDMAAAPGSKTTQIAALMNNQGAIVANEYSASRVKVLHANISRCGVSNVAL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 149 FCFDGTkavkldmvedTEGEppFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEG 225
Cdd:PRK11933  169 THFDGR----------VFGA--ALPETFDAILLDAPCSGEGtvrKDPDALKNWSPESNLEIAATQRELIESAFHALKPGG 236

                         170       180
                  ....*....|....*....|....*.
gi 1189131251 226 VLVYSTCTITLAENEEQVAWALTKFP 251
Cdd:PRK11933  237 TLVYSTCTLNREENQAVCLWLKETYP 262
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
 74-249 3.70e-29

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 115.74  E-value: 3.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  74 YLFLQNLPSALVSHVLNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDG 153
Cdd:PRK14903  218 LATVQGESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAELMKDQGKILAVDISREKIQLVEKHAKRLKLSSIEIKIADA 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 154 TKAVKldmvedtegeppFLPESFDRILLDAPCSGMG---QRPNMACTWSVKEVASYQPLQRKLFTAAVQLLKPEGVLVYS 230
Cdd:PRK14903  298 ERLTE------------YVQDTFDRILVDAPCTSLGtarNHPEVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYS 365

                         170       180
                  ....*....|....*....|
gi 1189131251 231 TCTITLAENEEQV-AWALTK 249
Cdd:PRK14903  366 TCTVTKEENTEVVkRFVYEQ 385
PUA_NSun6-like cd21150
PUA RNA-binding domain of the SAM-dependent methyltransferase NSun6 and similar proteins; The ...
 1-61 2.54e-27

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: 102.53  E-value: 2.54e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189131251   1 MKAGDVISVYSDIKGKCKKGA-KEFDGTKVFLGNGISELSRKEIFSGLPELKGMGIRMTEPV 61
Cdd:cd21150    31 LKKGDKVSVYADLEGKCKRGLtKPFEGRKVFVGNGIALMSRKDLFRGNNKPSGIAVEMTEPV 92
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-230 1.20e-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: 55.13  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  96 KILDLCAAPGGKTTHIAAlmHDQGEVIALDKIFNKVEKIKQNALLLGLNSIRAFCFDGTKAvkldmvedtegePPFLPES 175
Cdd:cd02440     1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL------------PPEADES 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1189131251 176 FDRILLDAPCSgmgqrpnmactwsvkevaSYQPLQRKLFTAAVQLLKPEGVLVYS 230
Cdd:cd02440    67 FDVIISDPPLH------------------HLVEDLARFLEEARRLLKPGGVLVLT 103
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 67-228 2.69e-06

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 46.14  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  67 FDSVLPRYlflqNLPSALVSHvLNPQPGEKILDLCAAPGgktTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGLNsI 146
Cdd:COG2226     1 FDRVAARY----DGREALLAA-LGLRPGARVLDLGCGTG---RLALALAERGARVTGVDISPEMLELARERAAEAGLN-V 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 147 RAFCFDGTkavkldmvedtegEPPFLPESFDRILldapcsgmgqrpnmaCTWSVKEVASyqplQRKLFTAAVQLLKPEGV 226
Cdd:COG2226    72 EFVVGDAE-------------DLPFPDGSFDLVI---------------SSFVLHHLPD----PERALAEIARVLKPGGR 119


                  ..
gi 1189131251 227 LV 228
Cdd:COG2226   120 LV 121
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 93-232 7.56e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.32  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  93 PGEKILDLCAAPGGKTTHIAALMHDQGEVIALDKIFNKVEKIKQNALLLGlnsirafcFDGTKAVKLDMvedTEGEPPFL 172
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLG--------FDNVEFEQGDI---EELPELLE 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 173 PESFDRILLDapcsgmgqrpnmactwsvkEVASYQPLQRKLFTAAVQLLKPEGVLVYSTC 232
Cdd:pfam13847  72 DDKFDVVISN-------------------CVLNHIPDPDKVLQEILRVLKPGGRLIISDP 112
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 93-228 1.51e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 38.72  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  93 PGEKILDLCAAPGGKTThiAALMHDQGEVIALDKIFNKVEKIKQNAlllGLNSIRAfcfDGTKAVKLDMVEDTEGEPpfl 172
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQ--VALQRGAGKVVGVDLGPMQLWKPRNDP---GVTFIQG---DIRDPETLDLLEELLGRK--- 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189131251 173 pesFDRILLDApcsgmgqRPNMACTWSVKEVASYQpLQRKLFTAAVQLLKPEGVLV 228
Cdd:pfam01728  90 ---VDLVLSDG-------SPFISGNKVLDHLRSLD-LVKAALEVALELLRKGGNFV 134
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 93-125 1.80e-03

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 38.90  E-value: 1.80e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1189131251  93 PGEKILDLCAAPGGKTTHIAALMHDQGEVIALD 125
Cdd:COG0293    50 PGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALD 82
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 68-309 2.32e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.74  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  68 DSVLPRYLFLQNLPSALvshvlnpQPGEKILDLCAAPGGKTTHIAALMHDQgeVIALDkiFNK--VEKIKQNALLLGLNS 145
Cdd:COG0500     8 DELLPGLAALLALLERL-------PKGGRVLDLGCGTGRNLLALAARFGGR--VIGID--LSPeaIALARARAAKAGLGN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 146 IRafcFdgtkavkldMVEDTEGEPPFLPESFDRILLDApcsgmgqrpnmactwsvkeVASYQPLQR--KLFTAAVQLLKP 223
Cdd:COG0500    77 VE---F---------LVADLAELDPLPAESFDLVVAFG-------------------VLHHLPPEEreALLRELARALKP 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 224 EGVLVYStctITLAENEEqvawaltkFPCLQLQPQEPQIGGEGMRGAGLSCEQLKQLQRFDpSAVPLPDTDMDSLREARR 303
Cdd:COG0500   126 GGVLLLS---ASDAAAAL--------SLARLLLLATASLLELLLLLRLLALELYLRALLAA-AATEDLRSDALLESANAL 193


                  ....*.
gi 1189131251 304 EDMLRL 309
Cdd:COG0500   194 EYLLSK 199
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 67-179 2.40e-03

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.98  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  67 FDSVLPRYLFLQNLPSALVSHV--------LNPQPGEKILDLCAAPGGKTTHIAALMHDQGEVIALDkiFN----KV--E 132
Cdd:PRK00216   17 FDSIAPKYDLMNDLLSFGLHRVwrrktikwLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLD--FSegmlAVgrE 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1189131251 133 KIKQNALLLGLNSIRAfcfdgtKAVKLdmvedtegepPFLPESFDRI 179
Cdd:PRK00216   95 KLRDLGLSGNVEFVQG------DAEAL----------PFPDNSFDAV 125
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 94-249 3.67e-03

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 38.62  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  94 GEKILDLCAAPGGKTthIAALMHDQGEVIALDkIFNK-VEKIKQNALLLGLNS----IRAFCFDGTKAvkldmvEDTEGE 168
Cdd:COG1092   217 GKRVLNLFSYTGGFS--VHAAAGGAKSVTSVD-LSATaLEWAKENAALNGLDDrhefVQADAFDWLRE------LAREGE 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251 169 ppflpeSFDRILLDAPcsgmgqrpnmacTW--SVKEVASYQPLQRKLFTAAVQLLKPEGVLVYSTCT--ITLAENEEQVA 244
Cdd:COG1092   288 ------RFDLIILDPP------------AFakSKKDLFDAQRDYKDLNRLALKLLAPGGILVTSSCSrhFSLDLFLEILA 349


                  ....*
gi 1189131251 245 WALTK 249
Cdd:COG1092   350 RAARD 354
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 97-225 7.21e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 35.23  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131251  97 ILDLCAAPGGKTTHIAALMHdqGEVIALDKIFNKVEKIKQNALLLGLNsIRAFCFDGTkavkldmvedtegEPPFLPESF 176
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGLN-VEFVQGDAE-------------DLPFPDGSF 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1189131251 177 DRILldapCSGMgqrpnMACTWsvkevasyQPLQRKLFTAAVQLLKPEG 225
Cdd:pfam13649  65 DLVV----SSGV-----LHHLP--------DPDLEAALREIARVLKPGG 96
rrmJ PRK11188
23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;
92-125 7.98e-03

23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE;


Pssm-ID: 183025  Cd Length: 209  Bit Score: 37.02  E-value: 7.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1189131251  92 QPGEKILDLCAAPGGKTTHIAALMHDQGEVIALD 125
Cdd:PRK11188   50 KPGMTVVDLGAAPGGWSQYAVTQIGDKGRVIACD 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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