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Conserved domains on  [gi|157821259|ref|NP_001100148|]
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5-methylcytosine rRNA methyltransferase NSUN4 [Rattus norvegicus]

Protein Classification

NOL1/NOP2/SUN domain family protein( domain architecture ID 1003105)

NOL1/NOP2/SUN domain (NSUN) family protein such as mammalian nucleolar protein NOP2 which is required for nucleolar maturation and ribosome biogenesis

Gene Ontology:  GO:0003723|GO:0000027|GO:0008173|GO:0001510

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nop2p super family cl33194
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 152-323 1.35e-33

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


The actual alignment was detected with superfamily member TIGR00446:

Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 125.66  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  152 YYLMDAASLLPVLALGLQHGDIVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSTSRTgrlqKVLHSYVPqdiRKG-N 226
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  227 HIRVTSWDGRKWGELeGDTYDKVLVDVPCTTDrHSLHEDENNIFQRSrKKERQMLPMLQVQLLGAGLLATKPGGHVVYST 306
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 157821259  307 CSLSHLQNEYVVQGAIE 323
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
 
Name Accession Description Interval E-value
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 152-323 1.35e-33

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


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 125.66  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  152 YYLMDAASLLPVLALGLQHGDIVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSTSRTgrlqKVLHSYVPqdiRKG-N 226
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  227 HIRVTSWDGRKWGELeGDTYDKVLVDVPCTTDrHSLHEDENNIFQRSrKKERQMLPMLQVQLLGAGLLATKPGGHVVYST 306
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 157821259  307 CSLSHLQNEYVVQGAIE 323
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 151-323 8.10e-31

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: 122.04  E-value: 8.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 151 DYYLMDAASLLPVLALGLQHGDIVLDLCAAPGGKTLALLQ----TGccrNLAANDLSTSRTGRLQKVLHsyvpqdiRKGN 226
Cdd:COG0144  230 LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAElmgnKG---RVVAVDISEHRLKRLRENLA-------RLGL 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 227 H-IRVTSWDGRKWGELEGDTYDKVLVDVPCT---TDRHslHEDennifQRSRKKER--QMLPMLQVQLLGAGLLATKPGG 300
Cdd:COG0144  300 SnVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEdiAELAALQRELLDAAARLLKPGG 372

                        170       180
                 ....*....|....*....|...
gi 157821259 301 HVVYSTCSLSHLQNEYVVQGAIE 323
Cdd:COG0144  373 RLVYSTCSLLPEENEEVVEAFLA 395
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 163-322 6.57e-26

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: 103.27  E-value: 6.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  163 VLALGLQHGDIVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSTSRTGRLQKVLHsyvpqdiRKG-NHIRVTSWDGRKWGE 240
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGvTNTIILNGDGRQPDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  241 -LEGDTYDKVLVDVPCT----TDRHSlhedenNIFQRSRKKERQMLPMLQVQLLGAGLLATKPGGHVVYSTCSLSHLQNE 315
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147


                  ....*..
gi 157821259  316 YVVQGAI 322
Cdd:pfam01189 148 AVIEYFL 154
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 148-347 8.65e-22

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


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 96.52  E-value: 8.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 148 GLMdyYLMDAASLLPVLAL--GLQHGDIVLDLCAAPGGKTLallQTGCCRN----LAANDLSTSRTgrlqKVLHSYVPqd 221
Cdd:PRK11933  91 GLF--YIQEASSMLPVAALfaDDNAPQRVLDMAAAPGSKTT---QIAALMNnqgaIVANEYSASRV----KVLHANIS-- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 222 iRKG-NHIRVTSWDGRKWGELEGDTYDKVLVDVPCT------TDRHSLH----EDENNIFQrsrkkerqmlpmLQVQLLG 290
Cdd:PRK11933 160 -RCGvSNVALTHFDGRVFGAALPETFDAILLDAPCSgegtvrKDPDALKnwspESNLEIAA------------TQRELIE 226

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157821259 291 AGLLATKPGGHVVYSTCSLSHLQNEYVVQGaielLANQYNIKVQVEDLShfrKLFMD 347
Cdd:PRK11933 227 SAFHALKPGGTLVYSTCTLNREENQAVCLW----LKETYPDAVEFEPLG---DLFPG 276
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 174-305 2.49e-05

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: 42.80  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 174 VLDLCAAPGGKTLALLQTGCCRNLaANDLSTSRTGRLQKVlhsyvpQDIRKGNHIRVTSWDGRKWGELEGDTYDKVLVDV 253
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVT-GVDISPVALELARKA------AAALLADNVEVLKGDAEELPPEADESFDVIISDP 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157821259 254 PCttdrhslhedennifqrsrkkerQMLPMLQVQLLGAGLLATKPGGHVVYS 305
Cdd:cd02440   75 PL-----------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 152-323 1.35e-33

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


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 125.66  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  152 YYLMDAASLLPVLALGLQHGDIVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSTSRTgrlqKVLHSYVPqdiRKG-N 226
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  227 HIRVTSWDGRKWGELeGDTYDKVLVDVPCTTDrHSLHEDENNIFQRSrKKERQMLPMLQVQLLGAGLLATKPGGHVVYST 306
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 157821259  307 CSLSHLQNEYVVQGAIE 323
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 151-323 8.10e-31

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: 122.04  E-value: 8.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 151 DYYLMDAASLLPVLALGLQHGDIVLDLCAAPGGKTLALLQ----TGccrNLAANDLSTSRTGRLQKVLHsyvpqdiRKGN 226
Cdd:COG0144  230 LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAElmgnKG---RVVAVDISEHRLKRLRENLA-------RLGL 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 227 H-IRVTSWDGRKWGELEGDTYDKVLVDVPCT---TDRHslHEDennifQRSRKKER--QMLPMLQVQLLGAGLLATKPGG 300
Cdd:COG0144  300 SnVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEdiAELAALQRELLDAAARLLKPGG 372

                        170       180
                 ....*....|....*....|...
gi 157821259 301 HVVYSTCSLSHLQNEYVVQGAIE 323
Cdd:COG0144  373 RLVYSTCSLLPEENEEVVEAFLA 395
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 163-322 6.57e-26

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: 103.27  E-value: 6.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  163 VLALGLQHGDIVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSTSRTGRLQKVLHsyvpqdiRKG-NHIRVTSWDGRKWGE 240
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGvTNTIILNGDGRQPDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  241 -LEGDTYDKVLVDVPCT----TDRHSlhedenNIFQRSRKKERQMLPMLQVQLLGAGLLATKPGGHVVYSTCSLSHLQNE 315
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DVKWLRQEADIAQLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEENE 147


                  ....*..
gi 157821259  316 YVVQGAI 322
Cdd:pfam01189 148 AVIEYFL 154
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 148-347 8.65e-22

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


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 96.52  E-value: 8.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 148 GLMdyYLMDAASLLPVLAL--GLQHGDIVLDLCAAPGGKTLallQTGCCRN----LAANDLSTSRTgrlqKVLHSYVPqd 221
Cdd:PRK11933  91 GLF--YIQEASSMLPVAALfaDDNAPQRVLDMAAAPGSKTT---QIAALMNnqgaIVANEYSASRV----KVLHANIS-- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 222 iRKG-NHIRVTSWDGRKWGELEGDTYDKVLVDVPCT------TDRHSLH----EDENNIFQrsrkkerqmlpmLQVQLLG 290
Cdd:PRK11933 160 -RCGvSNVALTHFDGRVFGAALPETFDAILLDAPCSgegtvrKDPDALKnwspESNLEIAA------------TQRELIE 226

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157821259 291 AGLLATKPGGHVVYSTCSLSHLQNEYVVQGaielLANQYNIKVQVEDLShfrKLFMD 347
Cdd:PRK11933 227 SAFHALKPGGTLVYSTCTLNREENQAVCLW----LKETYPDAVEFEPLG---DLFPG 276
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
152-319 5.24e-20

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 91.01  E-value: 5.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 152 YYLMDAASLLPVLALGLQHGDIVLDLCAAPGGKT--LA--LLQTGccrNLAANDLSTSRTGRLQkvlhsyvpQDIRK-G- 225
Cdd:PRK14902 232 ITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTthIAelLKNTG---KVVALDIHEHKLKLIE--------ENAKRlGl 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 226 NHIRVTSWDGRKWGELEGDTYDKVLVDVPCT---TDRHslhedENNIfqRSRKKERQM--LPMLQVQLLGAGLLATKPGG 300
Cdd:PRK14902 301 TNIETKALDARKVHEKFAEKFDKILVDAPCSglgVIRR-----KPDI--KYNKTKEDIesLQEIQLEILESVAQYLKKGG 373

                        170
                 ....*....|....*....
gi 157821259 301 HVVYSTCSLSHLQNEYVVQ 319
Cdd:PRK14902 374 ILVYSTCTIEKEENEEVIE 392
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 156-319 1.26e-16

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: 80.68  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  156 DAASLLPVLALGLQHGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSTSrtgRLQKVlhsYVPQDiRKGNHIRVTSWDG 235
Cdd:TIGR00563 224 DASAQWVATWLAPQNEETILDACAAPGGKTTHILELAPQAQVVALDIHEH---RLKRV---YENLK-RLGLTIKAETKDG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  236 RK-----WGELEgdTYDKVLVDVPCT-TDRHSLHEDennifQRSRKKERQM--LPMLQVQLLGAGLLATKPGGHVVYSTC 307
Cdd:TIGR00563 297 DGrgpsqWAENE--QFDRILLDAPCSaTGVIRRHPD-----IKWLRKPRDIaeLAELQSEILDAIWPLLKTGGTLVYATC 369

                         170
                  ....*....|..
gi 157821259  308 SLSHLQNEYVVQ 319
Cdd:TIGR00563 370 SVLPEENSEQIK 381
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 156-336 4.37e-15

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 76.12  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 156 DAASLLPVLALGLQHGDIVLDLCAAPGGKT--LALLqtgccrnlaAND----LSTSRT-GRLQKVLhsyvpQDIRKGNH- 227
Cdd:PRK14901 238 DRSAQLVAPLLDPQPGEVILDACAAPGGKTthIAEL---------MGDqgeiWAVDRSaSRLKKLQ-----ENAQRLGLk 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 228 -IRVTSWDGRKWGELEGD---TYDKVLVDVPC----TTDRHSlhedenNIFQRSRKKERQMLPMLQVQLLGAGLLATKPG 299
Cdd:PRK14901 304 sIKILAADSRNLLELKPQwrgYFDRILLDAPCsglgTLHRHP------DARWRQTPEKIQELAPLQAELLESLAPLLKPG 377

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 157821259 300 GHVVYSTCSLSHLQNEYVVQgaiELLANQYNIKVQVE 336
Cdd:PRK14901 378 GTLVYATCTLHPAENEAQIE---QFLARHPDWKLEPP 411
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
 156-319 1.95e-14

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 74.14  E-value: 1.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 156 DAASLLPVLaLGLQHGDIVLDLCAAPGGKTLALLQTGCCR-NLAANDLSTSRTGRLQKVLHSYvpqdirKGNHIRVTSWD 234
Cdd:PRK14903 224 ESSQIVPLL-MELEPGLRVLDTCAAPGGKTTAIAELMKDQgKILAVDISREKIQLVEKHAKRL------KLSSIEIKIAD 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 235 GRKWGELEGDTYDKVLVDVPCTtdrhSLHEDENN--IFQRSRKKERQMLPMLQVQLLGAGLLATKPGGHVVYSTCSLSHL 312
Cdd:PRK14903 297 AERLTEYVQDTFDRILVDAPCT----SLGTARNHpeVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYSTCTVTKE 372


                 ....*..
gi 157821259 313 QNEYVVQ 319
Cdd:PRK14903 373 ENTEVVK 379
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
156-308 2.58e-14

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


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 73.69  E-value: 2.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 156 DAASLLPVLALGLQHGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSTSRTGRLQKVLHsyvpqdiRKGNHIRVTSWDG 235
Cdd:PRK10901 230 DAAAQLAATLLAPQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQRLERVRENLQ-------RLGLKATVIVGDA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 236 RK----WGeleGDTYDKVLVDVPCTTD----RHS---LHEDENNIFQrsrkkerqmLPMLQVQLLGA--GLLatKPGGHV 302
Cdd:PRK10901 303 RDpaqwWD---GQPFDRILLDAPCSATgvirRHPdikWLRRPEDIAA---------LAALQSEILDAlwPLL--KPGGTL 368


                 ....*.
gi 157821259 303 VYSTCS 308
Cdd:PRK10901 369 LYATCS 374
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 126-315 3.23e-11

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 64.31  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 126 LRCFTFSKgDVSRFPPASvgSLGLMDyyLMDAASLLPVLALGLQHGDIVLDLCAAPGGKTLALLQ----TGccrNLAAND 201
Cdd:PRK14904 211 LPNFFLSK-DFSLFEPFL--KLGLVS--VQNPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAElmqnRG---QITAVD 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 202 LSTSRTGRLQKvLHSYVPQDIrkgnhIRVTSWDGRKWgeLEGDTYDKVLVDVPCT-----TDRHSLHedenniFQRSRKK 276
Cdd:PRK14904 283 RYPQKLEKIRS-HASALGITI-----IETIEGDARSF--SPEEQPDAILLDAPCTgtgvlGRRAELR------WKLTPEK 348

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157821259 277 ERQmLPMLQVQLL--GAGLLatKPGGHVVYSTCSLSHLQNE 315
Cdd:PRK14904 349 LAE-LVGLQAELLdhAASLL--KPGGVLVYATCSIEPEENE 386
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 174-305 2.49e-05

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: 42.80  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259 174 VLDLCAAPGGKTLALLQTGCCRNLaANDLSTSRTGRLQKVlhsyvpQDIRKGNHIRVTSWDGRKWGELEGDTYDKVLVDV 253
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVT-GVDISPVALELARKA------AAALLADNVEVLKGDAEELPPEADESFDVIISDP 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157821259 254 PCttdrhslhedennifqrsrkkerQMLPMLQVQLLGAGLLATKPGGHVVYS 305
Cdd:cd02440   75 PL-----------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 168-303 3.94e-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: 37.95  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821259  168 LQHGDIVLDLCAAPGGKTLALLQTGCCRNLAAnDLSTSRTGRLQKVLHSYVPQ-DIRKGNHIrvtswdgRKWGELEGDTY 246
Cdd:pfam01728  19 LKPGKTVLDLGAAPGGWSQVALQRGAGKVVGV-DLGPMQLWKPRNDPGVTFIQgDIRDPETL-------DLLEELLGRKV 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157821259  247 DKVLVDV-PCTTDRHSLHEdennifqrsrkkERQMLpMLQVQLLgAGLLATKPGGHVV 303
Cdd:pfam01728  91 DLVLSDGsPFISGNKVLDH------------LRSLD-LVKAALE-VALELLRKGGNFV 134
 
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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