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Conserved domains on  [gi|371123235|ref|NP_001243057|]
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5-methylcytosine rRNA methyltransferase NSUN4 isoform b [Homo sapiens]

Protein Classification

RsmB/NOP family class I SAM-dependent RNA methyltransferase( domain architecture ID 1000767)

RsmB/NOP family class I SAM-dependent RNA methyltransferase similar to Homo sapiens mitochondrial tRNA (cytosine(34)-C(5))-methyltransferase, which mediates methylation of cytosine to 5-methylcytosine (m5C) at position 34 of mt-tRNA(Met), and to 5-methylcytosine rRNA methyltransferase NSUN4 involved in mitochondrial ribosome small subunit (SSU) maturation by methylation of mitochondrial 12S rRNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsmB super family cl33775
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 86-277 5.08e-38

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


The actual alignment was detected with superfamily member COG0144:

Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 140.53  E-value: 5.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  86 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGccrNLAANDLSPSRI 161
Cdd:COG0144  216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAElmgnKG---RVVAVDISEHRL 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 162 ARLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslHEEennifKRSRKKERQI--L 235
Cdd:COG0144  288 KRLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEDIaeL 353

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 371123235 236 PVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIE 277
Cdd:COG0144  354 AALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLA 395
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 86-277 5.08e-38

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: 140.53  E-value: 5.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  86 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGccrNLAANDLSPSRI 161
Cdd:COG0144  216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAElmgnKG---RVVAVDISEHRL 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 162 ARLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslHEEennifKRSRKKERQI--L 235
Cdd:COG0144  288 KRLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEDIaeL 353

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 371123235 236 PVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIE 277
Cdd:COG0144  354 AALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLA 395
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 106-277 1.93e-34

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


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 126.81  E-value: 1.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  106 YYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSPSRIarlqKILHSYVPeeiRDG-N 180
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  181 QVRVTSWDGRKWGELeGDTYDRVLVDVPCTTDrHSLHEEENNIFKRSrKKERQILPVLQVQLLAAGLLATKPGGHVVYST 260
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 371123235  261 CSLSHLQNEYVVQGAIE 277
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 117-276 4.23e-27

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: 105.58  E-value: 4.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  117 VLALGLQPGDIVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQ-VRVTSWDGRKWGE 194
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGVTnTIILNGDGRQPDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  195 -LEGDTYDRVLVDVPCT----TDRHSlheeenNIfkRSRKKERQI--LPVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQ 267
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DV--KWLRQEADIaqLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEE 145


                  ....*....
gi 371123235  268 NEYVVQGAI 276
Cdd:pfam01189 146 NEAVIEYFL 154
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
105-273 8.71e-25

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 104.10  E-value: 8.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 105 EYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LA--LLQTGccrNLAANDLSPSRIARLQ---KILHsyvpeeIR 177
Cdd:PRK14902 231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTthIAelLKNTG---KVVALDIHEHKLKLIEenaKRLG------LT 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 178 DgnqVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslheeennifK---RSRKKERQI--LPVLQVQLL--AAGL 247
Cdd:PRK14902 302 N---IETKALDARKVHEKFAEKFDKILVDAPCSglgVIRR----------KpdiKYNKTKEDIesLQEIQLEILesVAQY 368

                        170       180
                 ....*....|....*....|....*.
gi 371123235 248 LatKPGGHVVYSTCSLSHLQNEYVVQ 273
Cdd:PRK14902 369 L--KKGGILVYSTCTIEKEENEEVIE 392
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 128-259 1.75e-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: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 128 VLDLCAAPGGKTLALLQTGCCRNLaANDLSPSRIARLQKILHSYVPEEIRDGNQvrvtswDGRKWGELEGDTYDRVLVDV 207
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVT-GVDISPVALELARKAAAALLADNVEVLKG------DAEELPPEADESFDVIISDP 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 371123235 208 PCttdrHSLHEeennifkrsrkkerqilpvLQVQLLAAGLLATKPGGHVVYS 259
Cdd:cd02440   75 PL----HHLVE-------------------DLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 86-277 5.08e-38

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: 140.53  E-value: 5.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  86 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGccrNLAANDLSPSRI 161
Cdd:COG0144  216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAElmgnKG---RVVAVDISEHRL 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 162 ARLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslHEEennifKRSRKKERQI--L 235
Cdd:COG0144  288 KRLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEDIaeL 353

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 371123235 236 PVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIE 277
Cdd:COG0144  354 AALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLA 395
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 106-277 1.93e-34

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


Pssm-ID: 188051 [Multi-domain]  Cd Length: 264  Bit Score: 126.81  E-value: 1.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  106 YYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSPSRIarlqKILHSYVPeeiRDG-N 180
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  181 QVRVTSWDGRKWGELeGDTYDRVLVDVPCTTDrHSLHEEENNIFKRSrKKERQILPVLQVQLLAAGLLATKPGGHVVYST 260
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 371123235  261 CSLSHLQNEYVVQGAIE 277
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 117-276 4.23e-27

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: 105.58  E-value: 4.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  117 VLALGLQPGDIVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQ-VRVTSWDGRKWGE 194
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGVTnTIILNGDGRQPDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  195 -LEGDTYDRVLVDVPCT----TDRHSlheeenNIfkRSRKKERQI--LPVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQ 267
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DV--KWLRQEADIaqLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEE 145


                  ....*....
gi 371123235  268 NEYVVQGAI 276
Cdd:pfam01189 146 NEAVIEYFL 154
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
105-273 8.71e-25

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 104.10  E-value: 8.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 105 EYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LA--LLQTGccrNLAANDLSPSRIARLQ---KILHsyvpeeIR 177
Cdd:PRK14902 231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTthIAelLKNTG---KVVALDIHEHKLKLIEenaKRLG------LT 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 178 DgnqVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslheeennifK---RSRKKERQI--LPVLQVQLL--AAGL 247
Cdd:PRK14902 302 N---IETKALDARKVHEKFAEKFDKILVDAPCSglgVIRR----------KpdiKYNKTKEDIesLQEIQLEILesVAQY 368

                        170       180
                 ....*....|....*....|....*.
gi 371123235 248 LatKPGGHVVYSTCSLSHLQNEYVVQ 273
Cdd:PRK14902 369 L--KKGGILVYSTCTIEKEENEEVIE 392
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 106-292 1.38e-20

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


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 91.89  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 106 YYLMDAASLLPVLAL--GLQPGDIVLDLCAAPGGKTLallQTGCCRN----LAANDLSPSRIarlqKILHSYVPeeiRDG 179
Cdd:PRK11933  93 FYIQEASSMLPVAALfaDDNAPQRVLDMAAAPGSKTT---QIAALMNnqgaIVANEYSASRV----KVLHANIS---RCG 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 180 -NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT------TDRHSLHEEENNifkrsrkkerQILPVLQVQ--LLAAGLLAT 250
Cdd:PRK11933 163 vSNVALTHFDGRVFGAALPETFDAILLDAPCSgegtvrKDPDALKNWSPE----------SNLEIAATQreLIESAFHAL 232

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 371123235 251 KPGGHVVYSTCSLSHLQNEYVVQGaielLANQYSIQVQVEDL 292
Cdd:PRK11933 233 KPGGTLVYSTCTLNREENQAVCLW----LKETYPDAVEFEPL 270
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 88-290 3.54e-19

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 87.68  E-value: 3.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  88 GDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LALLqTGCCRNLAANDLSPSRI---- 161
Cdd:PRK14901 221 GSIRQLPGYEEG-----WWTVQDRSAQLVAPLLDPQPGEVILDACAAPGGKTthIAEL-MGDQGEIWAVDRSASRLkklq 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 162 ---ARLQkiLHSyvpeeirdgnqVRVTSWDGRKWGELEGD---TYDRVLVDVPC----TTDRHSlheeenniFKRSRKKE 231
Cdd:PRK14901 295 enaQRLG--LKS-----------IKILAADSRNLLELKPQwrgYFDRILLDAPCsglgTLHRHP--------DARWRQTP 353

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371123235 232 RQI--LPVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQgaiELLANQYSIQVQVE 290
Cdd:PRK14901 354 EKIqeLAPLQAELLESLAPLLKPGGTLVYATCTLHPAENEAQIE---QFLARHPDWKLEPP 411
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 110-273 6.66e-19

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: 86.85  E-value: 6.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  110 DAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDG 189
Cdd:TIGR00563 224 DASAQWVATWLAPQNEETILDACAAPGGKTTHILELAPQAQVVALDIHEHRLKRVYENLK-------RLGLTIKAETKDG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  190 RK-----WGELEgdTYDRVLVDVPC----TTDRHSlheeenNIfkRSRKKERQI--LPVLQVQLLAAGLLATKPGGHVVY 258
Cdd:TIGR00563 297 DGrgpsqWAENE--QFDRILLDAPCsatgVIRRHP------DI--KWLRKPRDIaeLAELQSEILDAIWPLLKTGGTLVY 366

                         170
                  ....*....|....*
gi 371123235  259 STCSLSHLQNEYVVQ 273
Cdd:TIGR00563 367 ATCSVLPEENSEQIK 381
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
110-262 1.28e-17

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


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 82.93  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 110 DAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDG 189
Cdd:PRK10901 230 DAAAQLAATLLAPQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQRLERVRENLQ-------RLGLKATVIVGDA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 190 RK----WGeleGDTYDRVLVDVPCTTD----RHS---LHEEENNIFKrsrkkerqiLPVLQVQLLAA--GLLatKPGGHV 256
Cdd:PRK10901 303 RDpaqwWD---GQPFDRILLDAPCSATgvirRHPdikWLRRPEDIAA---------LAALQSEILDAlwPLL--KPGGTL 368


                 ....*.
gi 371123235 257 VYSTCS 262
Cdd:PRK10901 369 LYATCS 374
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
 110-273 5.72e-16

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 78.38  E-value: 5.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 110 DAASLLPVLaLGLQPGDIVLDLCAAPGGKTLALLQTGCCR-NLAANDLSPSRIARLQKILhsyvpeEIRDGNQVRVTSWD 188
Cdd:PRK14903 224 ESSQIVPLL-MELEPGLRVLDTCAAPGGKTTAIAELMKDQgKILAVDISREKIQLVEKHA------KRLKLSSIEIKIAD 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 189 GRKWGELEGDTYDRVLVDVPCTtdrhSLHEEENN--IFKRSRKKERQILPVLQVQLLAAGLLATKPGGHVVYSTCSLSHL 266
Cdd:PRK14903 297 AERLTEYVQDTFDRILVDAPCT----SLGTARNHpeVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYSTCTVTKE 372


                 ....*..
gi 371123235 267 QNEYVVQ 273
Cdd:PRK14903 373 ENTEVVK 379
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 89-269 1.01e-14

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 74.71  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235  89 DISRFPPA-RPGSLGVMeyylmDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGccrNLAANDLSPS---R 160
Cdd:PRK14904 219 DFSLFEPFlKLGLVSVQ-----NPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAElmqnRG---QITAVDRYPQkleK 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 161 IARLQKILHSYVPEEIRDgnqvrvtswDGRKWgeLEGDTYDRVLVDVPCT-----TDRHSLHeeenniFKRSRKKERQiL 235
Cdd:PRK14904 291 IRSHASALGITIIETIEG---------DARSF--SPEEQPDAILLDAPCTgtgvlGRRAELR------WKLTPEKLAE-L 352

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 371123235 236 PVLQVQLL--AAGLLatKPGGHVVYSTCSLSHLQNE 269
Cdd:PRK14904 353 VGLQAELLdhAASLL--KPGGVLVYATCSIEPEENE 386
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 128-259 1.75e-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: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 128 VLDLCAAPGGKTLALLQTGCCRNLaANDLSPSRIARLQKILHSYVPEEIRDGNQvrvtswDGRKWGELEGDTYDRVLVDV 207
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVT-GVDISPVALELARKAAAALLADNVEVLKG------DAEELPPEADESFDVIISDP 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 371123235 208 PCttdrHSLHEeennifkrsrkkerqilpvLQVQLLAAGLLATKPGGHVVYS 259
Cdd:cd02440   75 PL----HHLVE-------------------DLARFLEEARRLLKPGGVLVLT 103
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 119-257 1.33e-03

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: 38.44  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 119 ALGLQPGDIVLDLCAAPGGKTLALLQTGCcrNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDGRKWgELEGD 198
Cdd:COG2226   17 ALGLRPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAA-------EAGLNVEFVVGDAEDL-PFPDG 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 371123235 199 TYDRVLVdvpcttdRHSLHEeenniFKRSRKKERQILPVLqvqllaagllatKPGGHVV 257
Cdd:COG2226   87 SFDLVIS-------SFVLHH-----LPDPERALAEIARVL------------KPGGRLV 121
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 122-152 3.74e-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: 37.57  E-value: 3.74e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 371123235  122 LQPGDIVLDLCAAPGGKTLALLQTGCCRNLA 152
Cdd:pfam01728  19 LKPGKTVLDLGAAPGGWSQVALQRGAGKVVG 49
PRK14967 PRK14967
putative methyltransferase; Provisional
 113-215 4.07e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 38.11  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371123235 113 SLLPVLAL---GLQPGDIVLDLCAAPGGKTLALLQTGCCRnLAANDLSPS--RIARLQKILHSyVPEEIRDGNQVRVtsw 187
Cdd:PRK14967  22 TQLLADALaaeGLGPGRRVLDLCTGSGALAVAAAAAGAGS-VTAVDISRRavRSARLNALLAG-VDVDVRRGDWARA--- 96

                         90       100       110
                 ....*....|....*....|....*....|.
gi 371123235 188 dgrkwgeLEGDTYDRVLVD---VPCTTDRHS 215
Cdd:PRK14967  97 -------VEFRPFDVVVSNppyVPAPPDAPP 120
 
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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