NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1910601182|ref|NP_001374196|]
View 

5-methylcytosine rRNA methyltransferase NSUN4 isoform e [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 111-302 2.06e-36

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: 136.68  E-value: 2.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 111 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQtgCCRN---LAANDLSPSRIA 187
Cdd:COG0144   216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAE--LMGNkgrVVAVDISEHRLK 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 188 RLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslHEEennifKRSRKKERQI--LP 261
Cdd:COG0144   289 RLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEDIaeLA 354

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1910601182 262 VLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIE 302
Cdd:COG0144   355 ALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLA 395
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 111-302 2.06e-36

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: 136.68  E-value: 2.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 111 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQtgCCRN---LAANDLSPSRIA 187
Cdd:COG0144   216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAE--LMGNkgrVVAVDISEHRLK 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 188 RLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslHEEennifKRSRKKERQI--LP 261
Cdd:COG0144   289 RLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEDIaeLA 354

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1910601182 262 VLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIE 302
Cdd:COG0144   355 ALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLA 395
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 131-302 3.34e-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: 3.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 131 YYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSPSRIarlqKILHSYVPeeiRDG-N 205
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 206 QVRVTSWDGRKWGELeGDTYDRVLVDVPCTTDrHSLHEEENNIFKRSrKKERQILPVLQVQLLAAGLLATKPGGHVVYST 285
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 1910601182 286 CSLSHLQNEYVVQGAIE 302
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 142-301 6.55e-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: 6.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 142 VLALGLQPGDIVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQ-VRVTSWDGRKWGE 219
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGVTnTIILNGDGRQPDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 220 -LEGDTYDRVLVDVPCT----TDRHSlheeenNIfkRSRKKERQI--LPVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQ 292
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DV--KWLRQEADIaqLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEE 145


                  ....*....
gi 1910601182 293 NEYVVQGAI 301
Cdd:pfam01189 146 NEAVIEYFL 154
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
130-298 1.35e-24

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 104.10  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 130 EYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LA--LLQTGccrNLAANDLSPSRIARLQ---KILHsyvpeeIR 202
Cdd:PRK14902  231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTthIAelLKNTG---KVVALDIHEHKLKLIEenaKRLG------LT 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 203 DgnqVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslheeennifK---RSRKKERQI--LPVLQVQLL--AAGL 272
Cdd:PRK14902  302 N---IETKALDARKVHEKFAEKFDKILVDAPCSglgVIRR----------KpdiKYNKTKEDIesLQEIQLEILesVAQY 368

                         170       180
                  ....*....|....*....|....*.
gi 1910601182 273 LatKPGGHVVYSTCSLSHLQNEYVVQ 298
Cdd:PRK14902  369 L--KKGGILVYSTCTIEKEENEEVIE 392
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 153-284 3.14e-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: 48.20  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 153 VLDLCAAPGGKTLALLQTGCCRNLaANDLSPSRIARLQKILHSYVPEEIRDGNQvrvtswDGRKWGELEGDTYDRVLVDV 232
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVT-GVDISPVALELARKAAAALLADNVEVLKG------DAEELPPEADESFDVIISDP 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1910601182 233 PCttdrHSLHEeennifkrsrkkerqilpvLQVQLLAAGLLATKPGGHVVYS 284
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 ...
 111-302 2.06e-36

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: 136.68  E-value: 2.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 111 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQtgCCRN---LAANDLSPSRIA 187
Cdd:COG0144   216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAE--LMGNkgrVVAVDISEHRLK 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 188 RLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslHEEennifKRSRKKERQI--LP 261
Cdd:COG0144   289 RLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCSgtgTLRR--HPD-----IKWRRTPEDIaeLA 354

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1910601182 262 VLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIE 302
Cdd:COG0144   355 ALQRELLDAAARLLKPGGRLVYSTCSLLPEENEEVVEAFLA 395
nop2p TIGR00446
NOL1/NOP2/sun family putative RNA methylase; [Protein synthesis, tRNA and rRNA base ...
 131-302 3.34e-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: 3.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 131 YYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGCcrnLAANDLSPSRIarlqKILHSYVPeeiRDG-N 205
Cdd:TIGR00446  53 YYPQEASSMIPPIALEPREDERVLDMAAAPGGKTTQISQlmknKGC---IVANEISKSRT----KALISNIN---RMGvL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 206 QVRVTSWDGRKWGELeGDTYDRVLVDVPCTTDrHSLHEEENNIFKRSrKKERQILPVLQVQLLAAGLLATKPGGHVVYST 285
Cdd:TIGR00446 123 NTIVINADGRKFGAY-LLKFDAILLDAPCSGE-GVIRKDPSRKRNWS-EEDIKYCSLLQKELIDAAIDALKPGGVLVYST 199

                         170
                  ....*....|....*..
gi 1910601182 286 CSLSHLQNEYVVQGAIE 302
Cdd:TIGR00446 200 CSLEVEENEEVIDYILR 216
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 142-301 6.55e-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: 6.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 142 VLALGLQPGDIVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQ-VRVTSWDGRKWGE 219
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGVTnTIILNGDGRQPDQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 220 -LEGDTYDRVLVDVPCT----TDRHSlheeenNIfkRSRKKERQI--LPVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQ 292
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DV--KWLRQEADIaqLAQLQKELLSAAIDLLKPGGVLVYSTCSVLPEE 145


                  ....*....
gi 1910601182 293 NEYVVQGAI 301
Cdd:pfam01189 146 NEAVIEYFL 154
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
130-298 1.35e-24

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 104.10  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 130 EYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LA--LLQTGccrNLAANDLSPSRIARLQ---KILHsyvpeeIR 202
Cdd:PRK14902  231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTthIAelLKNTG---KVVALDIHEHKLKLIEenaKRLG------LT 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 203 DgnqVRVTSWDGRKWGELEGDTYDRVLVDVPCT---TDRHslheeennifK---RSRKKERQI--LPVLQVQLL--AAGL 272
Cdd:PRK14902  302 N---IETKALDARKVHEKFAEKFDKILVDAPCSglgVIRR----------KpdiKYNKTKEDIesLQEIQLEILesVAQY 368

                         170       180
                  ....*....|....*....|....*.
gi 1910601182 273 LatKPGGHVVYSTCSLSHLQNEYVVQ 298
Cdd:PRK14902  369 L--KKGGILVYSTCTIEKEENEEVIE 392
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 131-317 2.43e-20

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


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 91.89  E-value: 2.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 131 YYLMDAASLLPVLAL--GLQPGDIVLDLCAAPGGKTLallQTGCCRN----LAANDLSPSRIarlqKILHSYVPeeiRDG 204
Cdd:PRK11933   93 FYIQEASSMLPVAALfaDDNAPQRVLDMAAAPGSKTT---QIAALMNnqgaIVANEYSASRV----KVLHANIS---RCG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 205 -NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT------TDRHSLHEEENNifkrsrkkerQILPVLQVQ--LLAAGLLAT 275
Cdd:PRK11933  163 vSNVALTHFDGRVFGAALPETFDAILLDAPCSgegtvrKDPDALKNWSPE----------SNLEIAATQreLIESAFHAL 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1910601182 276 KPGGHVVYSTCSLSHLQNEYVVQGaielLANQYSIQVQVEDL 317
Cdd:PRK11933  233 KPGGTLVYSTCTLNREENQAVCLW----LKETYPDAVEFEPL 270
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 113-315 1.31e-18

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 86.52  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 113 GDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LALLqTGCCRNLAANDLSPSRI---- 186
Cdd:PRK14901  221 GSIRQLPGYEEG-----WWTVQDRSAQLVAPLLDPQPGEVILDACAAPGGKTthIAEL-MGDQGEIWAVDRSASRLkklq 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 187 ---ARLQkiLHSyvpeeirdgnqVRVTSWDGRKWGELEGD---TYDRVLVDVPC----TTDRHSlheeenniFKRSRKKE 256
Cdd:PRK14901  295 enaQRLG--LKS-----------IKILAADSRNLLELKPQwrgYFDRILLDAPCsglgTLHRHP--------DARWRQTP 353

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1910601182 257 RQI--LPVLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQgaiELLANQYSIQVQVE 315
Cdd:PRK14901  354 EKIqeLAPLQAELLESLAPLLKPGGTLVYATCTLHPAENEAQIE---QFLARHPDWKLEPP 411
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 135-298 1.82e-18

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: 86.07  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 135 DAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDG 214
Cdd:TIGR00563 224 DASAQWVATWLAPQNEETILDACAAPGGKTTHILELAPQAQVVALDIHEHRLKRVYENLK-------RLGLTIKAETKDG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 215 RK-----WGELEgdTYDRVLVDVPC----TTDRHSlheeenNIfkRSRKKERQI--LPVLQVQLLAAGLLATKPGGHVVY 283
Cdd:TIGR00563 297 DGrgpsqWAENE--QFDRILLDAPCsatgVIRRHP------DI--KWLRKPRDIaeLAELQSEILDAIWPLLKTGGTLVY 366

                         170
                  ....*....|....*
gi 1910601182 284 STCSLSHLQNEYVVQ 298
Cdd:TIGR00563 367 ATCSVLPEENSEQIK 381
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
135-287 4.48e-17

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


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 81.77  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 135 DAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDG 214
Cdd:PRK10901  230 DAAAQLAATLLAPQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQRLERVRENLQ-------RLGLKATVIVGDA 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 215 RK----WGeleGDTYDRVLVDVPCTTD----RHS---LHEEENNIFKrsrkkerqiLPVLQVQLLAA--GLLatKPGGHV 281
Cdd:PRK10901  303 RDpaqwWD---GQPFDRILLDAPCSATgvirRHPdikWLRRPEDIAA---------LAALQSEILDAlwPLL--KPGGTL 368


                  ....*.
gi 1910601182 282 VYSTCS 287
Cdd:PRK10901  369 LYATCS 374
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
 135-298 1.56e-15

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 77.22  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 135 DAASLLPVLaLGLQPGDIVLDLCAAPGGKTLALLQTGCCR-NLAANDLSPSRIARLQKILhsyvpeEIRDGNQVRVTSWD 213
Cdd:PRK14903  224 ESSQIVPLL-MELEPGLRVLDTCAAPGGKTTAIAELMKDQgKILAVDISREKIQLVEKHA------KRLKLSSIEIKIAD 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 214 GRKWGELEGDTYDRVLVDVPCTtdrhSLHEEENN--IFKRSRKKERQILPVLQVQLLAAGLLATKPGGHVVYSTCSLSHL 291
Cdd:PRK14903  297 AERLTEYVQDTFDRILVDAPCT----SLGTARNHpeVLRRVNKEDFKKLSEIQLRIVSQAWKLLEKGGILLYSTCTVTKE 372


                  ....*..
gi 1910601182 292 QNEYVVQ 298
Cdd:PRK14903  373 ENTEVVK 379
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 114-294 1.61e-14

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 74.33  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 114 DISRFPPA-RPGSLGVMeyylmDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGccrNLAANDLSPS---R 185
Cdd:PRK14904  219 DFSLFEPFlKLGLVSVQ-----NPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAElmqnRG---QITAVDRYPQkleK 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 186 IARLQKILHSYVPEEIRDgnqvrvtswDGRKWgeLEGDTYDRVLVDVPCT-----TDRHSLHeeenniFKRSRKKERQiL 260
Cdd:PRK14904  291 IRSHASALGITIIETIEG---------DARSF--SPEEQPDAILLDAPCTgtgvlGRRAELR------WKLTPEKLAE-L 352

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1910601182 261 PVLQVQLL--AAGLLatKPGGHVVYSTCSLSHLQNE 294
Cdd:PRK14904  353 VGLQAELLdhAASLL--KPGGVLVYATCSIEPEENE 386
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 153-284 3.14e-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: 48.20  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 153 VLDLCAAPGGKTLALLQTGCCRNLaANDLSPSRIARLQKILHSYVPEEIRDGNQvrvtswDGRKWGELEGDTYDRVLVDV 232
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVT-GVDISPVALELARKAAAALLADNVEVLKG------DAEELPPEADESFDVIISDP 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1910601182 233 PCttdrHSLHEeennifkrsrkkerqilpvLQVQLLAAGLLATKPGGHVVYS 284
Cdd:cd02440    75 PL----HHLVE-------------------DLARFLEEARRLLKPGGVLVLT 103
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 144-282 2.53e-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: 37.67  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 144 ALGLQPGDIVLDLCAAPGGKTLALLQTGCcrNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDGRKWgELEGD 223
Cdd:COG2226    17 ALGLRPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAA-------EAGLNVEFVVGDAEDL-PFPDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1910601182 224 TYDRVLVdvpcttdRHSLHEeenniFKRSRKKERQILPVLqvqllaagllatKPGGHVV 282
Cdd:COG2226    87 SFDLVIS-------SFVLHH-----LPDPERALAEIARVL------------KPGGRLV 121
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 147-177 4.88e-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: 4.88e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1910601182 147 LQPGDIVLDLCAAPGGKTLALLQTGCCRNLA 177
Cdd:pfam01728  19 LKPGKTVLDLGAAPGGWSQVALQRGAGKVVG 49
PRK14967 PRK14967
putative methyltransferase; Provisional
 138-240 9.27e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 36.95  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601182 138 SLLPVLAL---GLQPGDIVLDLCAAPGGKTLALLQTGCCRnLAANDLSPS--RIARLQKILHSyVPEEIRDGNQVRVtsw 212
Cdd:PRK14967   22 TQLLADALaaeGLGPGRRVLDLCTGSGALAVAAAAAGAGS-VTAVDISRRavRSARLNALLAG-VDVDVRRGDWARA--- 96

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1910601182 213 dgrkwgeLEGDTYDRVLVD---VPCTTDRHS 240
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH