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Conserved domains on  [gi|1910601188|ref|NP_001374199|]
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5-methylcytosine rRNA methyltransferase NSUN4 isoform h [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 ...
 135-259 2.18e-24

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: 102.39  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 135 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQtgCCRN---LAANDLSPSRIA 211
Cdd:COG0144   216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAE--LMGNkgrVVAVDISEHRLK 288

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1910601188 212 RLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT 259
Cdd:COG0144   289 RLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCS 330
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 135-259 2.18e-24

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: 102.39  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 135 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQtgCCRN---LAANDLSPSRIA 211
Cdd:COG0144   216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAE--LMGNkgrVVAVDISEHRLK 288

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1910601188 212 RLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT 259
Cdd:COG0144   289 RLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCS 330
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
154-259 1.63e-16

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 79.84  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 154 EYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LA--LLQTGccrNLAANDLSPSRIARLQ---KILHsyvpeeIR 226
Cdd:PRK14902  231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTthIAelLKNTG---KVVALDIHEHKLKLIEenaKRLG------LT 301

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1910601188 227 DgnqVRVTSWDGRKWGELEGDTYDRVLVDVPCT 259
Cdd:PRK14902  302 N---IETKALDARKVHEKFAEKFDKILVDAPCS 331
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 166-300 2.84e-16

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: 75.92  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 166 VLALGLQPGDIVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQ-VRVTSWDGRKWGE 243
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGVTnTIILNGDGRQPDQ 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1910601188 244 -LEGDTYDRVLVDVPCT----TDRHSlheeenNIfkRSRKKERQI--LPVLQVQLLAKAIYLYR 300
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DV--KWLRQEADIaqLAQLQKELLSAAIDLLK 129
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 159-310 8.58e-12

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: 65.66  E-value: 8.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 159 DAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDG 238
Cdd:TIGR00563 224 DASAQWVATWLAPQNEETILDACAAPGGKTTHILELAPQAQVVALDIHEHRLKRVYENLK-------RLGLTIKAETKDG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 239 RK-----WGELEgdTYDRVLVDVPC----TTDRHSlheeenNIfkRSRKKERQILPVLQVQL-LAKAIYlyrrvcPHRWS 308
Cdd:TIGR00563 297 DGrgpsqWAENE--QFDRILLDAPCsatgVIRRHP------DI--KWLRKPRDIAELAELQSeILDAIW------PLLKT 360


                  ..
gi 1910601188 309 NG 310
Cdd:TIGR00563 361 GG 362
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 177-278 6.07e-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: 47.42  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 177 VLDLCAAPGGKTLALLQTGCCRNLaANDLSPSRIARLQKILHSYVPEEIRDGNQvrvtswDGRKWGELEGDTYDRVLVDV 256
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVT-GVDISPVALELARKAAAALLADNVEVLKG------DAEELPPEADESFDVIISDP 74

                          90       100
                  ....*....|....*....|..
gi 1910601188 257 PCttdrHSLHEEENNIFKRSRK 278
Cdd:cd02440    75 PL----HHLVEDLARFLEEARR 92
 
Name Accession Description Interval E-value
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 135-259 2.18e-24

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: 102.39  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 135 DRGDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQtgCCRN---LAANDLSPSRIA 211
Cdd:COG0144   216 GPGPVTALPGFREG-----LFSVQDEASQLVALLLDPKPGERVLDLCAAPGGKTLHLAE--LMGNkgrVVAVDISEHRLK 288

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1910601188 212 RLQKILHsyvpeeiRDG-NQVRVTSWDGRKWGELEGDTYDRVLVDVPCT 259
Cdd:COG0144   289 RLRENLA-------RLGlSNVEVVVADARELLEWLPGKFDRVLLDAPCS 330
PRK14902 PRK14902
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
154-259 1.63e-16

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


Pssm-ID: 237857 [Multi-domain]  Cd Length: 444  Bit Score: 79.84  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 154 EYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LA--LLQTGccrNLAANDLSPSRIARLQ---KILHsyvpeeIR 226
Cdd:PRK14902  231 LITIQDESSMLVAPALDPKGGDTVLDACAAPGGKTthIAelLKNTG---KVVALDIHEHKLKLIEenaKRLG------LT 301

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1910601188 227 DgnqVRVTSWDGRKWGELEGDTYDRVLVDVPCT 259
Cdd:PRK14902  302 N---IETKALDARKVHEKFAEKFDKILVDAPCS 331
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 166-300 2.84e-16

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: 75.92  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 166 VLALGLQPGDIVLDLCAAPGGKTLALLQ-TGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQ-VRVTSWDGRKWGE 243
Cdd:pfam01189   1 AILLAPQEGETILDMCAAPGGKTTHIAElMKNQGTVVAVDINKHRLKRVAENIH-------RLGVTnTIILNGDGRQPDQ 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1910601188 244 -LEGDTYDRVLVDVPCT----TDRHSlheeenNIfkRSRKKERQI--LPVLQVQLLAKAIYLYR 300
Cdd:pfam01189  74 wLGGVLFDRILLDAPCSgtgvIRRHP------DV--KWLRQEADIaqLAQLQKELLSAAIDLLK 129
PRK10901 PRK10901
16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB;
159-259 3.12e-13

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


Pssm-ID: 236790 [Multi-domain]  Cd Length: 427  Bit Score: 69.83  E-value: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 159 DAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDG 238
Cdd:PRK10901  230 DAAAQLAATLLAPQNGERVLDACAAPGGKTAHILELAPQAQVVALDIDAQRLERVRENLQ-------RLGLKATVIVGDA 302

                          90       100
                  ....*....|....*....|....*
gi 1910601188 239 RK----WGeleGDTYDRVLVDVPCT 259
Cdd:PRK10901  303 RDpaqwWD---GQPFDRILLDAPCS 324
rsmB TIGR00563
16S rRNA (cytosine(967)-C(5))-methyltransferase; This protein is also known as sun protein. ...
 159-310 8.58e-12

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: 65.66  E-value: 8.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 159 DAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQTGCCRNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDG 238
Cdd:TIGR00563 224 DASAQWVATWLAPQNEETILDACAAPGGKTTHILELAPQAQVVALDIHEHRLKRVYENLK-------RLGLTIKAETKDG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 239 RK-----WGELEgdTYDRVLVDVPC----TTDRHSlheeenNIfkRSRKKERQILPVLQVQL-LAKAIYlyrrvcPHRWS 308
Cdd:TIGR00563 297 DGrgpsqWAENE--QFDRILLDAPCsatgVIRRHP------DI--KWLRKPRDIAELAELQSeILDAIW------PLLKT 360


                  ..
gi 1910601188 309 NG 310
Cdd:TIGR00563 361 GG 362
yebU PRK11933
rRNA (cytosine-C(5)-)-methyltransferase RsmF; Reviewed
 155-258 2.16e-11

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


Pssm-ID: 183387 [Multi-domain]  Cd Length: 470  Bit Score: 64.16  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 155 YYLMDAASLLPVLAL--GLQPGDIVLDLCAAPGGKTLallQTGCCRN----LAANDLSPSRIarlqKILHSYVPeeiRDG 228
Cdd:PRK11933   93 FYIQEASSMLPVAALfaDDNAPQRVLDMAAAPGSKTT---QIAALMNnqgaIVANEYSASRV----KVLHANIS---RCG 162

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1910601188 229 -NQVRVTSWDGRKWGELEGDTYDRVLVDVPC 258
Cdd:PRK11933  163 vSNVALTHFDGRVFGAALPETFDAILLDAPC 193
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
 159-295 7.76e-11

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 62.58  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 159 DAASLLPVLaLGLQPGDIVLDLCAAPGGKTLALLQTGCCR-NLAANDLSPSRIARLQKILhsyvpeEIRDGNQVRVTSWD 237
Cdd:PRK14903  224 ESSQIVPLL-MELEPGLRVLDTCAAPGGKTTAIAELMKDQgKILAVDISREKIQLVEKHA------KRLKLSSIEIKIAD 296

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 238 GRKWGELEGDTYDRVLVDVPCTtdrhSLHEEENN--IFKRSRKKERQILPVLQVQLLAKA 295
Cdd:PRK14903  297 AERLTEYVQDTFDRILVDAPCT----SLGTARNHpeVLRRVNKEDFKKLSEIQLRIVSQA 352
PRK14901 PRK14901
16S rRNA methyltransferase B; Provisional
 137-293 6.14e-09

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237856 [Multi-domain]  Cd Length: 434  Bit Score: 56.86  E-value: 6.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 137 GDISRFPPARPGslgvmEYYLMDAASLLPVLALGLQPGDIVLDLCAAPGGKT--LALLqTGCCRNLAANDLSPSRIARLQ 214
Cdd:PRK14901  221 GSIRQLPGYEEG-----WWTVQDRSAQLVAPLLDPQPGEVILDACAAPGGKTthIAEL-MGDQGEIWAVDRSASRLKKLQ 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 215 KILhsyvpeEIRDGNQVRVTSWDGRKWGELEGD---TYDRVLVDVPC----TTDRHSlheeenniFKRSRKKERQI--LP 285
Cdd:PRK14901  295 ENA------QRLGLKSIKILAADSRNLLELKPQwrgYFDRILLDAPCsglgTLHRHP--------DARWRQTPEKIqeLA 360


                  ....*...
gi 1910601188 286 VLQVQLLA 293
Cdd:PRK14901  361 PLQAELLE 368
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 177-278 6.07e-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: 47.42  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 177 VLDLCAAPGGKTLALLQTGCCRNLaANDLSPSRIARLQKILHSYVPEEIRDGNQvrvtswDGRKWGELEGDTYDRVLVDV 256
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVT-GVDISPVALELARKAAAALLADNVEVLKG------DAEELPPEADESFDVIISDP 74

                          90       100
                  ....*....|....*....|..
gi 1910601188 257 PCttdrHSLHEEENNIFKRSRK 278
Cdd:cd02440    75 PL----HHLVEDLARFLEEARR 92
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
 138-295 1.06e-06

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 50.06  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 138 DISRFPPA-RPGSLGVMeyylmDAASLLPVLALGLQPGDIVLDLCAAPGGKTLALLQ----TGccrNLAANDLSPS---R 209
Cdd:PRK14904  219 DFSLFEPFlKLGLVSVQ-----NPTQALACLLLNPQPGSTVLDLCAAPGGKSTFMAElmqnRG---QITAVDRYPQkleK 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 210 IARLQKILHSYVPEEIRDgnqvrvtswDGRKWgeLEGDTYDRVLVDVPCT-----TDRHSLHeeenniFKRSRKKERQiL 284
Cdd:PRK14904  291 IRSHASALGITIIETIEG---------DARSF--SPEEQPDAILLDAPCTgtgvlGRRAELR------WKLTPEKLAE-L 352

                         170
                  ....*....|.
gi 1910601188 285 PVLQVQLLAKA 295
Cdd:PRK14904  353 VGLQAELLDHA 363
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 171-201 3.50e-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: 3.50e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1910601188 171 LQPGDIVLDLCAAPGGKTLALLQTGCCRNLA 201
Cdd:pfam01728  19 LKPGKTVLDLGAAPGGWSQVALQRGAGKVVG 49
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 168-266 5.01e-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: 36.90  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910601188 168 ALGLQPGDIVLDLCAAPGGKTLALLQTGCcrNLAANDLSPSRIARLQKILHsyvpeeiRDGNQVRVTSWDGRKWgELEGD 247
Cdd:COG2226    17 ALGLRPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAA-------EAGLNVEFVVGDAEDL-PFPDG 86

                          90
                  ....*....|....*....
gi 1910601188 248 TYDRVLVdvpcttdRHSLH 266
Cdd:COG2226    87 SFDLVIS-------SFVLH 98
 
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.
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