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Conserved domains on  [gi|1755166695|ref|YP_009702302|]
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pEP424R [African swine fever virus]

Protein Classification

RlmE/FtsJ family methyltransferase( domain architecture ID 10484224)

RlmE/FtsJ family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to human cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 106-314 1.16e-22

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: 94.19  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755166695 106 VTNAWLKMYELLNTMN-FNNTSQAFCNCELPGGFISAINHFNYTMmhyptfnWVASSLYPSSetdaledhyglyqcnpdn 184
Cdd:pfam01728   2 RSRAAYKLLEIDEKFGlLKPGKTVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQ------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755166695 185 wlMQSPLLKKNVDYNDGDVTIASNVKNLALRATQrltPIHLYTADGGINVGHDYNKQEELNLKLHFGQALTGLLSLSKGG 264
Cdd:pfam01728  57 --LWKPRNDPGVTFIQGDIRDPETLDLLEELLGR---KVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGG 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755166695 265 NMILKHYTlNHAFTlSLICVFSHFFEELYITKPTSSRPTNSETYIVGKNR 314
Cdd:pfam01728 132 NFVCKVFQ-GEDFS-ELLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
 
Name Accession Description Interval E-value
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 106-314 1.16e-22

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: 94.19  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755166695 106 VTNAWLKMYELLNTMN-FNNTSQAFCNCELPGGFISAINHFNYTMmhyptfnWVASSLYPSSetdaledhyglyqcnpdn 184
Cdd:pfam01728   2 RSRAAYKLLEIDEKFGlLKPGKTVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQ------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755166695 185 wlMQSPLLKKNVDYNDGDVTIASNVKNLALRATQrltPIHLYTADGGINVGHDYNKQEELNLKLHFGQALTGLLSLSKGG 264
Cdd:pfam01728  57 --LWKPRNDPGVTFIQGDIRDPETLDLLEELLGR---KVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGG 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755166695 265 NMILKHYTlNHAFTlSLICVFSHFFEELYITKPTSSRPTNSETYIVGKNR 314
Cdd:pfam01728 132 NFVCKVFQ-GEDFS-ELLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 260-314 3.18e-03

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


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 38.51  E-value: 3.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1755166695 260 LSKGGNMILKhyTLNHAFTLSLICVFSHFFEELYITKPTSSRPTNSETYIVGKNR 314
Cdd:COG0293   154 LKPGGAFVVK--VFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGF 206
 
Name Accession Description Interval E-value
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 106-314 1.16e-22

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: 94.19  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755166695 106 VTNAWLKMYELLNTMN-FNNTSQAFCNCELPGGFISAINHFNYTMmhyptfnWVASSLYPSSetdaledhyglyqcnpdn 184
Cdd:pfam01728   2 RSRAAYKLLEIDEKFGlLKPGKTVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQ------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755166695 185 wlMQSPLLKKNVDYNDGDVTIASNVKNLALRATQrltPIHLYTADGGINVGHDYNKQEELNLKLHFGQALTGLLSLSKGG 264
Cdd:pfam01728  57 --LWKPRNDPGVTFIQGDIRDPETLDLLEELLGR---KVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGG 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755166695 265 NMILKHYTlNHAFTlSLICVFSHFFEELYITKPTSSRPTNSETYIVGKNR 314
Cdd:pfam01728 132 NFVCKVFQ-GEDFS-ELLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 260-314 3.18e-03

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


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 38.51  E-value: 3.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1755166695 260 LSKGGNMILKhyTLNHAFTLSLICVFSHFFEELYITKPTSSRPTNSETYIVGKNR 314
Cdd:COG0293   154 LKPGGAFVVK--VFQGEGFDELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGF 206
 
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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