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Conserved domains on  [gi|47087401|ref|NP_998598|]
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cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 [Danio rerio]

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 ...
 118-324 1.95e-26

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: 106.52  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087401   118 AWAKFYEILGTFQLLPDsalktgELNSIHLCEAPGAFISALNHflktsslHCDWNWIANTLNPYYEANGRGctitDDRLI 197
Cdd:pfam01728   5 AAYKLLEIDEKFGLLKP------GKTVLDLGAAPGGWSQVALQ-------RGAGKVVGVDLGPMQLWKPRN----DPGVT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087401   198 VHTlpwwffgsdntGDIMLQKHLLELPRFVSnmRSVDLVTADGSFDCQGDPGEQERLVAPLQHCEAICALLLLGTGGSFV 277
Cdd:pfam01728  68 FIQ-----------GDIRDPETLDLLEELLG--RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 47087401   278 LKMFTLFEHSSvcLLYLLACCFRSVNIFKPGTSKSGNSELYIVCLDY 324
Cdd:pfam01728 135 CKVFQGEDFSE--LLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
 
Name Accession Description Interval E-value
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 118-324 1.95e-26

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: 106.52  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087401   118 AWAKFYEILGTFQLLPDsalktgELNSIHLCEAPGAFISALNHflktsslHCDWNWIANTLNPYYEANGRGctitDDRLI 197
Cdd:pfam01728   5 AAYKLLEIDEKFGLLKP------GKTVLDLGAAPGGWSQVALQ-------RGAGKVVGVDLGPMQLWKPRN----DPGVT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087401   198 VHTlpwwffgsdntGDIMLQKHLLELPRFVSnmRSVDLVTADGSFDCQGDPGEQERLVAPLQHCEAICALLLLGTGGSFV 277
Cdd:pfam01728  68 FIQ-----------GDIRDPETLDLLEELLG--RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 47087401   278 LKMFTLFEHSSvcLLYLLACCFRSVNIFKPGTSKSGNSELYIVCLDY 324
Cdd:pfam01728 135 CKVFQGEDFSE--LLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 261-324 8.18e-05

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: 44.29  E-value: 8.18e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47087401 261 CEAI--CALLLLGTGGSFVLKMF--TLFEHssvcLLYLLACCFRSVNIFKPGTSKSGNSELYIVCLDY 324
Cdd:COG0293 143 VELAldFARKVLKPGGAFVVKVFqgEGFDE----LLKELKKLFKKVKHRKPKASRARSSEVYLVAKGF 206
 
Name Accession Description Interval E-value
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 118-324 1.95e-26

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: 106.52  E-value: 1.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087401   118 AWAKFYEILGTFQLLPDsalktgELNSIHLCEAPGAFISALNHflktsslHCDWNWIANTLNPYYEANGRGctitDDRLI 197
Cdd:pfam01728   5 AAYKLLEIDEKFGLLKP------GKTVLDLGAAPGGWSQVALQ-------RGAGKVVGVDLGPMQLWKPRN----DPGVT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47087401   198 VHTlpwwffgsdntGDIMLQKHLLELPRFVSnmRSVDLVTADGSFDCQGDPGEQERLVAPLQHCEAICALLLLGTGGSFV 277
Cdd:pfam01728  68 FIQ-----------GDIRDPETLDLLEELLG--RKVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 47087401   278 LKMFTLFEHSSvcLLYLLACCFRSVNIFKPGTSKSGNSELYIVCLDY 324
Cdd:pfam01728 135 CKVFQGEDFSE--LLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 261-324 8.18e-05

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: 44.29  E-value: 8.18e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47087401 261 CEAI--CALLLLGTGGSFVLKMF--TLFEHssvcLLYLLACCFRSVNIFKPGTSKSGNSELYIVCLDY 324
Cdd:COG0293 143 VELAldFARKVLKPGGAFVVKVFqgEGFDE----LLKELKKLFKKVKHRKPKASRARSSEVYLVAKGF 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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