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Conserved domains on  [gi|81875546|sp|Q8BWQ4|]
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RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2; AltName: Full=Cap methyltransferase 2; AltName: Full=Cap2 2'O-ribose methyltransferase 2; Short=MTr2; AltName: Full=FtsJ methyltransferase domain-containing protein 1

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 ...
 114-320 1.64e-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: 106.90  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81875546   114 AWCKFQEILCSFPLIPQEafqsgrLNSLHLCEAPGAFIASLNHYLKSHrfpcewsWVANSLNPYHEAndnlRMITDDRLm 193
Cdd:pfam01728   5 AAYKLLEIDEKFGLLKPG------KTVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQLW----KPRNDPGV- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81875546   194 anTLHcwyfgpdnTGDIMTLKYLTGLQDFLSGmsPIHLVTADGSFDCQGNPGEQEALVSSLHYCEAVTALITLGDGGSFV 273
Cdd:pfam01728  67 --TFI--------QGDIRDPETLDLLEELLGR--KVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 81875546   274 LKMFTlFEHCSvNLMYLLNCSFDQVHVFKPATSKAGNSEVYVVCLRY 320
Cdd:pfam01728 135 CKVFQ-GEDFS-ELLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
 
Name Accession Description Interval E-value
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 114-320 1.64e-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: 106.90  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81875546   114 AWCKFQEILCSFPLIPQEafqsgrLNSLHLCEAPGAFIASLNHYLKSHrfpcewsWVANSLNPYHEAndnlRMITDDRLm 193
Cdd:pfam01728   5 AAYKLLEIDEKFGLLKPG------KTVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQLW----KPRNDPGV- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81875546   194 anTLHcwyfgpdnTGDIMTLKYLTGLQDFLSGmsPIHLVTADGSFDCQGNPGEQEALVSSLHYCEAVTALITLGDGGSFV 273
Cdd:pfam01728  67 --TFI--------QGDIRDPETLDLLEELLGR--KVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 81875546   274 LKMFTlFEHCSvNLMYLLNCSFDQVHVFKPATSKAGNSEVYVVCLRY 320
Cdd:pfam01728 135 CKVFQ-GEDFS-ELLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 253-322 6.02e-08

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: 53.92  E-value: 6.02e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81875546 253 SLHYCEAV--TALITLGDGGSFVLKMF--TLFEhcsvNLMYLLNCSFDQVHVFKPATSKAGNSEVYVVCLRYKG 322
Cdd:COG0293 139 SMYLVELAldFARKVLKPGGAFVVKVFqgEGFD----ELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
 
Name Accession Description Interval E-value
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 114-320 1.64e-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: 106.90  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81875546   114 AWCKFQEILCSFPLIPQEafqsgrLNSLHLCEAPGAFIASLNHYLKSHrfpcewsWVANSLNPYHEAndnlRMITDDRLm 193
Cdd:pfam01728   5 AAYKLLEIDEKFGLLKPG------KTVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQLW----KPRNDPGV- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81875546   194 anTLHcwyfgpdnTGDIMTLKYLTGLQDFLSGmsPIHLVTADGSFDCQGNPGEQEALVSSLHYCEAVTALITLGDGGSFV 273
Cdd:pfam01728  67 --TFI--------QGDIRDPETLDLLEELLGR--KVDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 81875546   274 LKMFTlFEHCSvNLMYLLNCSFDQVHVFKPATSKAGNSEVYVVCLRY 320
Cdd:pfam01728 135 CKVFQ-GEDFS-ELLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 253-322 6.02e-08

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: 53.92  E-value: 6.02e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81875546 253 SLHYCEAV--TALITLGDGGSFVLKMF--TLFEhcsvNLMYLLNCSFDQVHVFKPATSKAGNSEVYVVCLRYKG 322
Cdd:COG0293 139 SMYLVELAldFARKVLKPGGAFVVKVFqgEGFD----ELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
 
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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