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Conserved domains on  [gi|153791865|ref|NP_060818|]
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cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 [Homo sapiens]

Protein Classification

FtsJ-like methyltransferase family protein( domain architecture ID 10484224)

FtsJ-like methyltransferase family protein 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
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 6.87e-28

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: 110.76  E-value: 6.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791865  114 AWCKFHEILCSFPLipqeaFQNGKlNSLHLCEAPGAFIASLNHYLKSHrfpchwsWVANTLNPYHEANddlmMIMDDRLI 193
Cdd:pfam01728   5 AAYKLLEIDEKFGL-----LKPGK-TVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQLWK----PRNDPGVT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791865  194 ANTlhwwyfgpdntGDIMTLKFLTGLQNFISSMatVHLVTADGSFDCQGNPGEQEALVSSLHYCEVVTALTTLGNGGSFV 273
Cdd:pfam01728  68 FIQ-----------GDIRDPETLDLLEELLGRK--VDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 153791865  274 LKMFtMFEHCSiNLMYLLNCCFDQVHVFKPATSKAGNSEVYVVCLHY 320
Cdd:pfam01728 135 CKVF-QGEDFS-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 6.87e-28

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: 110.76  E-value: 6.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791865  114 AWCKFHEILCSFPLipqeaFQNGKlNSLHLCEAPGAFIASLNHYLKSHrfpchwsWVANTLNPYHEANddlmMIMDDRLI 193
Cdd:pfam01728   5 AAYKLLEIDEKFGL-----LKPGK-TVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQLWK----PRNDPGVT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791865  194 ANTlhwwyfgpdntGDIMTLKFLTGLQNFISSMatVHLVTADGSFDCQGNPGEQEALVSSLHYCEVVTALTTLGNGGSFV 273
Cdd:pfam01728  68 FIQ-----------GDIRDPETLDLLEELLGRK--VDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 153791865  274 LKMFtMFEHCSiNLMYLLNCCFDQVHVFKPATSKAGNSEVYVVCLHY 320
Cdd:pfam01728 135 CKVF-QGEDFS-ELLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 253-322 8.20e-09

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: 56.23  E-value: 8.20e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791865 253 SLHYCEVV--TALTTLGNGGSFVLKMF--TMFEhcsiNLMYLLNCCFDQVHVFKPATSKAGNSEVYVVCLHYKG 322
Cdd:COG0293  139 SMYLVELAldFARKVLKPGGAFVVKVFqgEGFD----ELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
capping_2-OMTase_Nidovirales cd20762
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of nidovirales; Cap-0 specific ...
 182-322 1.90e-03

Cap-0 specific (nucleoside-2'-O-)-methyltransferase of nidovirales; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Nidovirales viruses, which comprise a family of ss(+)RNA viruses, cap their mRNAs. For one member, coronavirus, the 2'OMTase activity is located in the non-structural protein 16 (Nsp16). For others, the 2'OMTase activity may be located in replicase polyprotein 1ab.


Pssm-ID: 467737  Cd Length: 175  Bit Score: 39.99  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791865 182 DDLMMIMDDRL-IANTLHWWYFG---PDNTGDIMTLKFLTG---LQNFISSMATVHLVTADGsfDCQGNPGEQEALV--- 251
Cdd:cd20762    6 VQLCSYINDHLkVPPKPRVLHLGaagIYSPGDEVDYIPVTGgivLNHDFNDCVDHADIRPIN--DCNGRFGGKYDLIisd 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791865 252 ----SSLHYCEVVTALT-TLGNGGSFVLKMfTmfEHC-SINLMYLLNCcFDQVHVFKPAtSKAGNSEVYVVCLHYKG 322
Cdd:cd20762   84 iynpGTDNTELLLDYINnHLALGGSIIWKT-T--RRSnLTNLNQIAKY-FGSWTFFTTR-VNASSSEVFLVFKYYLL 155
 
Name Accession Description Interval E-value
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 114-320 6.87e-28

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: 110.76  E-value: 6.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791865  114 AWCKFHEILCSFPLipqeaFQNGKlNSLHLCEAPGAFIASLNHYLKSHrfpchwsWVANTLNPYHEANddlmMIMDDRLI 193
Cdd:pfam01728   5 AAYKLLEIDEKFGL-----LKPGK-TVLDLGAAPGGWSQVALQRGAGK-------VVGVDLGPMQLWK----PRNDPGVT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791865  194 ANTlhwwyfgpdntGDIMTLKFLTGLQNFISSMatVHLVTADGSFDCQGNPGEQEALVSSLHYCEVVTALTTLGNGGSFV 273
Cdd:pfam01728  68 FIQ-----------GDIRDPETLDLLEELLGRK--VDLVLSDGSPFISGNKVLDHLRSLDLVKAALEVALELLRKGGNFV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 153791865  274 LKMFtMFEHCSiNLMYLLNCCFDQVHVFKPATSKAGNSEVYVVCLHY 320
Cdd:pfam01728 135 CKVF-QGEDFS-ELLYLLKLGFEKVGVFKPPASRPESSEEYLVCLGF 179
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 253-322 8.20e-09

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: 56.23  E-value: 8.20e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791865 253 SLHYCEVV--TALTTLGNGGSFVLKMF--TMFEhcsiNLMYLLNCCFDQVHVFKPATSKAGNSEVYVVCLHYKG 322
Cdd:COG0293  139 SMYLVELAldFARKVLKPGGAFVVKVFqgEGFD----ELLKELKKLFKKVKHRKPKASRARSSEVYLVAKGFKG 208
capping_2-OMTase_Nidovirales cd20762
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of nidovirales; Cap-0 specific ...
 182-322 1.90e-03

Cap-0 specific (nucleoside-2'-O-)-methyltransferase of nidovirales; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Nidovirales viruses, which comprise a family of ss(+)RNA viruses, cap their mRNAs. For one member, coronavirus, the 2'OMTase activity is located in the non-structural protein 16 (Nsp16). For others, the 2'OMTase activity may be located in replicase polyprotein 1ab.


Pssm-ID: 467737  Cd Length: 175  Bit Score: 39.99  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791865 182 DDLMMIMDDRL-IANTLHWWYFG---PDNTGDIMTLKFLTG---LQNFISSMATVHLVTADGsfDCQGNPGEQEALV--- 251
Cdd:cd20762    6 VQLCSYINDHLkVPPKPRVLHLGaagIYSPGDEVDYIPVTGgivLNHDFNDCVDHADIRPIN--DCNGRFGGKYDLIisd 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791865 252 ----SSLHYCEVVTALT-TLGNGGSFVLKMfTmfEHC-SINLMYLLNCcFDQVHVFKPAtSKAGNSEVYVVCLHYKG 322
Cdd:cd20762   84 iynpGTDNTELLLDYINnHLALGGSIIWKT-T--RRSnLTNLNQIAKY-FGSWTFFTTR-VNASSSEVFLVFKYYLL 155
 
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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