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Conserved domains on  [gi|21356125|ref|NP_649971|]
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mitochondrial transcription factor B2 [Drosophila melanogaster]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
69-245 9.06e-10

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.).


The actual alignment was detected with superfamily member pfam00398:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 263  Bit Score: 59.30  E-value: 9.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356125    69 DTVMELNSGAGYFTRHLLDResqFRRIILLESMDHFMPKIQELHTLYPeRVKVRQGDFVNlWklvymdkmdggsrvadll 148
Cdd:pfam00398  32 DTVLEIGPGKGALTVILAKR---AKQVVAIEIDPRLAKLLQKKLSLDE-NLTVIHQDFLK-F------------------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356125   149 sDVPQKAFTDDINMLVFGAV---GSYPFFKHLINSLIFqtslfnlGRCEMILAMPPPIYIHLTcnNEIGYLIYRSTSVLF 225
Cdd:pfam00398  89 -EFPSLVTHIHQEFLVVGNLpynISTPIVKQLLFESRF-------GIVDMLLMLQKEFARRLL--ARPGSKLYSRLSVLR 158
                         170       180
                  ....*....|....*....|
gi 21356125   226 QILFEHKFIAKVPREDFLPQ 245
Cdd:pfam00398 159 QAFTDVKLVAKVPPSIFSPP 178
 
Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
69-245 9.06e-10

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 59.30  E-value: 9.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356125    69 DTVMELNSGAGYFTRHLLDResqFRRIILLESMDHFMPKIQELHTLYPeRVKVRQGDFVNlWklvymdkmdggsrvadll 148
Cdd:pfam00398  32 DTVLEIGPGKGALTVILAKR---AKQVVAIEIDPRLAKLLQKKLSLDE-NLTVIHQDFLK-F------------------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356125   149 sDVPQKAFTDDINMLVFGAV---GSYPFFKHLINSLIFqtslfnlGRCEMILAMPPPIYIHLTcnNEIGYLIYRSTSVLF 225
Cdd:pfam00398  89 -EFPSLVTHIHQEFLVVGNLpynISTPIVKQLLFESRF-------GIVDMLLMLQKEFARRLL--ARPGSKLYSRLSVLR 158
                         170       180
                  ....*....|....*....|
gi 21356125   226 QILFEHKFIAKVPREDFLPQ 245
Cdd:pfam00398 159 QAFTDVKLVAKVPPSIFSPP 178
 
Name Accession Description Interval E-value
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
69-245 9.06e-10

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 59.30  E-value: 9.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356125    69 DTVMELNSGAGYFTRHLLDResqFRRIILLESMDHFMPKIQELHTLYPeRVKVRQGDFVNlWklvymdkmdggsrvadll 148
Cdd:pfam00398  32 DTVLEIGPGKGALTVILAKR---AKQVVAIEIDPRLAKLLQKKLSLDE-NLTVIHQDFLK-F------------------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356125   149 sDVPQKAFTDDINMLVFGAV---GSYPFFKHLINSLIFqtslfnlGRCEMILAMPPPIYIHLTcnNEIGYLIYRSTSVLF 225
Cdd:pfam00398  89 -EFPSLVTHIHQEFLVVGNLpynISTPIVKQLLFESRF-------GIVDMLLMLQKEFARRLL--ARPGSKLYSRLSVLR 158
                         170       180
                  ....*....|....*....|
gi 21356125   226 QILFEHKFIAKVPREDFLPQ 245
Cdd:pfam00398 159 QAFTDVKLVAKVPPSIFSPP 178
 
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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