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Conserved domains on  [gi|240255977|ref|NP_193494|]
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NOL1/NOP2/sun family protein [Arabidopsis thaliana]

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; ...
 38-141 1.03e-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 pfam01189:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 199  Bit Score: 58.59  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255977   38 PIGETpEHLSGrFMVIKGIIFANASTEHLLGSLYANLHRMGITNTVVSNYNInTKLSRVFHINSKDMVLVNAPSTRTGLI 117
Cdd:pfam01189  19 PGGKT-THIAE-LMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDG-RQPDQWLGGVLFDRILLDAPCSGTGVI 95

                          90       100
                  ....*....|....*....|....
gi 240255977  118 SEFGSIKMSiNEEADIQRFGVLQK 141
Cdd:pfam01189  96 RRHPDVKWL-RQEADIAQLAQLQK 118
 
Name Accession Description Interval E-value
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 38-141 1.03e-10

16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.


Pssm-ID: 426109 [Multi-domain]  Cd Length: 199  Bit Score: 58.59  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255977   38 PIGETpEHLSGrFMVIKGIIFANASTEHLLGSLYANLHRMGITNTVVSNYNInTKLSRVFHINSKDMVLVNAPSTRTGLI 117
Cdd:pfam01189  19 PGGKT-THIAE-LMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDG-RQPDQWLGGVLFDRILLDAPCSGTGVI 95

                          90       100
                  ....*....|....*....|....
gi 240255977  118 SEFGSIKMSiNEEADIQRFGVLQK 141
Cdd:pfam01189  96 RRHPDVKWL-RQEADIAQLAQLQK 118
 
Name Accession Description Interval E-value
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
 38-141 1.03e-10

16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.


Pssm-ID: 426109 [Multi-domain]  Cd Length: 199  Bit Score: 58.59  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240255977   38 PIGETpEHLSGrFMVIKGIIFANASTEHLLGSLYANLHRMGITNTVVSNYNInTKLSRVFHINSKDMVLVNAPSTRTGLI 117
Cdd:pfam01189  19 PGGKT-THIAE-LMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDG-RQPDQWLGGVLFDRILLDAPCSGTGVI 95

                          90       100
                  ....*....|....*....|....
gi 240255977  118 SEFGSIKMSiNEEADIQRFGVLQK 141
Cdd:pfam01189  96 RRHPDVKWL-RQEADIAQLAQLQK 118
 
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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