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Conserved domains on  [gi|19075995|ref|NP_588495|]
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rRNA (uridine-N3-)-methyltransferase Bmt5 [Schizosaccharomyces pombe]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10563595)

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

CATH:  2.20.25.110
EC:  2.1.-.-|2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BMT5-like pfam10354
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
 61-226 4.51e-79

rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.


:

Pssm-ID: 463056  Cd Length: 162  Bit Score: 236.28  E-value: 4.51e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075995    61 LLLGEGNFSFAFSLLLHHVSsegfVLATSYDSKEDLKQKYPDAAEYISKIEINGGKVMHEIDATKLHLHKKLKTQKFDTI 140
Cdd:pfam10354   1 LLVGEGDFSFSLSLAENHGP----LTATSLDSEEELLEKYPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075995   141 FWNFPHSGKGIKDQDRNILDNQKMLLAFFKASKFLLSEKGVIVITLAETKPYTLWNLKGLAKDAGYTSLMTEKFDSSFYP 220
Cdd:pfam10354  77 IFNFPHVGGKSKDQDRNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEPYDSWNIEDLAKEAGLVLIRSFKFDASDYP 156


                  ....*.
gi 19075995   221 EYSHRR 226
Cdd:pfam10354 157 GYHHKR 162
 
Name Accession Description Interval E-value
BMT5-like pfam10354
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
 61-226 4.51e-79

rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.


Pssm-ID: 463056  Cd Length: 162  Bit Score: 236.28  E-value: 4.51e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075995    61 LLLGEGNFSFAFSLLLHHVSsegfVLATSYDSKEDLKQKYPDAAEYISKIEINGGKVMHEIDATKLHLHKKLKTQKFDTI 140
Cdd:pfam10354   1 LLVGEGDFSFSLSLAENHGP----LTATSLDSEEELLEKYPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075995   141 FWNFPHSGKGIKDQDRNILDNQKMLLAFFKASKFLLSEKGVIVITLAETKPYTLWNLKGLAKDAGYTSLMTEKFDSSFYP 220
Cdd:pfam10354  77 IFNFPHVGGKSKDQDRNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEPYDSWNIEDLAKEAGLVLIRSFKFDASDYP 156


                  ....*.
gi 19075995   221 EYSHRR 226
Cdd:pfam10354 157 GYHHKR 162
 
Name Accession Description Interval E-value
BMT5-like pfam10354
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
 61-226 4.51e-79

rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.


Pssm-ID: 463056  Cd Length: 162  Bit Score: 236.28  E-value: 4.51e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075995    61 LLLGEGNFSFAFSLLLHHVSsegfVLATSYDSKEDLKQKYPDAAEYISKIEINGGKVMHEIDATKLHLHKKLKTQKFDTI 140
Cdd:pfam10354   1 LLVGEGDFSFSLSLAENHGP----LTATSLDSEEELLEKYPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075995   141 FWNFPHSGKGIKDQDRNILDNQKMLLAFFKASKFLLSEKGVIVITLAETKPYTLWNLKGLAKDAGYTSLMTEKFDSSFYP 220
Cdd:pfam10354  77 IFNFPHVGGKSKDQDRNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEPYDSWNIEDLAKEAGLVLIRSFKFDASDYP 156


                  ....*.
gi 19075995   221 EYSHRR 226
Cdd:pfam10354 157 GYHHKR 162
 
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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