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Conserved domains on  [gi|60678272|ref|NP_001012765|]
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nucleolar protein 12 [Rattus norvegicus]

Protein Classification

nucleolar protein 12( domain architecture ID 10561190)

nucleolar protein 12 (NOL12) is a nucleolar protein required for pre-large subunit rRNA processing

Gene Ontology:  GO:0003723|GO:0003697
PubMed:  16430885|11452019

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nop25 pfam09805
Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear ...
 20-67 4.23e-14

Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear pore complex-associated pre-60S ribosomal subunit. The family functions as a highly conserved exonuclease that is required for the 5'-end maturation of 5.8S and 25S rRNAs, demonstrating that 5'-end processing also has a redundant pathway. Nop25 binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery; and there is evidence for both physical and functional links between late 60S subunit processing and export.


:

Pssm-ID: 430839 [Multi-domain]  Cd Length: 134  Bit Score: 66.52  E-value: 4.23e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 60678272    20 LNFDEEKRREYLTGFHKRKVERKKAAIEEIKQRLKQEQ----KKLREERHQE 67
Cdd:pfam09805  12 VVFDDDARKEYLTGFHKRKLQRRKKAQEQAEKKAREERieerKELREERKKE 63
 
Name Accession Description Interval E-value
Nop25 pfam09805
Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear ...
 20-67 4.23e-14

Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear pore complex-associated pre-60S ribosomal subunit. The family functions as a highly conserved exonuclease that is required for the 5'-end maturation of 5.8S and 25S rRNAs, demonstrating that 5'-end processing also has a redundant pathway. Nop25 binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery; and there is evidence for both physical and functional links between late 60S subunit processing and export.


Pssm-ID: 430839 [Multi-domain]  Cd Length: 134  Bit Score: 66.52  E-value: 4.23e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 60678272    20 LNFDEEKRREYLTGFHKRKVERKKAAIEEIKQRLKQEQ----KKLREERHQE 67
Cdd:pfam09805  12 VVFDDDARKEYLTGFHKRKLQRRKKAQEQAEKKAREERieerKELREERKKE 63
 
Name Accession Description Interval E-value
Nop25 pfam09805
Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear ...
 20-67 4.23e-14

Nucleolar protein 12 (25kDa); Members of this family of proteins are part of the yeast nuclear pore complex-associated pre-60S ribosomal subunit. The family functions as a highly conserved exonuclease that is required for the 5'-end maturation of 5.8S and 25S rRNAs, demonstrating that 5'-end processing also has a redundant pathway. Nop25 binds late pre-60S ribosomes, accompanying them from the nucleolus to the nuclear periphery; and there is evidence for both physical and functional links between late 60S subunit processing and export.


Pssm-ID: 430839 [Multi-domain]  Cd Length: 134  Bit Score: 66.52  E-value: 4.23e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 60678272    20 LNFDEEKRREYLTGFHKRKVERKKAAIEEIKQRLKQEQ----KKLREERHQE 67
Cdd:pfam09805  12 VVFDDDARKEYLTGFHKRKLQRRKKAQEQAEKKAREERieerKELREERKKE 63
 
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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