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Conserved domains on  [gi|1063711733|ref|NP_001327555|]
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Tetratricopeptide repeat (TPR)-like superfamily protein [Arabidopsis thaliana]

Protein Classification

pentatricopeptide repeat-containing protein( domain architecture ID 1006637)

pentatricopeptide repeat (PPR)-containing protein may form anti-parallel alpha helices and bind single-stranded RNA in a sequence-specific and modular manner; similar to Schizosaccharomyces pombe mitochondrial pentatricopeptide repeat-containing protein 8, a mitochondrial RNA-binding protein involved in mitochondrial translation

Gene Ontology:  GO:0003723
PubMed:  23635770

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PPR_3 super family cl37870
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
264-319 3.50e-03

Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat that were not captured by the model for pfam01535. In the case of the Arabidopsis protein UniProtKB:Q66GI4, the repeated helices in this N-terminal region, of protein-only RNase P (PRORP) enzymes, form the pentatricopeptide repeat (PPR) domain which enhances pre-tRNA binding affinity. PROPRP enzymes process precursor tRNAs in human mitochondria and in all tRNA-using compartments of Arabidopsis thaliana.


The actual alignment was detected with superfamily member pfam13812:

Pssm-ID: 316342 [Multi-domain]  Cd Length: 63  Bit Score: 36.18  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063711733 264 IFNKMKELKFPTSVFACNQLLLLYSMH-DRKKISDVLLLMERENIKPSRATYHFLIN 319
Cdd:pfam13812   2 ILREMVRDGIQLNVNTYTHLLHAYANVgNLKLALEIFERMKKKGIKPTLDTYNAILG 58
 
Name Accession Description Interval E-value
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
264-319 3.50e-03

Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat that were not captured by the model for pfam01535. In the case of the Arabidopsis protein UniProtKB:Q66GI4, the repeated helices in this N-terminal region, of protein-only RNase P (PRORP) enzymes, form the pentatricopeptide repeat (PPR) domain which enhances pre-tRNA binding affinity. PROPRP enzymes process precursor tRNAs in human mitochondria and in all tRNA-using compartments of Arabidopsis thaliana.


Pssm-ID: 316342 [Multi-domain]  Cd Length: 63  Bit Score: 36.18  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063711733 264 IFNKMKELKFPTSVFACNQLLLLYSMH-DRKKISDVLLLMERENIKPSRATYHFLIN 319
Cdd:pfam13812   2 ILREMVRDGIQLNVNTYTHLLHAYANVgNLKLALEIFERMKKKGIKPTLDTYNAILG 58
 
Name Accession Description Interval E-value
PPR_3 pfam13812
Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat ...
264-319 3.50e-03

Pentatricopeptide repeat domain; This family matches additional variants of the PPR repeat that were not captured by the model for pfam01535. In the case of the Arabidopsis protein UniProtKB:Q66GI4, the repeated helices in this N-terminal region, of protein-only RNase P (PRORP) enzymes, form the pentatricopeptide repeat (PPR) domain which enhances pre-tRNA binding affinity. PROPRP enzymes process precursor tRNAs in human mitochondria and in all tRNA-using compartments of Arabidopsis thaliana.


Pssm-ID: 316342 [Multi-domain]  Cd Length: 63  Bit Score: 36.18  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063711733 264 IFNKMKELKFPTSVFACNQLLLLYSMH-DRKKISDVLLLMERENIKPSRATYHFLIN 319
Cdd:pfam13812   2 ILREMVRDGIQLNVNTYTHLLHAYANVgNLKLALEIFERMKKKGIKPTLDTYNAILG 58
 
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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