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Conserved domains on  [gi|17505595|ref|NP_493083|]
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Ribonuclease P protein subunit p29 [Caenorhabditis elegans]

Protein Classification

ribonuclease P protein component 1( domain architecture ID 10650210)

ribonuclease P protein component 1 (Rpp29) is part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
POP4 smart00538
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ...
 88-178 3.63e-34

A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes and archaeal proteins;


:

Pssm-ID: 197780  Cd Length: 92  Bit Score: 116.60  E-value: 3.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505595     88 KIEKTILKSDYHGALLTIWLAENPTQIGISGIVVLETRHTFQMVTQEDRFVVIPKKGSVFRFILGD-RLFSLFGDGMRTR 166
Cdd:smart00538   1 LTPRKLLRHELIGLKVRVVASKNPSLVGIEGIVVDETRNTLVIETKEGRVKTVPKDGAVFEFELPGgEKVRIDGDLLVGR 80

                           90
                   ....*....|..
gi 17505595    167 PAWRGKKPRIKR 178
Cdd:smart00538  81 PEDRSKKKFKKL 92
 
Name Accession Description Interval E-value
POP4 smart00538
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ...
 88-178 3.63e-34

A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes and archaeal proteins;


Pssm-ID: 197780  Cd Length: 92  Bit Score: 116.60  E-value: 3.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505595     88 KIEKTILKSDYHGALLTIWLAENPTQIGISGIVVLETRHTFQMVTQEDRFVVIPKKGSVFRFILGD-RLFSLFGDGMRTR 166
Cdd:smart00538   1 LTPRKLLRHELIGLKVRVVASKNPSLVGIEGIVVDETRNTLVIETKEGRVKTVPKDGAVFEFELPGgEKVRIDGDLLVGR 80

                           90
                   ....*....|..
gi 17505595    167 PAWRGKKPRIKR 178
Cdd:smart00538  81 PEDRSKKKFKKL 92
RNase_P-MRP_p29 pfam01868
Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ...
 91-173 1.70e-29

Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic proteins. The archaeal proteins are found to be expressed within ribosomal operons and several of the sequences are described as ribonuclease P protein subunit p29 proteins. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured beta-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex. Rpp29 catalyzes the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits.


Pssm-ID: 460367  Cd Length: 84  Bit Score: 104.43  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505595    91 KTILKSDYHGALLTIWLAENPTQIGISGIVVLETRHTFQMVTQEDRFVVIPKKGSVFRFILGD-RLFSLFGDGMRTRPAW 169
Cdd:pfam01868   1 AKLLKADLHGAEVEVVRSKNPSLVGIKGIVVDETKNTFVIITKDNRVKTIPKEGSVFRFELPDgEVVEIHGSQLLYRPED 80


                  ....
gi 17505595   170 RGKK 173
Cdd:pfam01868  81 RAKK 84
POP4 COG1588
RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis];
110-179 3.25e-10

RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441196  Cd Length: 94  Bit Score: 54.45  E-value: 3.25e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17505595 110 NPTQIGISGIVVLETRHTFQMVTqEDRFVVIPKKGSVFRF-ILGDRLFSLFGDGMRTRPAWRGKKpRIKRL 179
Cdd:COG1588  24 NPSLVGISGRVVDETKNTLVIET-EDGVKRVPKSGATFEFtLPDGESVTVDGSLLLGRPEERLKK-LIKKK 92
PRK03879 PRK03879
ribonuclease P protein component 1; Validated
 108-180 1.03e-07

ribonuclease P protein component 1; Validated


Pssm-ID: 235169  Cd Length: 96  Bit Score: 48.01  E-value: 1.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17505595  108 AENPTQIGISGIVVLETRHTFQMVTqEDRFVVIPKKGSVFRFILGDRL---FSLFGDGMRTRPAWRGKKpRIKRLL 180
Cdd:PRK03879  23 STNPSLVGIKGRVVDETRNTLVIET-DGKEWMVPKDGATFEFELGRDDvvkVKVDGRLLVGRPEDRLKK-KIKKLR 96
 
Name Accession Description Interval E-value
POP4 smart00538
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ...
 88-178 3.63e-34

A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes and archaeal proteins;


Pssm-ID: 197780  Cd Length: 92  Bit Score: 116.60  E-value: 3.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505595     88 KIEKTILKSDYHGALLTIWLAENPTQIGISGIVVLETRHTFQMVTQEDRFVVIPKKGSVFRFILGD-RLFSLFGDGMRTR 166
Cdd:smart00538   1 LTPRKLLRHELIGLKVRVVASKNPSLVGIEGIVVDETRNTLVIETKEGRVKTVPKDGAVFEFELPGgEKVRIDGDLLVGR 80

                           90
                   ....*....|..
gi 17505595    167 PAWRGKKPRIKR 178
Cdd:smart00538  81 PEDRSKKKFKKL 92
RNase_P-MRP_p29 pfam01868
Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ...
 91-173 1.70e-29

Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic proteins. The archaeal proteins are found to be expressed within ribosomal operons and several of the sequences are described as ribonuclease P protein subunit p29 proteins. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured beta-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex. Rpp29 catalyzes the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits.


Pssm-ID: 460367  Cd Length: 84  Bit Score: 104.43  E-value: 1.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505595    91 KTILKSDYHGALLTIWLAENPTQIGISGIVVLETRHTFQMVTQEDRFVVIPKKGSVFRFILGD-RLFSLFGDGMRTRPAW 169
Cdd:pfam01868   1 AKLLKADLHGAEVEVVRSKNPSLVGIKGIVVDETKNTFVIITKDNRVKTIPKEGSVFRFELPDgEVVEIHGSQLLYRPED 80


                  ....
gi 17505595   170 RGKK 173
Cdd:pfam01868  81 RAKK 84
POP4 COG1588
RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis];
110-179 3.25e-10

RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441196  Cd Length: 94  Bit Score: 54.45  E-value: 3.25e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17505595 110 NPTQIGISGIVVLETRHTFQMVTqEDRFVVIPKKGSVFRF-ILGDRLFSLFGDGMRTRPAWRGKKpRIKRL 179
Cdd:COG1588  24 NPSLVGISGRVVDETKNTLVIET-EDGVKRVPKSGATFEFtLPDGESVTVDGSLLLGRPEERLKK-LIKKK 92
PRK03879 PRK03879
ribonuclease P protein component 1; Validated
 108-180 1.03e-07

ribonuclease P protein component 1; Validated


Pssm-ID: 235169  Cd Length: 96  Bit Score: 48.01  E-value: 1.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17505595  108 AENPTQIGISGIVVLETRHTFQMVTqEDRFVVIPKKGSVFRFILGDRL---FSLFGDGMRTRPAWRGKKpRIKRLL 180
Cdd:PRK03879  23 STNPSLVGIKGRVVDETRNTLVIET-DGKEWMVPKDGATFEFELGRDDvvkVKVDGRLLVGRPEDRLKK-KIKKLR 96
 
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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