NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13384772|ref|NP_079666|]
View 

ribonuclease P protein subunit p29 [Mus musculus]

Protein Classification

ribonuclease P protein subunit( domain architecture ID 10486930)

ribonuclease P protein subunit such as human RNase P subunit p29 (POP4) and archaeal RNase P component 1, which are part of RNase P, a protein-RNA complex that generates mature tRNA molecules by cleaving their 5'-ends

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RNase_P-MRP_p29 pfam01868
Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ...
 129-211 8.96e-40

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: 131.39  E-value: 8.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384772   129 AKLLKADLHGAIISVTKSKCPSYVGVTGILLQETKHVFKIITREDHLKVIPKLNCVFTIEIDDFISY-IYGSKFQLRASE 207
Cdd:pfam01868   1 AKLLKADLHGAEVEVVRSKNPSLVGIKGIVVDETKNTFVIITKDNRVKTIPKEGSVFRFELPDGEVVeIHGSQLLYRPED 80


                  ....
gi 13384772   208 RSAK 211
Cdd:pfam01868  81 RAKK 84
 
Name Accession Description Interval E-value
RNase_P-MRP_p29 pfam01868
Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ...
 129-211 8.96e-40

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: 131.39  E-value: 8.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384772   129 AKLLKADLHGAIISVTKSKCPSYVGVTGILLQETKHVFKIITREDHLKVIPKLNCVFTIEIDDFISY-IYGSKFQLRASE 207
Cdd:pfam01868   1 AKLLKADLHGAEVEVVRSKNPSLVGIKGIVVDETKNTFVIITKDNRVKTIPKEGSVFRFELPDGEVVeIHGSQLLYRPED 80


                  ....
gi 13384772   208 RSAK 211
Cdd:pfam01868  81 RAKK 84
POP4 smart00538
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ...
 126-216 2.09e-32

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: 112.75  E-value: 2.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384772    126 MIQAKLLKADLHGAIISVTKSKCPSYVGVTGILLQETKHVFKIITREDHLKVIPKLNCVFTIEIDD-FISYIYGSKFQLR 204
Cdd:smart00538   1 LTPRKLLRHELIGLKVRVVASKNPSLVGIEGIVVDETRNTLVIETKEGRVKTVPKDGAVFEFELPGgEKVRIDGDLLVGR 80

                           90
                   ....*....|..
gi 13384772    205 ASERSAKKFKAK 216
Cdd:smart00538  81 PEDRSKKKFKKL 92
PRK03879 PRK03879
ribonuclease P protein component 1; Validated
 124-191 1.17e-04

ribonuclease P protein component 1; Validated


Pssm-ID: 235169  Cd Length: 96  Bit Score: 39.92  E-value: 1.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13384772  124 PQMIqaklLKADLHGAIISVTKSKCPSYVGVTGILLQETKHVFkIITREDHLKVIPKLNCVFTIEIDD 191
Cdd:PRK03879   5 PSNI----LRHELIGLKVEVVDSTNPSLVGIKGRVVDETRNTL-VIETDGKEWMVPKDGATFEFELGR 67
 
Name Accession Description Interval E-value
RNase_P-MRP_p29 pfam01868
Ribonuclease P/MRP, subunit p29; This family consists of several archaeal and eukaryotic ...
 129-211 8.96e-40

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: 131.39  E-value: 8.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384772   129 AKLLKADLHGAIISVTKSKCPSYVGVTGILLQETKHVFKIITREDHLKVIPKLNCVFTIEIDDFISY-IYGSKFQLRASE 207
Cdd:pfam01868   1 AKLLKADLHGAEVEVVRSKNPSLVGIKGIVVDETKNTFVIITKDNRVKTIPKEGSVFRFELPDGEVVeIHGSQLLYRPED 80


                  ....
gi 13384772   208 RSAK 211
Cdd:pfam01868  81 RAKK 84
POP4 smart00538
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ...
 126-216 2.09e-32

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: 112.75  E-value: 2.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13384772    126 MIQAKLLKADLHGAIISVTKSKCPSYVGVTGILLQETKHVFKIITREDHLKVIPKLNCVFTIEIDD-FISYIYGSKFQLR 204
Cdd:smart00538   1 LTPRKLLRHELIGLKVRVVASKNPSLVGIEGIVVDETRNTLVIETKEGRVKTVPKDGAVFEFELPGgEKVRIDGDLLVGR 80

                           90
                   ....*....|..
gi 13384772    205 ASERSAKKFKAK 216
Cdd:smart00538  81 PEDRSKKKFKKL 92
PRK03879 PRK03879
ribonuclease P protein component 1; Validated
 124-191 1.17e-04

ribonuclease P protein component 1; Validated


Pssm-ID: 235169  Cd Length: 96  Bit Score: 39.92  E-value: 1.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13384772  124 PQMIqaklLKADLHGAIISVTKSKCPSYVGVTGILLQETKHVFkIITREDHLKVIPKLNCVFTIEIDD 191
Cdd:PRK03879   5 PSNI----LRHELIGLKVEVVDSTNPSLVGIKGRVVDETRNTL-VIETDGKEWMVPKDGATFEFELGR 67
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH