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Conserved domains on  [gi|5729986|ref|NP_006618|]
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ribonuclease P protein subunit p29 [Homo sapiens]

Protein Classification

ribonuclease P component 1 family protein( domain architecture ID 10486930)

ribonuclease (RNase) P component 1 family protein is a component of RNase MRP and/or RNase P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends; such as mammalian ribonuclease P protein subunit p29 (Rpp29/POP4)

CATH:  2.30.30.210
EC:  3.1.26.-
Gene Ontology:  GO:0030677|GO:0033204|GO:0006364|GO:0000172
PubMed:  10352175|19931535
SCOP:  4000863

Graphical summary

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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 ...
 128-210 1.40e-39

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: 131.01  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729986    128 AKLLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFKIITKEDRLKVIPKLNCVFTVETDGFISY-IYGSKFQLRSSE 206
Cdd:pfam01868   1 AKLLKADLHGAEVEVVRSKNPSLVGIKGIVVDETKNTFVIITKDNRVKTIPKEGSVFRFELPDGEVVeIHGSQLLYRPED 80


                  ....
gi 5729986    207 RSAK 210
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 ...
 128-210 1.40e-39

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: 131.01  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729986    128 AKLLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFKIITKEDRLKVIPKLNCVFTVETDGFISY-IYGSKFQLRSSE 206
Cdd:pfam01868   1 AKLLKADLHGAEVEVVRSKNPSLVGIKGIVVDETKNTFVIITKDNRVKTIPKEGSVFRFELPDGEVVeIHGSQLLYRPED 80


                  ....
gi 5729986    207 RSAK 210
Cdd:pfam01868  81 RAKK 84
POP4 smart00538
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ...
 125-215 1.12e-36

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: 123.92  E-value: 1.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729986     125 MIQAKLLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFKIITKEDRLKVIPKLNCVFTVET-DGFISYIYGSKFQLR 203
Cdd:smart00538   1 LTPRKLLRHELIGLKVRVVASKNPSLVGIEGIVVDETRNTLVIETKEGRVKTVPKDGAVFEFELpGGEKVRIDGDLLVGR 80

                           90
                   ....*....|..
gi 5729986     204 SSERSAKKFKAK 215
Cdd:smart00538  81 PEDRSKKKFKKL 92
POP4 COG1588
RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis];
140-216 7.98e-09

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


Pssm-ID: 441196  Cd Length: 94  Bit Score: 51.37  E-value: 7.98e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5729986  140 ISVTKSKCPSYVGITGILLQETKHIFKIITkEDRLKVIPKLNCVFTVETDGFISY-IYGSKFQLRSSERSAKKFKAKG 216
Cdd:COG1588  17 VEVVESTNPSLVGISGRVVDETKNTLVIET-EDGVKRVPKSGATFEFTLPDGESVtVDGSLLLGRPEERLKKLIKKKW 93
PRK03879 PRK03879
ribonuclease P protein component 1; Validated
 123-190 4.73e-05

ribonuclease P protein component 1; Validated


Pssm-ID: 235169  Cd Length: 96  Bit Score: 41.07  E-value: 4.73e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5729986   123 PQMIqaklLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFkIITKEDRLKVIPKLNCVFTVETDG 190
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 ...
 128-210 1.40e-39

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: 131.01  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729986    128 AKLLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFKIITKEDRLKVIPKLNCVFTVETDGFISY-IYGSKFQLRSSE 206
Cdd:pfam01868   1 AKLLKADLHGAEVEVVRSKNPSLVGIKGIVVDETKNTFVIITKDNRVKTIPKEGSVFRFELPDGEVVeIHGSQLLYRPED 80


                  ....
gi 5729986    207 RSAK 210
Cdd:pfam01868  81 RAKK 84
POP4 smart00538
A domain found in a protein subunit of human RNase MRP and RNase P ribonucleoprotein complexes ...
 125-215 1.12e-36

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: 123.92  E-value: 1.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729986     125 MIQAKLLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFKIITKEDRLKVIPKLNCVFTVET-DGFISYIYGSKFQLR 203
Cdd:smart00538   1 LTPRKLLRHELIGLKVRVVASKNPSLVGIEGIVVDETRNTLVIETKEGRVKTVPKDGAVFEFELpGGEKVRIDGDLLVGR 80

                           90
                   ....*....|..
gi 5729986     204 SSERSAKKFKAK 215
Cdd:smart00538  81 PEDRSKKKFKKL 92
POP4 COG1588
RNase P/RNase MRP subunit p29 [Translation, ribosomal structure and biogenesis];
140-216 7.98e-09

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


Pssm-ID: 441196  Cd Length: 94  Bit Score: 51.37  E-value: 7.98e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5729986  140 ISVTKSKCPSYVGITGILLQETKHIFKIITkEDRLKVIPKLNCVFTVETDGFISY-IYGSKFQLRSSERSAKKFKAKG 216
Cdd:COG1588  17 VEVVESTNPSLVGISGRVVDETKNTLVIET-EDGVKRVPKSGATFEFTLPDGESVtVDGSLLLGRPEERLKKLIKKKW 93
PRK03879 PRK03879
ribonuclease P protein component 1; Validated
 123-190 4.73e-05

ribonuclease P protein component 1; Validated


Pssm-ID: 235169  Cd Length: 96  Bit Score: 41.07  E-value: 4.73e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5729986   123 PQMIqaklLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFkIITKEDRLKVIPKLNCVFTVETDG 190
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.
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