Summary: Ribonuclease P
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Ribonuclease P Provide feedback
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Internal database links
|SCOOP:||ATP-cone Lipin_N Complex1_LYR RNase_E_G DUF3536 DUF3876 Complex1_LYR_1 AbiEi_4 CagY_I DUF4783|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000100Ribonuclease P (EC) (RNase P) [PUBMED:1689306, PUBMED:1700778, PUBMED:1374553] is a site specific endonuclease that generates mature tRNAs by catalysing the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. In bacteria RNase P is known to be composed of two components: a large RNA (about 400 base pairs) encoded by rnpB, and a small protein (119 to 133 amino acids) encoded by rnpA. The RNA moiety of RNase P carries the catalytic activity; the protein component plays an auxiliary, but essential, role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. The sequence of rnpA is not highly conserved, however there is, in the central part of the protein, a conserved basic region.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||tRNA binding (GO:0000049)|
|ribonuclease P activity (GO:0004526)|
|Biological process||tRNA processing (GO:0008033)|
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This superfamily contains a wide range of families that possess a structure similar to the second domain of ribosomal S5 protein.
The clan contains the following 14 members:ChlI DNA_mis_repair EFG_IV Fae GHMP_kinases_N IGPD Lon_C LpxC Ribonuclease_P Ribosomal_S5_C RNase_PH Topo-VIb_trans UPF0029 Xol-1_N
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Curation and family details
|Seed source:||Pfam-B_1558 (release 2.1)|
|Number in seed:||97|
|Number in full:||18106|
|Average length of the domain:||107.10 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||89.93 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Ribonuclease_P domain has been found. There are 10 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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