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77  structures 1398  species 0  interactions 1618  sequences 35  architectures

Family: MRP-L47 (PF06984)

Summary: Mitochondrial 39-S ribosomal protein L47 (MRP-L47)

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Mitochondrial 39-S ribosomal protein L47 (MRP-L47) Provide feedback

This family represents the N-terminal region (approximately 8 residues) of the eukaryotic mitochondrial 39-S ribosomal protein L47 (MRP-L47). Mitochondrial ribosomal proteins (MRPs) are the counterparts of the cytoplasmic ribosomal proteins, in that they fulfil similar functions in protein biosynthesis. However, they are distinct in number, features and primary structure [1].

Literature references

  1. Graack HR, Wittmann-Liebold B; , Biochem J 1998;329:433-448.: Mitochondrial ribosomal proteins (MRPs) of yeast. PUBMED:9445368 EPMC:9445368


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR010729

Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [ PUBMED:11297922 , PUBMED:11290319 ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.

Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [ PUBMED:11290319 , PUBMED:11114498 ].

This entry represents the N-terminal region (approximately 8 residues) of the eukaryotic mitochondrial 39-S ribosomal protein L47 (MRP-L47). Mitochondrial ribosomal proteins (MRPs) are the counterparts of the cytoplasmic ribosomal proteins, in that they fulfil similar functions in protein biosynthesis. However, they are distinct in number, features and primary structure [ PUBMED:9445368 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Ribo_L29 (CL0346), which has the following description:

Superfamily includes Ribosomal protein L29 family and its corresponding mitochondrial ribosomal family, L47.

The clan contains the following 2 members:

MRP-L47 Ribosomal_L29

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(8)
Full
(1618)
Representative proteomes UniProt
(2745)
RP15
(340)
RP35
(764)
RP55
(1247)
RP75
(1675)
Jalview View  View  View  View  View  View  View 
HTML View  View           
PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(8)
Full
(1618)
Representative proteomes UniProt
(2745)
RP15
(340)
RP35
(764)
RP55
(1247)
RP75
(1675)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(8)
Full
(1618)
Representative proteomes UniProt
(2745)
RP15
(340)
RP35
(764)
RP55
(1247)
RP75
(1675)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_6890 (release 10.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Vella Briffa B
Number in seed: 8
Number in full: 1618
Average length of the domain: 87.5 aa
Average identity of full alignment: 43 %
Average coverage of the sequence by the domain: 33.52 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.0 28.2
Noise cut-off 26.9 26.9
Model length: 87
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Structures

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 MRP-L47 domain has been found. There are 77 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A077ZCA1 View 3D Structure Click here
A0A0D2GR32 View 3D Structure Click here
A0A0K0E345 View 3D Structure Click here
A0A0K0J2T4 View 3D Structure Click here
A0A175VPH0 View 3D Structure Click here
A0A1C1CR57 View 3D Structure Click here
A0A1D6NSS3 View 3D Structure Click here
A0A2K6VE42 View 3D Structure Click here
A0A3P7FE58 View 3D Structure Click here
A0A3P7SCP1 View 3D Structure Click here
A1C6F8 View 3D Structure Click here
A1DH31 View 3D Structure Click here
A2QCC7 View 3D Structure Click here
A3LYY9 View 3D Structure Click here
A4HS22 View 3D Structure Click here
A4RHR8 View 3D Structure Click here
A5DH98 View 3D Structure Click here
A5E713 View 3D Structure Click here
A6RDX3 View 3D Structure Click here
A7EWR0 View 3D Structure Click here
A7TNQ2 View 3D Structure Click here
B8A1J9 View 3D Structure Click here
C0NXJ1 View 3D Structure Click here
C1H6F2 View 3D Structure Click here
C6T0Z6 View 3D Structure Click here
C6TFG9 View 3D Structure Click here
E7F6A5 View 3D Structure Click here
G4VDE9 View 3D Structure Click here
O97270 View 3D Structure Click here
P36517 View 3D Structure Click here
P87232 View 3D Structure Click here
Q08DT6 View 3D Structure Click here
Q0CXX1 View 3D Structure Click here
Q0U6J9 View 3D Structure Click here
Q1DNY5 View 3D Structure Click here
Q2H080 View 3D Structure Click here
Q2L6V2 View 3D Structure Click here
Q38EM7 View 3D Structure Click here
Q3B8R7 View 3D Structure Click here
Q4CLN1 View 3D Structure Click here