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1293  structures 8202  species 0  interactions 12174  sequences 67  architectures

Family: Ribosomal_L30 (PF00327)

Summary: Ribosomal protein L30p/L7e

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Ribosomal protein L30p/L7e Provide feedback

This family includes prokaryotic L30 and eukaryotic L7.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR016082

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 ].

Ribosomal protein L30 is one of the proteins from the large ribosomal subunit. L30 belongs to a family of ribosomal proteins which, on the basis of sequence similarities [ PUBMED:1549461 ], groups bacteria and archaea L30, yeast mitochondrial L33, and Drosophila melanogaster, Dictyostelium discoideum (Slime mold), fungal and mammalian L7 ribosomal proteins. L30 from bacteria are small proteins of about 60 residues, those from archaea are proteins of about 150 residues, and eukaryotic L7 are proteins of about 250 to 270 residues. L30 is missing in some groups of bacteria, such as the CPR group, the PVC group, Cyanobacteria, and some symbionts, which suggests that it is non-essential [ PUBMED:26083755 , PUBMED:23002217 ].

This entry represents a domain with a ferredoxin-like fold, with a core structure consisting of core: beta-alpha-beta-alpha-beta. This domain is found in prokaryotic ribosomal protein L30 (short-chain member of the family), as well as in archaeal L30 (L30a) (long-chain member of the family), the later containing an additional C-terminal (sub)domain. It is also found in nucleolar proteins with similarity to large ribosomal subunit L7 proteins. These are constituents of 66S pre-ribosomal particles and play an essential role in processing of precursors to the large ribosomal subunit RNAs [ PUBMED:8256515 , PUBMED:11087857 , PUBMED:15100437 ].

Domain organisation

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

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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...

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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.

Representative proteomes UniProt
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Representative proteomes UniProt

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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.

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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...


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: Prosite
Previous IDs: L30;
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD
Number in seed: 759
Number in full: 12174
Average length of the domain: 50.90 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 40.82 %

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 23.0 23.0
Trusted cut-off 23.0 23.0
Noise cut-off 22.9 22.9
Model length: 51
Family (HMM) version: 23
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


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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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The tree shows the occurrence of this domain across different species. More...


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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 Ribosomal_L30 domain has been found. There are 1293 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
A0A0P0XJU9 View 3D Structure Click here
A0A0R0FKY9 View 3D Structure Click here
A0A1D6GE21 View 3D Structure Click here
A0A1D6JDP4 View 3D Structure Click here
A0A1D6KA20 View 3D Structure Click here
A0A1D6MYM8 View 3D Structure Click here
A0A1D8PDL6 View 3D Structure Click here
A0A1D8PJ23 View 3D Structure Click here
A0B9U9 View 3D Structure Click here
A0BD73 View 3D Structure Click here
A0CEY2 View 3D Structure Click here
A0JZ67 View 3D Structure Click here
A0KF39 View 3D Structure Click here
A0L5Z1 View 3D Structure Click here
A0LIK8 View 3D Structure Click here
A0LRN8 View 3D Structure Click here
A0PXW4 View 3D Structure Click here
A0QSG7 View 3D Structure Click here
A0RUE6 View 3D Structure Click here
A1A087 View 3D Structure Click here
A1ALV9 View 3D Structure Click here
A1AVL8 View 3D Structure Click here
A1B045 View 3D Structure Click here
A1BJ16 View 3D Structure Click here
A1KB09 View 3D Structure Click here
A1R8S8 View 3D Structure Click here
A1RWR5 View 3D Structure Click here
A1S236 View 3D Structure Click here
A1SNK0 View 3D Structure Click here
A1T0C4 View 3D Structure Click here
A1T4S4 View 3D Structure Click here
A1TJT5 View 3D Structure Click here
A1UBQ6 View 3D Structure Click here
A1USR2 View 3D Structure Click here
A1VJ33 View 3D Structure Click here
A1W326 View 3D Structure Click here
A1WK98 View 3D Structure Click here
A1WVA4 View 3D Structure Click here
A2BME0 View 3D Structure Click here
A2SLD9 View 3D Structure Click here