UniProtKB - P10972 (RL24_HALMA)
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- BLAST>sp|P10972|RL24_HALMA 50S ribosomal protein L24 OS=Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) OX=272569 GN=rpl24 PE=1 SV=3 MSKQPDKQRKSQRRAPLHERHKQVRATLSADLREEYGQRNVRVNAGDTVEVLRGDFAGEE GEVINVDLDKAVIHVEDVTLEKTDGEEVPRPLDTSNVRVTDLDLEDEKREARLESEDDSA
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50S ribosomal protein L24
rpl24
Annotation score:3 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- rRNA binding Source: UniProtKB-KW
- structural constituent of ribosome Source: InterPro
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- translation Source: InterPro
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: 50S ribosomal protein L24Alternative name(s): Hl15 Hl16 Hmal24 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:rpl24 Ordered Locus Names:rrnAC1601 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 272569 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Haloarculaceae › Haloarcula › Haloarcula marismortui |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- large ribosomal subunit Source: InterPro
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000130767 | 2 – 120 | 50S ribosomal protein L24Add BLAST | 119 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"The structures of four macrolide antibiotics bound to the large ribosomal subunit."
Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.
Mol. Cell 10:117-128(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FOUR MACROLIDE ANTIBIOTICS. - Ref.11"Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit."
Hansen J.L., Moore P.B., Steitz T.A.
J. Mol. Biol. 330:1061-1075(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 272569.rrnAC1601 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 5 – 13 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 17 – 19 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 21 – 24 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 25 – 28 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 30 – 36 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 39 – 42 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 48 – 51 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 55 – 58 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 60 – 67 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 68 – 71 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 72 – 75 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 79 – 81 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 83 – 85 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 87 – 89 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 94 – 96 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 97 – 101 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 107 – 114 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 116 – 118 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P10972 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P10972 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P10972 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | arCOG04094 Archaea COG0198 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000216571 |
KEGG Orthology (KO) More...KOi | K02895 |
Identification of Orthologs from Complete Genome Data More...OMAi | VRIMRGD |
Database of Orthologous Groups More...OrthoDBi | POG093Z0H7W |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.30.30.30, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01326_A Ribosomal_L24_A, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005824 KOW IPR014722 Rib_L2_dom2 IPR005825 Ribosomal_L24/26_CS IPR005756 Ribosomal_L26/L24P_euk/arc IPR008991 Translation_prot_SH3-like_sf |
The PANTHER Classification System More...PANTHERi | PTHR11143 PTHR11143, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00467 KOW, 1 hit PF16906 Ribosomal_L26, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00739 KOW, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50104 SSF50104, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01080 rplX_A_E, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01108 RIBOSOMAL_L24, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MSKQPDKQRK SQRRAPLHER HKQVRATLSA DLREEYGQRN VRVNAGDTVE
60 70 80 90 100
VLRGDFAGEE GEVINVDLDK AVIHVEDVTL EKTDGEEVPR PLDTSNVRVT
110 120
DLDLEDEKRE ARLESEDDSA
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 21 | H → R AA sequence (PubMed:3191994).Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X55311 Genomic DNA Translation: CAA39019.1 AY596297 Genomic DNA Translation: AAV46518.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S10735 R5HS24 |
NCBI Reference Sequences More...RefSeqi | WP_004957398.1, NC_006396.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAV46518; AAV46518; rrnAC1601 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3128440 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hma:rrnAC1601 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|272569.17.peg.2290 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P10972 | 50S ribosomal protein L24 | 120 | |||
| 50S ribosomal protein L24 | 120 | ||||
| UPI0000050FA1 | 119 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P10972 | 50S ribosomal protein L24 | 120 | |||
| 50S ribosomal protein L24 | 120 | ||||
| UPI0000050FA1 | 119 | ||||
| 50S ribosomal protein L24 | 120 | ||||
| 50S ribosomal protein L24 | 120 | ||||
| +10 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P10972 | 50S ribosomal protein L24 | 120 | |||
| 50S ribosomal protein L24 | 120 | ||||
| UPI0000050FA1 | 119 | ||||
| 50S ribosomal protein L24 | 120 | ||||
| 50S ribosomal protein L24 | 120 | ||||
| +268 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X55311 Genomic DNA Translation: CAA39019.1 AY596297 Genomic DNA Translation: AAV46518.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S10735 R5HS24 |
NCBI Reference Sequences More...RefSeqi | WP_004957398.1, NC_006396.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1FFK | X-ray | 2.40 | Q | 2-120 | [»] | |
| 1JJ2 | X-ray | 2.40 | S | 2-120 | [»] | |
| 1K73 | X-ray | 3.01 | U | 2-120 | [»] | |
| 1K8A | X-ray | 3.00 | U | 2-120 | [»] | |
| 1K9M | X-ray | 3.00 | U | 2-120 | [»] | |
| 1KC8 | X-ray | 3.01 | U | 2-120 | [»] | |
| 1KD1 | X-ray | 3.00 | U | 2-120 | [»] | |
| 1KQS | X-ray | 3.10 | S | 2-120 | [»] | |
| 1M1K | X-ray | 3.20 | U | 2-120 | [»] | |
| 1M90 | X-ray | 2.80 | U | 2-120 | [»] | |
| 1N8R | X-ray | 3.00 | U | 2-120 | [»] | |
| 1NJI | X-ray | 3.00 | U | 2-120 | [»] | |
| 1Q7Y | X-ray | 3.20 | U | 2-120 | [»] | |
| 1Q81 | X-ray | 2.95 | U | 2-120 | [»] | |
| 1Q82 | X-ray | 2.98 | U | 2-120 | [»] | |
| 1Q86 | X-ray | 3.00 | U | 2-120 | [»] | |
| 1QVF | X-ray | 3.10 | S | 2-120 | [»] | |
| 1QVG | X-ray | 2.90 | S | 2-120 | [»] | |
| 1S72 | X-ray | 2.40 | T | 1-120 | [»] | |
| 1VQ4 | X-ray | 2.70 | T | 1-120 | [»] | |
| 1VQ5 | X-ray | 2.60 | T | 1-120 | [»] | |
| 1VQ6 | X-ray | 2.70 | T | 1-120 | [»] | |
| 1VQ7 | X-ray | 2.50 | T | 1-120 | [»] | |
| 1VQ8 | X-ray | 2.20 | T | 1-120 | [»] | |
| 1VQ9 | X-ray | 2.40 | T | 1-120 | [»] | |
| 1VQK | X-ray | 2.30 | T | 1-120 | [»] | |
| 1VQL | X-ray | 2.30 | T | 1-120 | [»] | |
| 1VQM | X-ray | 2.30 | T | 1-120 | [»] | |
| 1VQN | X-ray | 2.40 | T | 1-120 | [»] | |
| 1VQO | X-ray | 2.20 | T | 1-120 | [»] | |
| 1VQP | X-ray | 2.25 | T | 1-120 | [»] | |
| 1W2B | X-ray | 3.50 | S | 2-120 | [»] | |
| 1YHQ | X-ray | 2.40 | T | 1-120 | [»] | |
| 1YI2 | X-ray | 2.65 | T | 1-120 | [»] | |
| 1YIJ | X-ray | 2.60 | T | 1-120 | [»] | |
| 1YIT | X-ray | 2.80 | T | 1-120 | [»] | |
| 1YJ9 | X-ray | 2.90 | T | 1-120 | [»] | |
| 1YJN | X-ray | 3.00 | T | 1-120 | [»] | |
| 1YJW | X-ray | 2.90 | T | 1-120 | [»] | |
| 2OTJ | X-ray | 2.90 | T | 1-120 | [»] | |
| 2OTL | X-ray | 2.70 | T | 1-120 | [»] | |
| 2QA4 | X-ray | 3.00 | T | 1-120 | [»] | |
| 2QEX | X-ray | 2.90 | T | 1-120 | [»] | |
| 3CC2 | X-ray | 2.40 | T | 1-120 | [»] | |
| 3CC4 | X-ray | 2.70 | T | 1-120 | [»] | |
| 3CC7 | X-ray | 2.70 | T | 1-120 | [»] | |
| 3CCE | X-ray | 2.75 | T | 1-120 | [»] | |
| 3CCJ | X-ray | 2.70 | T | 1-120 | [»] | |
| 3CCL | X-ray | 2.90 | T | 1-120 | [»] | |
| 3CCM | X-ray | 2.55 | T | 1-120 | [»] | |
| 3CCQ | X-ray | 2.90 | T | 1-120 | [»] | |
| 3CCR | X-ray | 3.00 | T | 1-120 | [»] | |
| 3CCS | X-ray | 2.95 | T | 1-120 | [»] | |
| 3CCU | X-ray | 2.80 | T | 1-120 | [»] | |
| 3CCV | X-ray | 2.90 | T | 1-120 | [»] | |
| 3CD6 | X-ray | 2.75 | T | 1-120 | [»] | |
| 3CMA | X-ray | 2.80 | T | 1-120 | [»] | |
| 3CME | X-ray | 2.95 | T | 1-120 | [»] | |
| 3CPW | X-ray | 2.70 | S | 1-120 | [»] | |
| 3CXC | X-ray | 3.00 | S | 2-120 | [»] | |
| 3G4S | X-ray | 3.20 | T | 2-120 | [»] | |
| 3G6E | X-ray | 2.70 | T | 2-120 | [»] | |
| 3G71 | X-ray | 2.85 | T | 2-120 | [»] | |
| 3I55 | X-ray | 3.11 | T | 1-120 | [»] | |
| 3I56 | X-ray | 2.90 | T | 1-120 | [»] | |
| 3OW2 | X-ray | 2.70 | S | 2-120 | [»] | |
| 4ADX | electron microscopy | 6.60 | T | 1-120 | [»] | |
| 4V4R | X-ray | 5.90 | Y | 2-120 | [»] | |
| 4V4T | X-ray | 6.46 | Y | 2-120 | [»] | |
| 4V9F | X-ray | 2.40 | T | 1-120 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P10972 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P10972 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 272569.rrnAC1601 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAV46518; AAV46518; rrnAC1601 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3128440 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hma:rrnAC1601 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|272569.17.peg.2290 |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | arCOG04094 Archaea COG0198 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000216571 |
KEGG Orthology (KO) More...KOi | K02895 |
Identification of Orthologs from Complete Genome Data More...OMAi | VRIMRGD |
Database of Orthologous Groups More...OrthoDBi | POG093Z0H7W |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P10972 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.30.30.30, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01326_A Ribosomal_L24_A, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005824 KOW IPR014722 Rib_L2_dom2 IPR005825 Ribosomal_L24/26_CS IPR005756 Ribosomal_L26/L24P_euk/arc IPR008991 Translation_prot_SH3-like_sf |
The PANTHER Classification System More...PANTHERi | PTHR11143 PTHR11143, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00467 KOW, 1 hit PF16906 Ribosomal_L26, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00739 KOW, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50104 SSF50104, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01080 rplX_A_E, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01108 RIBOSOMAL_L24, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | RL24_HALMA | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P10972Primary (citable) accession number: P10972 Secondary accession number(s): Q5V1T4 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | November 22, 2017 | |
| This is version 138 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Ribosomal proteins
Ribosomal proteins families and list of entries - SIMILARITY comments
Index of protein domains and families
