UniProtKB - P60619 (RL37A_HALMA)
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- BLAST>sp|P60619|RL37A_HALMA 50S ribosomal protein L37Ae OS=Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) OX=272569 GN=rpl37ae PE=1 SV=2 MASKSGKTGSSGRFGARYGRVSRRRVAEIESEMNEDHACPNCGEDRVDRQGTGIWQCSYC DYKFTGGSYKPETPGGKTVRRSIRAALSEDEE
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50S ribosomal protein L37Ae
rpl37ae
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>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 39 | ZincUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 42 | ZincUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 57 | ZincUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 60 | ZincUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 39 – 60 | C4-typeUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 22 |
<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
- metal ion binding Source: UniProtKB-KW
- 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 |
| Ligand | Metal-binding, Zinc |
<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 L37AeUniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Alternative name(s): Ribosomal protein L43eUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi |
| <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:rpl37aeUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Ordered Locus Names:rrnAC1669 |
| <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
- ribosome Source: UniProtKB-KW
<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 ‘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_0000139841 | 1 – 92 | 50S ribosomal protein L37AeAdd BLAST | 92 |
<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>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
2 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
- Ref.6"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.8"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.rrnAC1669 |
<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 | 11 – 14 | 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 | 20 – 34 | 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 | 15 | |
| <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 | 37 – 39 | 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 | 40 – 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 | 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 | 45 – 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 | 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 | 54 – 57 | 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 | 58 – 60 | 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 | 63 – 65 | 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 | 68 – 72 | 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 | 74 – 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 | 8 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P60619 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P60619 |
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 | P60619 |
<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
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
Zinc finger
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 39 – 60 | C4-typeUniRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 22 |
<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 - Domaini
Zinc-fingerPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | arCOG04208 Archaea COG1997 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000229493 |
KEGG Orthology (KO) More...KOi | K02921 |
Database of Orthologous Groups More...OrthoDBi | POG093Z0L6X |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.20.25.30, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00327 Ribosomal_L37Ae, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002674 Ribosomal_L37ae IPR011331 Ribosomal_L37ae/L37e IPR011332 Ribosomal_zn-bd |
The PANTHER Classification System More...PANTHERi | PTHR43931 PTHR43931, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01780 Ribosomal_L37ae, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57829 SSF57829, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00280 eL43_euk_arch, 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.
10 20 30 40 50
MASKSGKTGS SGRFGARYGR VSRRRVAEIE SEMNEDHACP NCGEDRVDRQ
60 70 80 90
GTGIWQCSYC DYKFTGGSYK PETPGGKTVR RSIRAALSED EE
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
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 | AY596297 Genomic DNA Translation: AAV46581.1 Different initiation. |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAV46581; AAV46581; rrnAC1669 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hma:rrnAC1669 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|272569.17.peg.2356 |
<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 | |
|---|---|---|---|---|---|
| P60619 | 50S ribosomal protein L37Ae | 92 | |||
| 50S ribosomal protein L37Ae | 123 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| +3 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P60619 | 50S ribosomal protein L37Ae | 92 | |||
| 50S ribosomal protein L37Ae | 123 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| +10 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P60619 | 50S ribosomal protein L37Ae | 92 | |||
| 50S ribosomal protein L37Ae | 123 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| 50S ribosomal protein L37Ae | 102 | ||||
| +62 | |||||
<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 | AY596297 Genomic DNA Translation: AAV46581.1 Different initiation. |
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 | W | 12-19 | [»] | |
| 1JJ2 | X-ray | 2.40 | Y | 49-79 | [»] | |
| 1K73 | X-ray | 3.01 | 1 | 49-79 | [»] | |
| 1K8A | X-ray | 3.00 | 1 | 49-79 | [»] | |
| 1K9M | X-ray | 3.00 | 1 | 49-79 | [»] | |
| 1KC8 | X-ray | 3.01 | 1 | 49-79 | [»] | |
| 1KD1 | X-ray | 3.00 | 1 | 49-79 | [»] | |
| 1KQS | X-ray | 3.10 | Y | 49-79 | [»] | |
| 1M1K | X-ray | 3.20 | 1 | 49-79 | [»] | |
| 1M90 | X-ray | 2.80 | 1 | 49-79 | [»] | |
| 1N8R | X-ray | 3.00 | 1 | 49-79 | [»] | |
| 1NJI | X-ray | 3.00 | 1 | 49-79 | [»] | |
| 1Q7Y | X-ray | 3.20 | 1 | 49-79 | [»] | |
| 1Q81 | X-ray | 2.95 | 1 | 49-79 | [»] | |
| 1Q82 | X-ray | 2.98 | 1 | 49-79 | [»] | |
| 1Q86 | X-ray | 3.00 | 1 | 49-79 | [»] | |
| 1QVF | X-ray | 3.10 | Y | 49-79 | [»] | |
| 1QVG | X-ray | 2.90 | Y | 49-79 | [»] | |
| 1S72 | X-ray | 2.40 | Z | 11-82 | [»] | |
| 1VQ4 | X-ray | 2.70 | Z | 11-92 | [»] | |
| 1VQ5 | X-ray | 2.60 | Z | 11-92 | [»] | |
| 1VQ6 | X-ray | 2.70 | Z | 11-92 | [»] | |
| 1VQ7 | X-ray | 2.50 | Z | 11-92 | [»] | |
| 1VQ8 | X-ray | 2.20 | Z | 11-92 | [»] | |
| 1VQ9 | X-ray | 2.40 | Z | 11-92 | [»] | |
| 1VQK | X-ray | 2.30 | Z | 11-92 | [»] | |
| 1VQL | X-ray | 2.30 | Z | 11-92 | [»] | |
| 1VQM | X-ray | 2.30 | Z | 11-92 | [»] | |
| 1VQN | X-ray | 2.40 | Z | 11-92 | [»] | |
| 1VQO | X-ray | 2.20 | Z | 11-92 | [»] | |
| 1VQP | X-ray | 2.25 | Z | 11-92 | [»] | |
| 1W2B | X-ray | 3.50 | Y | 49-79 | [»] | |
| 1YHQ | X-ray | 2.40 | Z | 11-92 | [»] | |
| 1YI2 | X-ray | 2.65 | Z | 11-92 | [»] | |
| 1YIJ | X-ray | 2.60 | Z | 11-92 | [»] | |
| 1YIT | X-ray | 2.80 | Z | 11-92 | [»] | |
| 1YJ9 | X-ray | 2.90 | Z | 11-92 | [»] | |
| 1YJN | X-ray | 3.00 | Z | 11-92 | [»] | |
| 1YJW | X-ray | 2.90 | Z | 11-92 | [»] | |
| 2OTJ | X-ray | 2.90 | Z | 11-82 | [»] | |
| 2OTL | X-ray | 2.70 | Z | 11-82 | [»] | |
| 2QA4 | X-ray | 3.00 | Z | 1-92 | [»] | |
| 2QEX | X-ray | 2.90 | Z | 11-82 | [»] | |
| 3CC2 | X-ray | 2.40 | Z | 1-92 | [»] | |
| 3CC4 | X-ray | 2.70 | Z | 1-92 | [»] | |
| 3CC7 | X-ray | 2.70 | Z | 1-92 | [»] | |
| 3CCE | X-ray | 2.75 | Z | 1-92 | [»] | |
| 3CCJ | X-ray | 2.70 | Z | 1-92 | [»] | |
| 3CCL | X-ray | 2.90 | Z | 1-92 | [»] | |
| 3CCM | X-ray | 2.55 | Z | 1-92 | [»] | |
| 3CCQ | X-ray | 2.90 | Z | 1-92 | [»] | |
| 3CCR | X-ray | 3.00 | Z | 1-92 | [»] | |
| 3CCS | X-ray | 2.95 | Z | 1-92 | [»] | |
| 3CCU | X-ray | 2.80 | Z | 1-92 | [»] | |
| 3CCV | X-ray | 2.90 | Z | 1-92 | [»] | |
| 3CD6 | X-ray | 2.75 | Z | 1-92 | [»] | |
| 3CMA | X-ray | 2.80 | Z | 1-92 | [»] | |
| 3CME | X-ray | 2.95 | Z | 1-92 | [»] | |
| 3CPW | X-ray | 2.70 | Y | 1-92 | [»] | |
| 3G4S | X-ray | 3.20 | Z | 10-82 | [»] | |
| 3G6E | X-ray | 2.70 | Z | 10-82 | [»] | |
| 3G71 | X-ray | 2.85 | Z | 10-82 | [»] | |
| 3I55 | X-ray | 3.11 | Z | 1-92 | [»] | |
| 3I56 | X-ray | 2.90 | Z | 1-92 | [»] | |
| 4ADX | electron microscopy | 6.60 | Z | 1-92 | [»] | |
| 4V9F | X-ray | 2.40 | Z | 1-92 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P60619 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P60619 | |||||
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.rrnAC1669 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAV46581; AAV46581; rrnAC1669 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hma:rrnAC1669 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|272569.17.peg.2356 |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | arCOG04208 Archaea COG1997 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000229493 |
KEGG Orthology (KO) More...KOi | K02921 |
Database of Orthologous Groups More...OrthoDBi | POG093Z0L6X |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P60619 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.20.25.30, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00327 Ribosomal_L37Ae, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002674 Ribosomal_L37ae IPR011331 Ribosomal_L37ae/L37e IPR011332 Ribosomal_zn-bd |
The PANTHER Classification System More...PANTHERi | PTHR43931 PTHR43931, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01780 Ribosomal_L37ae, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF57829 SSF57829, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00280 eL43_euk_arch, 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 | RL37A_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 | P60619Primary (citable) accession number: P60619 Secondary accession number(s): Q5V1M1 | |
| <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: | March 15, 2004 |
| Last sequence update: | January 4, 2005 | |
| Last modified: | November 22, 2017 | |
| This is version 105 of the entry and version 2 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, 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
