Reviewed,
UniProtKB/Swiss-Prot O52704 (RL1_METTL)
Last modified
November 25, 2008.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 50S ribosomal protein L1P | ||
| Gene names |
| ||
| Organism | Methanococcus thermolithotrophicus | ||
| Taxonomic identifier | 2186 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanothermococcus |
Protein attributes
| Sequence length | 213 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Probably involved in E site tRNA release By similarity. Binds directly to 23S rRNA. Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA By similarity. |
| Subunit structure | Part of the 50S ribosomal subunit. HAMAP MF_01318 |
| Sequence similarities | Belongs to the ribosomal protein L1P family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Translation regulation |
| Ligand | RNA-binding rRNA-binding tRNA-binding |
| Molecular function | Repressor Ribonucleoprotein Ribosomal protein |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | ribosome Inferred from electronic annotation. Source: InterPro |
| Molecular function | rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosomeInferred from electronic annotation. Source: InterPro tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 213 | 213 | 50S ribosomal protein L1P HAMAP MF_01318 | PRO_0000125802 | ||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 3 – 15 | 13 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 25 – 32 | 8 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 40 – 42 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 45 – 49 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 60 – 63 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 67 – 74 | 8 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 80 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 82 – 90 | 9 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 92 – 101 | 10 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 103 – 108 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 109 – 111 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 112 – 117 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 120 – 126 | 7 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 131 – 133 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 139 – 147 | 9 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 149 – 153 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 157 – 166 | 10 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 171 – 188 | 18 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 189 – 191 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 192 – 195 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 196 – 202 | 7 | ||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | Linhart A., Piendl W. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA." Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W. Eur. J. Biochem. 256:97-105(1998) [PubMed: 9746351] [Abstract] Cited for: BINDING TO ENDOGENOUS 23S RRNA, TO METHANOCOCCUS VANNIELII L1 MRNA. |
| [3] | "Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface." Nevskaya N., Tishchenko S., Paveliev M., Smolinskaya Y., Fedorov R., Piendl W., Nakamura Y., Toyoda T., Garber M.B., Nikonov S. Acta Crystallogr. D 58:1023-1029(2002) [PubMed: 12037305] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF044919 Genomic DNA. Translation: AAC64510.1. | |||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01318. [Tree] | ||||||||||||
| InterPro | IPR002143. Ribosomal_L1. IPR016094. Ribosomal_L1_2-a/b-sand. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.30.190.20. Ribosomal_L1_2-a/b-sand. 1 hit. | ||||||||||||
| Pfam | PF00687. Ribosomal_L1. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF002155. Ribosomal_L1. 1 hit. | ||||||||||||
| ProDom | PD001314. Ribosomal_L1. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| PROSITE | PS01199. RIBOSOMAL_L1. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | RL1_METTL | ||||||||
| Accession | Primary (citable) accession number: O52704 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| 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 |

Clusters with


