P45748 (RIMN_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 106.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: tRNA threonylcarbamoyladenosine biosynthesis protein RimN Alternative name(s): Ribosome maturation factor RimN t(6)A37 threonylcarbamoyladenosine biosynthesis protein RimN | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 190 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Binds ATP, and to fully modified tRNA(Thr) and partially modified tRNA(Thr). Could also be required for the maturation of 16S rRNA. Binds to double-stranded RNA but does not interact tightly with either of the ribosomal subunits, or the 70S particles. Ref.4 Ref.5 |
| Subcellular location | Cytoplasm Potential HAMAP-Rule MF_01852. |
| Sequence similarities | Belongs to the SUA5 family. RimN subfamily. Contains 1 YrdC-like domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ribosome biogenesis rRNA processing tRNA processing |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding RNA-binding tRNA-binding |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | rRNA processing Inferred from electronic annotation. Source: UniProtKB-KW threonylcarbamoyladenosine biosynthetic processInferred from direct assay PubMed 22378793. Source: EcoCyc |
| Cellular_component | cytoplasm Inferred from direct assay PubMed 15126466. Source: EcoCyc |
| Molecular_function | ATP binding Inferred from direct assay Ref.5. Source: EcoCyc double-stranded RNA bindingInferred from direct assay Ref.6. Source: EcoCyc tRNA bindingInferred from direct assay Ref.6Ref.5. Source: EcoCyc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 190 | 190 | tRNA threonylcarbamoyladenosine biosynthesis protein RimN HAMAP-Rule MF_01852 | PRO_0000202018 | |||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||
| Domain | 7 – 190 | 184 | YrdC-like | ||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 50 | 1 | K → A: Loss of activity. Ref.5 | ||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 52 | 1 | R → A: Loss of activity. Ref.5 | ||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 56 | 1 | K → A: No change in activity. Ref.5 | ||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 110 | 1 | R → A: No change in activity. Ref.5 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Helix | 4 – 18 | 15 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 23 – 26 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 28 – 35 | 8 | |||||||||||||||||||||||||||||||||||||||
| Helix | 40 – 50 | 11 | |||||||||||||||||||||||||||||||||||||||
| Helix | 54 – 56 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 64 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 65 – 68 | 4 | |||||||||||||||||||||||||||||||||||||||
| Helix | 69 – 71 | 3 | |||||||||||||||||||||||||||||||||||||||
| Helix | 79 – 86 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 90 – 98 | 9 | |||||||||||||||||||||||||||||||||||||||
| Helix | 105 – 108 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 118 | 8 | |||||||||||||||||||||||||||||||||||||||
| Helix | 122 – 131 | 10 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 135 – 140 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 151 – 158 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 177 – 180 | 4 | |||||||||||||||||||||||||||||||||||||||
| Turn | 181 – 183 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 184 – 186 | 3 | |||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [2] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B. Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: B / BL21. |
| [4] | "The YrdC protein -- a putative ribosome maturation factor." Kaczanowska M., Ryden-Aulin M. Biochim. Biophys. Acta 1727:87-96(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MATURATION OF 16S RRNA. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA." El Yacoubi B., Lyons B., Cruz Y., Reddy R., Nordin B., Agnelli F., Williamson J.R., Schimmel P., Swairjo M.A., de Crecy-Lagard V. Nucleic Acids Res. 37:2894-2909(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ATP-BINDING, TRNA-BINDING, MUTAGENESIS OF LYS-50; ARG-52; LYS-56 AND ARG-110. Strain: K12 / MG1655 / ATCC 47076. |
| [6] | "The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding." Teplova M., Tereshko V., Sanishvili R., Joachimiak A., Bushueva T., Anderson W.F., Egli M. Protein Sci. 9:2557-2566(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), RNA-BINDING. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U18997 Genomic DNA. Translation: AAA58079.1. Frameshift. U00096 Genomic DNA. Translation: AAC76307.1. AP009048 Genomic DNA. Translation: BAE78009.1. | ||||||||||||
| PIR | E65120. | ||||||||||||
| RefSeq | NP_417741.1. NC_000913.2. YP_492150.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P45748. | ||||||||||||
| SMR | P45748. Positions 3-188. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-12916N. | ||||||||||||
| IntAct | P45748. 12 interactions. | ||||||||||||
| MINT | MINT-1230775. | ||||||||||||
| STRING | 511145.b3282. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P45748. | ||||||||||||
| PRIDE | P45748. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC76307; AAC76307; b3282. BAE78009; BAE78009; BAE78009. | ||||||||||||
| GeneID | 12933460. 947783. | ||||||||||||
| KEGG | ecj:Y75_p3894. eco:b3282. | ||||||||||||
| PATRIC | 32121998. VBIEscCol129921_3376. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB2689. | ||||||||||||
| EcoGene | EG12840. rimN. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0009. | ||||||||||||
| HOGENOM | HOG000076163. | ||||||||||||
| KO | K07566. | ||||||||||||
| OMA | FGLGCNP. | ||||||||||||
| ProtClustDB | PRK10634. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:G7698-MONOMER. ECOL316407:JW3243-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P45748. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.90.870.10. 1 hit. | ||||||||||||
| HAMAP | MF_01852. RimN. | ||||||||||||
| InterPro | IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR023535. tRNA-t6A_RimN_(YrdC). IPR006070. YrdC-like_dom. [Graphical view] | ||||||||||||
| Pfam | PF01300. Sua5_yciO_yrdC. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit. | ||||||||||||
| PROSITE | PS51163. YRDC. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P45748. | ||||||||||||
Entry information
| Entry name | RIMN_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P45748 Secondary accession number(s): Q2M6U7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
