C1E9Y5 · RTCB_MICCC
- ProteinRNA-splicing ligase RtcB homolog
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids513 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs.
Miscellaneous
Ligation probably proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RTCB reacts with GTP to form a covalent RTCB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP.
Catalytic activity
- a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP = a ribonucleotidyl-ribonucleotide-RNA + GMP + diphosphate
Cofactor
Note: Binds 2 manganese ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 127 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 130 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 130 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 234-238 | GMP (UniProtKB | ChEBI) | ||||
Sequence: NHYAE | ||||||
Binding site | 235 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 267 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 361 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 361-362 | GMP (UniProtKB | ChEBI) | ||||
Sequence: HN | ||||||
Binding site | 410-413 | GMP (UniProtKB | ChEBI) | ||||
Sequence: GGTM | ||||||
Binding site | 417 | GMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 436 | GMP-histidine intermediate | ||||
Sequence: H | ||||||
Binding site | 436-439 | GMP (UniProtKB | ChEBI) | ||||
Sequence: HGAG | ||||||
Binding site | 512 | GMP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | tRNA-splicing ligase complex | |
Molecular Function | GTP binding | |
Molecular Function | metal ion binding | |
Molecular Function | RNA ligase (ATP) activity | |
Molecular Function | RNA ligase (GTP) activity | |
Biological Process | tRNA splicing, via endonucleolytic cleavage and ligation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA-splicing ligase RtcB homolog
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Chlorophyta > Mamiellophyceae > Mamiellales > Mamiellaceae > Micromonas
Accessions
- Primary accessionC1E9Y5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000407235 | 1-513 | RNA-splicing ligase RtcB homolog | |||
Sequence: MGVMDLPGGRRTYAQEMEFLERVTPTQWRVREGFVPNMRVPGVFYVNKHLETLMFDELRQHVDRGDVGGFLPAVKQLANVACLPGIVSKSIALPDVHSGYGFAIGNVAAFDMSDPNAVVSPGGVGFDINCGVRVVRTNLHERDVTDIKEKLAQSLFDHIPVGVGSQGIIPTSPAGLEAALEMGMDWSLREGYAWAEDKEHCEEYGRMLNADPNKVSARAKKRGLPQMGTLGAGNHYAEIQVVDEIFDKHAADKMGIERLGQVMVMIHSGSRGLGHQVATDALTEMERAMARDGILVNDRQLACAKISSPEGQNYLSAMSCAANYAWVNRSSMTFLCRQAFAKMFDQTPDDLDMHVVYDVSHNIAKIEEHVVDGELKTLLVHRKGSTRAFPPHHPLIPVDYQYTGQPVLIGGTMGTCSYILTGTEKGMEETFGSTCHGAGRARSRNNSRNKLDYTEVLEKLKTKGIAIRVASPKLVMEEAPESYKDVTEVVNTCHDAGISKKAVKLRPIAVVKG |
Interaction
Subunit
Catalytic component of the tRNA-splicing ligase complex.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)56,239
- Last updated2009-05-26 v1
- Checksum186D1A358763F6F0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001328 EMBL· GenBank· DDBJ | ACO64763.1 EMBL· GenBank· DDBJ | Genomic DNA |