Q23651 · ELP3_CAEEL
- ProteinElongator complex protein 3
- Geneelpc-3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids547 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity).
In the elongator complex, acts as a tRNA uridine34 acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
In the elongator complex, acts as a tRNA uridine34 acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity).
Catalytic activity
- acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine34 in tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine34 in tRNA + CoA + 2 H+ + L-methionineThis reaction proceeds in the forward direction.
CHEBI:57288 + CHEBI:15377 + CHEBI:59789 + RHEA-COMP:11727 CHEBI:65315 Position: 34= CHEBI:17319 + RHEA-COMP:10407 CHEBI:74882 Position: 34+ CHEBI:57287 + 2 CHEBI:15378 + CHEBI:57844
Cofactor
Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 95 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 105 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 108 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 160 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 470-473 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: ELHV | ||||||
Binding site | 493-495 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: YGS | ||||||
Binding site | 526 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | elongator holoenzyme complex | |
Cellular Component | nucleus | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | phosphorylase kinase regulator activity | |
Molecular Function | tRNA binding | |
Molecular Function | tRNA uridine(34) acetyltransferase activity | |
Biological Process | embryonic morphogenesis | |
Biological Process | olfactory learning | |
Biological Process | oocyte development | |
Biological Process | regulation of transcription by RNA polymerase II | |
Biological Process | spermatogenesis | |
Biological Process | translation | |
Biological Process | tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation | |
Biological Process | tRNA wobble uridine modification | |
Biological Process | vulval development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongator complex protein 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ23651
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000283994 | 1-547 | Elongator complex protein 3 | |||
Sequence: MDQKGSQRALLAQTINEIVKLLIEAHNQKKDVNLNRLKCIVAQKNGLSFQPKLVDIIAGVPSDYKDSLLPKLKAKPVRTASGIAVVAVMSKPHRCPHINFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPYLQTRGRLNQLMQLGHSVDKVEFIVMGGTFMSLPEDYRDFFIRNLHDALSGHTSASVEEAVAYSERSKMKCIGITIETRPDYCLPRHLNDMLLYGCTRLEIGVQSTYEDVARDTNRGHTVKSVCETFHMAKDTGYKVVIHMMPDLPNVGLERDKEQFLELFESPAFRPDGLKLYPTLVIRGTGLYELWKTGRYQSYPPSVLVDLIATILSLVPPWTRVYRVQRDIPMPLVSSGVEHGNLREHAMAKMKELGLKCRDVRTREVGIQEIHNKVRPEDVELIRRDYTANGGWETFISYEDPKQDILIGLLRLRKISDKAHRPELKGNVSVVRELHVYGSVVSVADRDPKKFQHQGYGSLLMEEAERIAREEHGSDKIAVISGVGTREYYRKLGYELDGPYMSKMLDSAAA |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 78-368 | Radical SAM core | ||||
Sequence: RTASGIAVVAVMSKPHRCPHINFTGNICVYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYNPYLQTRGRLNQLMQLGHSVDKVEFIVMGGTFMSLPEDYRDFFIRNLHDALSGHTSASVEEAVAYSERSKMKCIGITIETRPDYCLPRHLNDMLLYGCTRLEIGVQSTYEDVARDTNRGHTVKSVCETFHMAKDTGYKVVIHMMPDLPNVGLERDKEQFLELFESPAFRPDGLKLYPTLVIRGTGLYELWKTGRYQSYPPSVLVDLIATILSLVPPWTRVYRVQRDIPMP | ||||||
Domain | 392-547 | N-acetyltransferase | ||||
Sequence: LKCRDVRTREVGIQEIHNKVRPEDVELIRRDYTANGGWETFISYEDPKQDILIGLLRLRKISDKAHRPELKGNVSVVRELHVYGSVVSVADRDPKKFQHQGYGSLLMEEAERIAREEHGSDKIAVISGVGTREYYRKLGYELDGPYMSKMLDSAAA |
Sequence similarities
Belongs to the ELP3 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length547
- Mass (Da)61,910
- Last updated2006-09-05 v2
- Checksum6C7FAAEC59D8C6A6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z78019 EMBL· GenBank· DDBJ | CAB01454.2 EMBL· GenBank· DDBJ | Genomic DNA |