ID ELP3_CAEEL Reviewed; 547 AA. AC Q23651; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 2. DT 27-MAR-2024, entry version 167. DE RecName: Full=Elongator complex protein 3 {ECO:0000305}; DE EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9}; DE AltName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305}; GN Name=elpc-3; ORFNames=ZK863.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator CC complex which is required for multiple tRNA modifications, including CC mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5- CC methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl CC uridine) (By similarity). In the elongator complex, acts as a tRNA CC uridine(34) acetyltransferase by mediating formation of CC carboxymethyluridine in the wobble base at position 34 in tRNAs (By CC similarity). {ECO:0000250|UniProtKB:D5VRB9, CC ECO:0000250|UniProtKB:Q9H9T3}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in CC tRNA = 5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA CC + 2 H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407, CC Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, CC ChEBI:CHEBI:74882; Evidence={ECO:0000250|UniProtKB:D5VRB9}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021; CC Evidence={ECO:0000250|UniProtKB:D5VRB9}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:Q02908}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250|UniProtKB:Q02908}; CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA CC biosynthesis. {ECO:0000250|UniProtKB:Q9H9T3}. CC -!- SUBUNIT: Component of the elongator complex. CC {ECO:0000250|UniProtKB:Q9H9T3}. CC -!- SIMILARITY: Belongs to the ELP3 family. {ECO:0000305}. CC -!- CAUTION: The elongator complex was originally thought to play a role in CC transcription elongation. However, it is no longer thought to play a CC direct role in this process and its primary function is thought to be CC in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z78019; CAB01454.2; -; Genomic_DNA. DR PIR; T28062; T28062. DR RefSeq; NP_506055.2; NM_073654.4. DR AlphaFoldDB; Q23651; -. DR SMR; Q23651; -. DR BioGRID; 44692; 3. DR STRING; 6239.ZK863.3.1; -. DR EPD; Q23651; -. DR PaxDb; 6239-ZK863-3; -. DR PeptideAtlas; Q23651; -. DR EnsemblMetazoa; ZK863.3.1; ZK863.3.1; WBGene00014123. DR GeneID; 179669; -. DR KEGG; cel:CELE_ZK863.3; -. DR UCSC; ZK863.3; c. elegans. DR AGR; WB:WBGene00014123; -. DR WormBase; ZK863.3; CE40344; WBGene00014123; elpc-3. DR eggNOG; KOG2535; Eukaryota. DR GeneTree; ENSGT00390000013141; -. DR HOGENOM; CLU_025983_2_1_1; -. DR InParanoid; Q23651; -. DR OMA; TFETRPD; -. DR OrthoDB; 46095at2759; -. DR PhylomeDB; Q23651; -. DR UniPathway; UPA00988; -. DR PRO; PR:Q23651; -. DR Proteomes; UP000001940; Chromosome V. DR Bgee; WBGene00014123; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0033588; C:elongator holoenzyme complex; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008607; F:phosphorylase kinase regulator activity; ISS:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0106261; F:tRNA uridine(34) acetyltransferase activity; IEA:RHEA. DR GO; GO:0048598; P:embryonic morphogenesis; IGI:WormBase. DR GO; GO:0008355; P:olfactory learning; IMP:WormBase. DR GO; GO:0048599; P:oocyte development; IGI:WormBase. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IGI:WormBase. DR GO; GO:0006412; P:translation; IMP:WormBase. DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central. DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:WormBase. DR GO; GO:0040025; P:vulval development; IGI:WormBase. DR CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR039661; ELP3. DR InterPro; IPR034687; ELP3-like. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR032432; Radical_SAM_C. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR01211; ELP3; 1. DR PANTHER; PTHR11135:SF0; ELONGATOR COMPLEX PROTEIN 3; 1. DR PANTHER; PTHR11135; HISTONE ACETYLTRANSFERASE-RELATED; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF16199; Radical_SAM_C; 1. DR PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1. DR SFLD; SFLDF00344; ELP3-like; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS51186; GNAT; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Acyltransferase; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase; KW tRNA processing; tRNA-binding. FT CHAIN 1..547 FT /note="Elongator complex protein 3" FT /id="PRO_0000283994" FT DOMAIN 78..368 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT DOMAIN 392..547 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532" FT BINDING 95 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:Q02908" FT BINDING 105 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:Q02908" FT BINDING 108 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:Q02908" FT BINDING 160 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" FT BINDING 470..473 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" FT BINDING 493..495 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" FT BINDING 526 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7" SQ SEQUENCE 547 AA; 61910 MW; 6C7FAAEC59D8C6A6 CRC64; MDQKGSQRAL LAQTINEIVK LLIEAHNQKK DVNLNRLKCI VAQKNGLSFQ PKLVDIIAGV PSDYKDSLLP KLKAKPVRTA SGIAVVAVMS KPHRCPHINF TGNICVYCPG GPDSDFEYST QSYTGYEPTS MRAIRARYNP YLQTRGRLNQ LMQLGHSVDK VEFIVMGGTF MSLPEDYRDF FIRNLHDALS GHTSASVEEA VAYSERSKMK CIGITIETRP DYCLPRHLND MLLYGCTRLE IGVQSTYEDV ARDTNRGHTV KSVCETFHMA KDTGYKVVIH MMPDLPNVGL ERDKEQFLEL FESPAFRPDG LKLYPTLVIR GTGLYELWKT GRYQSYPPSV LVDLIATILS LVPPWTRVYR VQRDIPMPLV SSGVEHGNLR EHAMAKMKEL GLKCRDVRTR EVGIQEIHNK VRPEDVELIR RDYTANGGWE TFISYEDPKQ DILIGLLRLR KISDKAHRPE LKGNVSVVRE LHVYGSVVSV ADRDPKKFQH QGYGSLLMEE AERIAREEHG SDKIAVISGV GTREYYRKLG YELDGPYMSK MLDSAAA //