ELP3_CAEEL
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 03-AUG-2022, entry version 159.
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 + carboxymethyluridine(34) in tRNA + CoA + 2
CC 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}.
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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; -.
DR EPD; Q23651; -.
DR PaxDb; Q23651; -.
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 CTD; 179669; -.
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; 320059at2759; -.
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 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:0008080; F:N-acetyltransferase activity; IEA:InterPro.
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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR039661; ELP3.
DR InterPro; IPR034687; ELP3-like.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032432; Radical_SAM_C.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR11135; PTHR11135; 1.
DR PANTHER; PTHR11135:SF7; PTHR11135:SF7; 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; SSF55729; 1.
DR TIGRFAMs; TIGR01211; ELP3; 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
