ID   ELP3_CHICK              Reviewed;         546 AA.
AC   Q5ZHS1;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=Elongator complex protein 3 {ECO:0000250|UniProtKB:Q9H9T3};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9};
DE   AltName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305};
GN   Name=ELP3 {ECO:0000250|UniProtKB:Q9H9T3}; ORFNames=RCJMB04_33o1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H9T3}. Nucleus
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; AJ721063; CAG32722.1; -; mRNA.
DR   RefSeq; NP_001034382.1; NM_001039293.1.
DR   AlphaFoldDB; Q5ZHS1; -.
DR   SMR; Q5ZHS1; -.
DR   STRING; 9031.ENSGALP00000026781; -.
DR   PaxDb; 9031-ENSGALP00000026781; -.
DR   Ensembl; ENSGALT00000111488; ENSGALP00000085025; ENSGALG00000016624.
DR   Ensembl; ENSGALT00010026050.1; ENSGALP00010014690.1; ENSGALG00010010880.1.
DR   Ensembl; ENSGALT00015047857; ENSGALP00015028242; ENSGALG00015019551.
DR   GeneID; 422021; -.
DR   KEGG; gga:422021; -.
DR   CTD; 55140; -.
DR   VEuPathDB; HostDB:geneid_422021; -.
DR   eggNOG; KOG2535; Eukaryota.
DR   GeneTree; ENSGT00390000013141; -.
DR   HOGENOM; CLU_025983_2_1_1; -.
DR   InParanoid; Q5ZHS1; -.
DR   OMA; TFETRPD; -.
DR   OrthoDB; 46095at2759; -.
DR   PhylomeDB; Q5ZHS1; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q5ZHS1; -.
DR   Proteomes; UP000000539; Chromosome 3.
DR   Bgee; ENSGALG00000016624; Expressed in muscle tissue and 13 other cell types or tissues.
DR   ExpressionAtlas; Q5ZHS1; baseline and differential.
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; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
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; 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   2: Evidence at transcript level;
KW   4Fe-4S; Acyltransferase; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Nucleus; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..546
FT                   /note="Elongator complex protein 3"
FT                   /id="PRO_0000283988"
FT   DOMAIN          81..371
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   DOMAIN          395..546
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         98
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         111
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         163
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         473..476
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         496..498
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         529
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
SQ   SEQUENCE   546 AA;  62092 MW;  5CF3764F583E1E0B CRC64;
     MGQKRKDLSH AELMMMTIAD IIKQLIEAHE QGKDVNLNKL KTKTSAKYGL SAQPRLVDII
     AAVPPQHRKA LVPKLKAKPI RTASGIAVVA VMCKPHRCPH INFTGNICVY CPGGPDSDFE
     YSTQSYTGYE PTSMRAIRAR YDPYLQTRHR VEQLKQLGHS VDKVEFIVMG GTFMALPEDY
     RDYFIRNLHD ALSGHTSNNV AEAVKYSERS LTKCVGITIE TRPDYCLKRH LSDMLSYGCT
     RLEIGVQSVY EDVARDTNRG HTVKAVCESF HLAKDAGFKV VAHMMPDLPN MGLERDTDQF
     VEFFENPAFR PDGMKLYPTL VIRGTGLYEL WKTGRYKSYP PSTLVDLVAR ILALVPPWTR
     VYRVQRDIPM PLVSSGVEHG NLRELALARM KDLGTQCRDV RTREVGIQEI HHKVRPYQIE
     LIRRDYVANG GWETFLSYED PEQDILVGLL RLRKCSEESF RPELKGGVSI VRELHVYGSV
     VPVSSRDPSK FQHQGFGMLL MEEAERIAKE EHGSWKIAVI SGVGTRNYYR KIGYELEGPY
     MVKRLQ
//