ID   A7SA82_NEMVE            Unreviewed;       549 AA.
AC   A7SA82;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Elongator complex protein 3 {ECO:0000256|ARBA:ARBA00020266, ECO:0000256|PIRNR:PIRNR005669};
DE            EC=2.3.1.- {ECO:0000256|PIRNR:PIRNR005669};
GN   ORFNames=NEMVEDRAFT_v1g168258 {ECO:0000313|EMBL:EDO39414.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO39414.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO39414.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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). In the elongator complex, acts as a tRNA uridine(34)
CC       acetyltransferase by mediating formation of carboxymethyluridine in the
CC       wobble base at position 34 in tRNAs. {ECO:0000256|PIRNR:PIRNR005669}.
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:0000256|ARBA:ARBA00034985};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021;
CC         Evidence={ECO:0000256|ARBA:ARBA00034985};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005669,
CC         ECO:0000256|PIRSR:PIRSR005669-1};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|PIRNR:PIRNR005669, ECO:0000256|PIRSR:PIRSR005669-1};
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00005043}.
CC   -!- SIMILARITY: Belongs to the ELP3 family. {ECO:0000256|ARBA:ARBA00005494,
CC       ECO:0000256|PIRNR:PIRNR005669}.
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DR   EMBL; DS469607; EDO39414.1; -; Genomic_DNA.
DR   RefSeq; XP_001631477.1; XM_001631427.1.
DR   AlphaFoldDB; A7SA82; -.
DR   STRING; 45351.A7SA82; -.
DR   EnsemblMetazoa; EDO39414; EDO39414; NEMVEDRAFT_v1g168258.
DR   GeneID; 5511066; -.
DR   KEGG; nve:5511066; -.
DR   eggNOG; KOG2535; Eukaryota.
DR   HOGENOM; CLU_025983_2_1_1; -.
DR   InParanoid; A7SA82; -.
DR   OMA; TFETRPD; -.
DR   OrthoDB; 46095at2759; -.
DR   PhylomeDB; A7SA82; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0106261; F:tRNA uridine(34) acetyltransferase activity; IEA:RHEA.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
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; SFLDG01086; elongater_protein-like; 1.
DR   SFLD; SFLDF00344; ELP3-like; 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   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR005669}; Iron {ECO:0000256|PIRSR:PIRSR005669-1};
KW   Iron-sulfur {ECO:0000256|PIRNR:PIRNR005669, ECO:0000256|PIRSR:PIRSR005669-
KW   1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR005669,
KW   ECO:0000256|PIRSR:PIRSR005669-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR005669};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005669};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR005669};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555,
KW   ECO:0000256|PIRNR:PIRNR005669}.
FT   DOMAIN          84..374
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          398..549
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   BINDING         101
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005669-1"
FT   BINDING         111
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005669-1"
FT   BINDING         114
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005669-1"
SQ   SEQUENCE   549 AA;  62273 MW;  95EE52920732544D CRC64;
     MGKKNKKEPV ASRAELMVMT VSDIVNQLIT AHEKGENINL NKVKGKAASK YGLASQPRLV
     DIIAAIPHSH RKVLLPKLKA KPVRTASGIA VVAVMCKPHR CPHINMTGNI CVYCPGGPDS
     DFEYSTQSYT GYEPTSMRAI RARYNPYLQT KHRVEQLKQL GHSVDKVEFI VMGGTFMCLD
     EGYRDFFIRN LHDALSGHTS NNVEEAVKYS ERSKTKCIGI TIETRPDYCL KKHLSSMLAY
     GCTRLEIGVQ SVYEDVARDT NRGHTVRAVC ESFHQSKDAG FKVVSHMMPD LPNVGLERDI
     DQFIEFFENP AFRADGLKIY PTLVIRGTGL YELWKTGRYK SYPPNTLVDL IARILALVPP
     WTRVYRVQRD IPMPLVSSGV EHGNLRELAL ARMKDLGTQC RDVRTREVGI QEIHHKVRPF
     EIEQIRRDYV ANGGWETFLS YEDPEQDILI GLLRLRKCSD QSFRPELKDR CSIVRELHVY
     GSVVPVSARD PSKFQHQGFG MLLMEEAERI AREEHGSIKI AVISGVGTRN YYRKLGYELE
     GPYMVKSLI
//