ID   ELP3_SCHPO              Reviewed;         544 AA.
AC   O14023;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Elongator complex protein 3;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9};
DE   AltName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305};
GN   Name=elp3 {ECO:0000303|PubMed:22768388,
GN   ECO:0000312|PomBase:SPAC29A4.20}; ORFNames=SPAC29A4.20;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=22768388; DOI=10.1016/j.celrep.2012.04.001;
RA   Bauer F., Matsuyama A., Candiracci J., Dieu M., Scheliga J., Wolf D.A.,
RA   Yoshida M., Hermand D.;
RT   "Translational control of cell division by Elongator.";
RL   Cell Rep. 1:424-433(2012).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=28775286; DOI=10.1038/s41598-017-07647-1;
RA   Villahermosa D., Fleck O.;
RT   "Elp3 and Dph3 of Schizosaccharomyces pombe mediate cellular stress
RT   responses through tRNALysUUU modifications.";
RL   Sci. Rep. 7:7225-7225(2017).
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) (PubMed:22768388). In the elongator complex, acts as a tRNA
CC       uridine(34) acetyltransferase, which mediates formation of
CC       carboxymethyluridine in the wobble base at position 34 in tRNAs (By
CC       similarity). {ECO:0000250|UniProtKB:D5VRB9,
CC       ECO:0000250|UniProtKB:Q02908, ECO:0000269|PubMed:22768388}.
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:0000269|PubMed:22768388}.
CC   -!- SUBUNIT: Component of the elongator complex.
CC       {ECO:0000250|UniProtKB:Q02908}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- DISRUPTION PHENOTYPE: Sensitive to methyl methanesulfonate (MMS, causes
CC       DNA breaks), thiabendazole (TBZ), sirolimus (TORC1 inhibitor), thermal
CC       stress, and cold (PubMed:28775286). Abnormal septation during thermal
CC       stress (PubMed:28775286). Global protein levels are unaffected
CC       (PubMed:28775286). {ECO:0000269|PubMed:28775286}.
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; CU329670; CAB10146.1; -; Genomic_DNA.
DR   PIR; T38469; T38469.
DR   RefSeq; NP_594862.1; NM_001020291.2.
DR   AlphaFoldDB; O14023; -.
DR   SMR; O14023; -.
DR   BioGRID; 278111; 341.
DR   STRING; 284812.O14023; -.
DR   iPTMnet; O14023; -.
DR   MaxQB; O14023; -.
DR   PaxDb; 4896-SPAC29A4-20-1; -.
DR   EnsemblFungi; SPAC29A4.20.1; SPAC29A4.20.1:pep; SPAC29A4.20.
DR   GeneID; 2541614; -.
DR   KEGG; spo:SPAC29A4.20; -.
DR   PomBase; SPAC29A4.20; elp3.
DR   VEuPathDB; FungiDB:SPAC29A4.20; -.
DR   eggNOG; KOG2535; Eukaryota.
DR   HOGENOM; CLU_025983_2_1_1; -.
DR   InParanoid; O14023; -.
DR   OMA; TFETRPD; -.
DR   PhylomeDB; O14023; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:O14023; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
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; ISS:PomBase.
DR   GO; GO:0140018; P:regulation of cytoplasmic translational fidelity; IMP:PomBase.
DR   GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IMP:PomBase.
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   4Fe-4S; Acyltransferase; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..544
FT                   /note="Elongator complex protein 3"
FT                   /id="PRO_0000310360"
FT   DOMAIN          79..369
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   DOMAIN          393..544
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         96
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         106
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         109
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         161
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         472..475
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         495..497
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT   BINDING         528
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
SQ   SEQUENCE   544 AA;  61850 MW;  ACF2CF7C49C6AB5B CRC64;
     MSTSSLAFLK AKACAEIVAE LIASENQNKV INLNALKMRI SKKHQLSESP RLTDIIAAIP
     PDAYLKESLM RKLRAKPVRT ASGIAVVAVM CKPHRCPHIA MTGNVCVYCP GGPDSDFEYS
     TQSYTGYEPT SMRAIRARYD PYEQARGRVE QLRSLGHTVD KVEYIIMGGT FMSLPESYRH
     TFIANLHNAL SGATTEDLDE AVKFSEQSET KCVGITIETR PDYCLDQHLD EMLRYGCTRL
     EIGVQSVYED VARDTNRGHT VKAVCETFQL AKDTGYKVVT HMMPDLPNVG MERDIFQFQE
     YFENPAFRTD GLKLYPTLVI RGTGLYELWK TGRYKNYTPN ALVDLIARIL ALVPPWTRIY
     RIQRDIPMPL VSSGVETGNL RELALNRMRD LGTKCRDIRA REVGMQEVHH KIHPEQVELL
     RRDYTANGGW ETFLSYEDPK QDILIGLLRL RQCSDKTYRP EFTSQPTSLV RELHVYGSAV
     PVHSRDPKKF QHQGFGTLLL EEAERIAKYE HGSKKISVIS GVGVRKYYQK LGYTLDGPYM
     SKWL
//