ID   C5YAW5_SORBI            Unreviewed;       571 AA.
AC   C5YAW5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=SORBI_3006G125900 {ECO:0000313|EMBL:EES12405.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:EES12405.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EES12405.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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; CM000765; EES12405.1; -; Genomic_DNA.
DR   RefSeq; XP_002448077.1; XM_002448032.1.
DR   AlphaFoldDB; C5YAW5; -.
DR   STRING; 4558.C5YAW5; -.
DR   EnsemblPlants; EES12405; EES12405; SORBI_3006G125900.
DR   GeneID; 8073682; -.
DR   Gramene; EES12405; EES12405; SORBI_3006G125900.
DR   KEGG; sbi:8073682; -.
DR   eggNOG; KOG2535; Eukaryota.
DR   HOGENOM; CLU_025983_2_1_1; -.
DR   InParanoid; C5YAW5; -.
DR   OMA; TFETRPD; -.
DR   OrthoDB; 46095at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000000768; Chromosome 6.
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; 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   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:UP000000768};
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          106..396
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          420..571
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         123
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         133
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         136
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   571 AA;  63730 MW;  F47E75BA5414D7D7 CRC64;
     MATAAAAAVA APEQPRRRKP APGRGGVALP AGISEEEARV RAIAEIVSAM GELSRRGEDV
     DLNALKSAAC RRYGLARAPK LVEMIAAVPE ADRAALLPRL RAKPVRTASG IAVVAVMSKP
     HRCPHIATTG NICVYCPGGP DSDFEYSTQS YTGYEPTSMR AIRARYNPYV QARSRIDQLK
     RLGHSVDKVE FILMGGTFMS LPADYRDYFI RNLHDALSGH TSANVEEAIC YSEHSAVKCI
     GMTIETRPDY CLGPHLRQML SYGCTRLEIG VQSTYEDVAR DTNRGHTVAA VADCFCLAKD
     AGFKVVAHMM PDLPNVGVER DLESFREFFE SPAFRADGLK IYPTLVIRGT GLYELWKTGR
     YRNYPPELLV DIVARILSMV PPWTRVYRVQ RDIPMPLVTS GVEKGNLREL ALARMEDLGL
     KCRDVRTREA GIQDIHHKIR PDEVELVRRD YAANEGWETF LSYEDTRQDI LIGLLRLRKC
     GRNVTCPELV GRCSIVRELH VYGTAVPVHG RDVDKLQHQG YGTLLMEEAE RIAQKEHRSK
     KLAVISGVGT RHYYRKLGYE LEGPYMVKTL A
//