ID A0A067CB50_SAPPC Unreviewed; 559 AA.
AC A0A067CB50;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=SPRG_07312 {ECO:0000313|EMBL:KDO27683.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO27683.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO27683.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO27683.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583215; KDO27683.1; -; Genomic_DNA.
DR RefSeq; XP_012201494.1; XM_012346104.1.
DR AlphaFoldDB; A0A067CB50; -.
DR STRING; 695850.A0A067CB50; -.
DR EnsemblProtists; KDO27683; KDO27683; SPRG_07312.
DR GeneID; 24129593; -.
DR KEGG; spar:SPRG_07312; -.
DR VEuPathDB; FungiDB:SPRG_07312; -.
DR OMA; TFETRPD; -.
DR OrthoDB; 46095at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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; 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; 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:UP000030745};
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 102..383
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 407..559
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 119
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 129
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 132
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 559 AA; 62855 MW; 3EAC3F1CC23FC38C CRC64;
MGLGLFHKKA HTPPAPITDD TDVMSSNAGV DSETYVKAIS SIVEEIIKAY EKQEPVNMTR
LKNDVAKGYR LPSMPKLVDI ISAIPEEYKE ELLPFLKAKP VRTASGIAVV AVMCKPHRCP
HIAMTGNICV YCPGGPDSDF EYSTQAYTGY EPTSMRAIRA RYNPYVQTKT RVDQLRRLGH
NVDRCVEFIV MGGTFLSLDK EYRDYFIRNL HDALSGHTSA SVAEACTAIT IETRPDYCLK
PHLNDMLAYG CTRIEIGVQS IYEDVARDSN RGHTVAAVCH SFQLAKDCGY KIVAHMMPDL
PNMGMERDLN GFKEYFENPL FRTDGLKIYP TLVIRGTGLY ELWKTGQYKN YSPNELVDLM
ARLLALVPPW TRVYRIQRDI PMPLVTSGVE NGNLRELALA RMKDLGLACR DVRTREVGMK
GIHDQVAPDH VELIRRDYVA NGGWETFLAY EDVDQDILVG LLRLRQASAT AFRPEIPPGT
SIVRELHVYG SAVPLHARDP TKFQHQGFGT LLMEEAERIA RDEHGSHKIV VISGVGTRDY
YRKLGYTLEG PYMVKDLEG
//
