ID A0A094CZT9_9PEZI Unreviewed; 581 AA.
AC A0A094CZT9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=V497_04133 {ECO:0000313|EMBL:KFY59686.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY59686.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY59686.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY59686.1}.
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DR EMBL; JPJZ01000874; KFY59686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CZT9; -.
DR STRING; 1420910.A0A094CZT9; -.
DR HOGENOM; CLU_025983_2_1_1; -.
DR OrthoDB; 46095at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000029268; 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; cd04301; NAT_SF; 1.
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:UP000029268};
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 103..393
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 417..575
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
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 130
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"
SQ SEQUENCE 581 AA; 65741 MW; 7E69705567176108 CRC64;
MATETATMLM PEKRRLPKDP NLPPENERYL RACSDVASAL IQEHEAQQDP SKPKKDINLN
SLRAKMSKKH RLSNIPPLTA IIAAIPEHYK KYILPKLIAK PIRTSSGIAV VAVMCKPHRC
PHIAYTGNIC VYCPGGPDSD FEYSTQSYTG YEPTSMRAIR ARYDPYEQAR GRVDQIKSLG
HSVDKVEYII MGGTFMSLAE SYRESFISQL HNALSGYQGT NVDEAVQAGE MSNIKCVGIT
IETRPDYCLQ PHLTDMLRYG CTRLEIGVQS LYEDVARDTN RGHTVASVAE TFCLAKDAGF
KVVSHMMPDL PNVGMERDLD QFREYFESPA FRTDGLKIYP TLVIRGTGLY ELWRTGRYKN
YTPNALIDIV ARILALIPPW TRIYRVQRDI PMPLVTSGVE NGNLRELALS RMKDFGTTCR
DVRTREVGIN EVKNKIRPSQ VELVRRDYAA NGGWETFLAY EDPKQDILIA LLRLRKCSPT
HTFRPELTGQ QTSMVRELHV YGSAVPVHAR DPRKFQHQGY GTLLMEEAER IARDEHGSAK
ISVISGVGVR SYYAKLGYHL DGVYMSKDIK RLEDDDSDDD F
//
