ID M0PHI3_9EURY Unreviewed; 582 AA.
AC M0PHI3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Histone acetyltransferase, ELP3 family protein {ECO:0000313|EMBL:EMA68245.1};
GN ORFNames=C461_06674 {ECO:0000313|EMBL:EMA68245.1};
OS Halorubrum aidingense JCM 13560.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1230454 {ECO:0000313|EMBL:EMA68245.1, ECO:0000313|Proteomes:UP000011575};
RN [1] {ECO:0000313|EMBL:EMA68245.1, ECO:0000313|Proteomes:UP000011575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13560 {ECO:0000313|EMBL:EMA68245.1,
RC ECO:0000313|Proteomes:UP000011575};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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|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|PIRSR:PIRSR005669-1};
CC -!- PATHWAY: tRNA modification. {ECO:0000256|ARBA:ARBA00005217}.
CC -!- SIMILARITY: Belongs to the ELP3 family.
CC {ECO:0000256|ARBA:ARBA00005494}.
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:EMA68245.1}.
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DR EMBL; AOJI01000019; EMA68245.1; -; Genomic_DNA.
DR RefSeq; WP_007999731.1; NZ_AOJI01000019.1.
DR AlphaFoldDB; M0PHI3; -.
DR STRING; 1230454.C461_06674; -.
DR PATRIC; fig|1230454.4.peg.1352; -.
DR OrthoDB; 49957at2157; -.
DR Proteomes; UP000011575; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR013785; Aldolase_TIM.
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; 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 Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR005669-1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR005669-
KW 1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR005669-1};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMA68245.1};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 96..401
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 410..582
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 COMPBIAS 14..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
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 118
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 121
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 582 AA; 65151 MW; 12C42CD16995EA66 CRC64;
MSTDAASDAD ADADGEGGAE KSGERDEPEA FTRACEALVD RILAGEIDRD DLESAKLDAC
SEFSSPKVPK NTEILDHTPA EARDDVIEVV QRKPVRTASG VSPIAIMTSP KLCPHGKCLY
CPGGPASEFS SAQSYTGHEP AAARGKQNDY DPYGQVTLRL EQLRKIGHPV DKAELILMGG
TMTARSHDYQ EWFVKRALQA MNDYDLDKEP EPAEGESFAP DPEAAEFEYL EDVIAENETN
EIRNIGTTFE TKPDWCDPEQ IDRMLDLGGT KVEVGVQTTY ERINREMHRG HGNEASRNAN
RRLRDAGFKV GFHMMPGQPG MTKEMCVEDF RQLFANPEWR PDYLKIYPTL VVGGTRVYDR
WRRDEFEPLS NEEAADVVAE VMDLIPKYTR LQRVQRDIPA DFIEGGVWKS NLRQLADQRA
EEKGIVQRDI RAREVGHNDA DPDPDDVELD VFTYEAGGGT EHFISFEDPV RDLLVGFCRL
RFPSFSPDQP GAPGTETDAT RRELADAALI RELHVYGTEV AIGGDGDWQH QGYGQKLLER
AEELARDAGY RKLAIISGIG AREYYRNKLG YHQDGPYVSK RL
//
