ID Q9HIM8_THEAC Unreviewed; 515 AA.
AC Q9HIM8;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Probable Histone and other Protein Acetyltransferase (Yeast HPA1) {ECO:0000313|EMBL:CAC12432.1};
GN OrderedLocusNames=Ta1311 {ECO:0000313|EMBL:CAC12432.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075 {ECO:0000313|EMBL:CAC12432.1, ECO:0000313|Proteomes:UP000001024};
RN [1] {ECO:0000313|EMBL:CAC12432.1, ECO:0000313|Proteomes:UP000001024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165
RC {ECO:0000313|Proteomes:UP000001024};
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.L., Koretke K.K., Volker C.,
RA Mewes H.W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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}.
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DR EMBL; AL445067; CAC12432.1; -; Genomic_DNA.
DR RefSeq; WP_010901717.1; NC_002578.1.
DR AlphaFoldDB; Q9HIM8; -.
DR STRING; 273075.gene:9572534; -.
DR PaxDb; 273075-Ta1311; -.
DR DNASU; 1456787; -.
DR EnsemblBacteria; CAC12432; CAC12432; CAC12432.
DR GeneID; 1456787; -.
DR KEGG; tac:Ta1311; -.
DR eggNOG; arCOG01361; Archaea.
DR HOGENOM; CLU_025983_2_1_2; -.
DR InParanoid; Q9HIM8; -.
DR OrthoDB; 49957at2157; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; 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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.30.750.200; -; 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; 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; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Iron {ECO:0000256|PIRSR:PIRSR005669-1};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR005669-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR005669-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001024};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 64..335
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 81
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 86
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 89
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 515 AA; 59073 MW; EFDF7438CA01AE93 CRC64;
MDFFEEMRDV LLSGQIKDKE DLEDVKLELS KKYGLDYVPS DVEILNSFNF SEDVKKILRR
KPTRTISGVA VVAAMTSPER CPHGKCIFCP GGVDNNSPQS YTGYEPAALR GRNNAYDPYM
ETFNRIKQLE TIGHDTSKID LIIMGGTFTA RDPAYQRNFV KGCLDAMNGS IGNSLEESIR
INETSRHRCI GLTVETKPDW FFEREIDEAL AYGTTKVELG VQNIDDRILA INNRGHTVAD
IARSTQLARD AGLKIVYHIM PGMYGSSFEK DLKSFDLMIN DERFKPDMLK IYPTLVTQGT
GLYNLWKNGK YRPYTTAETV DLIVEFMRRM PDWIRIQRIQ RDIPVQFIVA GVKRSDIRNL
VERRMREEGI KTGEIRYREI GHGTVKEENV ILKVEGYNAG GGKEYFISYV TESNRIIGFV
RLRIPSDRAH RQEVMNTAII RELKVFGQEV PVGRHEEDEW QHRGFGNRLV QEAERITLEE
GLHRILVISG IGVREYFRKR GYEDLGPYVA KRLSS
//
