ID L0K2X2_9EURY Unreviewed; 568 AA.
AC L0K2X2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Histone acetyltransferase, ELP3 family {ECO:0000313|EMBL:AGB38458.1};
GN ORFNames=Natoc_2697 {ECO:0000313|EMBL:AGB38458.1};
OS Natronococcus occultus SP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronococcus.
OX NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB38458.1, ECO:0000313|Proteomes:UP000010878};
RN [1] {ECO:0000313|EMBL:AGB38458.1, ECO:0000313|Proteomes:UP000010878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP4 {ECO:0000313|EMBL:AGB38458.1,
RC ECO:0000313|Proteomes:UP000010878};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA Klenk H.-P.;
RT "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003929; AGB38458.1; -; Genomic_DNA.
DR RefSeq; WP_015321898.1; NC_019974.1.
DR AlphaFoldDB; L0K2X2; -.
DR STRING; 694430.Natoc_2697; -.
DR GeneID; 14404484; -.
DR KEGG; nou:Natoc_2697; -.
DR eggNOG; arCOG01361; Archaea.
DR HOGENOM; CLU_025983_2_1_2; -.
DR OrthoDB; 49957at2157; -.
DR Proteomes; UP000010878; Chromosome.
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; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000010878};
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:AGB38458.1};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 81..384
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 112..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
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 101
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 104
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 568 AA; 64551 MW; 5F775B224E2845FD CRC64;
MSTETPEPTE TDAFEKVCET LVERILDGEI DRDEVEKAKL EACSEHSAPK VPKNSELLDH
APQEYREDLE AVLQRKPVRT ASGVSPVAIM TSPERCPHGK CLYCPGGPDS EFSSSQSYTG
EEPAAARGVQ NDYDPYGQVT LRLEQLREIG HPVDKVELIL MGGTMTARSH DYQEWFVKRA
LEAMNDYDVD KEPEPAEGVS FAEDPEEYEF KYLEDVIAEN ETNEIRNIGT TFETKPDWCD
PEQIDRMLEL GGTKVEVGVQ TTYERINREM HRGHGAQASI DANRRLRNAG FKVGFHMMPG
QPGMSKEMCL EDFRRLFEQE QWKPDYLKIY PTLIVRGTAT YDWWHKGEFD PLDNEEAAEL
VAEIKDMIPC YTRLQRVQRD IPADFIDAGV WKSNLRQLAR KRMDEHGWSC DCIRCREAGH
HDEEPEDVEL DVMSYDACGG TEQFISFEDF EKDLLVGFCR LRFPHGDGPA DRTAAAAANG
DRLRPELENA ALVRELHVYG SEVAMGDEGE TGQHQHKGYG RRLMERAEEL AADAGYDKIS
VISGIGAREY YRNKLGYHQD GPYVSKRL
//
