ID   ARCSA_THEAC             Reviewed;         510 AA.
AC   Q9HJP3;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Archaeosine synthase subunit alpha {ECO:0000303|PubMed:31740832};
DE            EC=4.3.3.- {ECO:0000269|PubMed:31740832};
DE   AltName: Full=Archaeosine synthase, lysine transferase subunit {ECO:0000303|PubMed:31740832};
GN   Name=arcS {ECO:0000303|PubMed:31740832};
GN   OrderedLocusNames=Ta0924 {ECO:0000312|EMBL:CAC12053.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=31740832; DOI=10.1038/s41589-019-0390-7;
RA   Yokogawa T., Nomura Y., Yasuda A., Ogino H., Hiura K., Nakada S., Oka N.,
RA   Ando K., Kawamura T., Hirata A., Hori H., Ohno S.;
RT   "Identification of a radical SAM enzyme involved in the synthesis of
RT   archaeosine.";
RL   Nat. Chem. Biol. 15:1148-1155(2019).
CC   -!- FUNCTION: Functions in the biosynthesis of archaeosine, a modified
CC       nucleoside present in the dihydrouridine loop (D-loop) of archaeal
CC       tRNAs. Catalyzes the addition of L-lysine to the cyano group of 7-
CC       cyano-7-deazaguanine (preQ0)-modified tRNAs at position 15, to generate
CC       q0kN15-tRNA, a q0N lysine adduct identified as 7-N-[(5S)-5-amino-5-
CC       carboxypentyl]formamidino-7-deazaguanosine.
CC       {ECO:0000269|PubMed:31740832}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-cyano-7-carbaguanosine(15) in tRNA + L-lysine = 7-N-[(5S)-5-
CC         amino-5-carboxypentyl]formamidino-7-deazaguanosine(15) in tRNA;
CC         Xref=Rhea:RHEA:63216, Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:16288,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:82850, ChEBI:CHEBI:145542;
CC         Evidence={ECO:0000269|PubMed:31740832};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63217;
CC         Evidence={ECO:0000305|PubMed:31740832};
CC   -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC       {ECO:0000269|PubMed:31740832}.
CC   -!- SUBUNIT: Forms a robust complex with the archaeosine synthase beta
CC       subunit RaSEA, likely an alpha(2)beta(2) heterotetrameric structure.
CC       Formation of this complex highly increases lysine transfer activity.
CC       {ECO:0000250|UniProtKB:Q5JHG7}.
CC   -!- SIMILARITY: Belongs to the archaeosine synthase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AL445065; CAC12053.1; -; Genomic_DNA.
DR   RefSeq; WP_010901333.1; NC_002578.1.
DR   AlphaFoldDB; Q9HJP3; -.
DR   SMR; Q9HJP3; -.
DR   STRING; 273075.Ta0924; -.
DR   EnsemblBacteria; CAC12053; CAC12053; CAC12053.
DR   GeneID; 1456459; -.
DR   KEGG; tac:Ta0924; -.
DR   eggNOG; arCOG00990; Archaea.
DR   HOGENOM; CLU_029831_0_0_2; -.
DR   OMA; YPAAHYD; -.
DR   OrthoDB; 21064at2157; -.
DR   BRENDA; 2.6.1.97; 6324.
DR   UniPathway; UPA00393; -.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 2.30.130.10; -; 1.
DR   Gene3D; 3.20.20.105; -; 1.
DR   InterPro; IPR040777; DUF5591.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   Pfam; PF17884; DUF5591; 1.
DR   Pfam; PF01472; PUA; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome; tRNA processing.
FT   CHAIN           1..510
FT                   /note="Archaeosine synthase subunit alpha"
FT                   /id="PRO_0000450070"
FT   DOMAIN          427..510
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
SQ   SEQUENCE   510 AA;  58243 MW;  AB1F28439D575143 CRC64;
     MIEDQALFGY ARYGKVDDVV YPSVIASGNG INYGDSDIEI LGDRIPRQIL YPAKIKQEIL
     ETDKLVIIPN GAELVRKPKD LVRIIMDIHS RYGFSKLIMI SGISDPYSIP ALVYLGISFF
     DSSILEMEGK MGYRFTPFGI EKADHDVSSE NAIFISDMMH IIQRSISDGT LRELIEKAVI
     SSKAAEMVRI ADYSYYQDFE SVFPVRTPYI KANTIEDLYR PDLIRYRNYI SESYVKPDAD
     IALILPCSAK KPYSRSKSHQ KVIGALGNLR RFIHEVIVTS PIGIVPRDLE ETYPARFYDI
     PVIGLWYEDE KIMMKRMMSS YMGRNRYRKV IAFIPEDLDF ITEAIPYPHE VIEFKSSNLQ
     RLREVIQREI AGGKAVNQKV AKYNSILRYQ FGEWILPLVS GYTIRRNYNQ DMIVKDGKIL
     FVYNENLGKF TINKASADMF IKNGKFLVEI DDFKPTSNVY AMGVVDATED IRQEDEVVLV
     HSGEVRGVGI AKMPARAMIE LKKGIAVKVR