ARCSA_THEKO
ID ARCSA_THEKO Reviewed; 568 AA.
AC Q5JHG7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=TK2156 {ECO:0000312|EMBL:BAD86345.1};
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, PATHWAY, AND
RP INTERACTION WITH RASEA.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
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:0000269|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:0000269|PubMed:31740832}.
CC -!- DISRUPTION PHENOTYPE: Archaeosine is no more detected among the
CC modified nucleosides in tRNA fractions. {ECO:0000269|PubMed:31740832}.
CC -!- SIMILARITY: Belongs to the archaeosine synthase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AP006878; BAD86345.1; -; Genomic_DNA.
DR RefSeq; WP_011251106.1; NC_006624.1.
DR AlphaFoldDB; Q5JHG7; -.
DR SMR; Q5JHG7; -.
DR STRING; 69014.TK2156; -.
DR EnsemblBacteria; BAD86345; BAD86345; TK2156.
DR GeneID; 3235376; -.
DR KEGG; tko:TK2156; -.
DR PATRIC; fig|69014.16.peg.2111; -.
DR eggNOG; arCOG00990; Archaea.
DR HOGENOM; CLU_029831_0_0_2; -.
DR InParanoid; Q5JHG7; -.
DR OMA; YPAAHYD; -.
DR OrthoDB; 21064at2157; -.
DR PhylomeDB; Q5JHG7; -.
DR BRENDA; 2.6.1.97; 5246.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000000536; 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; 3.10.450.90; -; 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; IPR029402; TGT_C2.
DR InterPro; IPR038250; TGT_C2_sf.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR Pfam; PF17884; DUF5591; 1.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF14810; TGT_C2; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome; tRNA processing.
FT CHAIN 1..568
FT /note="Archaeosine synthase subunit alpha"
FT /id="PRO_0000450071"
FT DOMAIN 496..565
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
SQ SEQUENCE 568 AA; 65475 MW; 4133AA73A9D42EA3 CRC64;
MEVIKHEGPG RLGVVRLGDY SFRTPALVGI DFTLSPFNSF FHPKEPGEYD FNLAPSIPLG
FYTPDEVIQK AIGRLWSVNY DGFNAFYLPA LRRTEYLEEF FKIIDRHNFD AVYLGNSKIL
IKEYRYFVRI LRELRERFPN VMIIADLEPF FYPLAVYLGI DAFDTRSLKL YDFEGKGFTQ
FSPFLWSNEP NSLDFAREVI LLVRKALEEG KLRYLVENFF PTQYNAGILR IADLEHPDYL
EKYTPIQKET VYFISDASIR RPEVKRWHER VLERFTPPKN VELLLLFPCS AKKPYSFSRS
HTLYRRAVKE ALGSGTSKVH ELILTSPFGV VPREWEWLAK YDIVVTGHWS EEEIKPAAEL
LAKTLEKYPE DIPIVAHLDE AYVEIAKLAS ELSGREIIFT DVKNGTTSHE SLRSLTETLR
EFQIEGTKED RTYRYFENIR KVFDFYFGVG AGEAILPENG QVKGSKMLRI FVEGQQTGTF
TDGVISVTPY GMQRIYDALK SYWVKIDFEL RGDVFAVGVE EADPRIRPDD IVGIVRDEKV
VGVGKAVLSG EEMVRAKKGV AVKVRKRV
