ID   ARCS_HALVD              Reviewed;         585 AA.
AC   D4GTN6;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Archaeosine synthase {ECO:0000303|PubMed:20129918};
DE            EC=2.6.1.97 {ECO:0000250|UniProtKB:Q58428};
DE   AltName: Full=Glutamine:preQ0-tRNA amidinotransferase {ECO:0000303|PubMed:20129918};
GN   Name=arcS {ECO:0000303|PubMed:20129918, ECO:0000312|EMBL:ADE04890.1};
GN   Synonyms=tgtA2 {ECO:0000303|PubMed:20129918};
GN   OrderedLocusNames=HVO_2008 {ECO:0000312|EMBL:ADE04890.1};
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DS2 / DS70;
RX   PubMed=20129918; DOI=10.1074/jbc.m110.102236;
RA   Phillips G., Chikwana V.M., Maxwell A., El-Yacoubi B., Swairjo M.A.,
RA   Iwata-Reuyl D., de Crecy-Lagard V.;
RT   "Discovery and characterization of an amidinotransferase involved in the
RT   modification of archaeal tRNA.";
RL   J. Biol. Chem. 285:12706-12713(2010).
CC   -!- FUNCTION: Is responsible for the final step in the biosynthesis of
CC       archaeosine, a modified nucleoside present in the dihydrouridine loop
CC       (D-loop) of archaeal tRNA. Catalyzes the conversion of 7-cyano-7-
CC       deazaguanine (preQ0)-modified tRNA to archaeosine-tRNA, transforming a
CC       nitrile group to a formamidine group. {ECO:0000269|PubMed:20129918}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-cyano-7-carbaguanosine(15) in tRNA + H2O + L-glutamine =
CC         archaeosine(15) in tRNA + L-glutamate; Xref=Rhea:RHEA:54084,
CC         Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:14170, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:82850,
CC         ChEBI:CHEBI:138803; EC=2.6.1.97;
CC         Evidence={ECO:0000250|UniProtKB:Q58428};
CC   -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC       {ECO:0000269|PubMed:20129918}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q58428}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lack archaeosine in tRNA
CC       and accumulate preQ0-modified tRNA. {ECO:0000269|PubMed:20129918}.
CC   -!- SIMILARITY: Belongs to the archaeosine synthase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CP001956; ADE04890.1; -; Genomic_DNA.
DR   RefSeq; WP_004041892.1; NZ_AOHU01000038.1.
DR   AlphaFoldDB; D4GTN6; -.
DR   SMR; D4GTN6; -.
DR   STRING; 309800.C498_05321; -.
DR   EnsemblBacteria; ADE04890; ADE04890; HVO_2008.
DR   GeneID; 8924122; -.
DR   KEGG; hvo:HVO_2008; -.
DR   PATRIC; fig|309800.29.peg.1037; -.
DR   eggNOG; arCOG00989; Archaea.
DR   eggNOG; arCOG00990; Archaea.
DR   HOGENOM; CLU_029831_0_0_2; -.
DR   OMA; YPAAHYD; -.
DR   OrthoDB; 21064at2157; -.
DR   UniPathway; UPA00393; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0002948; F:archaeosine synthase activity; IEA:UniProtKB-EC.
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   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; IPR029402; TGT_C2.
DR   InterPro; IPR038250; TGT_C2_sf.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
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; PF01702; TGT; 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   3: Inferred from homology;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..585
FT                   /note="Archaeosine synthase"
FT                   /id="PRO_0000442192"
FT   DOMAIN          516..584
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
SQ   SEQUENCE   585 AA;  64971 MW;  05C628DCB279B7FA CRC64;
     MTDYFEVHAR DGAARIGELR LSDSVTTPAV VDDVLADAGS LWAAERELPD GSDDVLTVLP
     HRSLPAGSAD EVRESFSVAY PDVDFPSAAV VTADTADDFG ADAYVLSDAQ GFVGHARAFR
     DNVIEAKENL PADTALVLSG VATPRNVSLL VYAGVDLVDE KLARARGLEG FYLTSDGEYF
     LEDLDELPCA CEACRKPASE FTRADAADHN ANALRAELAR VRRRVRDGRL RDYVEGQARH
     DQWLTALFRR FDQQYSFMEQ RVPVIRDSEL TAASEESIDR VEIQRFADRV TKRYRNRFDN
     PLVLLPCSAK KPYSESQSHR QFQEAVQYRA HMVSMTSPIG VVPQELELTY PAQHYDSVVT
     GDWSEDEKSF VAEVLRRYLE RNDYPRIIAH LPPGAYTDIV ERVADDLDLD VEFTVSEHPT
     TTESIGNLMR TLDGEPKFTR EEREHNVVKA LADYQLGPDA GDALFSDVAL EMTSRYPKLQ
     VWNDAGVQLA TMVPQYGVLS FTLEGAKVWR DSDAPTKTVE IDGFVPHGSV LAPGVVDADE
     DIRPGDEVVV EGPKAFAIGR AEMGGRELVE STRGIGVEIR HVEER