ID   ATGT_THEVO              Reviewed;         632 AA.
AC   Q977Z3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
DE            EC=2.4.2.48 {ECO:0000255|HAMAP-Rule:MF_01634};
DE   AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01634};
DE   AltName: Full=Archaeal tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
GN   Name=tgtA {ECO:0000255|HAMAP-Rule:MF_01634}; OrderedLocusNames=TV1524;
GN   ORFNames=TVG1580555;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC   -!- FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine
CC       (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal
CC       tRNAs. {ECO:0000255|HAMAP-Rule:MF_01634}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-
CC         carbaguanosine(15) in tRNA + guanine; Xref=Rhea:RHEA:43164,
CC         Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:10372, ChEBI:CHEBI:16235,
CC         ChEBI:CHEBI:45075, ChEBI:CHEBI:74269, ChEBI:CHEBI:82850; EC=2.4.2.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01634};
CC   -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01634}.
CC   -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01634}.
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DR   EMBL; BA000011; BAB60666.1; -; Genomic_DNA.
DR   RefSeq; WP_010917753.1; NC_002689.2.
DR   AlphaFoldDB; Q977Z3; -.
DR   SMR; Q977Z3; -.
DR   STRING; 273116.14325763; -.
DR   EnsemblBacteria; BAB60666; BAB60666; BAB60666.
DR   GeneID; 1442213; -.
DR   KEGG; tvo:TVG1580555; -.
DR   eggNOG; arCOG00989; Archaea.
DR   eggNOG; arCOG00991; Archaea.
DR   HOGENOM; CLU_030083_0_0_2; -.
DR   OMA; FPCSCPV; -.
DR   OrthoDB; 10236at2157; -.
DR   PhylomeDB; Q977Z3; -.
DR   UniPathway; UPA00393; -.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; 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   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_01634; TgtA_arch; 1.
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; IPR004804; TgtA.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   InterPro; IPR004521; Uncharacterised_CHP00451.
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; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
DR   TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Metal-binding; Transferase; tRNA processing; Zinc.
FT   CHAIN           1..632
FT                   /note="tRNA-guanine(15) transglycosylase"
FT                   /id="PRO_0000247888"
FT   DOMAIN          553..628
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ   SEQUENCE   632 AA;  71957 MW;  FFB7F1B1543E0C36 CRC64;
     MEIRERDGLA RIARFDTPHG TIETPTVLPV INPNIMDITP EEMKKYGVHG VITNSYIILR
     NDRLREEAEK YGVHSLIGYD GPVMTDSGTF QSYVYGSVEF NNRQVVEFQK TIGSDILTIL
     DIFTTPSSSR QEVENAITET YRRMLEVNDA GGMIAGPIQG GIYPDLRKRS AELMNSTNAS
     YLPIGGVVPL LESYEYDKLV DIILNSKLNV SFGKPIHLFG GGHPMFFAFA VYLGVDLFDS
     ASYVKYAKDD RLIYPDGTRD LARIIEIPEW SPLFDKYTVK ELKELPKEQR SVELSRHNLK
     AIFMEISEIR ERIYEESMDQ YLAQKAKSHP SLLKAYVKVM QYSKMLEKYQ DLFKKAAYFF
     YDSFSTKNTY VARLEKFTSK YLTSKKKETY VFSRKDWLPG YTNLNFVRDV YERTECNALI
     PWSGIMVPAE LENTYPIEQT VSSGLEPDPD VSAISESISP FDIRVYKGES VDSDKIRSFD
     LEKIRTIADY QFGYGIGKDF FKDDVRIFKS KTGRIRGVFD KGNKLIATLR NDGFFTLTFH
     GATLLYNVSK SPNLRVFVKN ESAEYNAKGY SVFFKFILDA DPDIIAKNET LVVNENGELV
     AVGKATVSGK ELREYSDGIA VKIHEGRDQS AK