ID   ATGT_NATPD              Reviewed;         520 AA.
AC   Q3IR98;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=NP_2508A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49345.1; -; Genomic_DNA.
DR   RefSeq; WP_011322971.1; NC_007426.1.
DR   AlphaFoldDB; Q3IR98; -.
DR   SMR; Q3IR98; -.
DR   STRING; 348780.NP_2508A; -.
DR   EnsemblBacteria; CAI49345; CAI49345; NP_2508A.
DR   GeneID; 3703241; -.
DR   KEGG; nph:NP_2508A; -.
DR   eggNOG; arCOG00989; Archaea.
DR   HOGENOM; CLU_030083_0_0_2; -.
DR   OMA; FPCSCPV; -.
DR   OrthoDB; 10236at2157; -.
DR   UniPathway; UPA00393; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_01634; TgtA_arch; 1.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR004804; TgtA.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Metal-binding; Reference proteome; Transferase;
KW   tRNA processing; Zinc.
FT   CHAIN           1..520
FT                   /note="tRNA-guanine(15) transglycosylase"
FT                   /id="PRO_0000247879"
FT   REGION          485..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        93
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ   SEQUENCE   520 AA;  57073 MW;  0319B50A8442C30D CRC64;
     MRDIFERRDG DAAGRIGELS VPRAGTTVET PALLPVVNPH IRTIAPAELE STFGAQILIT
     NGYILYGSDE YRERALADGL HDLFDFSGAI MTDSGSFQLS EYGEISVTNE EILRFQRDIG
     SDIGTPVDIP TPPEASREQT AADLETTKAR LEAAETVDTG EMLVNAPVQG GTYPDLREEA
     AEHAYGTTLD VFPVGAVVPL MNSYRYGDMI EAILGAKRGL GADAPVHLFG AGHPMMFALA
     VAAGCDLFDS AAYALYARDD RYLTVAGTDH LDDLEYLPCS CPVCADHTPA ELQAEDDTER
     ERLLARHNLH VSFQELRTIK QAIKKGNLLE LVERRARGHP AMVDGYRALL EAADQLERDD
     PVSKGSFFYL SGESARRPEV KRHHDRLSRL SVDGDRVLLS EGGDNSRFDE TWRLQPPFGP
     FPPALSDSYP LTAELPERLD DRAYEAAAKG VRRLVDDHPE TEFAVAHWGW PDAALDSLPD
     GVELLRLGAD SDHPERDSAQ SDMDGDEPKE DYPPGEDENA