ID   ATGT_NANEQ              Reviewed;         410 AA.
AC   Q74N90;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 92.
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=NEQ124;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR38979.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE017199; AAR38979.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q74N90; -.
DR   SMR; Q74N90; -.
DR   STRING; 228908.NEQ124; -.
DR   EnsemblBacteria; AAR38979; AAR38979; NEQ124.
DR   KEGG; neq:NEQ124; -.
DR   PATRIC; fig|228908.8.peg.129; -.
DR   HOGENOM; CLU_030083_0_0_2; -.
DR   OMA; YFERERN; -.
DR   UniPathway; UPA00393; -.
DR   Proteomes; UP000000578; 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; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Metal-binding; Reference proteome; Transferase;
KW   tRNA processing; Zinc.
FT   CHAIN           1..410
FT                   /note="tRNA-guanine(15) transglycosylase"
FT                   /id="PRO_0000247878"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ   SEQUENCE   410 AA;  47647 MW;  C7E3F1C0C7F56C8E CRC64;
     MKIKFEIKYK DAAGKVGKIK LNGKTIETPY LFPVINPFKQ ELPIKEIKKM GFNAIITNAY
     ILFKRKEEVM EKGIHNFLGF DGIIETDSGA YQLLQYGDID IENEDIIYFQ NEIGVDIGNI
     LDIPSYGKTY EEAKKDLEIT LERLKQAIEM ANFAINGPIQ GDKYLDLRYK ALEEVSKLDI
     DIYAIGGIVP YMNQYKIESL AKIIGPLLLD IPRDRPVHLF GLGHPLIMPL FVALGADLFD
     SASYSLFAKE ERILTPFRTF RLEDLTDSYI LDYKASELKG MENKTYIIAK HNLLVLRNEI
     NFIRDLIRQN RLWDYVIIKA HAHPSIYFAT KYVLENLYEK LKEHEPITKR VGILYQGELT
     ELRSDLRYAI EQLKKLDKSQ INDILDYAWP FGQFEIGEKD KKLFFQRFLK