ID   ATGT_SULTO              Reviewed;         491 AA.
AC   Q975U5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=STK_03270;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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; BA000023; BAB65304.1; -; Genomic_DNA.
DR   RefSeq; WP_010978287.1; NC_003106.2.
DR   AlphaFoldDB; Q975U5; -.
DR   SMR; Q975U5; -.
DR   STRING; 273063.STK_03270; -.
DR   PRIDE; Q975U5; -.
DR   EnsemblBacteria; BAB65304; BAB65304; STK_03270.
DR   GeneID; 1458241; -.
DR   KEGG; sto:STK_03270; -.
DR   PATRIC; fig|273063.9.peg.383; -.
DR   eggNOG; arCOG00989; Archaea.
DR   OMA; FPCSCPV; -.
DR   OrthoDB; 10236at2157; -.
DR   UniPathway; UPA00393; -.
DR   Proteomes; UP000001015; 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..491
FT                   /note="tRNA-guanine(15) transglycosylase"
FT                   /id="PRO_0000247886"
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         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ   SEQUENCE   491 AA;  56987 MW;  24264C29C062EA42 CRC64;
     MVGEFEIKDE DLAGRIGIIE TKSGKLETPV FFPVINPFKS EISIKDIENL GFKNLITNAY
     LIKKITNTKI QDIHSFLQFN GVIMTDSGAY QILQYGNIEV TNREIVEYER DINTDIAVYL
     DLPTGDTNSR DEAINSVKIT LERAKEIEDI VKNDSERIWV HPIQGGRFLD LVEYSAIEAD
     KNEAFKMLAL GSPTVVMEKY DYSLLIDMVF IAKSNVSRGK PFHLFGGGLP HIMPLVIALG
     VDSFDSASYI LYARDNRYIT RSRVYRLEEL EYFPCSCPIC LKYTPKELLE LPKEERTKLL
     ALHNLYVIKE ELNAIKQAIR EGRLFEYIQE KAYSHPAVYS AFKKILKYKD YLEKYDPRVK
     GNIRGIFLFD LKSLNRPEIV RHYNFLDRIN KNNDKAIIIC EKRENILKKV KNNENVDIYL
     FNPFYGLIPI NLIEVYPYFQ TEYPEEIDED VLRYIESKIV EFVRSKGYTK IDFIGCEKYL
     SHINSIGAFF S