ATGT_THEKO
ID ATGT_THEKO Reviewed; 580 AA.
AC Q5JHC0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-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=TK0760;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(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; AP006878; BAD84949.1; -; Genomic_DNA.
DR RefSeq; WP_011249711.1; NC_006624.1.
DR AlphaFoldDB; Q5JHC0; -.
DR SMR; Q5JHC0; -.
DR STRING; 69014.TK0760; -.
DR EnsemblBacteria; BAD84949; BAD84949; TK0760.
DR GeneID; 3235716; -.
DR KEGG; tko:TK0760; -.
DR PATRIC; fig|69014.16.peg.740; -.
DR eggNOG; arCOG00989; Archaea.
DR eggNOG; arCOG00991; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR InParanoid; Q5JHC0; -.
DR OMA; FPCSCPV; -.
DR OrthoDB; 10236at2157; -.
DR PhylomeDB; Q5JHC0; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.10.450.90; -; 1.
DR Gene3D; 3.20.20.105; -; 1.
DR Gene3D; 3.90.1020.10; -; 1.
DR HAMAP; MF_01634; TgtA_arch; 1.
DR InterPro; IPR038370; ArcTGT_C1_sf.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR032729; TGT_C1.
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; PF14809; TGT_C1; 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; Reference proteome; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..580
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_0000247883"
FT DOMAIN 504..579
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 192
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 580 AA; 66206 MW; E1FB815398275F3E CRC64;
MVDFRFEVKA RDASGRIGKL TVNGKTVETP AIMPVINPKQ LIVTPKELKE MGFGMIITNS
YIIYKTPELR EKALEVGIHK LLDYDGIIEV DSGSFQLMRY GGVEVTNREI VEFQHEIGVD
IGTFLDIPTP PDAPREKAEE DLRITLERAK EAEEIKEIAM NAAVQGSTYP DLRTYAAREL
SRMNFEIHPI GAVVPLMESY RYRDLVDVVI ASKVGLRPDR PVHLFGAGHP MIFALAVAMG
IDLFDSASYA LYAKDDRYMT PEGTKRLEEL EYFPCSCPVC SRYTPQELRE MPKEERTRLL
AIHNLWVIRE ELNRVKQAIK EGELWRLVDE RARSHPKLYA AYKRLLEYRE YLEKNEPVTK
ASAFFKVSEE ALRWPIVERA RERAERVRSK FPETISHPIF GEIPKYLSLS YPFAQSEGEE
DFTVEKPEKG EARKYVMAVA EYQFGEGAGE AFKDAFVELS RKTGMPRQIK AKGKHLATFR
AEDGLLTLGI EGAKRLHEVL PFPRMRVVVD EDAEPFARRG KNVFAKFVVD ADLNIRPYDE
VLVVNRNDEL LATGQTLLNG EELKIFQQGL AVKVRRGVEK
