TGT_CAEEL
ID TGT_CAEEL Reviewed; 400 AA.
AC Q23623;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03218};
DE EC=2.4.2.64 {ECO:0000255|HAMAP-Rule:MF_03218};
DE AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_03218};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_03218};
GN Name=tgt-1 {ECO:0000255|HAMAP-Rule:MF_03218}; ORFNames=ZK829.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Catalytic subunit of the queuine tRNA-ribosyltransferase
CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs
CC through a double-displacement mechanism. The nucleophile active site
CC attacks the C1' of nucleotide 34 to detach the guanine base from the
CC RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor
CC active site deprotonates the incoming queuine, allowing a nucleophilic
CC attack on the C1' of the ribose to form the product.
CC {ECO:0000255|HAMAP-Rule:MF_03218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(34) in tRNA + queuine = guanine + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:16633, Rhea:RHEA-COMP:10341, Rhea:RHEA-
CC COMP:10345, ChEBI:CHEBI:16235, ChEBI:CHEBI:74269, ChEBI:CHEBI:77674,
CC ChEBI:CHEBI:82831; EC=2.4.2.64; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03218};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03218};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03218}.
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DR EMBL; Z73899; CAA98076.1; -; Genomic_DNA.
DR PIR; T28024; T28024.
DR RefSeq; NP_502268.1; NM_069867.4.
DR AlphaFoldDB; Q23623; -.
DR SMR; Q23623; -.
DR IntAct; Q23623; 1.
DR STRING; 6239.ZK829.6; -.
DR EPD; Q23623; -.
DR PaxDb; Q23623; -.
DR PeptideAtlas; Q23623; -.
DR EnsemblMetazoa; ZK829.6.1; ZK829.6.1; WBGene00006566.
DR GeneID; 178131; -.
DR KEGG; cel:CELE_ZK829.6; -.
DR UCSC; ZK829.6; c. elegans.
DR CTD; 178131; -.
DR WormBase; ZK829.6; CE52839; WBGene00006566; tgt-1.
DR eggNOG; KOG3908; Eukaryota.
DR GeneTree; ENSGT00530000063679; -.
DR HOGENOM; CLU_022060_0_1_1; -.
DR InParanoid; Q23623; -.
DR OMA; GIDLFDC; -.
DR OrthoDB; 684306at2759; -.
DR PhylomeDB; Q23623; -.
DR PRO; PR:Q23623; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006566; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IBA:GO_Central.
DR Gene3D; 3.20.20.105; -; 1.
DR HAMAP; MF_00168; Q_tRNA_Tgt; 1.
DR InterPro; IPR004803; TGT.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Metal-binding; Reference proteome;
KW Transferase; tRNA processing; Zinc.
FT CHAIN 1..400
FT /note="Queuine tRNA-ribosyltransferase catalytic subunit"
FT /id="PRO_0000135567"
FT REGION 243..249
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT REGION 267..271
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 89..93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
SQ SEQUENCE 400 AA; 45186 MW; 4570AF9EE2380B09 CRC64;
MRYDVLARAG FARRGNLHLP HSIVETPVFM PVGTQGTMKG IVPEQLVSMD CRILLCNTYH
LGHRPGHERV KAAGGLHKMM NWNRSILTDS GGFQMVSLSK LMTVDENGVN FESPHTGEMM
ALPPEKSIEI QQALGADIMM QLDHVIHVLT TGDIVKEAMH RSIRWLDRCK VAHTRDDQAM
FPILQGGLNL ELRKECAKEM AKRAKVGIAI GGLSGGEEKD HFWRVVAACC AALPPHLPRY
VMGVGFPVDL VICSFLGADM FDCVYPTRTA RFGTAMVRRG GLMQLNQKRY KEDFLPIDKK
CECNTCKNYT RAYIHSIVGK ETVGCHLVSV HNIKHQLDLM RDVRQAIQSN SVEQFLKQFL
YDYYGPIQSE NPSKQDSEKM REVPQWVRDA VDHMGYKLDF
