ID A0A196SBD5_BLAHN Unreviewed; 405 AA.
AC A0A196SBD5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000256|HAMAP-Rule:MF_03218};
DE EC=2.4.2.64 {ECO:0000256|HAMAP-Rule:MF_03218};
DE AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_03218};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_03218};
GN ORFNames=AV274_3955 {ECO:0000313|EMBL:OAO14365.1};
OS Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO14365.1, ECO:0000313|Proteomes:UP000078348};
RN [1] {ECO:0000313|EMBL:OAO14365.1, ECO:0000313|Proteomes:UP000078348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348};
RA Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:18571, ChEBI:CHEBI:16235, ChEBI:CHEBI:17433, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:194431; EC=2.4.2.64; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03218};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03218};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03218}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_03218}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03218}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAO14365.1}.
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DR EMBL; LXWW01000255; OAO14365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A196SBD5; -.
DR STRING; 478820.A0A196SBD5; -.
DR OrthoDB; 167782at2759; -.
DR Proteomes; UP000078348; Unassembled WGS sequence.
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:tRNA-guanosine(34) queuine transglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 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 NCBIfam; TIGR00430; Q_tRNA_tgt; 1.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR43530; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1.
DR PANTHER; PTHR43530:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03218};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_03218};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03218}; Reference proteome {ECO:0000313|Proteomes:UP000078348};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03218};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03218}; Zinc {ECO:0000256|HAMAP-Rule:MF_03218}.
FT DOMAIN 23..383
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 264..270
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 103..107
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
SQ SEQUENCE 405 AA; 45500 MW; EECBA1B50A27755A CRC64;
MEEQPMKYDT PALVFDIVKK WNRARASVMT LRHGPVLTPV FMPVGTKGTI KGLTPDQMGD
ESMDCQILLG NTYHLSSKPG AQTVADFGGL HKFMQWDRNI LTDSGGFQMV SLLDLAEITE
NGVVFQHPAD GSTLVLRPED SIHYQNLIGA DIIMALDDVV HSCTDDDTRF TEATHRTVRW
LDRCIAAHAR KDEQNLFAIV QGGLDVSEGG LRDQCLQAFL DRDAKIPGYA IGGLAGGEDK
GSFWRVVERC TRKLPENKPR YVMGVGYPLD IVVCTALGAD MYDCVYPSRT GRFGTAMVPW
GLLKLKSSEC KDDERPIDPN CQCETCKHYS RAALYQLCKK EALGASLVTR HNLYYMIHFM
RDMRMSIIEG RFDSYVKEFM KNYFPKGDYP QWCVEALHVA GIDLK
//
