ID E9EXU8_METRA Unreviewed; 408 AA.
AC E9EXU8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=MAA_04847 {ECO:0000313|EMBL:EFY99918.1};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY99918.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFY99918.1, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFY99918.1, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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: 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:EFY99918.1}.
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DR EMBL; ADNJ02000001; EFY99918.1; -; Genomic_DNA.
DR RefSeq; XP_007821134.1; XM_007822943.1.
DR AlphaFoldDB; E9EXU8; -.
DR GeneID; 19259133; -.
DR KEGG; maj:MAA_04847; -.
DR HOGENOM; CLU_022060_1_1_1; -.
DR OrthoDB; 167782at2759; -.
DR Proteomes; UP000002498; 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};
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..382
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 257..263
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT REGION 281..285
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 101..105
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
SQ SEQUENCE 408 AA; 45103 MW; 35F80C649B82E98A CRC64;
MASNISSSPA LSFELVARCS TTRARASNLT LPHGPVQLPM FMPVATQASL KGITPQQLEE
TGCRLCLNNT YHLGLKPGQE VLDAIGGAHK FQGWKHNLLT DSGGFQMVSL LKLAKITEEG
VRFLSPHDGS PMLLTPEHSI SLQNTIGSDI IMQLDDVLVT TSPDKVRMRE AMERSVRWLD
RCIAAHKKPD SQNLFCIIQG GLDLEMRREC CKEMLARNTP GIAIGGLSGG EAKADYCRVV
EACTALLPDL KPRYVMGIGY PEDLVVSVAL GADMFDCVWP TRTARFGNAI TKHGVLNIRN
AKYANDFGPI EPGCECMCCR QGEGGMGITR AYVHHNTSKE TVSAHLLTMH NVWYQLNLMR
EVRQAIIEDR FPAYIRQFFA DLYESKTDYP DWAVEALKQV SVDLTVEG
//
