ID A0A0W4ZMM1_PNEJ7 Unreviewed; 399 AA.
AC A0A0W4ZMM1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=T551_02236 {ECO:0000313|EMBL:KTW29620.1};
OS Pneumocystis jirovecii (strain RU7) (Human pneumocystis pneumonia agent).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1408657 {ECO:0000313|EMBL:KTW29620.1, ECO:0000313|Proteomes:UP000053447};
RN [1] {ECO:0000313|Proteomes:UP000053447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU7 {ECO:0000313|Proteomes:UP000053447};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
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:KTW29620.1}.
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DR EMBL; LFWA01000009; KTW29620.1; -; Genomic_DNA.
DR RefSeq; XP_018229451.1; XM_018374499.1.
DR AlphaFoldDB; A0A0W4ZMM1; -.
DR STRING; 1408657.A0A0W4ZMM1; -.
DR GeneID; 28940754; -.
DR VEuPathDB; FungiDB:T551_02236; -.
DR eggNOG; KOG3908; Eukaryota.
DR OrthoDB; 167782at2759; -.
DR Proteomes; UP000053447; 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:UP000053447};
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 18..374
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 251..257
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT REGION 275..279
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT ACT_SITE 270
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 96..100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
SQ SEQUENCE 399 AA; 44735 MW; 20EA8E0F2351B948 CRC64;
MLPKGLTFDI IHECSVSKAR AGLLTLSHGS VETPVFMPVG TQATLKGITP QQLGHLGCRL
MLNNTYHLGL RPGQSVLDMI GGAHVFQGWP HNLLTDSGGF QMVSLLKLSR VTEEGVEFHS
PHDGSVMLLT PEHSISLQNS IGSDIIMQLD DVVHSLSPLE RVKEAMWRTI RWLDRCIAAN
KYPEKQSLYG IVQGGLDEEL RTTSCLEIIK RETPGIAIGG LSGGEEKSQM YKIVSICTNL
LPSNKPRYLM GVGYTEDLIV NVALGIDQFD CVYPTRTARF GNALTPYGVL NLRNKCFAND
YNPIDRDCKC PCCKSDEWGI TRAYIHHIVC KETVFAHLLT IHNVHYQLNL MKEIRNAIIH
DQFPTFVKKA FNRLYSKRKK DYPKWAIDSL NTVNINLLE
//
