ID   QTRT2_IXOSC             Reviewed;         394 AA.
AC   B7Q5K1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000255|HAMAP-Rule:MF_03043};
DE   AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03043};
GN   ORFNames=ISCW021855;
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel;
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Non-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). {ECO:0000255|HAMAP-
CC       Rule:MF_03043}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03043};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03043};
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_03043}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       QTRT2 subfamily. {ECO:0000255|HAMAP-Rule:MF_03043}.
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DR   EMBL; DS861789; EEC14123.1; -; Genomic_DNA.
DR   RefSeq; XP_002411784.1; XM_002411739.1.
DR   AlphaFoldDB; B7Q5K1; -.
DR   SMR; B7Q5K1; -.
DR   STRING; 6945.B7Q5K1; -.
DR   EnsemblMetazoa; XM_002411739.5; XP_002411784.4; LOC8036228.
DR   GeneID; 8036228; -.
DR   KEGG; isc:IscW_ISCW021855; -.
DR   VEuPathDB; VectorBase:ISCI021855; -.
DR   VEuPathDB; VectorBase:ISCW021855; -.
DR   HOGENOM; CLU_037350_0_0_1; -.
DR   InParanoid; B7Q5K1; -.
DR   OMA; MAGSRMK; -.
DR   OrthoDB; 883398at2759; -.
DR   PhylomeDB; B7Q5K1; -.
DR   Proteomes; UP000001555; 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:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0101030; P:tRNA-guanine transglycosylation; IBA:GO_Central.
DR   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_03043; QTRT2; 1.
DR   InterPro; IPR028592; QTRTD1.
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; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..394
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000383944"
FT   BINDING         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         367
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   394 AA;  43748 MW;  5B43C9FACCA6E866 CRC64;
     MRFSVVETFH GHRGRLGNIC GLRIGTGEQC LDTPTCLLYT QAGSAPHLTR DMLHKLGDVE
     NLPALFPLPP ITSFVDSVMQ FGKGLGSFVA LQSHPSFIRI QDPMVTTPSG FNDKAGVSVW
     DQGGRVHLNP LSFTRMMEAF QPTCYQALCD SDTPQDASRK RLQRAVDRSV SLLDQCLAMK
     ADSSCLQHSA ILGSVQGGYN RDFREISAKE TAKRDVDGFV IEGFHVNGPQ TKSLKFEEVA
     EILEEVIALL PQDKPRFLHG VLRPEFILKA VLYGIDIFDA SLAHAATEAG CALVFNCSSD
     KDLELMLGRD LLDQELEMDM KNARHREDFV PLLESCACYA CTNFTRAYIH HLLNTGEMLG
     QVLLSLHNIH HFLGFLKSIR KFMVQHGAKE LNGN