ID A0A061IU24_TRYRA Unreviewed; 336 AA.
AC A0A061IU24;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000256|HAMAP-Rule:MF_03043};
DE AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000256|HAMAP-Rule:MF_03043};
GN ORFNames=TRSC58_06252 {ECO:0000313|EMBL:ESL06079.1};
OS Trypanosoma rangeli SC58.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL06079.1, ECO:0000313|Proteomes:UP000031737};
RN [1] {ECO:0000313|EMBL:ESL06079.1, ECO:0000313|Proteomes:UP000031737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC58 {ECO:0000313|EMBL:ESL06079.1,
RC ECO:0000313|Proteomes:UP000031737};
RA Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C., Bartholomeu D.C.,
RA Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B., Lima F.M.,
RA Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M., Tyler K.M.,
RA de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H., Cunha O.L.,
RA Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M., Sincero T.C.,
RA Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D., Andersson B.,
RA Romanha A.J., Steindel M., de Vasconcelos A.T., Grisard E.C.;
RL Submitted (JUL-2013) 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:0000256|HAMAP-
CC Rule:MF_03043}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03043};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03043};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03043}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000256|HAMAP-Rule:MF_03043}.
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:ESL06079.1}.
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DR EMBL; AUPL01006252; ESL06079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061IU24; -.
DR EnsemblProtists; ESL06079; ESL06079; TRSC58_06252.
DR VEuPathDB; TriTrypDB:TRSC58_06252; -.
DR OrthoDB; 167782at2759; -.
DR Proteomes; UP000031737; 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_03043; QTRT2; 1.
DR InterPro; IPR028592; QTRTD1.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR46064; QUEUINE TRNA-RIBOSYLTRANSFERASE ACCESSORY SUBUNIT 2; 1.
DR PANTHER; PTHR46064:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE ACCESSORY SUBUNIT 2; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03043};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03043};
KW Reference proteome {ECO:0000313|Proteomes:UP000031737};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03043};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_03043}.
FT DOMAIN 211..318
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
SQ SEQUENCE 336 AA; 37793 MW; 41429755CA7C4082 CRC64;
MANCYPLLVV PCKRGGIPCL TPDQARAIMK EEERVISVSI FDAGEYVEPC KIAKRGFAEF
CGLENFTTIL TVRSPHIGMH ASVPATDAGL SANHEKGRIS VGMDKWKEMV LSLRPTMIVT
PYDSVSTHEL QVKRRRTAVG RSVKWAVSAD SLHAQGNWKL MKPVCAVEGK AEYIFMEELC
QNETSQEYTA HIQQAVKKGQ VMCTAISLPA VLMCLRDNVR FIECALPWIL AEKGIGMVFD
ICPAEGVSPS RYETQIDLND DCFAEDIRPL SPDCSCYTCK RHMRAYIHHL LTVQEMNSKT
LLVIHNLARL IQLVRLYRLA GAEYREVLLN WLFAQI
//
