QTRT2_CHICK
ID QTRT2_CHICK Reviewed; 425 AA.
AC Q5ZM96;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Name=QTRT2 {ECO:0000255|HAMAP-Rule:MF_03043};
GN Synonyms=QTRTD1 {ECO:0000255|HAMAP-Rule:MF_03043}; ORFNames=RCJMB04_2m13;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 QTRT1 and an accessory
CC subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043}.
CC Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03043};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03043};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03043}. Note=May associate
CC with the mitochondrion outer membrane. {ECO:0000255|HAMAP-
CC 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; AJ719488; CAG31147.1; -; mRNA.
DR RefSeq; NP_001025952.1; NM_001030781.1.
DR AlphaFoldDB; Q5ZM96; -.
DR SMR; Q5ZM96; -.
DR STRING; 9031.ENSGALP00000024354; -.
DR PaxDb; Q5ZM96; -.
DR GeneID; 418351; -.
DR KEGG; gga:418351; -.
DR CTD; 79691; -.
DR VEuPathDB; HostDB:geneid_418351; -.
DR eggNOG; KOG3909; Eukaryota.
DR InParanoid; Q5ZM96; -.
DR OrthoDB; 883398at2759; -.
DR PhylomeDB; Q5ZM96; -.
DR PRO; PR:Q5ZM96; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..425
FT /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT /id="PRO_0000383925"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ SEQUENCE 425 AA; 47065 MW; 8D0C3EE00CAFF3A5 CRC64;
MRVKLCGAAG GRLGTLAGLG RSGAAALALP GCLLYTRTGT APHLTLDTLR EVSGVPPVAQ
LTLPAMAELH DVLAEYKEGA AKFIGMPDTV LYCSLQDPVA PCPSGYNTNK TVSLWSSSGR
MEMTASKFMD IQRAIQPDWF QCIADGDTIS GEVTRKRAKK SVDRSLSFLD ACLQLLEKTP
ELQGSVMFGT IEGGDVLEER LRSARETAKR PVGGFLLDGF QGRAMAKETK MNLISSVTAE
LPEDKPRIIH GVGKPDEVLE CIERGVDIFE SFFPFQVTER GCALVFGYDY LSDPKAEAAL
KQNGAQDLEK NSPEEDQEEE VVKADPEMTP FEIFLKEKRY HDDFRPLLEG CTCYCCQRHT
RAYLHHLLVS SELLAGVLLM MHNFQHYFSF FSAIRDALRD DKLDQLKKLI FRQALQGPEN
AKIDQ
