ID W5QE75_SHEEP Unreviewed; 423 AA.
AC W5QE75;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 Name=QTRT2 {ECO:0000256|HAMAP-Rule:MF_03043,
GN ECO:0000313|Ensembl:ENSOARP00000021023.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000021023.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000021023.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000021023.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000021023.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 QTRT1 and an accessory
CC subunit QTRT2. {ECO:0000256|HAMAP-Rule:MF_03043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03043}.
CC Mitochondrion outer membrane {ECO:0000256|HAMAP-Rule:MF_03043};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03043};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03043}. Note=May associate
CC with the mitochondrion outer membrane. {ECO:0000256|HAMAP-
CC Rule:MF_03043}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000256|HAMAP-Rule:MF_03043}.
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DR EMBL; AMGL01008344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5QE75; -.
DR SMR; W5QE75; -.
DR STRING; 9940.ENSOARP00000021023; -.
DR PaxDb; 9940-ENSOARP00000021023; -.
DR Ensembl; ENSOART00000021317.1; ENSOARP00000021023.1; ENSOARG00000019572.1.
DR eggNOG; KOG3909; Eukaryota.
DR HOGENOM; CLU_037350_0_0_1; -.
DR OMA; MAGSRMK; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000019572; Expressed in pituitary gland and 53 other cell types or tissues.
DR GO; GO:0005741; C:mitochondrial outer membrane; 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 Membrane {ECO:0000256|HAMAP-Rule:MF_03043};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03043};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03043};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|HAMAP-Rule:MF_03043};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03043}; Zinc {ECO:0000256|HAMAP-Rule:MF_03043}.
FT DOMAIN 21..421
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
SQ SEQUENCE 423 AA; 47473 MW; 632F62FF3C4D8539 CRC64;
YQDLEESLMK LNLTKVVNGC RLGKIKNLGK TGDRSMDIPG CLLYTKAGSA PHLTHHTLHK
IHGVPAMAQL TLSSLAEHHE VLAEYKEGVG KFIGMPESLL YCSLHDPVSP CPAGYVTNKS
VSVWGVGGRV EMTASKFMAI QQALQPDWFQ CISDGEATCN EATSIKRARK SVDRTLLFLD
NCLRLQEESE VLQKSSIIGV IEGGDVTEER LRSARETAKR PVGGFLLDGF QGSPATLETR
LHLLSSVTAE LPEDKPRLIC GVSRPDEVLE CIERGVDLFE SFFPYQVTER GCALTFSFDY
QPNPEETLLQ QNGTQEEIKY VDQTKKSKTT SCNQEMTSYE INLKEKKYQE DFSPLVRGCS
CYCCKNHTRA YVHHLLVTNE LLAGVLLMMH NFEHYFGFFH SIREALKSDR LAQLKELIRR
QAS
//
