ID QTRT2_DANRE Reviewed; 416 AA.
AC Q7ZVJ6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 27-MAR-2024, entry version 105.
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};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) 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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH45519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC045519; AAH45519.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q7ZVJ6; -.
DR SMR; Q7ZVJ6; -.
DR STRING; 7955.ENSDARP00000113635; -.
DR PaxDb; 7955-ENSDARP00000106901; -.
DR AGR; ZFIN:ZDB-GENE-060427-4; -.
DR ZFIN; ZDB-GENE-060427-4; qtrt2.
DR eggNOG; KOG3909; Eukaryota.
DR InParanoid; Q7ZVJ6; -.
DR PhylomeDB; Q7ZVJ6; -.
DR PRO; PR:Q7ZVJ6; -.
DR Proteomes; UP000000437; Genome assembly.
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:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..416
FT /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT /id="PRO_0000383926"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ SEQUENCE 416 AA; 46090 MW; 2E9C3A2B1D039A1C CRC64;
MKLELSRVVQ GCRLGVLTGL GKSGQHSLEV PGCLLHTRCA TVPHLTQDTL LTLSDLPAVT
QVSVDSLAEH HEVLEEFKEG VRKFAGLHDT VIFCSLHDSA SPSPAGHVTN KTVSVWGSGG
RIELTAARFM SIQAAVQPDC YQSMADGETW QANTSRKRVR KAVDRTLAHL DECLVLHQKT
QELKHAEIFG VVEGGDILEE RLRSARETAK RPVGGFVLDG FHSSAMDQDV RAQLIQETSA
ELPQEKPRLV LGVGRPDEVI SCVEAGVDLF ESFFPFQVTE RGCALSFNYT IDPDPETAGT
SASTVLECNG ETPEVKKPSA NEDVENMTPF EINLKDKRYR DDFRPLVEGC VCYCCQKHMR
AYVHHLLVTN ELLAGVLLML HNMAHYLGFF KALRDAITSD RLQDFKNTVL HRRQGD
//
