ID S9XCD0_SCHCR Unreviewed; 639 AA.
AC S9XCD0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=SPOG_02668 {ECO:0000313|EMBL:EPY51496.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY51496.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY51496.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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 phosducin family.
CC {ECO:0000256|ARBA:ARBA00009686}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000256|HAMAP-Rule:MF_03043}.
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DR EMBL; KE546991; EPY51496.1; -; Genomic_DNA.
DR RefSeq; XP_013024063.1; XM_013168609.1.
DR AlphaFoldDB; S9XCD0; -.
DR STRING; 653667.S9XCD0; -.
DR EnsemblFungi; EPY51496; EPY51496; SPOG_02668.
DR GeneID; 25036990; -.
DR eggNOG; KOG1672; Eukaryota.
DR eggNOG; KOG3909; Eukaryota.
DR HOGENOM; CLU_425884_0_0_1; -.
DR OMA; ELAWDMW; -.
DR OrthoDB; 11459at2759; -.
DR Proteomes; UP000015464; 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 CDD; cd02989; Phd_like_TxnDC9; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR21148:SF25; PHOSDUCIN-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR21148; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 9; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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:UP000015464};
KW Transferase {ECO:0000313|EMBL:EPY51496.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03043};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_03043}.
FT DOMAIN 7..366
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT BINDING 303
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"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
SQ SEQUENCE 639 AA; 72421 MW; A5A81E61A660DAA0 CRC64;
MAAYPSSARI SSVSLKNKVL QTPCFIFPTS KGTIPHLTPD NINHNEVPVV YFGLEDSLDL
LEKSPILNAD GEIDKWVAGT PSQSILIAPR RSSPLPSVSA GPHHIQVLTS SGLRKLTNEV
YVKAITKLRP EIAIPLNDNP SNAPGVKRKP KMIERSVTWT DELLTVLQNK QLTEKVKVFF
PIPNVEAPFL NPLIERFREN DYQQNISGLA CYGNLQSIPS ELSIYPKLFL RPLLTPLAIL
QSIHQGADIV MADLVNQASD AGIVFTFSFP PPVEDLQNRK LELAWDMWHN RFATDLSSLQ
PGCNCNICQS YSRAYVHHLL QTRELVGWIM VQQHNIHVFH NFFCGIRDSI AAGSFLEDTE
RFERIYAPNF PRTTGLGPRK RGYQMDLTDV QPIENKPNWV QLKTETDDDK TSHMIQKKEN
AQEFQEPELP ERDTTVGNFA DTYAAQSENK SGSELEEDLL AELDEIDDSA YRENRMQSLK
EEFERVSAAK EKGHMQYLTV ESEREVMDLT TSSKRVVIHF FHPDFRRCKI MDSHLEKISK
SHWETKFIRI EAANAPFLAL KLGLKVLPVV LCYVDASLVS KLVGFADLGN NDDFDTPVLE
FWLLKWAAIE KIKENIPQGK KSIMGFKDTK NESEDSDLD
//
