ID   CTU1_DROWI              Reviewed;         343 AA.
AC   B4NN33;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_03053};
DE   AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   ORFNames=GK22963;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC       wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds
CC       tRNAs and probably acts by catalyzing adenylation of tRNAs, an
CC       intermediate required for 2-thiolation. It is unclear whether it acts
CC       as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1
CC       onto the uridine of tRNAs at wobble position. {ECO:0000255|HAMAP-
CC       Rule:MF_03053}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053}.
CC   -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03053}.
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DR   EMBL; CH964282; EDW85772.1; -; Genomic_DNA.
DR   RefSeq; XP_002074786.1; XM_002074750.2.
DR   AlphaFoldDB; B4NN33; -.
DR   SMR; B4NN33; -.
DR   STRING; 7260.FBpp0252106; -.
DR   EnsemblMetazoa; FBtr0253614; FBpp0252106; FBgn0224925.
DR   GeneID; 6652355; -.
DR   KEGG; dwi:6652355; -.
DR   eggNOG; KOG2840; Eukaryota.
DR   HOGENOM; CLU_026481_1_2_1; -.
DR   InParanoid; B4NN33; -.
DR   OMA; MNLDQKQ; -.
DR   OrthoDB; 860739at2759; -.
DR   PhylomeDB; B4NN33; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_03053; CTU1; 1.
DR   InterPro; IPR032442; CTU1_C.
DR   InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR   InterPro; IPR020554; UPF0021_CS.
DR   PANTHER; PTHR11807:SF12; PTHR11807:SF12; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF16503; zn-ribbon_14; 1.
DR   PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR   TIGRFAMs; TIGR00269; TIGR00269; 1.
DR   PROSITE; PS01263; UPF0021; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..343
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000368251"
SQ   SEQUENCE   343 AA;  38574 MW;  1CA0E73F9EAA78A7 CRC64;
     MPVYCKSQCG NRAVLRRPKT GDALCKECFF AAFEAEIHHT ISSNQLFQPG QKIAVAASGG
     KDSTVLAHVL KLLNEKHNYG LDLVLLSIDE GISGYRDDSL ETVKQNRDDY QMSLKILSYE
     ELYGWTMDRI VAQIGRSNNC TFCGVFRRQA LDRGAKLLQV DSIATGHNAD DIAETVLMNI
     LRGDTARLRR CTDIRTGGGE DSIPRVKPLK YSYEKDIVMY AHYKKLVYFS TECVFAPNAY
     RGHARAFLKD LEKVRPSVIM DIIYSGEQLR FKDTVKKPVR GTCSRCGFVS SQQPCKACVL
     LEGLNRGLPK LGIGKKSKGD RMIAEQNREL DLRERANLVK NDF