ID   CTU2_DROWI              Reviewed;         403 AA.
AC   B4MYR2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   ORFNames=GK18201;
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). May act by
CC       forming a heterodimer with NCS6/CTU1 that ligates sulfur from
CC       thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
CC       {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03054}.
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DR   EMBL; CH963913; EDW77251.1; -; Genomic_DNA.
DR   RefSeq; XP_002066265.1; XM_002066229.1.
DR   AlphaFoldDB; B4MYR2; -.
DR   SMR; B4MYR2; -.
DR   STRING; 7260.FBpp0247344; -.
DR   PRIDE; B4MYR2; -.
DR   EnsemblMetazoa; FBtr0248852; FBpp0247344; FBgn0220200.
DR   GeneID; 6643580; -.
DR   KEGG; dwi:6643580; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_2_1_1; -.
DR   InParanoid; B4MYR2; -.
DR   OMA; YVRHKFR; -.
DR   OrthoDB; 1442062at2759; -.
DR   PhylomeDB; B4MYR2; -.
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; IEA:InterPro.
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_03054; CTU2; 1.
DR   InterPro; IPR019407; CTU2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR20882; PTHR20882; 1.
DR   Pfam; PF10288; CTU2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..403
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369279"
SQ   SEQUENCE   403 AA;  45282 MW;  183746C6510567CC CRC64;
     MCSIGEDDFG DTGGLHAMTA GGPVQIATGG TGECQKCGQH SDDLFKVNFR SEECRDCFLN
     YARHKFRAAL GAAKALPRDS DVLLLLDGSI ESIVLLDMLH YAQTQNTFKR LHCQAKVLYL
     DESVVQEQQS LDIDRLQKLQ DRYTPFDLFV IELGTDLSNL RPLKNYTPKT SREESDLKIK
     LDKLRTLSAR QDYLQQQRKR FLASVAHQLN CTHVFVPSIS KDLATQFLTS IALGRGGSAA
     LDVALCDDRL DHDIKLLRPL KDLNEQEVQL YVRARNLEDL KLGPSLATYG QEKGETASLQ
     NLTAAFVRNL QENYAATVST VFRTGNKIAP NRHVDQDMCQ QCQSPLDSLL SDTLLAIEYS
     RVVSLEGSKL SNHNNDLEQL SMQRLNKDDR LCHACRNVQD EYL