ID   CTU1_DROYA              Reviewed;         343 AA.
AC   B4P3W7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   13-NOV-2013, entry version 35.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1;
DE            EC=2.7.7.-;
DE   AltName: Full=Cytoplasmic tRNA adenylyltransferase 1;
GN   ORFNames=GE22576;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
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
CC       tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln).
CC       Directly binds tRNAs and probably acts by catalyzing adenylation
CC       of tRNAs, an intermediate required for 2-thiolation. It is unclear
CC       whether it acts as a sulfurtransferase that transfers sulfur from
CC       thiocarboxylated URM1 onto the uridine of tRNAs at wobble position
CC       (By similarity).
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-
CC       tRNA biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3
CC       subfamily.
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DR   EMBL; CM000157; EDW89450.1; -; Genomic_DNA.
DR   RefSeq; XP_002089738.1; XM_002089702.1.
DR   ProteinModelPortal; B4P3W7; -.
DR   STRING; 7245.FBpp0267586; -.
DR   EnsemblMetazoa; FBtr0269094; FBpp0267586; FBgn0239795.
DR   GeneID; 6528703; -.
DR   KEGG; dya:Dyak_GE22576; -.
DR   FlyBase; FBgn0239795; Dyak\GE22576.
DR   eggNOG; COG0037; -.
DR   KO; K14168; -.
DR   OrthoDB; EOG7PGDRH; -.
DR   UniPathway; UPA00988; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
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; IPR012089; 2-thiocytidine_tRNA_synth_TtcA.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; tRNA-lysidine/thiocyt_synth.
DR   InterPro; IPR000541; tRNA_2-thiolation_protein.
DR   InterPro; IPR020554; UPF0021_CS.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR   TIGRFAMs; TIGR00269; TIGR00269; 1.
DR   PROSITE; PS01263; UPF0021; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; RNA-binding; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN         1    343       Cytoplasmic tRNA 2-thiolation protein 1.
FT                                /FTId=PRO_0000368252.
SQ   SEQUENCE   343 AA;  38476 MW;  B3E05BAF0B795465 CRC64;
     MPISCKSQCG NRAVLKRPKT GDALCKECFF AAFEAEIHHT ISSSNLFRLG EKVAVAASGG
     KDSTVLAHVL KLLNERHNYG LELVLLSIDE GITGYRDDSL ETVKQNRDDY QMPLKILSYE
     ELYGWTMDRI VAQIGRSNNC TFCGVFRRQA LDRGAKLLGV DSIATGHNAD DIAETVLMNV
     LRGDTARLRR CTSIRTGGGE DTIPRVKPLK YSYEKEIVMY AHYKKLVYFS TECVFAPNAY
     RGHARAFLKD LEKVRPSVIM DIIYSGEQLR FKDTVKKPER GTCIRCGFVS SQQPCKACVL
     LEGLNRGLPK LGIGKKSKGE RMIAKQDQEL ALRERAHLVK NDF
//