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 09-FEB-2010, entry version 14. 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; Arthropoda; Hexapoda; Insecta; Pterygota; OC 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM000157; EDW89450.1; -; Genomic_DNA. DR RefSeq; XP_002089738.1; -. DR GeneID; 6528703; -. DR KEGG; dya:Dyak_GE22576; -. DR FlyBase; FBgn0239795; Dyak\GE22576. DR OrthoDB; EOG97SSM5; -. DR PhylomeDB; B4P3W7; -. 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 InterPro; IPR012089; 2-thiocytidine_tRNA_synth_TtcA. DR InterPro; IPR011063; PP_loop. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR000541; UPF0021_C. DR InterPro; IPR020554; UPF0021_CS. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR Pfam; PF01171; ATP_bind_3; 1. DR PIRSF; PIRSF004976; ATPase_YdaO; 1. DR TIGRFAMs; TIGR00269; UPF0021; 1. DR PROSITE; PS01263; UPF0021; 1. PE 3: Inferred from homology; KW Cytoplasm; RNA-binding; Transferase; 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 //