CTU1_DROYA
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 03-AUG-2022, entry version 69.
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=GE22576;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC 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 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}.
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; XM_002089702.2.
DR AlphaFoldDB; B4P3W7; -.
DR SMR; B4P3W7; -.
DR STRING; 7245.FBpp0267586; -.
DR EnsemblMetazoa; FBtr0269094; FBpp0267586; FBgn0239795.
DR GeneID; 6528703; -.
DR KEGG; dya:Dyak_GE22576; -.
DR eggNOG; KOG2840; Eukaryota.
DR HOGENOM; CLU_026481_1_2_1; -.
DR OMA; MNLDQKQ; -.
DR OrthoDB; 860739at2759; -.
DR PhylomeDB; B4P3W7; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000002282; Chromosome 2L.
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; RNA-binding; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..343
FT /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT /id="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