CTU1_DROGR
ID CTU1_DROGR Reviewed; 343 AA.
AC B4J5B3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=GH20281;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916367; EDW01755.1; -; Genomic_DNA.
DR RefSeq; XP_001986888.1; XM_001986852.1.
DR AlphaFoldDB; B4J5B3; -.
DR SMR; B4J5B3; -.
DR STRING; 7222.FBpp0154187; -.
DR EnsemblMetazoa; FBtr0155695; FBpp0154187; FBgn0127745.
DR GeneID; 6560206; -.
DR KEGG; dgr:6560206; -.
DR eggNOG; KOG2840; Eukaryota.
DR HOGENOM; CLU_026481_1_2_1; -.
DR InParanoid; B4J5B3; -.
DR OMA; MNLDQKQ; -.
DR OrthoDB; 860739at2759; -.
DR PhylomeDB; B4J5B3; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000001070; 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_0000368242"
SQ SEQUENCE 343 AA; 38507 MW; 5AC3F8457A4E3270 CRC64;
MPIDCKAKCG NKAALKRPKT GDALCKDCFF AAFEAEIHHT IVSSRLFRRG EKVAVAASGG
KDSTVLAHVM KLLNERHDYG LDLVLLSIDE GITGYRDDSL ETVKQNRDDY QMPLKILSYE
ELYGWTMDRI VAQIGRSNNC TFCGVFRRQA LDRGAKLLGV DSIATGHNAD DIAETVLMNI
LRGDTARLRR CTNIRTGGGE DSIPRVKPLK YSYEKEIVMY AHYKRLVYFS TECVFAPNAY
RGHARAFLKD LEKVRPSVIM DIIYSGEQLR FKDTAKKPVR GICERCGFVS SQQPCKACVL
LEGLNRGLPK LGIGKKSKGD RMIAQQNQEL ALRERANLVK NDF