ID   CTU1_CAEBR              Reviewed;         372 AA.
AC   A8WR63;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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};
DE   AltName: Full=Thiolation of uridine in tRNA protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   Name=tut-1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   Synonyms=ctu-1 {ECO:0000255|HAMAP-Rule:MF_03053}; ORFNames=CBG01646;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE601298; CAP22971.1; -; Genomic_DNA.
DR   RefSeq; XP_002634096.1; XM_002634050.1.
DR   AlphaFoldDB; A8WR63; -.
DR   SMR; A8WR63; -.
DR   STRING; 6238.CBG01646; -.
DR   EnsemblMetazoa; CBG01646.1; CBG01646.1; WBGene00024852.
DR   GeneID; 8576091; -.
DR   KEGG; cbr:CBG_01646; -.
DR   CTD; 8576091; -.
DR   WormBase; CBG01646; CBP00437; WBGene00024852; Cbr-tut-1.
DR   eggNOG; KOG2840; Eukaryota.
DR   HOGENOM; CLU_026481_1_2_1; -.
DR   InParanoid; A8WR63; -.
DR   OMA; MNLDQKQ; -.
DR   OrthoDB; 860739at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR   GO; GO:0048598; P:embryonic morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0048599; P:oocyte development; IEA:EnsemblMetazoa.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0007283; P:spermatogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0006412; P:translation; IEA:EnsemblMetazoa.
DR   GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR   GO; GO:0040025; P:vulval development; IEA:EnsemblMetazoa.
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   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.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..372
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000368238"
FT   REGION          335..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   372 AA;  41317 MW;  E8926904A14302DB CRC64;
     MEKRRGPPPC QSEEGCSNSA KIRKAKNGAQ LCGPCFSKSF EDDVHETIIN NNLFKRGERV
     AIGASGGKDS TVLAFVMKTL NDRHDYGLDL QLLSIDEGIK GYRDDSLLAV EKNRVEYGLP
     LTILSYNDLY GWTMDDIVAK IGKKNNCTFC GVFRRQALDR GAFKIGATKL VTGHNADDMA
     ETVLMNVLRG DIARLERCTN IVTGEEGDLP RAKPLKYCFE RDIVMYARSN QLEYFYTECI
     YAPNAYRGYA RKYVRDLEKV HPRAILDLIR SGEKVSVKKE VEMPTLKTCE RCGYMTSQKM
     CKACLLIEGL NTGNTDLGVR KSKKTKKVIV ETEGGKKEDG GCGSGGGGCG CAGAADETEN
     EETRKRLKDL QF