ID   CTU1_KLULA              Reviewed;         371 AA.
AC   Q6CWX6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
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   Name=NCS6 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   Synonyms=CTU1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   OrderedLocusNames=KLLA0B00737g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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. Prior mcm(5) tRNA
CC       modification by the elongator complex is required for 2-thiolation. May
CC       also be involved in protein urmylation. {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; CR382122; CAH01956.1; -; Genomic_DNA.
DR   RefSeq; XP_451563.1; XM_451563.1.
DR   AlphaFoldDB; Q6CWX6; -.
DR   SMR; Q6CWX6; -.
DR   STRING; 28985.XP_451563.1; -.
DR   EnsemblFungi; CAH01956; CAH01956; KLLA0_B00737g.
DR   GeneID; 2897489; -.
DR   KEGG; kla:KLLA0_B00737g; -.
DR   eggNOG; KOG2840; Eukaryota.
DR   HOGENOM; CLU_026481_1_2_1; -.
DR   InParanoid; Q6CWX6; -.
DR   OMA; CLHINLG; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000000598; Chromosome B.
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:0002143; P:tRNA wobble position uridine thiolation; IEA:EnsemblFungi.
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   PROSITE; PS01263; UPF0021; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..371
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000368262"
SQ   SEQUENCE   371 AA;  41781 MW;  804F3AF41D896BFD CRC64;
     MFTPPTDPKK SVKVKVSQLC ELCHARKAVM KRPKNLQRIC KECFFSVFET EIHNTIVSNN
     LFHRGERIAV GASGGKDSTV LAYVLKLLND RHDYGVEIVL LSIDEGIVGY RDDSLATVKR
     NQVQYDLPLE IVSYKDLYNW TMDEIVACAG IRNSCTYCGV FRRQALDRGA AKLGIKHVVT
     GHNADDMAET VLMNILRGDV ARLEKSTSIL TQSSGSPIKR SKPFKYSYQK EIVLYAHYKK
     LDYFSTECSY APEAFRGTAR ELMKNLEAIR PSCIIDIIHS GESLKLKPKR AKKAPPPSHM
     EIRPDGSVSL QNEFIDGNRC ERCGYLSSNK ICKACMLLEG LEQNRAKIQL EKDSTTEGAA
     KLSRTLEKLQ F