ID   CTU2_DEBHA              Reviewed;         448 AA.
AC   Q6BKN2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=NCS2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Synonyms=CTU2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   OrderedLocusNames=DEHA2F20504g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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). May act by
CC       forming a heterodimer with NCS6 that ligates sulfur from
CC       thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
CC       Prior mcm(5) tRNA modification by the elongator complex is required for
CC       2-thiolation. May also be involved in protein urmylation.
CC       {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03054}.
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DR   EMBL; CR382138; CAG89627.2; -; Genomic_DNA.
DR   RefSeq; XP_461239.2; XM_461239.1.
DR   AlphaFoldDB; Q6BKN2; -.
DR   STRING; 4959.XP_461239.2; -.
DR   EnsemblFungi; CAG89627; CAG89627; DEHA2F20504g.
DR   GeneID; 2903283; -.
DR   KEGG; dha:DEHA2F20504g; -.
DR   VEuPathDB; FungiDB:DEHA2F20504g; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_1_0_1; -.
DR   InParanoid; Q6BKN2; -.
DR   OMA; SCSMLRQ; -.
DR   OrthoDB; 1442062at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000000599; Chromosome F.
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; IEA:InterPro.
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_03054; CTU2; 1.
DR   InterPro; IPR019407; CTU2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR20882; PTHR20882; 1.
DR   Pfam; PF10288; CTU2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..448
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369295"
SQ   SEQUENCE   448 AA;  51115 MW;  EF7CE7CC20A4A7D7 CRC64;
     MSQPIQYLDV SENIPCSRCK TETAILISRK EKFCKDCFVR FIRGKQRKQM QDEKYKVKYG
     KNEENSPVQK VLLTLSCGVS SLVLVDVMTS LLKEQFDMHK GKQGFELVLL NINEYELKAL
     DRSVKDVLEQ LVQRFKPINI TYKILSLESY VLDQSLLEKI VLNGDFTAYS QSIHHDRDYT
     LSEVLDLCPN KSSLEDLLTI IYDELILRTA CLESCETILY GHSMTRIANE IIALTVKGRG
     SSIYQTVSDH SVNFRNKDYK IIFPLRDVLF AEILAYSKLS ELDTFAVEST KPVSKITKNM
     TIRDLTTNYF NQLDATGYAS TASTVVKTGD KLGAPKFEED SSICQVCGTE IHQDPKEWLR
     RITVNKAAPL ETEEEKEYAE QYKKASSLIE EPSSTQSKTP INICYGCTVT ISGIKNESGF
     IWPIKYPAND EEREILNEYI LTDDEDDQ