ID   CTU2_CANGA              Reviewed;         469 AA.
AC   Q6FLE5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=CAGL0L04026g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380958; CAG61919.1; -; Genomic_DNA.
DR   RefSeq; XP_448949.1; XM_448949.1.
DR   AlphaFoldDB; Q6FLE5; -.
DR   STRING; 5478.XP_448949.1; -.
DR   PRIDE; Q6FLE5; -.
DR   EnsemblFungi; CAG61919; CAG61919; CAGL0L04026g.
DR   GeneID; 2890763; -.
DR   KEGG; cgr:CAGL0L04026g; -.
DR   CGD; CAL0135126; CAGL0L04026g.
DR   VEuPathDB; FungiDB:CAGL0L04026g; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_1_0_1; -.
DR   InParanoid; Q6FLE5; -.
DR   OMA; SCSMLRQ; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000002428; Chromosome L.
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:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
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_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..469
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369293"
SQ   SEQUENCE   469 AA;  54275 MW;  BE9E1C5A778F4D5B CRC64;
     MTAEQCQRCN KNAVEVISRK ELFCAECFRV FVMQKQRKQM MSDDYYRDIF KVMYKDKIRS
     AEEAEQQNKN STILIPLSFG SSSLMMLDIV HLTLLEQKMQ HQKTGFNVDV LICYRESNDE
     LLTNIQSNIK ELSTVRYSEN KDNIRFHTLC LDSMFEIDKE LIDQVVLHNV EFTGRQVSIN
     ESEHANLSLQ TVLTSCPNRS TKEDIIDFVT KHLVKKYAYQ NGQKAILWGH SMTRLADEII
     SCVVKGRGAQ ISSKLNTTNL DVNYGSRFKN LYPLKDILLT EVDAYCALFD LSKYLIKYEL
     QDSLLVNKLK KEKHIGNQRL AKNMTINELA RKYFNDIEGE YSNVIATVLR TGDKLDEPLA
     TLGEKHCRIC KSTVHDDVSK WLRDITVNVG QPLESQLERD LHEKWATSHI GLETTAYYQL
     RDRVWEQGDD VDLCYGCIVT MQGVKNLNVP WPKNNEQELN EVLAEYSLE