ID   CTU2_ASHGO              Reviewed;         461 AA.
AC   Q75BK0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
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}; OrderedLocusNames=ACR271C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016816; AAS51497.1; -; Genomic_DNA.
DR   RefSeq; NP_983673.1; NM_209026.1.
DR   AlphaFoldDB; Q75BK0; -.
DR   STRING; 33169.AAS51497; -.
DR   EnsemblFungi; AAS51497; AAS51497; AGOS_ACR271C.
DR   GeneID; 4619808; -.
DR   KEGG; ago:AGOS_ACR271C; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_1_0_1; -.
DR   InParanoid; Q75BK0; -.
DR   OMA; SCSMLRQ; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..461
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369286"
SQ   SEQUENCE   461 AA;  52405 MW;  5D6FDBF10928C846 CRC64;
     MKCKRCTTSE GCLVSRNETF CGECFSRFVL LKFRKQMMMD EYCQQVFKVL YADKHRTAVE
     ADEQNKRSVV LVPLSLGSSS LAMLDLLNQT LSEQRAAHNR TGFQVKVVLC GFSADMDELK
     RLAESLQTER LAMNSDCIKL YLLDLDRSFS TCEIHKLLLA NDNHGSRKIA TRENATLSSI
     LDQFSRRSSR DDMLWFARQH LIKKFASQHQ VKVIMWGHSV TRLADEVMSL VIKGRGAQIA
     ATLDSTGMDV EYGALFKNLY PLRDVLLSEI DAYCSLSKLQ RYIYNYSLQG SLFIKSQDEA
     AQANRAVPMA KNMTINELTR QYFDAVEKDY SNVISTIVRT ASKLDYPISN GTEVIYCSIC
     NNRVYVDPSK WLKSITVNNC HPPASDEDMS MLQMWESSSK GKETLARNQA RSNIWSTAAE
     APLCYGCVVT LNETKDRELN WPSREHDVSQ VLAEFTLTDE E