ID   CTU2_PICST              Reviewed;         448 AA.
AC   A3M0F4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 69.
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}; ORFNames=PICST_50402;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000502; ABN68699.2; -; Genomic_DNA.
DR   RefSeq; XP_001386728.2; XM_001386691.1.
DR   AlphaFoldDB; A3M0F4; -.
DR   STRING; 4924.XP_001386728.2; -.
DR   PRIDE; A3M0F4; -.
DR   EnsemblFungi; ABN68699; ABN68699; PICST_50402.
DR   GeneID; 4840963; -.
DR   KEGG; pic:PICST_50402; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_1_0_1; -.
DR   InParanoid; A3M0F4; -.
DR   OMA; SCSMLRQ; -.
DR   OrthoDB; 1442062at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000002258; Chromosome 8.
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_0000369301"
SQ   SEQUENCE   448 AA;  50980 MW;  476300521FEE1AE0 CRC64;
     MSENNPVKYL ADSDTECQRC KAVPAVLITR KEAFCKNCFI RFIRGKQRKS MIDERYKVKY
     GAVQEKIGQQ KVLLALSGGV SSLVLTDVVA SLLQEQIESH KGRMGFELVL LNIDEFELES
     LNKRIEEILP ILVERYAPVN IQYKVLSIES FLIDRAMIQK VLLNKDFTAI AQRLSDEQNK
     YTVADMLKLC PNKSSMEDLL TVIYEELILR TAFIENCETI IYGHSMTRIA NEILALTVRG
     RGSSVYKAIA DHTVQFMDKE FTILFPLRDV LFAEIIAYAD LIELNKLEVK STIVKSKITK
     NLTIRDLTTN YFSHLDATGY ASTASTVVKT GEKLGAPQFK HSYGRCQICG VEIYQDPKEW
     LRRITVNDAA PIETEEEQEY VNLYKEALSS SETLDTENTH PVNICYGCIV TLSGAKQDTA
     FVWPLKDKDT NHEDKKVLDE YILTDDEE