ID   CTU2_VANPO              Reviewed;         485 AA.
AC   A7TGI5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=Kpol_1048p22;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480387; EDO18592.1; -; Genomic_DNA.
DR   RefSeq; XP_001646450.1; XM_001646400.1.
DR   AlphaFoldDB; A7TGI5; -.
DR   STRING; 436907.A7TGI5; -.
DR   EnsemblFungi; EDO18592; EDO18592; Kpol_1048p22.
DR   GeneID; 5546892; -.
DR   KEGG; vpo:Kpol_1048p22; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_1_0_1; -.
DR   InParanoid; A7TGI5; -.
DR   OMA; SCSMLRQ; -.
DR   OrthoDB; 1442062at2759; -.
DR   PhylomeDB; A7TGI5; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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..485
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369304"
SQ   SEQUENCE   485 AA;  56353 MW;  1AA5DB5081D058BB CRC64;
     MSDSHSHSDI LLCQRCNKNH ASVISRKEKF CTDCFRNFVS LKQRKQMMSD QYYQDIFKVM
     YKDKLRSEQD AHLQNLNSKI LVPLSFGSSS LVMLDILNDT LLEQSITHRG KTGFTVDVII
     CFHDEQIQNQ IKENVSKLIN AKYKENNQKI KFHLVDINQF FDNSPHLQSL VLQETDFLIK
     SLNLKDQSII EKKLTLSEIL DQCSDRSTYQ DLLAFVTKHA IKKYAFQHDF KAILWGHSMT
     RLADEVISLI VKGRGSAISS SLNTDDFDEN YGNKFKNLYP LKDILLTEID AYCYNSGLHN
     YLINYNIQDA LLVNKINQNT DKIQTNSLKN KTINELARNY FEVIEGDYSN VISTVVRTGD
     KLAEPKSQEN FKISKCNLCM QKIYSDPSQW ITSITENKGH PLETDEEKEN YQRWKNYNND
     KLKNSEMDFF RLNEFVKENG SKACLCYGCT ITLNTFKDKS VVWPVHDDKE LNSVLEDYVL
     TDHEE