ID   CTU2_YEAS6              Reviewed;         493 AA.
AC   B5VQS7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
DE   AltName: Full=Needs CLA4 to survive protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
DE   AltName: Full=Thiolation of uridine in cytoplasmic tRNA 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   TUC2 {ECO:0000255|HAMAP-Rule:MF_03054}; ORFNames=AWRI1631_142030;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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   -!- SUBUNIT: Interacts with NCS6 and URM1. May act by forming a heterodimer
CC       with NCS6. {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; ABSV01001998; EDZ69720.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VQS7; -.
DR   PRIDE; B5VQS7; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000008988; 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; Phosphoprotein; tRNA processing.
FT   CHAIN           1..493
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369306"
FT   MOD_RES         489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53923"
SQ   SEQUENCE   493 AA;  56408 MW;  F587799AF1117D7D CRC64;
     MECQRCPASA RNPATVESRK EKFCDECFIK FVSTKQRKQM MKDEYFRNLF KVIYPFEKEG
     SVSKILLPLS LSDSGSLVML DIVHDLLLEQ TKQHNNRTGF TVDVLTVFTE ENVSVIKERM
     ESLINEKMSQ LNKISNIFNV HFIDVNEFFN NASEVSTFII DNENFEIFSK SKSVDDSNIL
     TLKEILGKYC LNNSSRSDLI SIIKTQLIKH FAYENGYNAI MWGHSMTKLS EVIISLVVKG
     KGSQIATFLD SESFDTLNNK PCKYKNLYPM KDLLSVEIES FLQIRNLAQF LINVEETNVK
     PNCLIARKSL PSLGQQKLVK NMTINEITNK YFQDIQNDYS NIISTVSRTA DKLTQPKSSM
     AKPSQCQICQ SKIYTNPSNW LNRITVTSPY PVETTEEKYL FKQWQDSKLG QSHTHYVELL
     NEIKQGASNS LDVEDGDVKL CYGCLILLNT SIKDKNLVWP KVDTMDITAN ATNNNKELSQ
     ILDQFEINSD GEE