CTU2_YEAS7
ID CTU2_YEAS7 Reviewed; 493 AA.
AC A6ZRW4; B0KZW1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 50.
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=SCY_4675;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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 -!- 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; EF125227; ABN58637.1; -; Genomic_DNA.
DR EMBL; AAFW02000067; EDN62696.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRW4; -.
DR PRIDE; A6ZRW4; -.
DR EnsemblFungi; EDN62696; EDN62696; SCY_4675.
DR HOGENOM; CLU_024534_1_0_1; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000007060; 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_0000359410"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53923"
SQ SEQUENCE 493 AA; 56441 MW; 41BC7A37E465D7B3 CRC64;
MECQRCSASA RNPATVESRK EKFCDECFIK FVSTKQRKQM MKDEYFRNLF KVIYPFEKEG
SVSKILLPLS LSDSGSLVML DIVHDLLLEQ TKQHNNRTGF TVDVLTVFTE ENVSVIKERM
ESLINEKMSQ LNKISNIFNV HFIDVNEFFN NASEVSTFII DNENFEIFSK SKSVDDSNIL
TLKEILGKYC LNSSSRSDLI SIIKTQLIKH FAYENGYNAI MWGHSMTKLS EVIISLVVKG
KGSQIATFLD SESFDTLNNK PCKYKNLYPM KDLLSVEIES FLQIRNLAQF LINVEETNVK
PNCLIARKSL PSLGQQKLVK NMTINEITNK YFQDIQNDYS NIISTVLRTA DKLTQPKSSM
AKPSQCQICQ SKIYTNPSNW LNRITVTSPY PVETTEEKYL FKQWQDSKLG QSHTHYVELL
NEIKQGASNS LDVEDSDVKL CYGCLILLNT SIKDKNLVWP KVDTMDITAN ATNKNKELSQ
ILDQFEINSD GEE