CTU2_YEAST
ID CTU2_YEAST Reviewed; 493 AA.
AC P53923; B0KZR6; B0KZS5; B0KZU3; B0KZW1; B0L006; D6W163; Q66R25;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
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}; OrderedLocusNames=YNL119W;
GN ORFNames=N1913;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-7; LEU-71; SER-193;
RP SER-409; GLY-428; SER-436 AND ASN-474.
RC STRAIN=ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270,
RC YJM 320, YJM 326, YJM 339, YJM 627, and YJM230;
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=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=14551258; DOI=10.1091/mbc.e03-02-0079;
RA Goehring A.S., Rivers D.M., Sprague G.F. Jr.;
RT "Urmylation: a ubiquitin-like pathway that functions during invasive growth
RT and budding in yeast.";
RL Mol. Biol. Cell 14:4329-4341(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=14671320; DOI=10.1073/pnas.2536857100;
RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M.,
RA Ahlquist P.;
RT "Systematic, genome-wide identification of host genes affecting replication
RT of a positive-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18664566; DOI=10.1074/jbc.m804043200;
RA Nakai Y., Nakai M., Hayashi H.;
RT "Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related
RT system that resembles bacterial sulfur transfer systems.";
RL J. Biol. Chem. 283:27469-27476(2008).
RN [11]
RP FUNCTION.
RX PubMed=18755837; DOI=10.1261/rna.1184108;
RA Huang B., Lu J., Bystroem A.S.;
RT "A genome-wide screen identifies genes required for formation of the wobble
RT nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces
RT cerevisiae.";
RL RNA 14:2183-2194(2008).
RN [12]
RP FUNCTION IN 2-THIOLATION OF TRNA, AND INTERACTION WITH NCS6 AND URM1.
RX PubMed=19145231; DOI=10.1038/nature07643;
RA Leidel S., Pedrioli P.G.A., Bucher T., Brost R., Costanzo M., Schmidt A.,
RA Aebersold R., Boone C., Hofmann K., Peter M.;
RT "Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of
RT eukaryotic transfer RNA.";
RL Nature 458:228-233(2009).
RN [13]
RP FUNCTION IN 2-THIOLATION OF TRNA.
RX PubMed=19151091; DOI=10.1093/nar/gkn1023;
RA Noma A., Sakaguchi Y., Suzuki T.;
RT "Mechanistic characterization of the sulfur-relay system for eukaryotic 2-
RT thiouridine biogenesis at tRNA wobble positions.";
RL Nucleic Acids Res. 37:1335-1352(2009).
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 and in
CC invasive and pseudohyphal growth. Inhibits replication of Brome mosaic
CC virus. {ECO:0000255|HAMAP-Rule:MF_03054, ECO:0000269|PubMed:14551258,
CC ECO:0000269|PubMed:14671320, ECO:0000269|PubMed:18664566,
CC ECO:0000269|PubMed:18755837, ECO:0000269|PubMed:19145231,
CC ECO:0000269|PubMed:19151091}.
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 ECO:0000269|PubMed:19145231}.
CC -!- INTERACTION:
CC P53923; P53088: NCS6; NbExp=3; IntAct=EBI-28871, EBI-24137;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18664566}.
CC -!- MISCELLANEOUS: Present with 2860 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03054}.
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DR EMBL; EF125216; ABN58538.1; -; Genomic_DNA.
DR EMBL; EF125217; ABN58547.1; -; Genomic_DNA.
DR EMBL; EF125218; ABN58556.1; -; Genomic_DNA.
DR EMBL; EF125219; ABN58565.1; -; Genomic_DNA.
DR EMBL; EF125220; ABN58574.1; -; Genomic_DNA.
DR EMBL; EF125221; ABN58583.1; -; Genomic_DNA.
DR EMBL; EF125222; ABN58592.1; -; Genomic_DNA.
DR EMBL; EF125223; ABN58601.1; -; Genomic_DNA.
DR EMBL; EF125224; ABN58610.1; -; Genomic_DNA.
DR EMBL; EF125225; ABN58619.1; -; Genomic_DNA.
DR EMBL; EF125226; ABN58628.1; -; Genomic_DNA.
DR EMBL; EF125228; ABN58646.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93388.1; -; Genomic_DNA.
DR EMBL; Z71396; CAA96001.1; -; Genomic_DNA.
DR EMBL; AY723860; AAU09777.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10429.1; -; Genomic_DNA.
DR PIR; S63060; S63060.
DR RefSeq; NP_014280.3; NM_001182957.3.
DR AlphaFoldDB; P53923; -.
DR BioGRID; 35707; 345.
DR DIP; DIP-6649N; -.
DR IntAct; P53923; 6.
DR MINT; P53923; -.
DR STRING; 4932.YNL119W; -.
DR iPTMnet; P53923; -.
DR MaxQB; P53923; -.
DR PaxDb; P53923; -.
DR PRIDE; P53923; -.
DR EnsemblFungi; YNL119W_mRNA; YNL119W; YNL119W.
DR GeneID; 855603; -.
DR KEGG; sce:YNL119W; -.
DR SGD; S000005063; NCS2.
DR VEuPathDB; FungiDB:YNL119W; -.
DR eggNOG; KOG2594; Eukaryota.
DR GeneTree; ENSGT00390000008797; -.
DR HOGENOM; CLU_024534_1_0_1; -.
DR InParanoid; P53923; -.
DR OMA; SCSMLRQ; -.
DR BioCyc; YEAST:G3O-33141-MON; -.
DR UniPathway; UPA00988; -.
DR ChiTaRS; NCS2; yeast.
DR PRO; PR:P53923; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53923; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA: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; IMP:SGD.
DR GO; GO:0032447; P:protein urmylation; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0034227; P:tRNA thio-modification; IMP:UniProtKB.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IMP:SGD.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP: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 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..493
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000203432"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT VARIANT 7
FT /note="P -> S (in strain: YJM230 and YJM320)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 71
FT /note="H -> L (in strain: SK1, V1-09, YJM1129, YJM269,
FT YJM270, YJM320, YJM326, YJM230, YJM339 and YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 193
FT /note="N -> S (in strain: SK1, V1-09, YJM230, YJM320 and
FT YJM339)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 409
FT /note="L -> S (in strain: YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 428
FT /note="S -> G (in strain: YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 436
FT /note="G -> S (in strain: YJM230 and YJM320)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 474
FT /note="K -> N (in strain: YJM1129, YJM269, YJM270, YJM326
FT and YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT CONFLICT 36
FT /note="Q -> R (in Ref. 4; AAU09777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 56473 MW; 420FE465B982C43E CRC64;
MECQRCPASA RNPATVESRK EKFCDECFIK FVSTKQRKQM MKDEYFRNLF KVIYPFEKEG
SVSKILLPLS HSDSGSLVML 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 NIISTVLRTA DKLTQPKSSM
AKPSQCQICQ SKIYTNPSNW LNRITVTSPY PVETTEEKYL FKQWQDSKLG QSHTHYVELL
NEIKQGASNS LDVEDGDVKL CYGCLILLNT SIKDKNLVWP KVDTMDITAN ATNKNKELSQ
ILDQFEINSD GEE
