ID   CTU2_SCHPO              Reviewed;         366 AA.
AC   Q9UUC7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=ctu2; Synonyms=ncs2; ORFNames=SPBC19C2.13c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH CTU1.
RX   PubMed=18391219; DOI=10.1073/pnas.0709404105;
RA   Dewez M., Bauer F., Dieu M., Raes M., Vandenhaute J., Hermand D.;
RT   "The conserved wobble uridine tRNA thiolase Ctu1-Ctu2 is required to
RT   maintain genome integrity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5459-5464(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 ctu1 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, ECO:0000269|PubMed:18391219}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SUBUNIT: Interacts with ctu1. {ECO:0000269|PubMed:18391219}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054,
CC       ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03054}.
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DR   EMBL; CU329671; CAB52040.1; -; Genomic_DNA.
DR   PIR; T39804; T39804.
DR   RefSeq; NP_595698.1; NM_001021595.2.
DR   AlphaFoldDB; Q9UUC7; -.
DR   SMR; Q9UUC7; -.
DR   BioGRID; 277412; 26.
DR   DIP; DIP-29901N; -.
DR   IntAct; Q9UUC7; 1.
DR   STRING; 4896.SPBC19C2.13c.1; -.
DR   MaxQB; Q9UUC7; -.
DR   PaxDb; Q9UUC7; -.
DR   EnsemblFungi; SPBC19C2.13c.1; SPBC19C2.13c.1:pep; SPBC19C2.13c.
DR   GeneID; 2540896; -.
DR   KEGG; spo:SPBC19C2.13c; -.
DR   PomBase; SPBC19C2.13c; ctu2.
DR   VEuPathDB; FungiDB:SPBC19C2.13c; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_3_0_1; -.
DR   InParanoid; Q9UUC7; -.
DR   OMA; GKLCYGC; -.
DR   PhylomeDB; Q9UUC7; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q9UUC7; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IPI:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IDA:PomBase.
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; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..366
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000359408"
SQ   SEQUENCE   366 AA;  40742 MW;  7D59F90208A79E09 CRC64;
     MQNTALDNSA DSKCSKCDNK ATVLTKSDAV CDSCFVRRIE NKIRRQFELV RPNLQGRKSK
     RAMLAISGGI SSMAMLETAN YLSKYRDDNY RPMFDELLAV HFQWGTDSAV AKTIEESISK
     NYPKCPFKVI GEAELLNRTI ATDSRGNIEI NADNEKFNPE VISSLASRQD LLYRIRDKLL
     VSYARKANCD TIVFGDSGTT IAARVLELVA EGRGFAIPWY TSVCSKLPNC DTFLLRPLRE
     VLSSDLKSYM NIKGLAFCDS LIEARPNTIH GVTESYFSSL NDTFPSLVST VVKMSSKLHV
     PSTEAICTIC NLPMQEDAET WLQKTTVEHP DSVEGIKNQN VCYGCSVSLK SLKGTLHIPD
     IEKEGI