ID   CTU1_SCHPO              Reviewed;         335 AA.
AC   O94282;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_03053};
DE   AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   Name=ncs6; Synonyms=ctu1; ORFNames=SPBC2G5.03;
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, INTERACTION WITH CTU2, AND MUTAGENESIS OF 62-LYS--ASP-63; CYS-142
RP   AND CYS-145.
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). Directly binds
CC       tRNAs and probably acts by catalyzing adenylation of tRNAs, an
CC       intermediate required for 2-thiolation. It is unclear whether it acts
CC       as a sulfurtransferase that transfers sulfur from thiocarboxylated urm1
CC       onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA
CC       modification by the elongator complex is required for 2-thiolation. May
CC       also be involved in protein urmylation. {ECO:0000255|HAMAP-
CC       Rule:MF_03053, ECO:0000269|PubMed:18391219}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC   -!- SUBUNIT: Interacts with ctu2. {ECO:0000269|PubMed:18391219}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053,
CC       ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03053}.
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DR   EMBL; CU329671; CAA21879.1; -; Genomic_DNA.
DR   PIR; T40160; T40160.
DR   RefSeq; NP_596064.1; NM_001021975.2.
DR   AlphaFoldDB; O94282; -.
DR   SMR; O94282; -.
DR   BioGRID; 276844; 44.
DR   DIP; DIP-29900N; -.
DR   IntAct; O94282; 1.
DR   STRING; 4896.SPBC2G5.03.1; -.
DR   iPTMnet; O94282; -.
DR   MaxQB; O94282; -.
DR   PaxDb; O94282; -.
DR   PRIDE; O94282; -.
DR   EnsemblFungi; SPBC2G5.03.1; SPBC2G5.03.1:pep; SPBC2G5.03.
DR   GeneID; 2540314; -.
DR   KEGG; spo:SPBC2G5.03; -.
DR   PomBase; SPBC2G5.03; -.
DR   VEuPathDB; FungiDB:SPBC2G5.03; -.
DR   eggNOG; KOG2840; Eukaryota.
DR   HOGENOM; CLU_026481_1_0_1; -.
DR   InParanoid; O94282; -.
DR   OMA; CLHINLG; -.
DR   PhylomeDB; O94282; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:O94282; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IPI:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IPI:PomBase.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IMP:PomBase.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_03053; CTU1; 1.
DR   InterPro; IPR032442; CTU1_C.
DR   InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR   InterPro; IPR020554; UPF0021_CS.
DR   PANTHER; PTHR11807:SF12; PTHR11807:SF12; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF16503; zn-ribbon_14; 1.
DR   PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR   TIGRFAMs; TIGR00269; TIGR00269; 1.
DR   PROSITE; PS01263; UPF0021; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..335
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000316593"
FT   MUTAGEN         62..63
FT                   /note="KD->AA: No thiolation of tRNA(Lys)."
FT                   /evidence="ECO:0000269|PubMed:18391219"
FT   MUTAGEN         142
FT                   /note="C->A: No thiolation of tRNA(Lys)."
FT                   /evidence="ECO:0000269|PubMed:18391219"
FT   MUTAGEN         145
FT                   /note="C->A: No thiolation of tRNA(Lys)."
FT                   /evidence="ECO:0000269|PubMed:18391219"
SQ   SEQUENCE   335 AA;  37861 MW;  DB1CA07DC4A6DA20 CRC64;
     MSNKLCQLCN ERRPALVRPK TGQKICKECF YYVFETEIHN VIIENKLFVR GERVGIGASG
     GKDSTVLAYV MKLLNERYDY GLELYLISVD EGIRGYRDDS LDTVKRNQQQ YGLPMKIVSY
     ADLYDGWTMD NVVARIGTKN NCTYCGVFRR QALDRAALSL DIHHLVTGHN ADDIAETILM
     NLLRGDVARL PRSTEITTQS DSSPTKRSKP FKYSYEKEIV LYAHYKKLDY FSTECTYSPE
     AFRGTARAMI KQLENIRPSS ILDIIYSGES MQLASSVQEQ LPQQTTCERC GFISSNRICK
     ACMLLEGLNK GITGLGLGSD RKTKKLQSQI PACAE