ID   CTU1_CRYNB              Reviewed;         363 AA.
AC   P0CS71; Q55RW8; Q5KGC1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 45.
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 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   Synonyms=CTU1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   OrderedLocusNames=CNBE4140;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053}.
CC   -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03053}.
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DR   EMBL; AAEY01000028; EAL20493.1; -; Genomic_DNA.
DR   RefSeq; XP_775140.1; XM_770047.1.
DR   AlphaFoldDB; P0CS71; -.
DR   SMR; P0CS71; -.
DR   EnsemblFungi; AAW43763; AAW43763; CNE04150.
DR   EnsemblFungi; EAL20493; EAL20493; CNBE4140.
DR   GeneID; 4936425; -.
DR   KEGG; cnb:CNBE4140; -.
DR   VEuPathDB; FungiDB:CNBE4140; -.
DR   HOGENOM; CLU_026481_1_2_1; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000001435; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IEA:EnsemblFungi.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
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; IEA:EnsemblFungi.
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   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.
PE   3: Inferred from homology;
KW   Cytoplasm; RNA-binding; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..363
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000410050"
FT   REGION          340..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   363 AA;  40294 MW;  DD431C55D144DC50 CRC64;
     MPPTPCSLCH TARALVKRPK TGQQVCKDCF FEVFETEVHN TIVEGEGIFK RGERVAIGAS
     GGKDSTVLAH VLSVLNKRYD YGLDLYLLSI DEGITGYRDD SLETVKQNQA EYGLPLKILS
     YSELYGWTMD KIVEQVGKKN NCTFCGVFRR QALDRGAAQL GVDHIVTGHN ADDIAETVLM
     NIMRGDIARL ARCTAVTTQS EDTIKRSKPF KYAYEKEIVM YAYFKKLTYF STECIYSPDA
     YRGHARVFLK DLEAVRPSAI VDIIHSGESF VLEQSVQRGM KALQTCLRCG YISSNDLCKA
     CALLEGLESG LSRSALRQTQ ESTSAAPEGH RTIPMFERYA SLNGTPRTPP TPAEPVEGIE
     RAA