ID   CTU1_PICST              Reviewed;         376 AA.
AC   A3GGB3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   25-MAY-2022, entry version 81.
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}; ORFNames=PICST_39100;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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). 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; AAVQ01000001; EAZ63900.2; -; Genomic_DNA.
DR   RefSeq; XP_001387923.2; XM_001387886.1.
DR   AlphaFoldDB; A3GGB3; -.
DR   SMR; A3GGB3; -.
DR   STRING; 4924.XP_001387923.2; -.
DR   EnsemblFungi; EAZ63900; EAZ63900; PICST_39100.
DR   GeneID; 4851312; -.
DR   KEGG; pic:PICST_39100; -.
DR   eggNOG; KOG2840; Eukaryota.
DR   HOGENOM; CLU_026481_1_2_1; -.
DR   InParanoid; A3GGB3; -.
DR   OMA; MNLDQKQ; -.
DR   OrthoDB; 860739at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000002258; Chromosome 1.
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; 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: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   PROSITE; PS01263; UPF0021; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..376
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000368267"
SQ   SEQUENCE   376 AA;  41984 MW;  4A30076B85B9F26D CRC64;
     MTEISAKKVK VSALCELCHA RKAVMKRPKN LQKLCKDCFY KVFETEIHNT IVDAKLFSPG
     DKVAIGASGG KDSTVLASVL KTLNERYDYG LILVLLSIDE GIKGYRDDSL ATVKRNQVQY
     EMPLEIISYR DLYNWTMDEI VSCAGIRSSC TYCGVLRRQA LDRGAAKLGI NHVVTGHNAD
     DMAETVLMNL LRGDTARLEK SCAIITQSAG SPIKRSKPFK YTYQKEIVLY AHYKKLDYFS
     TECTYAPEAF RGTARELLKS LESIRPSCIM DIIYSGEHLV LAPKKKKITT SYKTNKKKTH
     TENEVNADGS VSLGRKKQFE DGNRCEKCGY LSSNRICKAC MLLAGLEMNR AKVSIDNNTA
     VDGAAVLTRT LEQLSF