ID   CTU1_VANPO              Reviewed;         363 AA.
AC   A7TER7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Kpol_1050p20;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS480381; EDO19163.1; -; Genomic_DNA.
DR   RefSeq; XP_001647021.1; XM_001646971.1.
DR   AlphaFoldDB; A7TER7; -.
DR   SMR; A7TER7; -.
DR   STRING; 436907.A7TER7; -.
DR   PRIDE; A7TER7; -.
DR   EnsemblFungi; EDO19163; EDO19163; Kpol_1050p20.
DR   GeneID; 5547494; -.
DR   KEGG; vpo:Kpol_1050p20; -.
DR   eggNOG; KOG2840; Eukaryota.
DR   HOGENOM; CLU_026481_1_2_1; -.
DR   InParanoid; A7TER7; -.
DR   OMA; MNLDQKQ; -.
DR   OrthoDB; 860739at2759; -.
DR   PhylomeDB; A7TER7; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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   TIGRFAMs; TIGR00269; TIGR00269; 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..363
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000368269"
SQ   SEQUENCE   363 AA;  41325 MW;  617D7EACD935A9CA CRC64;
     MFTAPSDPVN VRKELKVTQL CELCHSRKAI IRRPKNLQKI CKLCFFHVFE TEIHETIVSN
     DLFYRGERVA VGASGGKDST VLAYVLKLLN ERHDYGIEIV LLSIDEGIVG YRDDSLATVK
     RNQQQYQLPL EIFSYQDLYD WTMDDIVETA GIRNSCTYCG VLRRQALDRG AAKLEIKHVV
     TGHNADDMAE TVLMNILRGD VARLEKSTSI MTSSTGSPIK RSKPFKYCYQ KEIVLYAHYK
     KLDYFSTECT YAPEAFRGTA RELMKNFEAI RPSCIIDIIA SGESFVLKQK MGKQNKKKII
     TYNDGNRCER CGYLSSNKIC KACMLLEGLE KSRAQIKIQV QVPGEPQQEG PAKVLRTLER
     LTF