ID   CTU1_YEAS1              Reviewed;         359 AA.
AC   B3LHQ7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 48.
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};
DE   AltName: Full=Needs CLA4 to survive protein 6 {ECO:0000255|HAMAP-Rule:MF_03053};
DE   AltName: Full=Thiolation of uridine in cytoplasmic tRNA protein 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   TUC1 {ECO:0000255|HAMAP-Rule:MF_03053}; ORFNames=SCRG_01198;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Interacts with NCS2 and URM1. May act by forming a heterodimer
CC       with NCS2. Component of a large molecular weight complex of more than
CC       250 kDa. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053}.
CC       Mitochondrion {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; CH408044; EDV10415.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LHQ7; -.
DR   SMR; B3LHQ7; -.
DR   EnsemblFungi; EDV10415; EDV10415; SCRG_01198.
DR   HOGENOM; CLU_026481_1_0_1; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; Mitochondrion; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..359
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000368271"
SQ   SEQUENCE   359 AA;  40086 MW;  EC3BA9D54F642CD3 CRC64;
     MSFTAPSDPV NKPTKVKVSQ LCELCHSRKA LIRRPKNLSK LCKQCFCLVF ETEIHNTIVA
     NNLFQRGEKV AVGASGGKDS TVLAHMLKLL NDRYDYGIEI VLLSIDEGII GYRDDSLATV
     KRNQQQYGLP LEIFSFKDLY DWTMDEIVSV AGIRNSCTYC GVFRRQSLDR GAAKLGISHV
     VTGHNADDMA ETVLMNILRG DVARLEKSTA IITQSSGSPI KRSKPFKYSY QKEIVLYAHY
     MKLDYFSTEC TYAPEAFRGT AREYMKNLEA VRPSCIIDII QSGENLALKA KKSNARKRVV
     KFVDGNRCAR CGYLSSNNIC KACMLLEGLE KSRAQVAIEN DTSADGAALK LRALEKLSF