ID   CTU1_BOVIN              Reviewed;         347 AA.
AC   Q0VC66;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=ATP-binding domain-containing protein 3 {ECO:0000255|HAMAP-Rule:MF_03053};
DE   AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   Name=CTU1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN   Synonyms=ATPBD3 {ECO:0000255|HAMAP-Rule:MF_03053},
GN   NCS6 {ECO:0000255|HAMAP-Rule:MF_03053};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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. {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: Component of a complex at least composed of URM1, CTU2/NCS2
CC       and CTU1/ATPBD3. May form a heterodimer with CTU2/NCS2.
CC       {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; BC120329; AAI20330.1; -; mRNA.
DR   RefSeq; NP_001071422.1; NM_001077954.1.
DR   AlphaFoldDB; Q0VC66; -.
DR   SMR; Q0VC66; -.
DR   STRING; 9913.ENSBTAP00000050053; -.
DR   PaxDb; Q0VC66; -.
DR   Ensembl; ENSBTAT00000055031; ENSBTAP00000050053; ENSBTAG00000039212.
DR   GeneID; 522824; -.
DR   KEGG; bta:522824; -.
DR   CTD; 90353; -.
DR   VEuPathDB; HostDB:ENSBTAG00000039212; -.
DR   eggNOG; KOG2840; Eukaryota.
DR   GeneTree; ENSGT00390000001041; -.
DR   HOGENOM; CLU_026481_1_0_1; -.
DR   InParanoid; Q0VC66; -.
DR   OMA; CLHINLG; -.
DR   OrthoDB; 860739at2759; -.
DR   TreeFam; TF352405; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000039212; Expressed in rumen papilla and 102 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
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; IBA:GO_Central.
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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..347
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT                   /id="PRO_0000282390"
FT   REGION          315..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..347
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z7A3"
SQ   SEQUENCE   347 AA;  36599 MW;  52CB494EADC6BD69 CRC64;
     MPAPQCASCH KARAALRRPR SGQALCGSCF CAAFEAEVLH TVVAGRLLPP GAVVAVGASG
     GKDSTVLAHV LRELAPRLGI SLHLVAVDEG IGGYRDAALA AVRRQAARWE LPLTVVAYAD
     LFGGWTMDAV ARSTAGSGRS RACCTFCGVL RRRALEEGAR LVGATHVVTG HNADDMAETV
     LMNFLRGDAG RLARGGGLGS PGEGGALPRC RPLQLASQKE VVLYAHFRRL DYFSEECVYA
     PEAFRGHARD LLKMLEAARP SAVLDLVHSA ERLALAPTAR PPPPGACSRC GALASRALCQ
     ACALLDGLNR GRPRLAIGKG RRGLDEEGPP REPQPSRPLT SEPVPDF