CTU1_CAEEL
ID CTU1_CAEEL Reviewed; 373 AA.
AC O76365;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=Thiolation of uridine in tRNA protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Name=tut-1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Synonyms=ctu-1 {ECO:0000255|HAMAP-Rule:MF_03053}; ORFNames=F29C4.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION IN 2-THIOLATION OF TRNA, AND DISRUPTION PHENOTYPE.
RX PubMed=18391219; DOI=10.1073/pnas.0709404105;
RA Dewez M., Bauer F., Dieu M., Raes M., Vandenhaute J., Hermand D.;
RT "The conserved wobble uridine tRNA thiolase Ctu1-Ctu2 is required to
RT maintain genome integrity.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5459-5464(2008).
RN [3]
RP TRNA-BINDING.
RX PubMed=19145231; DOI=10.1038/nature07643;
RA Leidel S., Pedrioli P.G.A., Bucher T., Brost R., Costanzo M., Schmidt A.,
RA Aebersold R., Boone C., Hofmann K., Peter M.;
RT "Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of
RT eukaryotic transfer RNA.";
RL Nature 458:228-233(2009).
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, ECO:0000269|PubMed:18391219}.
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 -!- DISRUPTION PHENOTYPE: Required for normal germline maturation and for
CC viability. Viable at 20 degrees Celsius. At a higher temperature (25
CC degrees Celsius), the hatched eggs progress through the L1-L4 larval
CC stages with kinetics similar to those of wild type but present an
CC important delay in germline maturation. Whereas gravid wild-type worms
CC are present 53 hours after hatching, germline maturation are still
CC ongoing in the mutant after 66 hours, and the first adults containing
CC eggs are observed 75 hours after hatching, when a large number of new
CC L1 are already present in the wild type. Strikingly, the eggs that
CC finally appeared in the mutant display aberrant morphology and size
CC resulting in both low progeny and high mortality.
CC {ECO:0000269|PubMed:18391219}.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03053}.
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DR EMBL; FO080227; CCD62179.1; -; Genomic_DNA.
DR PIR; T33145; T33145.
DR RefSeq; NP_499865.1; NM_067464.3.
DR AlphaFoldDB; O76365; -.
DR SMR; O76365; -.
DR STRING; 6239.F29C4.6.1; -.
DR EPD; O76365; -.
DR PaxDb; O76365; -.
DR PeptideAtlas; O76365; -.
DR PRIDE; O76365; -.
DR EnsemblMetazoa; F29C4.6.1; F29C4.6.1; WBGene00017928.
DR EnsemblMetazoa; F29C4.6.2; F29C4.6.2; WBGene00017928.
DR GeneID; 176826; -.
DR KEGG; cel:CELE_F29C4.6; -.
DR UCSC; F29C4.6.1; c. elegans.
DR CTD; 176826; -.
DR WormBase; F29C4.6; CE17723; WBGene00017928; tut-1.
DR eggNOG; KOG2840; Eukaryota.
DR GeneTree; ENSGT00390000001041; -.
DR HOGENOM; CLU_026481_1_2_1; -.
DR InParanoid; O76365; -.
DR OMA; MNLDQKQ; -.
DR OrthoDB; 860739at2759; -.
DR PhylomeDB; O76365; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:O76365; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00017928; Expressed in germ line (C elegans) and 4 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:0016783; F:sulfurtransferase activity; IMP:WormBase.
DR GO; GO:0000049; F:tRNA binding; IDA:WormBase.
DR GO; GO:0048598; P:embryonic morphogenesis; IGI:WormBase.
DR GO; GO:0048599; P:oocyte development; IGI:WormBase.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0007283; P:spermatogenesis; IGI:WormBase.
DR GO; GO:0006412; P:translation; IMP:WormBase.
DR GO; GO:0034227; P:tRNA thio-modification; IMP:WormBase.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:WormBase.
DR GO; GO:0040025; P:vulval development; IGI:WormBase.
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 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..373
FT /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT /id="PRO_0000368239"
SQ SEQUENCE 373 AA; 41332 MW; B5E4A95EE348B841 CRC64;
MEKRRGPPPC QSGSGCSNPA KIRKAKDGAQ LCGPCFSRNF EDDVHEAIVN NKLFKRGERV
AIGASGGKDS TVLAYVMKTL NDRHDYGLDL QLLSIDEGIK GYRDDSLLAV EKNRVEYGLP
LTILSYRDLY GWTMDDIVAK IGKKNNCTFC GVFRRQALDR GAFKIGATKL VTGHNADDMA
ETLLMNVLRG DIARLERCTN IVTGEEGDLP RAKPLKYCFE RDIVMYARTN QLEYFYTECI
YAPNAYRGYA RKYVRDLEKV HPRAILDLIR SGEKVSVKKE VEMPTLKICE RCGYMTSQKL
CKACLLIEGL NTGNTDLGVR KSKKSKKVTV EADELNKEGG CGSGGGGGGC GCAGAEDAAE
NEETRQRLKD LQF