ID   CTU2_DANRE              Reviewed;         501 AA.
AC   Q6DC53; F1QNK0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=ctu2; Synonyms=ncs2; ORFNames=zgc:101113;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) 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). May act by
CC       forming a heterodimer with ctu1/atpbd3 that ligates sulfur from
CC       thiocarboxylated urm1 onto the uridine of tRNAs at wobble position.
CC       {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}.
CC   -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03054}.
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DR   EMBL; CR547125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC078233; AAH78233.1; -; mRNA.
DR   RefSeq; NP_001003560.1; NM_001003560.1.
DR   AlphaFoldDB; Q6DC53; -.
DR   STRING; 7955.ENSDARP00000068045; -.
DR   PaxDb; Q6DC53; -.
DR   PRIDE; Q6DC53; -.
DR   Ensembl; ENSDART00000073555; ENSDARP00000068045; ENSDARG00000051851.
DR   GeneID; 445166; -.
DR   KEGG; dre:445166; -.
DR   CTD; 348180; -.
DR   ZFIN; ZDB-GENE-040801-79; ctu2.
DR   eggNOG; KOG2594; Eukaryota.
DR   GeneTree; ENSGT00390000008797; -.
DR   HOGENOM; CLU_024534_2_0_1; -.
DR   InParanoid; Q6DC53; -.
DR   OMA; SCSMLRQ; -.
DR   OrthoDB; 1442062at2759; -.
DR   PhylomeDB; Q6DC53; -.
DR   TreeFam; TF313203; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q6DC53; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000051851; Expressed in ovary and 28 other tissues.
DR   ExpressionAtlas; Q6DC53; baseline.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
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_03054; CTU2; 1.
DR   InterPro; IPR019407; CTU2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR20882; PTHR20882; 1.
DR   Pfam; PF10288; CTU2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..501
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000289178"
FT   CONFLICT        164
FT                   /note="S -> F (in Ref. 1; CR547125)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  55825 MW;  0B3F803A9CAC2DB9 CRC64;
     MCQVEEDYNG LECNQEKIPV SGLNRKCMKC KEGTAVLIIR VSDAFCRSCF KEYFIHKFRA
     MLGKNRVIFP QEKVLLAVSG GAASCTMLSQ VQEGLSRDAP KKLRFMPGIV YIDDGGACGR
     SEDERQTSIS QLKNIFTQTG FPYFIVPLEK VFSLPTSVLV PGTSDPDPSN PCYKQAVDKY
     LKEKQKLREE EAVCAVAQLN LEDSAYLPEH KLALQRLFSS LKTLSAKQEM LQTLRQHLIL
     HVARENSYSK VMMGESCSRL AVKLLSNIAL GRGAALASDT GFSDPRFGDV VIVRPMRDYS
     SKEITFYNRM FHVPSVFIPG LDTKSHDKAS IQRLTESFVT NLQADFPSTV STIYRTSEKL
     HTVRPPQSQS TEPEPASKCL LCLCALDTTA DKASAFHATL ISEQLSQLRL QEGSVDLVAG
     SSDQCCVEDQ TCGTSGCCSS KRTPVQQDLK TLLCYSCRLT VKDMAAVNTL PPYILTEAEK
     RQRRSQMKVE ISEYLLEEDQ D