ID   CTU2_DICDI              Reviewed;         523 AA.
AC   Q55EX7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=ctu2; ORFNames=DDB_G0268714;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000004; EAL72946.1; -; Genomic_DNA.
DR   RefSeq; XP_646893.1; XM_641801.1.
DR   AlphaFoldDB; Q55EX7; -.
DR   SMR; Q55EX7; -.
DR   STRING; 44689.DDB0302516; -.
DR   PaxDb; Q55EX7; -.
DR   EnsemblProtists; EAL72946; EAL72946; DDB_G0268714.
DR   GeneID; 8616578; -.
DR   KEGG; ddi:DDB_G0268714; -.
DR   dictyBase; DDB_G0268714; ctu2.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_521211_0_0_1; -.
DR   InParanoid; Q55EX7; -.
DR   OMA; SCSMLRQ; -.
DR   PhylomeDB; Q55EX7; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q55EX7; -.
DR   Proteomes; UP000002195; Chromosome 1.
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   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..523
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369281"
FT   REGION          53..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  59126 MW;  DDE3B0F4012E9480 CRC64;
     MSSEELPSCG INDNDINNTI PINTRKVQII PNGNTQCVKC LYNVANNVKD KKLSKKEKKE
     QKLKEEENNN NNNEEPITQQ QKPIGKPIIN FRSEQLCWEC YRELILKKFK LNIVKVRESK
     RDAEKLLVAL SGGTCSSMLL ELLKQCTEGS GKAKMFLDIK CVHIDESSIT PYQNHNDTIE
     FLKEFNNVKL GFPNLEIIPL EDILGTVTPL GERTNQLKLQ FAQLSSETSK EDLLLYYRNQ
     LLIQVAHKLN CKKVILGTSS NRLAVQLVAS TSKGRGFSVP NETSVIIEQP SNDIKFYQPM
     RDFLLKEIFI YYRHLNILPV PVMFSILNLK PKHSINTLCE DFLHCLQDIS NQTVHTLLRS
     VDKLISPSID SNYNCSICSS PLTSAEIKSL EKVILDNNNN INKENKNNNN NNNNNNNNNG
     CCSTTKTEDS SCCNKTEDNS SNNNNNNTGC CSSSSSTSTS SITVNKETLC YSCKILYRDF
     KSTPNIAPYI KENSKQLLTT SQLKNEIKDF LLNSDDDDDD EDN