ID   CTU2_ASPNC              Reviewed;         366 AA.
AC   A2R475;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=ncs2; Synonyms=ctu2; ORFNames=An14g06820;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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 ncs6 that ligates sulfur from
CC       thiocarboxylated urm1 onto the uridine of tRNAs at wobble position.
CC       Prior mcm(5) tRNA modification by the elongator complex is required for
CC       2-thiolation. May also be involved in protein urmylation.
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; AM270327; CAK46675.1; -; Genomic_DNA.
DR   RefSeq; XP_001401305.1; XM_001401268.1.
DR   AlphaFoldDB; A2R475; -.
DR   PaxDb; A2R475; -.
DR   EnsemblFungi; CAK46675; CAK46675; An14g06820.
DR   GeneID; 4987540; -.
DR   KEGG; ang:ANI_1_1636124; -.
DR   VEuPathDB; FungiDB:An14g06820; -.
DR   HOGENOM; CLU_024534_3_0_1; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000006706; Chromosome 1R.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
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: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.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..366
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369290"
SQ   SEQUENCE   366 AA;  41184 MW;  0F2D3F4C1C3517F9 CRC64;
     MPGKELPDRC MNCHEAEPAF LLRERHVCQE CYIRFLNFKP FRRMERYRLR RNMPQTGPCK
     LLLPLSYGVS STVLLHMLHR QLEALRSKKH GPAGFEILVL VVEPSTISPV PPHEEGFALA
     QQTFPLCSFT RLPFHSIFEL DPDVHQIMSQ YAGEHFTDDT SLSDEERLNR FRRSITTATS
     KSDVDQILLN KLVVAFAKKM ECRGIVWGDS DSKLAAKTLA NVAKGRGSAV TWQVCDGMSP
     FGLEFNFPLR DVFTAEIRTY ATLFPELAGI IVHDEPPSEN TLTKNLSIDE LMIRYVSTQG
     EKYPGVMLNV TRTASKLQSS GTSIGGLQCN FCGAFMTTNE NITGEQGNEQ LQFCYACARS
     QPELSC