ID   CTU2_NEOFI              Reviewed;         370 AA.
AC   A1DDV3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=ncs2; Synonyms=ctu2; ORFNames=NFIA_074800;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027696; EAW17560.1; -; Genomic_DNA.
DR   RefSeq; XP_001259457.1; XM_001259456.1.
DR   AlphaFoldDB; A1DDV3; -.
DR   STRING; 36630.CADNFIAP00007414; -.
DR   EnsemblFungi; EAW17560; EAW17560; NFIA_074800.
DR   GeneID; 4585824; -.
DR   KEGG; nfi:NFIA_074800; -.
DR   VEuPathDB; FungiDB:NFIA_074800; -.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_3_0_1; -.
DR   OMA; SCSMLRQ; -.
DR   OrthoDB; 1442062at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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.
DR   Pfam; PF10288; CTU2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..370
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369298"
SQ   SEQUENCE   370 AA;  40809 MW;  0B7B7F304AB0953B CRC64;
     MPGKQLSDPC VDCSDAEAIL TLRTRRLCQT CYARFVNFKV FKRMENYRLR RNMPKTGPCK
     LLLPLSCGIS SSVLLHILNA QIQLELAKSH PSPGFDLHVL VIEPSSISHS SPSYDEGFGL
     LQQTFPLHSF TRIPLHSIFE LDPELQEVIS QFSKDGFVDD AGLSAKERLD AFRASIPTST
     SKVDVDYVLI TRLVVAFAKK IACRGVLWGD SDTRLAAKTL ANVAKGRGSS LTWQVCDGMS
     PFGVEFNFPL RDLFKAEVDN YASFFPELTR IIIPDEPPSE NVLTKNLSID ELMMRYVQTQ
     GEKYPGVMAN VTRTASKLQA SLTPANVPQC SFCGAFMLNS GNNGGGDTTG ASRALELCYA
     CTRSRPELTC