ID   CTU2_XENTR              Reviewed;         516 AA.
AC   Q28ES8; B3DL40; Q5FVY8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=ctu2; Synonyms=ncs2; ORFNames=TGas114e15.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Neurula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH89700.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR762362; CAJ83521.1; -; mRNA.
DR   EMBL; BC089700; AAH89700.1; ALT_INIT; mRNA.
DR   EMBL; BC167302; AAI67302.1; -; mRNA.
DR   EMBL; BC170700; AAI70700.1; -; mRNA.
DR   EMBL; BC170702; AAI70702.1; -; mRNA.
DR   RefSeq; NP_001034829.1; NM_001039740.1.
DR   RefSeq; XP_012816477.1; XM_012961023.1.
DR   AlphaFoldDB; Q28ES8; -.
DR   STRING; 8364.ENSXETP00000024569; -.
DR   PaxDb; Q28ES8; -.
DR   GeneID; 548371; -.
DR   KEGG; xtr:548371; -.
DR   CTD; 348180; -.
DR   Xenbase; XB-GENE-5732028; ctu2.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_2_0_1; -.
DR   InParanoid; Q28ES8; -.
DR   OrthoDB; 1442062at2759; -.
DR   PhylomeDB; Q28ES8; -.
DR   TreeFam; TF313203; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000011252; Expressed in egg cell and 14 other tissues.
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..516
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000289181"
FT   CONFLICT        208
FT                   /note="S -> C (in Ref. 2; AAH89700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="A -> T (in Ref. 2; AAH89700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332
FT                   /note="P -> Q (in Ref. 2; AAH89700)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   516 AA;  57857 MW;  32C34377D8A10775 CRC64;
     MCEEEEVYCP ELQDTTQGKS LGKTCMKCKE SSAVLLIRAG DAFCKSCFKE YFVHKFRATL
     GKNRVIYPGE KVLLAFSGGP SSSAMVQQVQ EGMSRDAPKK LRFVPGILFI DEGTTCGMSH
     EERQQNMSEV QNVLQQTGFP FYIVSLEQVF SLPGSILQRG VPEQRANYKQ EVDRFMVQQQ
     AQGETGCSDI LENLAKLGVN VSESSRESDK MFQSTCRHPP DTHTQKLIQL FASAKTLTAK
     HQLLHTLRSH LILHIARTCG YSKVMSGESC TRLSVSLLSN ISLGRGAFLP LDTGFCDSRY
     GDVDIIRPMR EYSLKEIAFY NRLFHVSSVF IPALNTKVLE NSSIQQLSEV FINRLQADFP
     STVSTVYRTS EKLNVSKIDA NQGTCAKERC LLCLSPLDTQ VGEASAFHAT QISHYISQKI
     LMKFNDPANS SGKSCCQEGK CCKGPGYGDF CQPRALQAPS FVDMLCYGCR LTVKDLQSLD
     ALPQYVLHEA EHRSRRIEMR KEIEEFLLDK DEENLH