ID   CTU2_BOVIN              Reviewed;         501 AA.
AC   Q3SZG9; F1MJ97;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=CTU2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Synonyms=NCS2 {ECO:0000255|HAMAP-Rule:MF_03054};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-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   -!- SUBUNIT: Component of a complex at least composed of URM1, CTU2/NCS2
CC       and CTU1/ATPBD3. {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; DAAA02046253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC102862; AAI02863.1; -; mRNA.
DR   RefSeq; NP_001030521.1; NM_001035444.2.
DR   AlphaFoldDB; Q3SZG9; -.
DR   STRING; 9913.ENSBTAP00000032466; -.
DR   PaxDb; Q3SZG9; -.
DR   PRIDE; Q3SZG9; -.
DR   Ensembl; ENSBTAT00000032535; ENSBTAP00000032466; ENSBTAG00000020943.
DR   GeneID; 614194; -.
DR   KEGG; bta:614194; -.
DR   CTD; 348180; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020943; -.
DR   VGNC; VGNC:27824; CTU2.
DR   eggNOG; KOG2594; Eukaryota.
DR   GeneTree; ENSGT00390000008797; -.
DR   HOGENOM; CLU_024534_2_0_1; -.
DR   InParanoid; Q3SZG9; -.
DR   OrthoDB; 1442062at2759; -.
DR   TreeFam; TF313203; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000020943; Expressed in digestive system secreted substance and 108 other tissues.
DR   ExpressionAtlas; Q3SZG9; baseline and differential.
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   Acetylation; Cytoplasm; Phosphoprotein; Reference proteome;
KW   tRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q2VPK5"
FT   CHAIN           2..501
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000289174"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2VPK5"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2VPK5"
FT   CONFLICT        223
FT                   /note="F -> I (in Ref. 2; AAI02863)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  54353 MW;  AB8B3A740DE56797 CRC64;
     MCEMSEEYRE SAPKGPPPPR LGTGDQKCVK CKEGLPVVVI RAGDAFCRDC FKALYVHKFR
     AMLGKSRLIF PGEKVLLAWS GGPSSSSMVW QVLEGLSRDS AKRLRFVPGV VYIDEGAACG
     QSPEDRARTL AEVKLALQTT GFPWHAVALE EVFSLPPSAL RCSAQEAAGT EGAYKAAVDS
     FLQQQHALGT NGVERQSQHC AQDPQSPTGP PTTAQTQALS RLFDSVKTLT AKEELLQTLR
     THLILHVARN HGYSKVMTGD SCTRLAIKLM TSLALGRGAF LAWDTGFSDE RHGDVVVVRP
     MREHTLKEVA FYNRLFAVPS ICTPALDTKA PEKASIHRLM EAFILRLQAQ FPSTVSTVYR
     TSEKLVKAPR AGCAAGPRCL LCMCTLDVDT ADSATAFGAQ TSHLPQMQTP VTQARAAAGP
     CCCAGMGGAP GCCKREDPRA QVMEQLCYGC RVNMKDLPSL ELLPPYILSE AQLRSQRATA
     EQEIREYLLG DSEDEAGTGE S