ID A0A2K6SWL8_SAIBB Unreviewed; 470 AA.
AC A0A2K6SWL8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 10-JUN-2026, entry version 30.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Name=CTU2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Synonyms=NCS2 {ECO:0000256|HAMAP-Rule:MF_03054};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000011766.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000011766.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2026) to UniProtKB.
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:0000256|HAMAP-Rule:MF_03054}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- SUBUNIT: Component of a complex at least composed of URM1, CTU2/NCS2
CC and CTU1/ATPBD3. {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03054}.
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DR AlphaFoldDB; A0A2K6SWL8; -.
DR Ensembl; ENSSBOT00000028553.1; ENSSBOP00000011766.1; ENSSBOG00000022690.1.
DR GeneTree; ENSGT00390000008797; -.
DR OMA; KQRKQMM; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:TreeGrafter.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:TreeGrafter.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_03054; CTU2; 1.
DR InterPro; IPR019407; CTU2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR20882; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 2; 1.
DR PANTHER; PTHR20882:SF14; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 2; 1.
DR Pfam; PF10288; CTU2; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03054};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
FT REGION 145..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 51178 MW; 06AB412B45C3AA07 CRC64;
GCFKAFYTHK FRAMLGKNRL IFPGEKVLLA WSGGPSSSSM VWQVLEGLSQ DSAKRLRFVP
GVIFVDEGAA CGRSPEERAK TLAEVKPILQ TIGFPWHVVA LEEVFSLPPS VLRCSSQEPA
APEGAYKAAV DSFLQQQHVL GAGGGPGLAH GEEQLPQPHA QPPWDPQRLL RPPAAVQTEA
LSHLFCSVRT LTAKEELLQT LRAHLILHVA RAHGYSKVMT GDSCTRLAIK LMTNLALGRG
AFLAWDTGFS DERHGDVVVV RPMREHTLKE VAFYNRLFSV PSVFTPAVDT KAPEKASIHR
LMEAFILRLQ TQFPSTVSTV YRTSEKLVKA PRDGPGAGDC SPRCLLCMCA LDVDAADSAT
AFGVQTCSHP SQIQSPTSLT ETGTPQGSCC SSGGGRAQSR CQEASSREDP QACILEQLCY
GCRVNMKDLP SLEPLPQYIQ AEAQLRTQRA WVLAELRDCL IEDSDEVGQS
//
