ID A0A8U0UBA1_SALNM Unreviewed; 532 AA.
AC A0A8U0UBA1;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 10-JUN-2026, entry version 18.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Name=LOC120046250 {ECO:0000313|RefSeq:XP_038847254.1};
GN Synonyms=CTU2 {ECO:0000256|HAMAP-Rule:MF_03054}, NCS2
GN {ECO:0000256|HAMAP-Rule:MF_03054};
OS Salvelinus namaycush (Lake trout) (Salmo namaycush).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salvelinus.
OX NCBI_TaxID=8040 {ECO:0000313|Proteomes:UP000808372, ECO:0000313|RefSeq:XP_038847254.1};
RN [1] {ECO:0000313|RefSeq:XP_038847254.1}
RP IDENTIFICATION.
RC TISSUE=White muscle {ECO:0000313|RefSeq:XP_038847254.1};
RG RefSeq;
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 -!- 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 RefSeq; XP_038847254.1; XM_038991326.1.
DR AlphaFoldDB; A0A8U0UBA1; -.
DR GeneID; 120046250; -.
DR KEGG; snh:120046250; -.
DR OrthoDB; 25129at2759; -.
DR Proteomes; UP000808372; Chromosome 1.
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:UP000808372};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
FT REGION 413..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..442
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 58399 MW; F5A58AF75BF9414A CRC64;
MCQVDEEYNG QLEHRVTPRV SKKCVKCKEN TAVLIIRAGD AFCRGCFKEY FIHKFRAMLG
KNRVIFPGEK VLLAVSGGPA SSSMLSQVQE GLSRDAPKKL RFVPGIIYID EGGASGQSME
ERERAVAQLE SVFRATNYHY HIVHLEQVLS LPSSVLEAGS SATEKPQTGS SYKAAVDQFI
QTKKNQHPDL SVENAQSHLS SLSMQEVENG VTSPITPEHT QALQRLFASV RTLTAKEDLL
HTLRLHLILH TARTQGYTKV MMGDSCSRLA IKLLSNISLG RGASLATDTG FSDPRYGDVV
IVRPMRDYSS KEIAYYNRMF DIPSVFIPGL DTKAQDKASI QHVTESFVTK LQTDFPSTVS
TIYRTSEKLH TACPPQNTNT QPFAKCLLCV CALDTKLEEF SAYQATLISE QLSQRRGPGP
GFTPGAAAPG LPPASSASQG QCYSSGGGQH QGCMTGEGGC CSSAKKPETV DLKSLLCYSC
RLTIKDMTAE DALPQYILSE AERRKRRSQM REEISEFLLE EDEAILSVNG SL
//
