ID A0A670YS51_PSETE Unreviewed; 418 AA.
AC A0A670YS51;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
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 ECO:0000313|Ensembl:ENSPTXP00000013849.1};
GN Synonyms=NCS2 {ECO:0000256|HAMAP-Rule:MF_03054};
OS Pseudonaja textilis (Eastern brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Hydrophiinae; Pseudonaja.
OX NCBI_TaxID=8673 {ECO:0000313|Ensembl:ENSPTXP00000013849.1, ECO:0000313|Proteomes:UP000472273};
RN [1] {ECO:0000313|Ensembl:ENSPTXP00000013849.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPTXP00000013849.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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 AlphaFoldDB; A0A670YS51; -.
DR Ensembl; ENSPTXT00000014288.1; ENSPTXP00000013849.1; ENSPTXG00000009635.1.
DR GeneTree; ENSGT00390000008797; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000472273; 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:UP000472273};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 45827 MW; 159358F055E3AF32 CRC64;
MCDGGQGGCG EEPLPRERPR GRCDSKCVKC KEASPVVIIR AGDAFCKGCF KDYFVHKFRA
MLGKNRCIYP GEKVLLAFSG GLASSSMLRQ VQEGLNREAA KKLRFRPGII YIDEGAVCGR
SLDEREKTCG QVEAVLRATG FPYHLVFLEE VFDLPTSVLS SLSHNATGQA PSYKEAVADF
LRWQQHLEGC WWPGRLAALH EAGSSLASHA QDLSRLFAGI KSLTAKEELL QTLRTHLVLH
VARRNRYTKV MVGDSCTRVS VKLLTNLSLG RGAFLAMDTG FLDSRYGDVL ILRPMREYPA
KEIAFYNYLF GVPTVFTPGL DTKASDRASI HLLIETFLCK LQLEFPSTVS TVYRTGEKLS
AVPPEAQPDV PTAPASCLLC LCPLDTNVGE WSSLGGGDGG PASRLTFGTS WDSRMDKG
//
