ID A0A6J3DQ60_AYTFU Unreviewed; 486 AA.
AC A0A6J3DQ60;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 10-JUN-2026, entry version 26.
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|RefSeq:XP_032051692.1};
GN Synonyms=NCS2 {ECO:0000256|HAMAP-Rule:MF_03054};
OS Aythya fuligula (Tufted duck) (Anas fuligula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Aythyinae; Aythya.
OX NCBI_TaxID=219594 {ECO:0000313|Proteomes:UP000504639, ECO:0000313|RefSeq:XP_032051692.1};
RN [1] {ECO:0000313|RefSeq:XP_032051692.1}
RP IDENTIFICATION.
RC TISSUE=Lung {ECO:0000313|RefSeq:XP_032051692.1};
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_032051692.1; XM_032195801.1.
DR AlphaFoldDB; A0A6J3DQ60; -.
DR FunCoup; A0A6J3DQ60; 731.
DR GeneID; 116494099; -.
DR KEGG; aful:116494099; -.
DR CTD; 348180; -.
DR InParanoid; A0A6J3DQ60; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000504639; Chromosome 12.
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:UP000504639};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
FT REGION 195..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 52764 MW; 0F09D93FD250C214 CRC64;
MCEANRGCGE CAAGLGVGLG APRRRPAAVC RQPRPCVKCG DSAAAVVIRI GDGFCRACFR
EYFVHKFRAM LGKNRVIFPG EKVLLALSGG PASSAMLRQV QEGLSRETAK RLRFVPGLVH
IDEGAVCGQS PAQREQNLAQ MEALLQETGF PYYLASLEQA LELPGSVLRR GPGAAGEPCP
SYKEAVEGFI QQQRQEVADG DGDTSSAGLS TQHGPGGHPA APRLPPAALT AELLRLFEAA
ETLTAKEELL QMLRGHLILH TARTRGYPKV MTGESCTRVA VKLLTNLALG RGAFLAVDTG
FVDSRHGDVT LVRPMREYMA KEIAFYNHFF GVPTVITPPL STKRREKTSI HRLMESFLLG
LQADFPSTIS TVYRTGEKLS AAPAEASSEL QRCLLCLCAL DIDGEEELAL EPTLVTEETG
DGADSRAAFI PLLCYSCRLT FKEMGPPATL PSYVRTEARH RSCRARMKEQ IQEFLLEDDE
EEPGTS
//
