ID A0A8C5T0N8_9PASS Unreviewed; 409 AA.
AC A0A8C5T0N8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
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 Malurus cyaneus samueli.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Meliphagoidea; Maluridae; Malurus.
OX NCBI_TaxID=2593467 {ECO:0000313|Ensembl:ENSMCSP00000001061.1, ECO:0000313|Proteomes:UP000694560};
RN [1] {ECO:0000313|Ensembl:ENSMCSP00000001061.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMCSP00000001061.1}
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; A0A8C5T0N8; -.
DR Ensembl; ENSMCST00000001087.1; ENSMCSP00000001061.1; ENSMCSG00000000776.1.
DR OrthoDB; 25129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000694560; 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:UP000694560};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..16
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 44705 MW; 25A09B3F599B3F69 CRC64;
GSGAGVPGDR PGVPGDRPCP RSHPRTCMKC GQGTAALVIR VGDPFCRGCF REYFVHKFRA
MLGKNRVIFP GEKVLLAVSG GPASSAMIRQ VQEGLSREAA KRLRFVPSLV YIEEGAVCGQ
SPEQREQTLA QMETLLQATG FPYHLVHLEE VLGTRVLQPV QHGRPFLQGG CGQLHPAAAA
GWGRWHLCAW SQRPGQDSRT PGTPRLPDPA QTQELLRAFE AAGTATAREE LLQMLRTHLI
VQTARNRGYT KVMTGESLTR VAIKLLTNLS LGRGAFLAVD TGFRDQRHGD VMVVRPMRDY
TAKEIAFYNH FFGVPTVIVP PLFTKRREKL SIHQLIERFL LGLQEEFPAT ISTVYRTGEK
LSPEPAKASS ESQRCLLCLC GLDIEGDTSP SHCGTAGAGA TPQGYPSGW
//
