ID A0A1G4J7G2_9SACH Unreviewed; 471 AA.
AC A0A1G4J7G2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 08-OCT-2025, entry version 24.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Name=NCS2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Synonyms=CTU2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN ORFNames=LADA_0D08526G {ECO:0000313|EMBL:SCU85606.1};
OS Lachancea dasiensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU85606.1, ECO:0000313|Proteomes:UP000190274};
RN [1] {ECO:0000313|EMBL:SCU85606.1, ECO:0000313|Proteomes:UP000190274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10888 {ECO:0000313|EMBL:SCU85606.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 NCS6 that ligates sulfur from
CC thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
CC Prior mcm(5) tRNA modification by the elongator complex is required for
CC 2-thiolation. May also be involved in protein urmylation.
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 EMBL; LT598454; SCU85606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4J7G2; -.
DR STRING; 1266660.A0A1G4J7G2; -.
DR OrthoDB; 25129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000190274; Chromosome D.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:EnsemblFungi.
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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03054};
KW Reference proteome {ECO:0000313|Proteomes:UP000190274};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
SQ SEQUENCE 471 AA; 54000 MW; 1AFCD3A0AB554F3D CRC64;
MAHTAKCKRC SSAQVVLISR KEPFCAECFC KFISLKQRKQ MMSDPYFQDI FKVMYQDKVK
SAEEAEKLNA ESKVLVPLSL GSSSIVMLDV LNSTLAEQLE THRGKAGFHV DILVCYFEKE
RRDIEERLTS LFNGRLRKNK HHYKVHLVDI NAFFDSSKLM RVHLQDSNYV VRYSDASSDH
RADYTVDELL GTCSNRSARE DLLNVIRTAT IKLFASHGSY KAVLWGHSMT RLADEIISLV
VKGRASQIAS SMDDTSFDET FQSSFKNLHP MRDVLLSEID AYCHIFDLTQ YTYHYTPQDT
LLVERSTIPV VTGSKLTRNM TINELARQYF DNIEGNYSNV ISTVVRTGAK LDDPKNNLPT
VSRCRVCNNK LFKDGSEWLR QITVNHSHPI ENEEDQTLYD AWTESELGKI RGEYLKLTAE
MEQNGKTLST CYGCILTLGE VRHKNVYWPE SPPNLLRDAL EEFVLTDDEE E
//
