ID A0A1X7RKC3_ZYMT9 Unreviewed; 358 AA.
AC A0A1X7RKC3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 08-OCT-2025, entry version 16.
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=ZT3D7_G3013 {ECO:0000313|EMBL:SMQ47865.1};
OS Zymoseptoria tritici (strain ST99CH_3D7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ47865.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ47865.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; LT853693; SMQ47865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RKC3; -.
DR STRING; 1276538.A0A1X7RKC3; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000215127; Chromosome 2.
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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03054};
KW Reference proteome {ECO:0000313|Proteomes:UP000215127};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
SQ SEQUENCE 358 AA; 40127 MW; 6AD00E06881D52B2 CRC64;
MPGRRLPDEP IDTALCRRCQ EVEPAIVVRT EPVCKSCFSK YVQTKVVKRL ESFRVRHSEP
GNERMVLLPL SYTASSVTLL HVLSQHLQGQ TEKTGRTGFK LCVLHILGGN SANEDDEAPF
DDLKARYPQH DYHTVRLSEA LASDDVVRSL FADSSNLEIR ADDPEQSLRS LLLKAPSATS
RQDIEQTLKQ RLTISFAKSH ACDAVIWDHS ATKLAERTIS ETAKGRGISL PWIVADGDSL
HGIPFYHPLR ELLNNELKSY VEFADPPFDA RFSTVDTKPI VSTKNTTIDD LVEQYFESVE
QDYPSIVANV VRTTGKLPVK AIEQAEQCEL CCTPLQDRAP EKSRLCHGCI RMLPQAQD
//
