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Database: UniProt
Entry: A0A059JE54_TRIIM
LinkDB: A0A059JE54_TRIIM
Original site: A0A059JE54_TRIIM 
ID   A0A059JE54_TRIIM        Unreviewed;       341 AA.
AC   A0A059JE54;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   08-OCT-2025, entry version 34.
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=H109_02434 {ECO:0000313|EMBL:KDB25737.1};
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB25737.1, ECO:0000313|Proteomes:UP000024533};
RN   [1] {ECO:0000313|EMBL:KDB25737.1, ECO:0000313|Proteomes:UP000024533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816 {ECO:0000313|EMBL:KDB25737.1,
RC   ECO:0000313|Proteomes:UP000024533};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA   Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA   Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA   Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Trichophyton interdigitale MR816.";
RL   Submitted (FEB-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDB25737.1}.
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DR   EMBL; AOKY01000182; KDB25737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059JE54; -.
DR   STRING; 1215338.A0A059JE54; -.
DR   HOGENOM; CLU_024534_3_0_1; -.
DR   OMA; EGDSTWA; -.
DR   OrthoDB; 25129at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000024533; Unassembled WGS sequence.
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:UP000024533};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03054}.
SQ   SEQUENCE   341 AA;  37742 MW;  49FD6455F0E9588F CRC64;
     MDKYKDGPKD KTPTLILPLS FGVSSLSLLH LLDDQLAHQR GNEYKRVPYK LHVLSVKSPT
     LDAPEGSETT RLGLLRSAFP EHTFTEIPFH SIFRYDKNVA EFMLQHSTGS EINDASISDE
     DRLEAFRSSL STMTSRADID GVLLRKLVVA FANSEGCDGV LWGDSDTRLA AKTLAGVANG
     RGTALPWEVC DGPTPWGVHF TFPVRDIFKS ELVQYASARF PDLLSKTGSK EPKIFNEQAT
     KNISISELMT QYVEQQGEKY PGVMANIVRT IDKLQPSRLH SGLQCVYCGV PLESAQMDPA
     TLSILEERDL TSDKDVTSKP TCYGCARTFL DFKLPTPSSK S
//
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