ID A0A4Z0Z8V1_9PEZI Unreviewed; 479 AA.
AC A0A4Z0Z8V1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, 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=E0Z10_g1348 {ECO:0000313|EMBL:TGJ87393.1};
OS Xylaria hypoxylon.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=37992 {ECO:0000313|EMBL:TGJ87393.1, ECO:0000313|Proteomes:UP000297716};
RN [1] {ECO:0000313|EMBL:TGJ87393.1, ECO:0000313|Proteomes:UP000297716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 108379 {ECO:0000313|EMBL:TGJ87393.1,
RC ECO:0000313|Proteomes:UP000297716};
RA Buettner E., Leonhardt S., Gebauer A.M., Liers C., Hofrichter M.,
RA Kellner H.;
RT "Draft genome sequence of Xylaria hypoxylon DSM 108379, a ubiquitous
RT saprotrophic-parasitic fungi on hardwood.";
RL Submitted (MAR-2019) 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:TGJ87393.1}.
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DR EMBL; SKBN01000014; TGJ87393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z0Z8V1; -.
DR STRING; 37992.A0A4Z0Z8V1; -.
DR OrthoDB; 25129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000297716; 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; 2.
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:UP000297716};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
FT REGION 115..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..158
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 51429 MW; 2301E3ED09B8F2B1 CRC64;
MVTTDVGAAL PLCARCKEQE GVLDLRSDLI CRICFTTFIA SKAIKRLEVL QRETRGAKLP
LRSQRYLVAL SRGPSSTALL HILNENVRRQ RERNQRVKFE LVVVFVDVDV DAGAEQKGTS
QPTASDPAPP APTNGTAGTV DTTTSRPSSD PTSTSTDVFT THFPELTIRK APLSSILSSP
AIDWSLLPAQ NTSLPPSQRL ADFFSRLPSA SARADVSRLL IRHTLFAAAA EHDCAVILLG
YNTTSLAELT LSEAAKGRGF GIPWFVNDGA FPLPRAVDIA ISNSEVGIDS VSKDLASLQT
NDSISVGTAS TSIHIYSPLR EIFRKEILLY LSLVSSSSGP LTDLFPSSSP HAANGGTDRS
AGAVVSHRDL SLDDVVRRFF VDVEASYPSV VANVVRTTGK LNRMAPIIPG TRTDTDMGVV
GQQCRLCGVG LDLFGDERWK GEIGEADTTT SSAVVEDGNV QGGKRNRLCY GCERSVKGR
//
