CTU2_PYRTR
ID CTU2_PYRTR Reviewed; 380 AA.
AC B2W6W8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN Name=ncs2; Synonyms=ctu2; ORFNames=PTRG_05556;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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:0000255|HAMAP-Rule:MF_03054}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}.
CC -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03054}.
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DR EMBL; DS231619; EDU48476.1; -; Genomic_DNA.
DR RefSeq; XP_001935889.1; XM_001935854.1.
DR AlphaFoldDB; B2W6W8; -.
DR SMR; B2W6W8; -.
DR STRING; 45151.EDU48476; -.
DR EnsemblFungi; EDU48476; EDU48476; PTRG_05556.
DR GeneID; 6343809; -.
DR eggNOG; KOG2594; Eukaryota.
DR HOGENOM; CLU_024534_3_0_1; -.
DR InParanoid; B2W6W8; -.
DR OMA; SCSMLRQ; -.
DR OrthoDB; 1442062at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_03054; CTU2; 1.
DR InterPro; IPR019407; CTU2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR20882; PTHR20882; 1.
DR Pfam; PF10288; CTU2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; tRNA processing.
FT CHAIN 1..380
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000369302"
SQ SEQUENCE 380 AA; 41933 MW; 7D026BF9BAFD9CF1 CRC64;
MPGKEIVDAS NEPCRRCKAS SVLVVRSEPL CHDCFARYIH TKCIKRLETF RVNFTAEQQP
RVLVPLSFGI SSVTLLHVLD LHQRTQKSKT GRTGFNISAV YIEDPEQSIM AEDLLDQVRE
QYSGHQYASL PLHDVFRLVQ DDASIRSLVP ETQYASTPEE KLVHMINSLT SATARADVLS
TLKTRLIVEH AKLTGCESIL WGDSTTRLAQ KTLSETAKGR GFSLPWQVSD GPSPFGLNFH
YPLRDVLKKE LVSYMNMAET GLKTLVHETS IGATQASTSS KNTTIDDLMK QYFESVEDNF
PSIVANVVRT ASRLEAQPDA LSEPKCSLCS MPVSGGRFGI HGWGGDQQDG DDFGSTHANR
TICYGCTRSV PKATSSTNGN