CTU2_KLULA
ID CTU2_KLULA Reviewed; 463 AA.
AC Q6CIU0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN Name=NCS2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN Synonyms=CTU2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN OrderedLocusNames=KLLA0F24002g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382126; CAG98857.1; -; Genomic_DNA.
DR RefSeq; XP_456149.1; XM_456149.1.
DR AlphaFoldDB; Q6CIU0; -.
DR STRING; 28985.XP_456149.1; -.
DR EnsemblFungi; CAG98857; CAG98857; KLLA0_F24002g.
DR GeneID; 2895229; -.
DR KEGG; kla:KLLA0_F24002g; -.
DR eggNOG; KOG2594; Eukaryota.
DR HOGENOM; CLU_024534_1_0_1; -.
DR InParanoid; Q6CIU0; -.
DR OMA; SCSMLRQ; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000000598; Chromosome F.
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: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:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:EnsemblFungi.
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..463
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000369296"
SQ SEQUENCE 463 AA; 52840 MW; 45DA1DD625152C3D CRC64;
MVICKRCKLL DATLVSRKEP FCDECFVKFI SLKQRKQMMS DDYFQDIFKI SYPDKKRGQA
EADKQNQDSN VLVPLSLGSS SLAVLDILND TLLEQKQTHR GKTGFHVEVI TICGQAEFEE
VRGKIELLKS KYKENSDKIL FHIVDRNQFF AVPFDLQEIT LYIDNFNTLV RSSNNPSTTV
EKVLASAPNK TAKEDLLNII YTHLIKKFAL QRNFKAILWG HSMTKLADEV ISLTVKGRGA
EIAGYLDDSS LDSKYNTAFR NFHPGRDVLL SEIDAYCHIK GLSQFSHNYV VQDTLFYDKF
VDKPTKNVKL IKNMTMNELA RQYFDNIEGD YSNVISTVVR TGAKLSNPDN ELNQIMHCSI
CNAIIYKNPV NWLDGITVSK PFVIHNEEEL TNYNAWEAAN PDKAEKLNKM SDTPAKNVGV
CYGCITTLTG MKDRKLEWIR RDDKAELTAV LQEYEIPSDD SEQ