CTU2_LODEL
ID CTU2_LODEL Reviewed; 448 AA.
AC A5DSD3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
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}; ORFNames=LELG_00269;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981524; EDK42091.1; -; Genomic_DNA.
DR RefSeq; XP_001527749.1; XM_001527699.1.
DR AlphaFoldDB; A5DSD3; -.
DR STRING; 379508.A5DSD3; -.
DR EnsemblFungi; EDK42091; EDK42091; LELG_00269.
DR GeneID; 5235476; -.
DR KEGG; lel:LELG_00269; -.
DR VEuPathDB; FungiDB:LELG_00269; -.
DR eggNOG; KOG2594; Eukaryota.
DR HOGENOM; CLU_024534_1_0_1; -.
DR InParanoid; A5DSD3; -.
DR OMA; SCSMLRQ; -.
DR OrthoDB; 1442062at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000001996; 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..448
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000369297"
SQ SEQUENCE 448 AA; 50422 MW; 0785345489D5D3EB CRC64;
MKSLEYLTET GIKCLKCDEG AIIKVRSDVY CKQCYLRFIR GKQRKQMSSD KYKVKYLRDG
ASHSTEKVLL AFSGGVSSLV LLDVLARLLE EQKNTHRDLQ GFELVVANIS ESDGTNLESL
LSSSSIMQTL LELVGNYEVS IKVKVVTPNI DPVFLRRIGV DYEFNTFANN LSIEEQSVSS
LAEILRASPN RSSSEDLRDV IFHQELLRLA QSEGCGTIVY GHSMSRLAIE VLALTVKGRG
SNVHSTILDR VEDYCGDQIS IIYPFRDLFE YELREYAVLS DLMQYESAFA KYAVPKSKVS
KNMTVREILS MYLDRWDESG YLSTASTVVK IGEKLTVPTS QNNSSTYCCD ICAKKIYQDP
KDWLQMITVN EPAPLVSDEE RDYLHQYLTS HTDTISKSGE HVNLCYGCIT AINGAGGDSG
VIWPLQKDVK FDHGEKEKAK VLKEYSLE