CTU2_PICGU
ID CTU2_PICGU Reviewed; 420 AA.
AC A5DAK5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 57.
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=PGUG_00310;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408155; EDK36212.2; -; Genomic_DNA.
DR RefSeq; XP_001486933.1; XM_001486883.1.
DR AlphaFoldDB; A5DAK5; -.
DR STRING; 4929.XP_001486933.1; -.
DR EnsemblFungi; EDK36212; EDK36212; PGUG_00310.
DR GeneID; 5128977; -.
DR KEGG; pgu:PGUG_00310; -.
DR VEuPathDB; FungiDB:PGUG_00310; -.
DR eggNOG; KOG2594; Eukaryota.
DR HOGENOM; CLU_024534_1_0_1; -.
DR InParanoid; A5DAK5; -.
DR OMA; SCSMLRQ; -.
DR OrthoDB; 1442062at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000001997; 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..420
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000369300"
SQ SEQUENCE 420 AA; 46516 MW; 5DA4FA3640CBF871 CRC64;
MSLAVEYISD KTPCQRCSTK DAVLLARREN YCGDCFIRFI RGKQRRSMQD EAYKVKYKTV
ENPHRVLLAL SGGSSSLVLL DAVASLLQEQ AGQHGGRQGF ALTVVNVDER ERLKLDKSFQ
DIISELKSRY LPVDIDFVSL DYDMYVDGRL LHHIKVASDF SSYSIPLNKG TNINDILKGC
NSKSSEEDLL SIILNELLLK TAITHQCGTL LYGHSMTRLA DEVLALTIKG RGSTIHSSVL
DHTEEISGQT INVKYPLRDV LMGEIEAYCK LAKLDSVVMS STIPDPVINK NKTVRGLTAQ
YFRQLDATGY SSTASTVVRT AAKLAAPTVG TKSGTCKVCG VEIRQDPHQW LRRITVAENE
KVENNSEESG EIGADKKEDV GEQIDLCYGC TVTIGDAPSF RWPLSDKDII AEYTLDSDED