CTU2_CANAL
ID CTU2_CANAL Reviewed; 452 AA.
AC Q59ZY9; A0A1D8PSH9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 78.
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=CAALFM_CR03550WA; ORFNames=CaO19.11877, CaO19.4399;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017630; AOW31093.1; -; Genomic_DNA.
DR RefSeq; XP_715175.2; XM_710082.2.
DR AlphaFoldDB; Q59ZY9; -.
DR BioGRID; 1226310; 1.
DR STRING; 237561.Q59ZY9; -.
DR PRIDE; Q59ZY9; -.
DR GeneID; 3643216; -.
DR KEGG; cal:CAALFM_CR03550WA; -.
DR CGD; CAL0000189560; NCS2.
DR VEuPathDB; FungiDB:CR_03550W_A; -.
DR eggNOG; KOG2594; Eukaryota.
DR HOGENOM; CLU_024534_1_0_1; -.
DR InParanoid; Q59ZY9; -.
DR OrthoDB; 1442062at2759; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q59ZY9; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016783; F:sulfurtransferase activity; IBA:GO_Central.
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:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
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..452
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000369292"
SQ SEQUENCE 452 AA; 51001 MW; 2193D06D7C447ABA CRC64;
MPEAIVYLTE TEICQKCKTE NAVVHARVEK LCSNCYIRFI RGKLRKQMHD ERYKVKFGRA
VEQYGTQRIL LALSGGESSL VLLDIFGSLL QEQNELHKGK QGFELVVVNL DEYELDSLNN
RIQKVFPELL AKYQPVKISL NVLSLDSYVD EESLHRILLT PDFRAMSKSI DPTRVTLTEI
LRLCPNKSSA EDLLTIVYND LILRVAAKED CQTVVYGHCM TRLANEIIAL TVKGRGSIIH
KSIADHTETI DDKEIKVMFP LREILQAEIS AYVKLAELNK YVISSTVQKS KINKNLTIRD
LTTNYFKQLD ATGYASTAST VAKTGEKLGS PSNVLCQCQI CGADIHQNPS NWLKRITVTD
PAAITTDEEK EYYEMFRASL SPDNEDKNNS DSPIDICFGC TVTLGGVKGD TGFIWPLQGS
SELKYEYRND NQEKQKVLDE FVLTDDEGDI EV