CTU1_YEAST
ID CTU1_YEAST Reviewed; 359 AA.
AC P53088; D6VTU4; Q92322;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_03053};
DE AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03053};
DE AltName: Full=Needs CLA4 to survive protein 6 {ECO:0000255|HAMAP-Rule:MF_03053};
DE AltName: Full=Thiolation of uridine in cytoplasmic tRNA protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Name=NCS6 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Synonyms=CTU1 {ECO:0000255|HAMAP-Rule:MF_03053},
GN TUC1 {ECO:0000255|HAMAP-Rule:MF_03053}; OrderedLocusNames=YGL211W;
GN ORFNames=YGL210W-A;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8813766;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<799::aid-yea965>3.0.co;2-u;
RA Kail M., Juettner E., Vaux D.;
RT "Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces
RT cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and
RT containing three novel transcribed open reading frames.";
RL Yeast 12:799-807(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153757;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<475::aid-yea101>3.0.co;2-0;
RA Feuermann M., Simeonava L., Souciet J.-L., Potier S.;
RT "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII
RT reveals 11 open reading frames: two correspond to new genes.";
RL Yeast 13:475-477(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP IDENTIFICATION OF FRAMESHIFTS.
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [6]
RP FUNCTION.
RX PubMed=14551258; DOI=10.1091/mbc.e03-02-0079;
RA Goehring A.S., Rivers D.M., Sprague G.F. Jr.;
RT "Urmylation: a ubiquitin-like pathway that functions during invasive growth
RT and budding in yeast.";
RL Mol. Biol. Cell 14:4329-4341(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP FUNCTION.
RX PubMed=17592039; DOI=10.1261/rna.558707;
RA Bjoerk G.R., Huang B., Persson O.P., Bystroem A.S.;
RT "A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required
RT for viability in yeast.";
RL RNA 13:1245-1255(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18664566; DOI=10.1074/jbc.m804043200;
RA Nakai Y., Nakai M., Hayashi H.;
RT "Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related
RT system that resembles bacterial sulfur transfer systems.";
RL J. Biol. Chem. 283:27469-27476(2008).
RN [10]
RP FUNCTION.
RX PubMed=18332122; DOI=10.1128/mcb.01542-07;
RA Johansson M.J.O., Esberg A., Huang B., Bjoerk G.R., Bystroem A.S.;
RT "Eukaryotic wobble uridine modifications promote a functionally redundant
RT decoding system.";
RL Mol. Cell. Biol. 28:3301-3312(2008).
RN [11]
RP FUNCTION IN 2-THIOLATION OF TRNA.
RX PubMed=18755837; DOI=10.1261/rna.1184108;
RA Huang B., Lu J., Bystroem A.S.;
RT "A genome-wide screen identifies genes required for formation of the wobble
RT nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces
RT cerevisiae.";
RL RNA 14:2183-2194(2008).
RN [12]
RP FUNCTION IN 2-THIOLATION OF TRNA, TRNA-BINDING, AND INTERACTION WITH NCS2
RP AND URM1.
RX PubMed=19145231; DOI=10.1038/nature07643;
RA Leidel S., Pedrioli P.G.A., Bucher T., Brost R., Costanzo M., Schmidt A.,
RA Aebersold R., Boone C., Hofmann K., Peter M.;
RT "Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of
RT eukaryotic transfer RNA.";
RL Nature 458:228-233(2009).
RN [13]
RP FUNCTION IN 2-THIOLATION OF TRNA.
RX PubMed=19151091; DOI=10.1093/nar/gkn1023;
RA Noma A., Sakaguchi Y., Suzuki T.;
RT "Mechanistic characterization of the sulfur-relay system for eukaryotic 2-
RT thiouridine biogenesis at tRNA wobble positions.";
RL Nucleic Acids Res. 37:1335-1352(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). Directly binds
CC tRNAs and probably acts by catalyzing adenylation of tRNAs, an
CC intermediate required for 2-thiolation. It is unclear whether it acts
CC as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1
CC onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA
CC modification by the elongator complex is required for 2-thiolation. May
CC also be involved in protein urmylation. May also be involved in protein
CC urmylation and in invasive and pseudohyphal growth. {ECO:0000255|HAMAP-
CC Rule:MF_03053, ECO:0000269|PubMed:14551258,
CC ECO:0000269|PubMed:17592039, ECO:0000269|PubMed:18332122,
CC ECO:0000269|PubMed:18664566, ECO:0000269|PubMed:18755837,
CC ECO:0000269|PubMed:19145231, ECO:0000269|PubMed:19151091}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SUBUNIT: Interacts with NCS2 and URM1. May act by forming a heterodimer
CC with NCS2. Component of a large molecular weight complex of more than
CC 250 kDa. {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:18664566,
CC ECO:0000269|PubMed:19145231}.
CC -!- INTERACTION:
CC P53088; P53923: NCS2; NbExp=3; IntAct=EBI-24137, EBI-28871;
CC P53088; P40554: URM1; NbExp=3; IntAct=EBI-24137, EBI-24940;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49498.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA96927.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U33754; AAC49498.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z72733; CAA96927.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006941; DAA07905.1; -; Genomic_DNA.
DR PIR; S71668; S64230.
DR RefSeq; NP_011304.2; NM_001181076.1.
DR AlphaFoldDB; P53088; -.
DR SMR; P53088; -.
DR BioGRID; 33045; 322.
DR DIP; DIP-7935N; -.
DR IntAct; P53088; 7.
DR STRING; 4932.YGL211W; -.
DR iPTMnet; P53088; -.
DR MaxQB; P53088; -.
DR PaxDb; P53088; -.
DR PRIDE; P53088; -.
DR EnsemblFungi; YGL211W_mRNA; YGL211W; YGL211W.
DR GeneID; 852661; -.
DR KEGG; sce:YGL211W; -.
DR SGD; S000003179; NCS6.
DR VEuPathDB; FungiDB:YGL211W; -.
DR eggNOG; KOG2840; Eukaryota.
DR GeneTree; ENSGT00390000001041; -.
DR HOGENOM; CLU_026481_1_0_1; -.
DR InParanoid; P53088; -.
DR OMA; MNLDQKQ; -.
DR BioCyc; YEAST:G3O-30688-MON; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:P53088; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53088; protein.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0032447; P:protein urmylation; IMP:SGD.
DR GO; GO:0034227; P:tRNA thio-modification; IMP:UniProtKB.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IMP:SGD.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:UniProtKB.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_03053; CTU1; 1.
DR InterPro; IPR032442; CTU1_C.
DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR InterPro; IPR020554; UPF0021_CS.
DR PANTHER; PTHR11807:SF12; PTHR11807:SF12; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR Pfam; PF16503; zn-ribbon_14; 1.
DR PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR PROSITE; PS01263; UPF0021; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Mitochondrion; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..359
FT /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT /id="PRO_0000219889"
FT CONFLICT 356..359
FT /note="KLSF -> NSA (in Ref. 1; AAC49498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39987 MW; F04BB5B93F642CC6 CRC64;
MSFTAPSDPV NKPTKVKVSQ LCELCHSRKA LIRRPKNLSK LCKQCFCLVF ETEIHNTIVA
NNLFQRGEKV AVGASGGKDS TVLAHMLKLL NDRYDYGIEI VLLSIDEGII GYRDDSLATV
KRNQQQYGLP LEIFSFKDLY DWTMDEIVSV AGIRNSCTYC GVFRRQSLDR GAAKLGISHV
VTGHNADDMA ETVLMNILRG DVARLEKSTA IITQSSGSPI KRSKPFKYSY QKEIVLYAHY
MKLDYFSTEC TYAPEAFRGT AREYMKNLEA VRPSCIIDII QSGENLALKA KKSNAGKRVV
KFVDGNRCAR CGYLSSNNIC KACMLLEGLE KSRAQVAIEN DTSADGAALK LRALEKLSF
