CTU1_LACBS
ID CTU1_LACBS Reviewed; 354 AA.
AC B0DK66;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
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};
GN Name=NCS6 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Synonyms=CTU1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN ORFNames=LACBIDRAFT_330073;
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=486041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686;
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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. {ECO:0000255|HAMAP-
CC Rule:MF_03053}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03053}.
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; DS547115; EDR05014.1; -; Genomic_DNA.
DR RefSeq; XP_001884404.1; XM_001884369.1.
DR AlphaFoldDB; B0DK66; -.
DR SMR; B0DK66; -.
DR STRING; 486041.B0DK66; -.
DR EnsemblFungi; EDR05014; EDR05014; LACBIDRAFT_330073.
DR GeneID; 6079927; -.
DR KEGG; lbc:LACBIDRAFT_330073; -.
DR HOGENOM; CLU_026481_1_0_1; -.
DR InParanoid; B0DK66; -.
DR OrthoDB; 860739at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IEA:EnsemblFungi.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
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; IEA:EnsemblFungi.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS: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 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 TIGRFAMs; TIGR00269; TIGR00269; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..354
FT /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT /id="PRO_0000368263"
SQ SEQUENCE 354 AA; 39760 MW; C614C45EDB572328 CRC64;
MAPQTCAICQ KAKAMVKRPK TGEQICRECF FYVFETEVHN TITQANLFKP GDRVAIGASG
GKDSTVLAYV MKMLNERYQY GLELFLLSID EGITGYRDDS LETVKRNQQQ YDMPLKILSY
DELYGWTMDA IVSQVGRKNN CTFCGVFRRQ ALDRGAAMLN VDHIVTGHNA DDIAETVLMN
IMRGDIARLG RCTSICTQGE DTIRRSKPFK YAYEKEIVMY AYFKKLDYFS TECIYSPDAY
RGHARVFLKD LEAARPSAII DIIHSGEAFE VREEVKATQR VQQVCQRCGY MSSNALCKAC
TLLEGLERGM ANSGITDRAR KKLDAEGPAP DNLRTIPFFK PPSGGPLIAI ESVS