TCD2_YEAST
ID TCD2_YEAST Reviewed; 447 AA.
AC P36101; D6VXQ7; Q6B2N9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=tRNA threonylcarbamoyladenosine dehydratase 2;
DE EC=6.1.-.-;
DE AltName: Full=t(6)A37 dehydratase 2;
GN Name=TCD2; OrderedLocusNames=YKL027W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23242255; DOI=10.1038/nchembio.1137;
RA Miyauchi K., Kimura S., Suzuki T.;
RT "A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed
RT tRNA hypermodification.";
RL Nat. Chem. Biol. 9:105-111(2013).
CC -!- FUNCTION: Catalyzes the ATP-dependent dehydration of
CC threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic
CC t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine.
CC {ECO:0000269|PubMed:23242255}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Displays only the t(6)A but not the ct(6)A
CC modification in tRNAs. Unable to sustain respiratory growth under non-
CC fermenting conditions. {ECO:0000269|PubMed:23242255}.
CC -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: ct(6)A is involved in promoting decoding efficiency. It
CC is an unstable modification that can be easily hydrolyzed and converted
CC to t(6)A during nucleoside preparation by conventional methods
CC (PubMed:23242255). {ECO:0000305|PubMed:23242255}.
CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
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DR EMBL; Z28027; CAA81862.1; -; Genomic_DNA.
DR EMBL; AY692691; AAT92710.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09127.1; -; Genomic_DNA.
DR PIR; S37844; S37844.
DR RefSeq; NP_012898.1; NM_001179593.1.
DR AlphaFoldDB; P36101; -.
DR SMR; P36101; -.
DR BioGRID; 34104; 165.
DR IntAct; P36101; 2.
DR MINT; P36101; -.
DR STRING; 4932.YKL027W; -.
DR iPTMnet; P36101; -.
DR MaxQB; P36101; -.
DR PaxDb; P36101; -.
DR PRIDE; P36101; -.
DR EnsemblFungi; YKL027W_mRNA; YKL027W; YKL027W.
DR GeneID; 853841; -.
DR KEGG; sce:YKL027W; -.
DR SGD; S000001510; TCD2.
DR VEuPathDB; FungiDB:YKL027W; -.
DR eggNOG; KOG2018; Eukaryota.
DR GeneTree; ENSGT00940000176473; -.
DR HOGENOM; CLU_013325_9_3_1; -.
DR InParanoid; P36101; -.
DR OMA; SLNRHSC; -.
DR BioCyc; YEAST:G3O-31833-MON; -.
DR PRO; PR:P36101; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36101; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061503; F:tRNA threonylcarbamoyladenosine dehydratase; IMP:SGD.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0061504; P:cyclic threonylcarbamoyladenosine biosynthetic process; IMP:SGD.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR43267; PTHR43267; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..447
FT /note="tRNA threonylcarbamoyladenosine dehydratase 2"
FT /id="PRO_0000120586"
FT TRANSMEM 9..29
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT CONFLICT 41
FT /note="Q -> P (in Ref. 3; AAT92710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50266 MW; 89B3EFD54DE6FF3A CRC64;
MVEKDTWKLI TATALFTVAV TTITDYAWTS WQAQKQVIAQ QKNKNKGGQT KSDTDKYHQY
DEQFIRQSLK NNVEFLGEDT IEKLSNQYVV VVGAGGVGSW VVNSLVRSGC RKIRVVDFDQ
VSLSSLNRHS CAILNDVGTP KVECLRRHMR EIAPWCEIDP INELWTLQNG ERLTLGNGTP
DFIVDCIDNI DTKVDLLEFA YNHGIKVISS MGASAKSDPT KLNVGDLATT EEDPLARVVR
RKLKKRGILS GIPVVFSAEK PDPKKAKLLP LPDEEYERGK VDELSALKDF RVRILPVLGT
MPSLFGLTIT TWILSNISDK PLEPVEGKNR IKVYDGIYQS LAGQMSRVGI PSQRIPLALK
DVSYLVEEVF KGKSPISGIS TRLTLTKWDP SKPISLQNVV VLTKNEQKVH EDRVLKGKES
LQDVYDAKVL KLVSQRFREE AYYSQFR
