Basic Information

NametRNA threonylcarbamoyladenosine dehydratase 1 (EC 6.1.-.-) (t(6)A37 dehydratase 1)
Uniprot IDP38756
Systematic gene nameYHR003C
Standard gene nameTCD1
Gene namesTCD1 YHR003C
Description from SGDYHR003C TCD1 SGDID:S000001045, Chr VIII from 111317-110028, Genome Release 64-3-1, reverse complement, Verified ORF, "tRNA threonylcarbamoyladenosine dehydratase; required for the ct6A tRNA base modification, where an adenosine at position 37 is modified to form a cyclized active ester with an oxazolone ring; localized to the mitochondrial outer membrane; TCD1 has a paralog, TCD2, that arose from the whole genome duplication"
Protein length429
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MANNTWKLIA TTALISVFST QLAKSVWKEY KLSCAANKNK TVSRPRQYDD
HLFREQLARN YAFLGEEGMR KIKEQYIVIV GAGEVGSWVC TMLIRSGCQK
IMIIDPENIS IDSLNTHCCA VLSDIGKPKV QCLKEHLSKI APWSEIKARA
KAWTKENSHD LIFADGESPT FIVDCLDNLE SKVDLLEYAH HNKIDVISSM
GVATKSDPTR VSINDISMTE FDPISRCVRR KLRKRGIATG ISVVFSNEML
DPRRDDILSP IDCEHRAINA VRDEALRHLP ELGTMPGIFG LSIATWILTK
VSGYPMKENE VKNRLKFYDS ILETFQKQMA RLNENKERSS LLGLEEVGYI
VEEMFRGKSP ISGYSTKLAL TKWEANKEIS LTNVVLMTKE EQEIHEKRIL
LDGEKLTAVY SEEVLDFIER LFKEEEYYS

Legend

  • X Phoshorylation
  • X Ubiquitination

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


Use imported representation

Loading structure from server... It may take a while.

If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.

References

[259, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[259, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[259, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[259, Phos]MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications)
[259, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[307, Ubi]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[423, Ubi]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)