Basic Information
Name | NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase) |
Uniprot ID | Q12181 |
Systematic gene name | YPR048W |
Standard gene name | TAH18 |
Gene names | TAH18 YPR048W YP9499.06 |
Description from SGD | YPR048W TAH18 SGDID:S000006252, Chr XVI from 659182-661053, Genome Release 64-3-1, Verified ORF, "Conserved NAPDH-dependent diflavin reductase; component of an early step in the cytosolic Fe-S protein assembly (CIA) machinery; transfers electrons from NADPH to the Fe-S cluster of Dre2p; plays a pro-death role under oxidative stress; Tah18p-dependent nitric oxide synthesis confers high-temperature stress tolerance; possible target for development of antifungal drugs" |
Protein length | 623 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSSSKKIVIL YGSETGNAHD FATILSHRLH RWHFSHTFCS IGDYDPQDIL
KCRYLFIICS TTGQGELPRN VNALKGERPV TFWSFLKRKN LPSNLLNHIQ
TAMLGLGDSS YPKFNYGIRK LHQRIVTQLG ANELFDRLEA DDQAMAGSNK
GTGLGIESVY FEYEKKVLSF LLSKYPNRKV NGQIIKREEL DPEVYLEPAS
YLQLSDEHAN EKFTSTKVIF EGDESLKVGR VNINKRITSE GHFQDVRQFK
FSNVDKIQEN YEPGDTVTIY PCNTDEDVSR FLANQSHWLE IADKPLNFTS
GVPNDLKDGG LVRPMTLRNL LKYHCDFMSI PRTSFFLKIW TFATDVTKME
RGQEQLNDQR EKLRQFATDQ DMQDLYDYCN RPRRSILEVL EDFISVKLPW
KYVLDYLPII KPRYYSISSG PGDPNIELTV AIVKYKTILR KIRRGICTNY
IARLQEGEQI RYKLQNNHII KKEFLNKPMI LVGPGVGLAP LLSVVKAEIS
KDIKLLFGCR YKDKDYIYKD MLEDWFRKGK IALHSSFSRD EENSPGVKYV
QDYLWRLGEE ITNLVVNKDA VFFLCGSSGK MPIQVRLTFI EMLKKWGNFS
DEETAKKYLK EMEKSDRYIQ ETW
KCRYLFIICS TTGQGELPRN VNALKGERPV TFWSFLKRKN LPSNLLNHIQ
TAMLGLGDSS YPKFNYGIRK LHQRIVTQLG ANELFDRLEA DDQAMAGSNK
GTGLGIESVY FEYEKKVLSF LLSKYPNRKV NGQIIKREEL DPEVYLEPAS
YLQLSDEHAN EKFTSTKVIF EGDESLKVGR VNINKRITSE GHFQDVRQFK
FSNVDKIQEN YEPGDTVTIY PCNTDEDVSR FLANQSHWLE IADKPLNFTS
GVPNDLKDGG LVRPMTLRNL LKYHCDFMSI PRTSFFLKIW TFATDVTKME
RGQEQLNDQR EKLRQFATDQ DMQDLYDYCN RPRRSILEVL EDFISVKLPW
KYVLDYLPII KPRYYSISSG PGDPNIELTV AIVKYKTILR KIRRGICTNY
IARLQEGEQI RYKLQNNHII KKEFLNKPMI LVGPGVGLAP LLSVVKAEIS
KDIKLLFGCR YKDKDYIYKD MLEDWFRKGK IALHSSFSRD EENSPGVKYV
QDYLWRLGEE ITNLVVNKDA VFFLCGSSGK MPIQVRLTFI EMLKKWGNFS
DEETAKKYLK EMEKSDRYIQ ETW
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[238, 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) |
[239, 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) |
[239, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[535, 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) |
[535, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |