TAH18/YPR048W Protein Information

Standard Name	Tah18p 1
Systematic Name	Ypr048wp
ORF Classification	Verified
Description	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 (2, 3, 4)
Name Description	Top1T722A mutant Hypersensitive 1

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	623
Molecular Weight (Da)	72,327
Isoelectric Point (pI)	8.78

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Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Tah18p (InterPro)
Physical Interactions	There are 17 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000006C0BF \| Q12181 MIPS: YPR048W NCBI: 1314119 \| 6325305 \| 74583816 \| 805031 \| NP_015373.1 GenBank/EMBL/DDBJ: DAA11472.1 \| Z49219 \| Z71255
External Classifications	EC: 1.-.-.- [Oxidoreductases]

Amino Acid Sequence (or in FASTA format)
1 MSSSKKIVIL YGSETGNAHD FATILSHRLH RWHFSHTFCS IGDYDPQDIL 51 KCRYLFIICS TTGQGELPRN VNALKGERPV TFWSFLKRKN LPSNLLNHIQ 101 TAMLGLGDSS YPKFNYGIRK LHQRIVTQLG ANELFDRLEA DDQAMAGSNK 151 GTGLGIESVY FEYEKKVLSF LLSKYPNRKV NGQIIKREEL DPEVYLEPAS 201 YLQLSDEHAN EKFTSTKVIF EGDESLKVGR VNINKRITSE GHFQDVRQFK 251 FSNVDKIQEN YEPGDTVTIY PCNTDEDVSR FLANQSHWLE IADKPLNFTS 301 GVPNDLKDGG LVRPMTLRNL LKYHCDFMSI PRTSFFLKIW TFATDVTKME 351 RGQEQLNDQR EKLRQFATDQ DMQDLYDYCN RPRRSILEVL EDFISVKLPW 401 KYVLDYLPII KPRYYSISSG PGDPNIELTV AIVKYKTILR KIRRGICTNY 451 IARLQEGEQI RYKLQNNHII KKEFLNKPMI LVGPGVGLAP LLSVVKAEIS 501 KDIKLLFGCR YKDKDYIYKD MLEDWFRKGK IALHSSFSRD EENSPGVKYV 551 QDYLWRLGEE ITNLVVNKDA VFFLCGSSGK MPIQVRLTFI EMLKKWGNFS 601 DEETAKKYLK EMEKSDRYIQ ETW*

Amino Acid Sequence (or in FASTA format)

       1  MSSSKKIVIL YGSETGNAHD FATILSHRLH RWHFSHTFCS IGDYDPQDIL
      51  KCRYLFIICS TTGQGELPRN VNALKGERPV TFWSFLKRKN LPSNLLNHIQ
     101  TAMLGLGDSS YPKFNYGIRK LHQRIVTQLG ANELFDRLEA DDQAMAGSNK
     151  GTGLGIESVY FEYEKKVLSF LLSKYPNRKV NGQIIKREEL DPEVYLEPAS
     201  YLQLSDEHAN EKFTSTKVIF EGDESLKVGR VNINKRITSE GHFQDVRQFK
     251  FSNVDKIQEN YEPGDTVTIY PCNTDEDVSR FLANQSHWLE IADKPLNFTS
     301  GVPNDLKDGG LVRPMTLRNL LKYHCDFMSI PRTSFFLKIW TFATDVTKME
     351  RGQEQLNDQR EKLRQFATDQ DMQDLYDYCN RPRRSILEVL EDFISVKLPW
     401  KYVLDYLPII KPRYYSISSG PGDPNIELTV AIVKYKTILR KIRRGICTNY
     451  IARLQEGEQI RYKLQNNHII KKEFLNKPMI LVGPGVGLAP LLSVVKAEIS
     501  KDIKLLFGCR YKDKDYIYKD MLEDWFRKGK IALHSSFSRD EENSPGVKYV
     551  QDYLWRLGEE ITNLVVNKDA VFFLCGSSGK MPIQVRLTFI EMLKKWGNFS
     601  DEETAKKYLK EMEKSDRYIQ ETW*

external links for Tah18p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Tah18p

1)	Reid, R., et al. (1998) In preparation
2)	Vernis L, et al. (2009) A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast. PLoS ONE 4(2):e4376
3)	Netz DJ, et al. (2010) Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis. Nat Chem Biol 6(10):758-65
4)	Nishimura A, et al. (2013) The flavoprotein Tah18-dependent NO synthesis confers high-temperature stress tolerance on yeast cells. Biochem Biophys Res Commun 430(1):137-43