Protein domain of unknown function DUF1023 is an α/β hydrolase

2005 ◽  
Vol 59 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Mingzhu Zheng ◽  
Krzysztof Ginalski ◽  
Leszek Rychlewski ◽  
Nick V. Grishin
2016 ◽  
Vol 291 (46) ◽  
pp. 24065-24075 ◽  
Author(s):  
Min Luo ◽  
Thameesha T. Gamage ◽  
Benjamin W. Arentson ◽  
Katherine N. Schlasner ◽  
Donald F. Becker ◽  
...  

2016 ◽  
Author(s):  
Artemis Giannakopoulou ◽  
Angela Chaparro-Garcia ◽  
Sophien Kamoun

A recent study by Kroj et al. (New Phytologist, 2016) surveyed nucleotide binding-leucine rich repeat (NLR) proteins from plant genomes for the presence of extraneous integrated domains that may serve as decoys or sensors for pathogen effectors. They reported that a FAM75 domain of unknown function occurs near the C-terminus of the potato late blight NLR protein R3a. Here, we investigated in detail the domain architecture of the R3a protein, its potato paralog R3b, and their tomato ortholog I2. We conclude that the R3a, R3b, and I2 proteins do not carry additional domains besides the classic NLR modules, and that the FAM75 domain match is likely a false positive among computationally predicted NLR-integrated domains.


2020 ◽  
Vol 3 (4) ◽  
pp. e201900631
Author(s):  
Biswanath Jana ◽  
Dor Salomon ◽  
Eran Bosis

Bacteroidetes are Gram-negative bacteria that are abundant in the environment as well as in the gut microbiota of animals. Many bacteroidetes encode large proteins containing an N-terminal domain of unknown function, named TANFOR. In this work, we show that TANFOR-containing proteins carry polymorphic C-terminal toxin domains with predicted antibacterial and anti-eukaryotic activities. We also show that a C-terminal domain that is prevalent in TANFOR-containing proteins represents a novel family of antibacterial DNase toxins, which we named BaCT (Bacteroidetes C-terminal Toxin). Finally, we discover that TANFOR-encoding gene neighborhoods are enriched with genes that encode substrates of the type IX secretion system (T9SS), which is involved in exporting proteins from the periplasm across the outer membrane. Based on these findings, we conclude that TANFOR-containing proteins are a new class of polymorphic toxins, and we hypothesize that they are T9SS substrates.


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