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1.

antitoxin Xre-like helix-turn-helix domain-containing protein

This entry represents the N-terminal domain of the antitoxin component Xre of a type II toxin-antitoxin (TA) system, which is the helix-turn-helix (HTH) DNA binding domain, structurally similar to the Cro repressor, therefore, also referred to as HTH/Cro-like DNA-binding domain [2]. This domain is also found in other antitoxin components, associated with a C-terminal toxin-binding domain Pfam:PF09722 [1,2]. [1]. 30792174. An NAD(+) Phosphorylase Toxin Triggers Mycobacterium. tuberculosis Cell Death.. Freire DM, Gutierrez C, Garza-Garcia A, Grabowska AD, Sala AJ,. Ariyachaokun K, Panikova T, Beckham KSH, Colom A, Pogenberg V,. Cianci M, Tuukkanen A, Boudehen YM, Peixoto A, Botella L,. Svergun DI, Schnappinger D, Schneider TR, Genevaux P, de. Carvalho LPS, Wilmanns M, Parret AHA, Neyrolles O;. Mol Cell. 2019;73:1282-1291.. [2]. 30315706. The RES domain toxins of RES-Xre toxin-antitoxin modules induce. cell stasis by degrading NAD+.. Skjerning RB, Senissar M, Winther KS, Gerdes K, Brodersen DE;. Mol Microbiol. 2019;111:221-236. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Date:
2024-08-14
Family Accession:
NF042861.3
Method:
HMM
2.

antitoxin Xre/MbcA/ParS toxin-binding domain-containing protein

This entry represents the C-terminal domain of antitoxin components of a type II toxin-antitoxin (TA) system, including Xre from Pseudomonas putida, MbcA from Mycobacterium sp. and ParS from Sphingobium sp. [1,2,3,4]. This domain interacts with the toxin component and sterically blocks its active site, neutralising its effect [2,3]. These antitoxins also have a HTH domain at the N-terminal. [1]. 30598453. ParST is a widespread toxin-antitoxin module that targets. nucleotide metabolism.. Piscotta FJ, Jeffrey PD, Link AJ;. Proc Natl Acad Sci U S A. 2019;116:826-834.. [2]. 30792174. An NAD(+) Phosphorylase Toxin Triggers Mycobacterium. tuberculosis Cell Death.. Freire DM, Gutierrez C, Garza-Garcia A, Grabowska AD, Sala AJ,. Ariyachaokun K, Panikova T, Beckham KSH, Colom A, Pogenberg V,. Cianci M, Tuukkanen A, Boudehen YM, Peixoto A, Botella L,. Svergun DI, Schnappinger D, Schneider TR, Genevaux P, de. Carvalho LPS, Wilmanns M, Parret AHA, Neyrolles O;. Mol Cell. 2019;73:1282-1291.. [3]. 30315706. The RES domain toxins of RES-Xre toxin-antitoxin modules induce. cell stasis by degrading NAD+.. Skjerning RB, Senissar M, Winther KS, Gerdes K, Brodersen DE;. Mol Microbiol. 2019;111:221-236.. [4]. 33384857. Bacterial type II toxin-antitoxin systems acting through. post-translational modifications.. Zhang SP, Feng HZ, Wang Q, Kempher ML, Quan SW, Tao X, Niu S,. Wang Y, Feng HY, He YX;. Comput Struct Biotechnol J. 2020;19:86-93. (from Pfam)

Date:
2024-08-14
Family Accession:
NF021255.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

MbcA/ParS/Xre antitoxin family protein

MbcA/ParS/Xre antitoxin family protein similar to Sphingobium sp. Prs ADP-ribosylating antitoxin, the antitoxin component of a type II toxin-antitoxin (TA) system, which neutralizes the bacteriostatic effect of cognate toxin ParT by inserting into its active site

Date:
2021-01-19
Family Accession:
10560704
Method:
Sparcle

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