Yeast killer toxin |
Zymocin, PaT |
Modified U34 (wobble uridine) base-containing tRNA. In Pichia acaciae, predominantly tRNAGln. |
Yeast |
Toxin domain fused to N-terminal secreted chitinase domain which might breach fungal cell wall |
α-Sarcin-like |
BECR fold domains (sarcin, restrictocin, hirsutellin, mitogillin, etc.) |
Backbone cleavage in rRNA sarcin-ricin loop |
Filamentous fungi |
Several such RNases with 1–3 BECR domains are found across fungi |
Ricin-like |
Ricin, saporin, pokeweed antiviral protein, Shiga |
N-glycoside hydrolysis of rRNA sarcin-ricin loop base |
plants, ciliates, bacteria |
Found in a class of ciliate toxin with architectural parallels to bacterial polymorphic toxins |
Toxin-antitoxin (T-A) |
BECR fold domains (Barnase, EndoU, Colicin-like, RelE-like) MazF/PemK/EndoA, PIN (VapC, etc.) domains, HEPN domains |
mRNA (BECR, MazF/PemK/EndoA, RNase LS and RNase LsoA: HEPN), tRNAMet (VapC: PIN), tRNA (BECR), rRNA sarcin-ricin loop (PIN), rRNA S16 (Colicin E3, E4, E6: Colicin E3-like) |
Bacteria, archaea |
Widespread intra-genomic conflict systems |
Polymorphic toxins |
Various BECR fold domains, deaminase |
tRNA, likely other targets |
Bacteria, archaea |
The toxin domains typical vary via replacement by alternative cassettes |
Colicin-like |
BECR fold domains, colicin E3-like |
Probably tRNA (BECR), rRNA S16 (Colicin E3, E4, E6: Colicin E3-like) |
Bacteria |
Differ from above in being secreted by lysis of the producing cell and being encoded on plasmids |
CRISPR/Cas |
Cas2, HEPN, active RAMPs and Csx3. Cmr and Cas9 in some subtypes |
mRNAs, Csx3 exonucleolytically targets terminal polyA tails |
Bacteria, archaea |
A wide range of actions which are both directed by complementary CRISPR spacer RNAs and independently of them |
Restriction-modification systems |
HEPN (PrrC-like RNases) |
tRNALys
|
Bacteria |
inactivation of R-M system by phage leads to activation of PrrC, which targets endogenous tRNA |
Abortive infection (Abi) |
HEPN (AbiA-CTD, AbiD, AbiF, AbiJ, AbiU2, AbiV) |
Unknown |
Bacteria |
Part of an extensive antiphage defense which might also directly target phage components |
Phage growth limitation (Pgl) |
HEPN (RloC-like, pEK499_p136-like families), SNase |
Unknown |
Bacteria |
Sporadic coupling to RNases could cleave phage RNAs in attacks complementary to Pgl DNA modification |
Ter-dependent anti-phage system |
HEPN (DUF4145-like) |
Unknown |
Bacteria |
Sporadic coupling to HEPN domain could work with core system |
Prokaryotic nucleotide or nucleotide-derived secondary messenger-based systems |
HEPN |
Unknown |
Bacteria |
Combines with CARF sensor and mCpol nucleotide secondary messenger synthetase |
prokaryotic PIWI-based systems |
PIWI/argonaute, HEPN |
Unknown |
Bacteria |
In bacteria, pPIWI is adjacent to effector RNAse domains |
Animal innate immunity |
RNaseL – permuted version of HEPN domain |
Viral RNA |
Eukaryotes |
Activated in vertebrates by oligoadenylate (OA) linear secondary messenger nucleotide |