PMID:42146377

TIR-like NADases act in bacterial immunity and the RNA vault.

DUF4062 is a family of TIR-like NADases that hydrolyse NAD+ to ADP-ribose and nicotinamide (preprint).

"we show that domain of unknown function 4062 (DUF4062) is a widespread family of TIR-like NADases that hydrolyze NAD+ to ADP-ribose and nicotinamide"
A conserved Glu is the likely catalytic residue of DUF4062.

"Sequence alignments identified a conserved Glu as a likely catalytic residue, corresponding to the known catalytic site of TIR NADases"
Klebsiella Swarozyc defends against phage by NAD+ depletion, and this requires E97.

"NAD+ levels were reduced upon phage infection in cells expressing WT KpSwz, but not the E97A mutant"
Not all DUF4062 proteins are active; of four human DUF4062-NACHT proteins only TEP1 hydrolysed NAD+.

"We purified full-length human NWD1, NWD2, NPHP3, and TEP1 (Figure 5B), incubated them with NAD+ and NADP+, and analyzed reaction products by HPLC. Only TEP1 hydrolyzed NAD+ and NADP+"

file:SYNE7/Synpcc7942_0873/Synpcc7942_0873-bioinformatics/RESULTS.md

Synpcc7942_0873 (Q31PW6): NTPase motifs, DUF4062 domain context and the conserved Glu

The protein has no Walker A or Walker B motif.

"The query has no Walker A motif (GxxxxGK[ST]: 0 hits; relaxed [GA]xxxxGK[ST]: 0 hits; any GK[ST]: 0 hits) and no Walker B motif (hhhhD[DE]: 0 hits)."
Short DUF4062 proteins almost never carry an NTPase domain.

"DUF4062 proteins of 450 aa or less, like this 362-aa protein, almost never carry an NTPase domain."
Glu83 is the conserved DUF4062 Glu.

"Glu83 is identical in 93% of them, the third most conserved position overall"

file:SYNE7/Synpcc7942_0873/Synpcc7942_0873-deep-research-claude-code.md

Deep research report on Synpcc7942_0873 (claude-code provider)

No gene-specific experimental literature exists for Synpcc7942_0873.

"**No gene-specific experimental literature exists.**"