AT1G35460.1 :

DomainDescriptionEvalueBitsGAStartEnd
Peptidase_M6Immune inhibitor A peptidase M62.9E-051120.8090174
PhaP_BmegPolyhydroxyalkanoic acid inclusion protein (PhaP_Bmeg)0.0028622.20132156
DUF2935Protein of unknown function (DUF2935)1.8E-051421.20138254
TSCPDTSCPD domain1.8E-051422.00157232
HLHHelix-loop-helix DNA-binding domain4.6E-144120.70193238
PhaP_BmegPolyhydroxyalkanoic acid inclusion protein (PhaP_Bmeg)0.0053522.20222253
IKKbetaNEMObindI-kappa-kinase-beta NEMO binding domain4.2E-061625.00224249

 259

Peptidase_M6
PhaP_Bmeg
DUF2935
TSCPD
HLH
PhaP_Bmeg
IKKbetaNEMObind


References:

HLH
7553065 Transcription factors 2: helix-loop-helix. Protein Profile 1995;2:621-702.

Peptidase_M6
11429458 Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation. Microbiology 2001;147:1805-1813.
10475957 Characterization of the exosporium of Bacillus cereus. J Appl Microbiol 1999;87:241-245.
2089225 Molecular characterization of immune inhibitor A, a secreted virulence protease from Bacillus thuringiensis. Mol Microbiol 1990;4:2137-2146.
9371455 Characterization of the Vibrio cholerae El Tor lipase operon lipAB and a protease gene downstream of the hly region. J Bacteriol 1997;179:7072-7080.
12029046 The InhA2 metalloprotease of Bacillus thuringiensis strain 407 is required for pathogenicity in insects infected via the oral route. J Bacteriol 2002;184:3296-3304.

PhaP_Bmeg

IKKbetaNEMObind
18462684 Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure. 2008;16:798-808.

DUF2935

TSCPD