Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) which encode 217 and 353 amino acids, respectively. Tectonin I is homologous to the C-terminal two-thirds of tectonin II. Both proteins contain six tandem repeats that are each 33-37 amino acids in length and define a new consensus sequence. Homologous repeats are found in L-6, a bacterial lipopolysaccharide-binding lectin from horseshoe crab hemocytes. The repetitive sequences of the tectonins and L-6 are reminiscent of the WD repeats of the beta-subunit of G proteins, suggesting that they form beta-propeller domains. The tectonins may be lectins that function as part of a transmembrane signalling complex during phagocytosis [ (PUBMED:9497393) ]. It has been demonstrated that tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion [ (PUBMED:22342342) ].
Family alignment:
There are 16106 TECPR domains in 2266 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing TECPR domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with TECPR domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing TECPR domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Cloning and characterization of Physarum polycephalum tectonins.Homologues of Limulus lectin L-6.
J Biol Chem. 1998; 273: 6565-74
Display abstract
Previous investigators have reported the presence of two dominantproteins, tectonin I (25 kDa) and tectonin II (39 kDa), in nuclei andnuclear matrix from plasmodia of Physarum polycephalum. We demonstrate, bya modification of the nuclear isolation protocol and by proteasesensitivity, that the tectonins are not nuclear proteins but rather arelocated on the exterior surface of the plasma membrane. We report thesequences of cDNAs of tectonins I and II, which encode 217 and 353 aminoacids, respectively. Tectonin I is homologous to the C-terminal two-thirdsof tectonin II. Both proteins contain six tandem repeats that are each33-37 amino acids in length and define a new consensus sequence.Homologous repeats are found in L-6, a bacteriallipopolysaccharide-binding lectin from horseshoe crab hemocytes. Therepetitive sequences of the tectonins and L-6 are reminiscent of the WDrepeats of the beta-subunit of G proteins, suggesting that they formbeta-propeller domains. Tectonin II has an additional N-terminal domainthat includes a 47-residue sequence highly similar to thegalactoside-binding sequence of the B-chain of ricin. The tectonins may belectins that function as part of a transmembrane signaling complex duringphagocytosis.
