TECPRBeta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins. |
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| SMART accession number: | SM00706
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| Description: |
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| Interpro abstract (IPR006624): |
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)].
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| Family alignment: |
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There are 1360
TECPR domains in 200 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Huh CG, Aldrich J, Mottahedeh J, Kwon H, Johnson C, Marsh R
- 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.
- Links (links to other resources describing this domain)
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