Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; TECPR1 is a tethering factor involved in autophagy. It promotes the autophagosome fusion with lysosomes by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns3P) present at the surface of autophagosomes. TECPR1 is also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. It contains 2 DysFN (Dysferlin domains of unknown function, N-terminal), 2 Hyd_WA domains that is a probably beta-propeller, a PH-like domain, a TECPR domain, and a DysFC (C-terminal). The PH domain mediates the binding to phosphatidylinositol-3-phosphate (PtdIns3P). Binding to the ATG5-ATG12 conjugate exposes the PH domain, allowing the association with PtdIns3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058  609 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 687
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 124249058  688 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVHG 729
Cdd:cd13300    81 IYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122

Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058   982 GSSWLHVgtDQPFASVSIGACYQVWAVARDGSAFYRGSVSPSQPAGDCWYHIPSppkqKLTQVSVGQTSVYALDENGNLW 1061
Cdd:pfam19193   60 GGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVDG----SLKYYSCGPGGCWGVNSNDDIY 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058  1062 YRAGITPSYPQGSSWEHVSNNVRKVSVGPLDQVWVIAnkvqgshglSRGTVCRRMGVQPREPKGQGWDYGIGG-GWDHIS 1140
Cdd:pfam19193  134 YRRYVGPSTCGGTGWTQVPGKLKMIEVGSDGSVFGVN---------SNGNVYQRTGISSSNPTGTGWTQIPGSlSIKHVS 204

                   .
gi 124249058  1141 V 1141
Cdd:pfam19193  205 Y 205

Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region.

                            10        20        30
                    ....*....|....*....|....*....|....
gi 124249058    893 GWQYASDFPASYHGYKTMKDFVRRRCWARKCKLV 926
Cdd:smart00694    1 GWQYSDNFWANYHKTEKMTDFVRRRRWVRRRRHK 34

Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. 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. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion.

                           10        20        30
                   ....*....|....*....|....*....|
gi 124249058   959 ALWAVSDKGDVLCRLGVSELNPAGSSWLHV 988
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; TECPR1 is a tethering factor involved in autophagy. It promotes the autophagosome fusion with lysosomes by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns3P) present at the surface of autophagosomes. TECPR1 is also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. It contains 2 DysFN (Dysferlin domains of unknown function, N-terminal), 2 Hyd_WA domains that is a probably beta-propeller, a PH-like domain, a TECPR domain, and a DysFC (C-terminal). The PH domain mediates the binding to phosphatidylinositol-3-phosphate (PtdIns3P). Binding to the ATG5-ATG12 conjugate exposes the PH domain, allowing the association with PtdIns3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058  609 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 687
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 124249058  688 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVHG 729
Cdd:cd13300    81 IYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122

Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058   982 GSSWLHVgtDQPFASVSIGACYQVWAVARDGSAFYRGSVSPSQPAGDCWYHIPSppkqKLTQVSVGQTSVYALDENGNLW 1061
Cdd:pfam19193   60 GGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVDG----SLKYYSCGPGGCWGVNSNDDIY 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058  1062 YRAGITPSYPQGSSWEHVSNNVRKVSVGPLDQVWVIAnkvqgshglSRGTVCRRMGVQPREPKGQGWDYGIGG-GWDHIS 1140
Cdd:pfam19193  134 YRRYVGPSTCGGTGWTQVPGKLKMIEVGSDGSVFGVN---------SNGNVYQRTGISSSNPTGTGWTQIPGSlSIKHVS 204

                   .
gi 124249058  1141 V 1141
Cdd:pfam19193  205 Y 205

Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region.

                            10        20        30
                    ....*....|....*....|....*....|....
gi 124249058    893 GWQYASDFPASYHGYKTMKDFVRRRCWARKCKLV 926
Cdd:smart00694    1 GWQYSDNFWANYHKTEKMTDFVRRRRWVRRRRHK 34

Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. 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. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion.

                           10        20        30
                   ....*....|....*....|....*....|
gi 124249058   959 ALWAVSDKGDVLCRLGVSELNPAGSSWLHV 988
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 124249058    234 SSWSLVetPGEVVQISCGPHDLIWATLWEGQALVREG 270
Cdd:smart00706    1 GSWTQV--PGELVQVSVGPSDTVWAVNSDGNIYRRTG 35

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058    615 VKTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIYYVVHEEKKYLH---VFLNEVTVLVPV---LNEAKHSFAL 688
Cdd:smart00233    2 IKEGWLYKKSGGGKKSWKKRYFVL---------FNSTLLYYKSKKDKKSYKPkgsIDLSGCTVREAPdpdSSKKPHCFEI 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 124249058    689 YTPERTRqrwpVRLAAATEQDMNDWLALLSLSC 721
Cdd:smart00233   73 KTSDRKT----LLLQAESEEEREKWVEALRKAI 101

Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 124249058    766 MFWRQMGGHLRIIEANSRGVVWGIGYDHTAWVYT 799
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVNSDGNIYRRT 34

Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; TECPR1 is a tethering factor involved in autophagy. It promotes the autophagosome fusion with lysosomes by associating with both the ATG5-ATG12 conjugate and phosphatidylinositol-3-phosphate (PtdIns3P) present at the surface of autophagosomes. TECPR1 is also involved in selective autophagy against bacterial pathogens, by being required for phagophore/preautophagosomal structure biogenesis and maturation. It contains 2 DysFN (Dysferlin domains of unknown function, N-terminal), 2 Hyd_WA domains that is a probably beta-propeller, a PH-like domain, a TECPR domain, and a DysFC (C-terminal). The PH domain mediates the binding to phosphatidylinositol-3-phosphate (PtdIns3P). Binding to the ATG5-ATG12 conjugate exposes the PH domain, allowing the association with PtdIns3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058  609 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 687
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 124249058  688 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVHG 729
Cdd:cd13300    81 IYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122

Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058   982 GSSWLHVgtDQPFASVSIGACYQVWAVARDGSAFYRGSVSPSQPAGDCWYHIPSppkqKLTQVSVGQTSVYALDENGNLW 1061
Cdd:pfam19193   60 GGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVDG----SLKYYSCGPGGCWGVNSNDDIY 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058  1062 YRAGITPSYPQGSSWEHVSNNVRKVSVGPLDQVWVIAnkvqgshglSRGTVCRRMGVQPREPKGQGWDYGIGG-GWDHIS 1140
Cdd:pfam19193  134 YRRYVGPSTCGGTGWTQVPGKLKMIEVGSDGSVFGVN---------SNGNVYQRTGISSSNPTGTGWTQIPGSlSIKHVS 204

                   .
gi 124249058  1141 V 1141
Cdd:pfam19193  205 Y 205

Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058   207 GRLSVWAVSLQGKVWYREDVSHPNPEGSSWSLVetPGEVVQISCGPHDLiWATLWEGQALVREGVCRNNPKGSYWSMVep 286
Cdd:pfam19193   77 GDGQVWGVNSADDIYCLNGDDASSYAGLPWTQV--DGSLKYYSCGPGGC-WGVNSNDDIYYRRYVGPSTCGGTGWTQV-- 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124249058   287 PGSengIMHVSAGV-SVVWAITKDRKVWFRRGVNSHNPCGTSW--IEMVGEMTMVNVGLnDQVWGIS 350
Cdd:pfam19193  152 PGK---LKMIEVGSdGSVFGVNSNGNVYQRTGISSSNPTGTGWtqIPGSLSIKHVSYDL-GRLWGVN 214

Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal proteins, dysferlin, myoferlin and hypothetical proteins. Due to an insertion of a dysferlin domain within a second dysferlin domain we have chosen to predict these domains in two parts: the N-terminal region and the C-terminal region.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124249058    821 SDVKSVYIYENQ-RWNPVtGYTSRGLPTdRFMWSDVTGLQECTKAGTKPPSLQWTWVSD-WYVD 882
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62

Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. 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. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion.

                           10        20        30
                   ....*....|....*....|....*....|
gi 124249058   302 VVWAITKDRKVWFRRGVNSHNPCGTSWIEM 331
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. 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. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion.

                           10        20        30
                   ....*....|....*....|....*....|
gi 124249058   210 SVWAVSLQGKVWYREDVSHPNPEGSSWSLV 239
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, compartmentalising many activities related to lipid metabolism and functioning in the decomposition of toxic hydrogen peroxide. Sequence similarity was identified between two hypothetical proteins and the peroxin integral membrane protein Pex24p.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058   826 VYIYENQRWNPVT-GYTSRGLPTDRFMWSDvtglqECTKAGTKPPSL-----------QWTWV--SDWYVDFSVPGG--- 888
Cdd:pfam06398  254 VEIFENQRRWLLGiGWTSSLLSYERYDWTD-----EYRIALNEAPPGvdhledfeppeGWRWVdnSKWRLDLTPDGWvee 328

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 124249058   889 --------TDQEGWQYASDFPASYHGYKTMKDFVRRRCWAR 921
Cdd:pfam06398  329 rflttvnpDEDEGWVYDDNTWKEPSTEDGFSKYTRRRRWIR 369

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058  626 WKPhKWVDVRVALeqftghdgardsilFIYYVVHEEKKYLHVF-LNEVTVLVPVLNE-AKHSFALYTPERTrqrwpVRLA 703
Cdd:cd13298    22 WKK-RWVVLRPCQ--------------LSYYKDEKEYKLRRVInLSELLAVAPLKDKkRKNVFGIYTPSKN-----LHFR 81

                          90
                  ....*....|....
gi 124249058  704 AATEQDMNDWLALL 717
Cdd:cd13298    82 ATSEKDANEWVEAL 95

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058  616 KTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIYYVVHEEKKYLH--VFLNEVTVLVPVLN-EAKHSFALYTPE 692
Cdd:cd00821     1 KEGYLLKRGGGGLKSWKKRWFVL---------FEGVLLYYKSKKDSSYKPKgsIPLSGILEVEEVSPkERPHCFELVTPD 71

                          90       100
                  ....*....|....*....|....*
gi 124249058  693 RTRqrwpVRLAAATEQDMNDWLALL 717
Cdd:cd00821    72 GRT----YYLQADSEEERQEWLKAL 92

Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from plasmodia of Physarum polycephalum (Slime mold) and both proteins contain six tandem repeats that are each 33-37 amino acids in length. 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. Tectonin beta-propeller repeat-containing protein 1 (TECPR1) has a critical function during autophagosome maturation and autophagosome-lysosome fusion.

                           10        20        30
                   ....*....|....*....|....*....|
gi 124249058   255 LIWATLWEGQALVREGVCRNNPKGSYWSMV 284
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249058    615 VKTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIYYVVHEEKKYLH---VFLNEVTVLVPV---LNEAKHSFAL 688
Cdd:smart00233    2 IKEGWLYKKSGGGKKSWKKRYFVL---------FNSTLLYYKSKKDKKSYKPkgsIDLSGCTVREAPdpdSSKKPHCFEI 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 124249058    689 YTPERTRqrwpVRLAAATEQDMNDWLALLSLSC 721
Cdd:smart00233   73 KTSDRKT----LLLQAESEEEREKWVEALRKAI 101

Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a 6 bladed beta propeller structure.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249058  1041 LTQVSVGQTSVYALDENGNLWYRagitpsypQGSSWEHVSNNVRKVSVGPlDQVWVI--ANKV 1101
Cdd:pfam19193    2 LKQIDAGQGQVWGVDSAGNVYYL--------TGSSWVRVPGRLKHVSVGP-AGVWGVnsNNKI 55

Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal hypothetical proteins;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 124249058    766 MFWRQMGGHLRIIEANSRGVVWGIGYDHTAWVYT 799
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVNSDGNIYRRT 34