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 1958668496 279 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 357
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958668496 358 LYTPERTRQRWPVRLAATTEQDMNDWLTLLSLSCCESRKVHG 399
Cdd:cd13300    81 IYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122

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 1958668496  491 SDVKSVYIYENQ-RWNPVtGYTSRGLPTdRYMWSDVTGLQECTKAGTKPPSLQWTWVSD-WYVD 552
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 1958668496  15 QVWGISCEDRaVYFRQGVTPSELSGKTWKAI 45
Cdd:pfam06462   1 QVWAVTSDGR-VYFRTGVTPSNPTGTSWEHV 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 1958668496 279 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 357
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958668496 358 LYTPERTRQRWPVRLAATTEQDMNDWLTLLSLSCCESRKVHG 399
Cdd:cd13300    81 IYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122

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 1958668496  491 SDVKSVYIYENQ-RWNPVtGYTSRGLPTdRYMWSDVTGLQECTKAGTKPPSLQWTWVSD-WYVD 552
Cdd:smart00693   1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62

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 1958668496 496 VYIYENQRWNPVT-GYTSRGLPTDRYMWSDvtglqECTKAGTKPPSL-----------QWTWV--SDWYVD--------- 552
Cdd:pfam06398 254 VEIFENQRRWLLGiGWTSSLLSYERYDWTD-----EYRIALNEAPPGvdhledfeppeGWRWVdnSKWRLDltpdgwvee 328

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958668496 553 --FSVLGGTDQEGWQYASDFPASYHGYKTMKDFVRRRCWAR 591
Cdd:pfam06398 329 rfLTTVNPDEDEGWVYDDNTWKEPSTEDGFSKYTRRRRWIR 369

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668496 285 VKTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIY---YVVHEEKKYLHVFLNEVTVLVPVLNE---AKHSFAL 358
Cdd:pfam00169   2 VKEGWLLKKGGGKKKSWKKRYFVL---------FDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDspkRKFCFEL 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958668496 359 YTPERTRQRwPVRLAATTEQDMNDWLTLLSLSC 391
Cdd:pfam00169  73 RTGERTGKR-TYLLQAESEEERKDWIKAIQSAI 104

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

                           10        20
                   ....*....|....*....|....*.
gi 1958668496  744 SSWEHVSNNVRKVSVGPLDQVWVIAN 769
Cdd:smart00706   1 GSWTQVPGELVQVSVGPSDTVWAVNS 26

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

                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958668496    1 MVGEMTMVNVGLNDQVWGISCeDRAVYFRQG 31
Cdd:smart00706   6 VPGELVQVSVGPSDTVWAVNS-DGNIYRRTG 35

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 1958668496 279 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 357
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958668496 358 LYTPERTRQRWPVRLAATTEQDMNDWLTLLSLSCCESRKVHG 399
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 1958668496 652 GSSWLHVgtDQPFASVSIGACYQVWAVARDGSAFYRGSVSPSQPAGDCWYHIPSppkqKLTQVSVGQTSVYALDENGNLW 731
Cdd:pfam19193  60 GGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVDG----SLKYYSCGPGGCWGVNSNDDIY 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668496 732 YRAGITPSYPQGSSWEHVSNNVRKVSVGPLDQVWVIAnkvqgshglSRGTVCRRMGVQPREPKGQGWDYGIGG-GWDHIS 810
Cdd:pfam19193 134 YRRYVGPSTCGGTGWTQVPGKLKMIEVGSDGSVFGVN---------SNGNVYQRTGISSSNPTGTGWTQIPGSlSIKHVS 204

                  .
gi 1958668496 811 V 811
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 1958668496  563 GWQYASDFPASYHGYKTMKDFVRRRCWARKCKLV 596
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 1958668496 720 SVYALDENGNLWYRAGITPSYPQGSSWEHV 749
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 1958668496 629 ALWAVSDKGDVLCRLGVSELNPAGSSWLHV 658
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 1958668496 674 QVWAVARDGSAFYRGSVSPSQPAGDCWYHI 703
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 1958668496  285 VKTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIYYVVHEEKKYLH---VFLNEVTVLVPV---LNEAKHSFAL 358
Cdd:smart00233   2 IKEGWLYKKSGGGKKSWKKRYFVL---------FNSTLLYYKSKKDKKSYKPkgsIDLSGCTVREAPdpdSSKKPHCFEI 72

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958668496  359 YTPERTRqrwpVRLAATTEQDMNDWLTLLSLSC 391
Cdd:smart00233  73 KTSDRKT----LLLQAESEEEREKWVEALRKAI 101

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 1958668496  15 QVWGISCEDRaVYFRQGVTPSELSGKTWKAI 45
Cdd:pfam06462   1 QVWAVTSDGR-VYFRTGVTPSNPTGTSWEHV 30

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

                           10        20
                   ....*....|....*....|....*.
gi 1958668496  744 SSWEHVSNNVRKVSVGPLDQVWVIAN 769
Cdd:smart00706   1 GSWTQVPGELVQVSVGPSDTVWAVNS 26

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

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958668496  653 SSWLHVgtDQPFASVSIGACYQVWAVARDGSAFYR 687
Cdd:smart00706   1 GSWTQV--PGELVQVSVGPSDTVWAVNSDGNIYRR 33