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 1907166123  85 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 163
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907166123 164 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVHG 205
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 1907166123  297 SDVKSVYIYENQ-RWNPVtGYTSRGLPTdRFMWSDVTGLQECTKAGTKPPSLQWTWVSD-WYVD 358
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 1907166123 435 ALWAVSDKGDVLCRLGVSELNPAGSSWLHV 464
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 1907166123  85 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 163
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907166123 164 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVHG 205
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 1907166123  297 SDVKSVYIYENQ-RWNPVtGYTSRGLPTdRFMWSDVTGLQECTKAGTKPPSLQWTWVSD-WYVD 358
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 1907166123 435 ALWAVSDKGDVLCRLGVSELNPAGSSWLHV 464
Cdd:pfam06462   1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166123  91 VKTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIY---YVVHEEKKYLHVFLNEVTVLVPVLNE---AKHSFAL 164
Cdd:pfam00169   2 VKEGWLLKKGGGKKKSWKKRYFVL---------FDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDspkRKFCFEL 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907166123 165 YTPERTRQRwPVRLAAATEQDMNDWLALLSLSC 197
Cdd:pfam00169  73 RTGERTGKR-TYLLQAESEEERKDWIKAIQSAI 104

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

                           10        20
                   ....*....|....*....|....*.
gi 1907166123  550 SSWEHVSNNVRKVSVGPLDQVWVIAN 575
Cdd:smart00706   1 GSWTQVPGELVQVSVGPSDTVWAVNS 26

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 1907166123  85 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYLHVFLNEVTVLVPVLNEA-KHSFA 163
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907166123 164 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVHG 205
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 1907166123  297 SDVKSVYIYENQ-RWNPVtGYTSRGLPTdRFMWSDVTGLQECTKAGTKPPSLQWTWVSD-WYVD 358
Cdd:smart00693   1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62

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 1907166123 473 VSIGACyQVWAVARDGSAFYRgsvspsqpAGDCWYHIPSppkqKLTQVSVGQTSVYALDENGNLWYRagitpsypQGSSW 552
Cdd:pfam19193   5 IDAGQG-QVWGVDSAGNVYYL--------TGSSWVRVPG----RLKHVSVGPAGVWGVNSNNKIYKY--------VGGSW 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907166123 553 EHVSNNVRKVSVGPLDQVWVIAnkvqgshglSRGTVCRRMGVQPREPKGQGWDYgIGGGWDHISV 617
Cdd:pfam19193  64 VPVDGSLKQVDAGGDGQVWGVN---------SADDIYCLNGDDASSYAGLPWTQ-VDGSLKYYSC 118

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 1907166123 435 ALWAVSDKGDVLCRLGVSELNPAGSSWLHV 464
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 1907166123 480 QVWAVARDGSAFYRGSVSPSQPAGDCWYHI 509
Cdd:pfam06462   1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

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 1907166123  92 KTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIYYVVHEEKKYLH--VFLNEVTVLVPVLN-EAKHSFALYTPE 168
Cdd:cd00821     1 KEGYLLKRGGGGLKSWKKRWFVL---------FEGVLLYYKSKKDSSYKPKgsIPLSGILEVEEVSPkERPHCFELVTPD 71

                          90       100
                  ....*....|....*....|....*
gi 1907166123 169 RTRqrwpVRLAAATEQDMNDWLALL 193
Cdd:cd00821    72 GRT----YYLQADSEEERQEWLKAL 92

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 1907166123   91 VKTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIYYVVHEEKKYLH---VFLNEVTVLVPV---LNEAKHSFAL 164
Cdd:smart00233   2 IKEGWLYKKSGGGKKSWKKRYFVL---------FNSTLLYYKSKKDKKSYKPkgsIDLSGCTVREAPdpdSSKKPHCFEI 72

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1907166123  165 YTPERTRqrwpVRLAAATEQDMNDWLALLSLSC 197
Cdd:smart00233  73 KTSDRKT----LLLQAESEEEREKWVEALRKAI 101

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

                           10        20
                   ....*....|....*....|....*.
gi 1907166123  550 SSWEHVSNNVRKVSVGPLDQVWVIAN 575
Cdd:smart00706   1 GSWTQVPGELVQVSVGPSDTVWAVNS 26

KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA (Caenorhabditis elegans homolog unc-104) and KIFIB transport synaptic vesicle precursors that contain synaptic vesicle proteins, such as synaptophysin, synaptotagmin and the small GTPase RAB3A, but they do not transport organelles that contain plasma membrane proteins. They have a N-terminal motor domain, followed by a coiled-coil domain, and a C-terminal PH domain. KIF1A adopts a monomeric form in vitro, but acts as a processive dimer in vivo. KIF1B has alternatively spliced isoforms distinguished by the presence or absence of insertion sequences in the conserved amino-terminal region of the protein; this results in their different motor activities. KIF1A and KIF1B bind to RAB3 proteins through the adaptor protein mitogen-activated protein kinase (MAPK) -activating death domain (MADD; also calledDENN), which was first identified as a RAB3 guanine nucleotide exchange factor (GEF). 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
                  ....*....|....*....|....*....|..
gi 1907166123 159 KHSFALYTPERTrqrwpVRLAAATEQDMNDWL 190
Cdd:cd01233    69 PNVFAVYTPTNS-----YLLQARSEKEMQDWL 95