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 530385707  604 VEQSVWVKTGALQWWCDWKPHKWVDVRLALEQFTGHDGVRDSILFIYYVVHEEKKYIHIFLNEVVALVPVLNET-KHSFA 682
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530385707  683 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVQG 724
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 530385707   922 TSGPWLEVPPiALRDVSIipespGAEGsghsiaLWAVSDKGDVLCRlgvselnpAGSSWLHVgtDQPFASISIGACYQVW 1001
Cdd:pfam19193   25 TGSSWVRVPG-RLKHVSV-----GPAG------VWGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVW 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385707  1002 AVARDGSAFYRGSVYPSQPAGDCWYHIPSpprqRLKQVSAGQTSVYALDENGNLWYRQGITPSYPQGSSWEHVSNNVCRV 1081
Cdd:pfam19193   83 GVNSADDIYCLNGDDASSYAGLPWTQVDG----SLKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGKLKMI 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530385707  1082 SVGPLDQVWVIAnkvqgshslSRGTVCHRTGVQPHEPKGHGWDYGIGG-GWDHISV 1136
Cdd:pfam19193  159 EVGSDGSVFGVN---------SNGNVYQRTGISSSNPTGTGWTQIPGSlSIKHVSY 205

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 530385707    816 SDVKCVHIYENQ-RWNPVtGYTSRGLPTdRYMWSDASGLQECTKAGTKPPSLQWAWVSD-WFVD 877
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62

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

                            10        20        30
                    ....*....|....*....|....*....|....
gi 530385707    761 MFWRQMGGHLRMVEANSRGVVWGIGYDHTAWVYT 794
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 530385707  604 VEQSVWVKTGALQWWCDWKPHKWVDVRLALEQFTGHDGVRDSILFIYYVVHEEKKYIHIFLNEVVALVPVLNET-KHSFA 682
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530385707  683 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVQG 724
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 530385707   922 TSGPWLEVPPiALRDVSIipespGAEGsghsiaLWAVSDKGDVLCRlgvselnpAGSSWLHVgtDQPFASISIGACYQVW 1001
Cdd:pfam19193   25 TGSSWVRVPG-RLKHVSV-----GPAG------VWGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVW 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385707  1002 AVARDGSAFYRGSVYPSQPAGDCWYHIPSpprqRLKQVSAGQTSVYALDENGNLWYRQGITPSYPQGSSWEHVSNNVCRV 1081
Cdd:pfam19193   83 GVNSADDIYCLNGDDASSYAGLPWTQVDG----SLKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGKLKMI 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530385707  1082 SVGPLDQVWVIAnkvqgshslSRGTVCHRTGVQPHEPKGHGWDYGIGG-GWDHISV 1136
Cdd:pfam19193  159 EVGSDGSVFGVN---------SNGNVYQRTGISSSNPTGTGWTQIPGSlSIKHVSY 205

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 530385707    816 SDVKCVHIYENQ-RWNPVtGYTSRGLPTdRYMWSDASGLQECTKAGTKPPSLQWAWVSD-WFVD 877
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 530385707   819 KCVHIYENQRWNPVT-GYTSRGLPTDRYMWSDASG--LQECTKAGT-----KPPSlQWAWV--SDWFVDFSVPGG----- 883
Cdd:pfam06398  252 FTVEIFENQRRWLLGiGWTSSLLSYERYDWTDEYRiaLNEAPPGVDhledfEPPE-GWRWVdnSKWRLDLTPDGWveerf 330

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 530385707   884 ------TDQEGWQYASDFPASYHGSKTMKDFVRRRCWAR 916
Cdd:pfam06398  331 lttvnpDEDEGWVYDDNTWKEPSTEDGFSKYTRRRRWIR 369

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 530385707   1069 SSWEHVSNNVCRVSVGPLDQVWVIAnkvqgshslSRGTVCHRTG 1112
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVN---------SDGNIYRRTG 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 530385707    610 VKTGALQWWCDWKPHKWVDVRLALeqftghdgvRDSILFIYYVVHEEKKYIH---IFLNE---VVALVPVLNETKHSFAL 683
Cdd:smart00233    2 IKEGWLYKKSGGGKKSWKKRYFVL---------FNSTLLYYKSKKDKKSYKPkgsIDLSGctvREAPDPDSSKKPHCFEI 72

                            90       100       110
                    ....*....|....*....|....*....|...
gi 530385707    684 YTPERTRqrwpVRLAAATEQDMNDWLALLSLSC 716
Cdd:smart00233   73 KTSDRKT----LLLQAESEEEREKWVEALRKAI 101

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 530385707  604 VEQSVWVKTGALQWWCDWKPHKWVDVRLALEQFTGHDGVRDSILFIYYVVHEEKKYIHIFLNEVVALVPVLNET-KHSFA 682
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530385707  683 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVQG 724
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 530385707   922 TSGPWLEVPPiALRDVSIipespGAEGsghsiaLWAVSDKGDVLCRlgvselnpAGSSWLHVgtDQPFASISIGACYQVW 1001
Cdd:pfam19193   25 TGSSWVRVPG-RLKHVSV-----GPAG------VWGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVW 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385707  1002 AVARDGSAFYRGSVYPSQPAGDCWYHIPSpprqRLKQVSAGQTSVYALDENGNLWYRQGITPSYPQGSSWEHVSNNVCRV 1081
Cdd:pfam19193   83 GVNSADDIYCLNGDDASSYAGLPWTQVDG----SLKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGKLKMI 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530385707  1082 SVGPLDQVWVIAnkvqgshslSRGTVCHRTGVQPHEPKGHGWDYGIGG-GWDHISV 1136
Cdd:pfam19193  159 EVGSDGSVFGVN---------SNGNVYQRTGISSSNPTGTGWTQIPGSlSIKHVSY 205

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 530385707     64 PIRRREEAYENQ-RWNPmGGFCEKLLlSDRWGWSDVSGLQHRPLDRVALPSPHWEWESD-WYVD 125
Cdd:smart00693    1 PIRFTEEMYENQrRWLG-GGWKTTLL-PYRPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62

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 530385707    888 GWQYASDFPASYHGSKTMKDFVRRRCWARKCKLV 921
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 530385707   302 VVWAVTKDWKVWFRRGVNSHNPCGTSWIEM 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
                   ....*....|....*....|....*..
gi 530385707   210 SVWAVSLQGKVWYREDVSHSNPEGSSW 236
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSW 27

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 530385707   954 ALWAVSDKGDVLCRLGVSELNPAGSSWLHV 983
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530385707  650 YYVVHEEKKYIHIF-LNEVVALVPVLNE-TKHSFALYTPERTrqrwpVRLAAATEQDMNDWLALL 712
Cdd:cd13298    36 YYKDEKEYKLRRVInLSELLAVAPLKDKkRKNVFGIYTPSKN-----LHFRATSEKDANEWVEAL 95

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 530385707   999 QVWAVARDGSAFYRGSVYPSQPAGDCWYHI 1028
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

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

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 530385707    234 SSWSLLdtPGEVVQISCGPHDLLWATLWEGQALVREG 270
Cdd:smart00706    1 GSWTQV--PGELVQVSVGPSDTVWAVNSDGNIYRRTG 35

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 530385707   1069 SSWEHVSNNVCRVSVGPLDQVWVIAnkvqgshslSRGTVCHRTG 1112
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVN---------SDGNIYRRTG 35

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 530385707   345 QVWGIGCEDRaVYFRQGVTPSELSGKTWKAI 375
Cdd:pfam06462    1 QVWAVTSDGR-VYFRTGVTPSNPTGTSWEHV 30

PH domain; PH stands for pleckstrin homology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530385707   610 VKTGALQWWCDWKPHKWVDVRLALeqftghdgvRDSILFIY---YVVHEEKKYIHIFLNEVVALVPVLNE---TKHSFAL 683
Cdd:pfam00169    2 VKEGWLLKKGGGKKKSWKKRYFVL---------FDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDspkRKFCFEL 72

                           90       100       110
                   ....*....|....*....|....*....|...
gi 530385707   684 YTPERTRQRwPVRLAAATEQDMNDWLALLSLSC 716
Cdd:pfam00169   73 RTGERTGKR-TYLLQAESEEERKDWIKAIQSAI 104

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 530385707  677 TKHSFALYTPERTrqrwpVRLAAATEQDMNDWL 709
Cdd:cd01233    68 RPNVFAVYTPTNS-----YLLQARSEKEMQDWL 95

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.

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gi 530385707  1088 QVWVIAnkvqgshslSRGTVCHRTGVQPHEPKGHGWDY 1125
Cdd:pfam06462    1 QVWAVT---------SDGRVYFRTGVTPSNPTGTSWEH 29