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 1622922031  652 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYAHIFLNEVVALVPVLNET-KHSFA 730
Cdd:cd13300      1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622922031  731 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVQG 772
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 1622922031  998 GHSIALWAISDKGDVLCRLGVSALNPAGSSWLHVgtDQPFASISIGAcYQVWAVARDGSAFYRGSVYPSQPAGDCWYHIP 1077
Cdd:pfam19193   76 GGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQV--DGSLKYYSCGP-GGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVP 152

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622922031 1078 SpprqRLKQVSVG-QTSVYALDENGNLWYRQGITPSYPQGSSWEHVS-NNVCRVSVGPLDQVWVI 1140
Cdd:pfam19193  153 G----KLKMIEVGsDGSVFGVNSNGNVYQRTGISSSNPTGTGWTQIPgSLSIKHVSYDLGRLWGV 213

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 1622922031   864 SDVKCVHIYENQ-RWNPVtGYTSRGLPTdRYMWSDASGLQECTKAGTKPPSLQWAWVSD-WFVD 925
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 1622922031   809 MFWRQIGGHLRMVEANSQGVVWGIGYDHTAWVYT 842
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 1622922031  652 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYAHIFLNEVVALVPVLNET-KHSFA 730
Cdd:cd13300      1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622922031  731 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVQG 772
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 1622922031  998 GHSIALWAISDKGDVLCRLGVSALNPAGSSWLHVgtDQPFASISIGAcYQVWAVARDGSAFYRGSVYPSQPAGDCWYHIP 1077
Cdd:pfam19193   76 GGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQV--DGSLKYYSCGP-GGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVP 152

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622922031 1078 SpprqRLKQVSVG-QTSVYALDENGNLWYRQGITPSYPQGSSWEHVS-NNVCRVSVGPLDQVWVI 1140
Cdd:pfam19193  153 G----KLKMIEVGsDGSVFGVNSNGNVYQRTGISSSNPTGTGWTQIPgSLSIKHVSYDLGRLWGV 213

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 1622922031   864 SDVKCVHIYENQ-RWNPVtGYTSRGLPTdRYMWSDASGLQECTKAGTKPPSLQWAWVSD-WFVD 925
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 1622922031  867 KCVHIYENQRWNPVT-GYTSRGLPTDRYMWSDASG--LQECTKAGT-----KPPSlQWAWV--SDWFVDFSVPGG----- 931
Cdd:pfam06398  252 FTVEIFENQRRWLLGiGWTSSLLSYERYDWTDEYRiaLNEAPPGVDhledfEPPE-GWRWVdnSKWRLDLTPDGWveerf 330

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622922031  932 ------TDQEGWQYASDFPASYHGSKTMKDFVRRRCWAR 964
Cdd:pfam06398  331 lttvnpDEDEGWVYDDNTWKEPSTEDGFSKYTRRRRWIR 369

PH domain; PH stands for pleckstrin homology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922031  658 VKTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIY---YVVHEEKKYAHIFLNEVVALVPVLNE---TKHSFAL 731
Cdd:pfam00169    2 VKEGWLLKKGGGKKKSWKKRYFVL---------FDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDspkRKFCFEL 72

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622922031  732 YTPERTRQRwPVRLAAATEQDMNDWLALLSLSC 764
Cdd:pfam00169   73 RTGERTGKR-TYLLQAESEEERKDWIKAIQSAI 104

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1622922031  1117 SSWEHVSNNVCRVSVGPLDQVWVIAnkvqgshslSRGTVCHRTG 1160
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 1622922031 1136 QVWVIAnkvqgshslSRGTVCHRTGVQPHEPKGHGWDY 1173
Cdd:pfam06462    1 QVWAVT---------SDGRVYFRTGVTPSNPTGTSWEH 29

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 1622922031  652 VEQSVWVKTGALQWWCDWKPHKWVDVRVALEQFTGHDGARDSILFIYYVVHEEKKYAHIFLNEVVALVPVLNET-KHSFA 730
Cdd:cd13300      1 VERSSWVKTGALQWWSDWKPHKWADCRVALEQGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGeKPSFA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622922031  731 LYTPERTRQRWPVRLAAATEQDMNDWLALLSLSCCESRKVQG 772
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 1622922031  998 GHSIALWAISDKGDVLCRLGVSALNPAGSSWLHVgtDQPFASISIGAcYQVWAVARDGSAFYRGSVYPSQPAGDCWYHIP 1077
Cdd:pfam19193   76 GGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQV--DGSLKYYSCGP-GGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVP 152

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622922031 1078 SpprqRLKQVSVG-QTSVYALDENGNLWYRQGITPSYPQGSSWEHVS-NNVCRVSVGPLDQVWVI 1140
Cdd:pfam19193  153 G----KLKMIEVGsDGSVFGVNSNGNVYQRTGISSSNPTGTGWTQIPgSLSIKHVSYDLGRLWGV 213

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 1622922031  255 GRLSVWAVSLQGKVWYREDVSHSNPEGSSWSLLDtpGEVVQISCGPhdllwATLW----EGQALVREGINRSNPKGSSWS 330
Cdd:pfam19193   77 GDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVD--GSLKYYSCGP-----GGCWgvnsNDDIYYRRYVGPSTCGGTGWT 149

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922031  331 VVepPGSengVMHVSVGVN-VVWAVTKDQKVWFRRGVNSHNPCGTSWIEMVGEMLMVNVGMND-QVWGIG 398
Cdd:pfam19193  150 QV--PGK---LKMIEVGSDgSVFGVNSNGNVYQRTGISSSNPTGTGWTQIPGSLSIKHVSYDLgRLWGVN 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 1622922031   864 SDVKCVHIYENQ-RWNPVtGYTSRGLPTdRYMWSDASGLQECTKAGTKPPSLQWAWVSD-WFVD 925
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 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 1622922031   936 GWQYASDFPASYHGSKTMKDFVRRRCWARKCKLV 969
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
                   ....*....|....*....|....*..
gi 1622922031  258 SVWAVSLQGKVWYREDVSHSNPEGSSW 284
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSW 27

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 1622922031  867 KCVHIYENQRWNPVT-GYTSRGLPTDRYMWSDASG--LQECTKAGT-----KPPSlQWAWV--SDWFVDFSVPGG----- 931
Cdd:pfam06398  252 FTVEIFENQRRWLLGiGWTSSLLSYERYDWTDEYRiaLNEAPPGVDhledfEPPE-GWRWVdnSKWRLDLTPDGWveerf 330

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622922031  932 ------TDQEGWQYASDFPASYHGSKTMKDFVRRRCWAR 964
Cdd:pfam06398  331 lttvnpDEDEGWVYDDNTWKEPSTEDGFSKYTRRRRWIR 369

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 1622922031 1002 ALWAISDKGDVLCRLGVSALNPAGSSWLHV 1031
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 1622922031 1047 QVWAVARDGSAFYRGSVYPSQPAGDCWYHI 1076
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30

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

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1622922031   282 SSWSLLdtPGEVVQISCGPHDLLWATLWEGQALVREG 318
Cdd:smart00706    1 GSWTQV--PGELVQVSVGPSDTVWAVNSDGNIYRRTG 35

PH domain; PH stands for pleckstrin homology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622922031  658 VKTGALQWWCDWKPHKWVDVRVALeqftghdgaRDSILFIY---YVVHEEKKYAHIFLNEVVALVPVLNE---TKHSFAL 731
Cdd:pfam00169    2 VKEGWLLKKGGGKKKSWKKRYFVL---------FDGSLLYYkddKSGKSKEPKGSISLSGCEVVEVVASDspkRKFCFEL 72

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622922031  732 YTPERTRQRwPVRLAAATEQDMNDWLALLSLSC 764
Cdd:pfam00169   73 RTGERTGKR-TYLLQAESEEERKDWIKAIQSAI 104

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1622922031  1117 SSWEHVSNNVCRVSVGPLDQVWVIAnkvqgshslSRGTVCHRTG 1160
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 1622922031  393 QVWGIGCEDRaVYFRQGVTPSELSGKTWKAI 423
Cdd:pfam06462    1 QVWAVTSDGR-VYFRTGVTPSNPTGTSWEHV 30

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 1622922031  725 TKHSFALYTPERTrqrwpVRLAAATEQDMNDWL 757
Cdd:cd01233     68 RPNVFAVYTPTNS-----YLLQARSEKEMQDWL 95

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 1622922031 1084 LKQVSVGQTSVYALDENGNLWYRqgitpsypQGSSWEHVSNNVCRVSVGPlDQVWVI--ANKV 1144
Cdd:pfam19193    2 LKQIDAGQGQVWGVDSAGNVYYL--------TGSSWVRVPGRLKHVSVGP-AGVWGVnsNNKI 55