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Conserved domains on  [gi|195591795|ref|XP_002085624|]
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tectonin beta-propeller repeat-containing protein [Drosophila simulans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 821-953 8.82e-38

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


:

Pssm-ID: 459768  Cd Length: 124  Bit Score: 137.77  E-value: 8.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   821 YNGMPCGTELEISGCVYDDADQIRFDLQSHstvkvqphrVEKHRVIAFHLNPRFNERTTVLNSMKESEWLDEIRNDKMAF 900
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG---------VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPF 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 195591795   901 APGATFSLKIRALQDHYLIIVNNAVYTDYKYRIDPESVTRLYVSGRIKLFNVL 953
Cdd:pfam00337   72 QPGQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Tectonin super family cl41172
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 210-398 7.98e-18

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


The actual alignment was detected with superfamily member pfam19193:

Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 83.84  E-value: 7.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   210 VWAITAHGRAMFRTGVSKTAPEGL---------------------RWTAVP-TPTGSELSQISVGPTGLVWAVLYNGRVI 267
Cdd:pfam19193   12 VWGVDSAGNVYYLTGSSWVRVPGRlkhvsvgpagvwgvnsnnkiyKYVGGSwVPVDGSLKQVDAGGDGQVWGVNSADDIY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   268 VRTGVTRDNLVGDSWLDVktpvaASSLRivHVSVGTDAVWCVTNDHHAWFRRGVkgeaagiSEDSAIGKGWVEMVGNISM 347
Cdd:pfam19193   92 CLNGDDASSYAGLPWTQV-----DGSLK--YYSCGPGGCWGVNSNDDIYYRRYV-------GPSTCGGTGWTQVPGKLKM 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 195591795   348 VSVAANDQVFAVGAADRcLYHRSGVTSADPTGKKWRLIQCPMQISRTSSSL 398
Cdd:pfam19193  158 IEVGSDGSVFGVNSNGN-VYQRTGISSSNPTGTGWTQIPGSLSIKHVSYDL 207
Tectonin super family cl41172
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1165-1333 3.08e-15

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


The actual alignment was detected with superfamily member pfam19193:

Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 76.14  E-value: 3.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1165 WAIASNGDVLIRhgvcslnpRGDAWEHItsDQPLVGISVGPTGQVWTVARNGMVFFRYGISRQNPCGDAWQQVEapagVT 1244
Cdd:pfam19193   47 WGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVD----GS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1245 FKAISVGRAGIWALDNQQRLAVRKEISRTFPEGSHWQFLPNAanvpphtdqhcgFRSVSVGS--EVWAISLNGIICRRCG 1322
Cdd:pfam19193  113 LKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGK------------LKMIEVGSdgSVFGVNSNGNVYQRTG 180

                          170
                   ....*....|.
gi 195591795  1323 ITKENPAGVGW 1333
Cdd:pfam19193  181 ISSSNPTGTGW 191
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 639-767 5.83e-12

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13300:

Pssm-ID: 473070  Cd Length: 122  Bit Score: 64.03  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  639 VELSSWVKSADARYQRPGGEFE--DCIIELEwvssgSGTGTNSSENSRsgdsgtFTVLSPDGAATK-IQFPLSDITCVQ- 714
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKwaDCRVALE-----QGTGSDGRQDSI------FFVYYTYHGEKKyIQFFLSEITCVVp 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195591795  715 CCSEAGAPRIAIHAPHLPVNCSPVKLQFSSDSEMEDWLSHLSSVCSQINTLVG 767
Cdd:cd13300    70 VNNGGEKPSFAIYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122
DysFC smart00694
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1092-1125 1.56e-11

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.


:

Pssm-ID: 128935  Cd Length: 34  Bit Score: 59.92  E-value: 1.56e-11
                            10        20        30
                    ....*....|....*....|....*....|....
gi 195591795   1092 GWQYAIDFPANYHAHKKLTDCVRQRRWMKRCRLS 1125
Cdd:smart00694    1 GWQYSDNFWANYHKTEKMTDFVRRRRWVRRRRHK 34
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 64-125 3.06e-10

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.


:

Pssm-ID: 214777  Cd Length: 62  Bit Score: 57.15  E-value: 3.06e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195591795     64 PIRIREESYENE-RWLPIeGFSKTLLPTdRYRYSSADGSVERGVDKIRLPSMAWQWDGD-WHLD 125
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1021-1081 9.66e-08

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.


:

Pssm-ID: 214777  Cd Length: 62  Bit Score: 50.22  E-value: 9.66e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195591795   1021 DTHTYYVYENQ-RWNPIsGFTAKSLPTdRHMWSDATGRQKRSKEHTKLLSTHCEWISD-WAID 1081
Cdd:smart00693    2 IRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 966-1000 2.96e-05

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


:

Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 42.10  E-value: 2.96e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 195591795    966 MHWRQMGGHIKRIFNSGVDVVWGISCDNTGWVYNG 1000
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
 
Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 821-953 8.82e-38

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 137.77  E-value: 8.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   821 YNGMPCGTELEISGCVYDDADQIRFDLQSHstvkvqphrVEKHRVIAFHLNPRFNERTTVLNSMKESEWLDEIRNDKMAF 900
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG---------VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPF 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 195591795   901 APGATFSLKIRALQDHYLIIVNNAVYTDYKYRIDPESVTRLYVSGRIKLFNVL 953
Cdd:pfam00337   72 QPGQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 822-952 6.56e-34

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 126.55  E-value: 6.56e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795    822 NGMPCGTELEISGCVYDDADQIRFDLQSHSTvkvqphrvekhRVIAFHLNPRFNERTTVLNSMKESEWLDEIRNDKMAFA 901
Cdd:smart00908    2 GGLSPGSSITIRGIVLPDAKRFSINLQCGPN-----------ADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQ 70

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 195591795    902 PGATFSLKIRALQDHYLIIVNNAVYTDYKYRIDPESVTRLYVSGRIKLFNV 952
Cdd:smart00908   71 PGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 815-952 5.77e-29

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 112.73  E-value: 5.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  815 PYYNTLYNGMPCGTELEISGCVYDDADQIRFDLQSHSTVkvqphrvekhrvIAFHLNPRFNERTTVLNSMKESEWLDEIR 894
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSD------------IALHFNPRFDENVIVRNSFLNGNWGPEER 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 195591795  895 NDKMAFAPGATFSLKIRALQDHYLIIVNNAVYTDYKYRIDPESVTRLYVSGRIKLFNV 952
Cdd:cd00070    69 SGGFPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 210-398 7.98e-18

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


Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 83.84  E-value: 7.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   210 VWAITAHGRAMFRTGVSKTAPEGL---------------------RWTAVP-TPTGSELSQISVGPTGLVWAVLYNGRVI 267
Cdd:pfam19193   12 VWGVDSAGNVYYLTGSSWVRVPGRlkhvsvgpagvwgvnsnnkiyKYVGGSwVPVDGSLKQVDAGGDGQVWGVNSADDIY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   268 VRTGVTRDNLVGDSWLDVktpvaASSLRivHVSVGTDAVWCVTNDHHAWFRRGVkgeaagiSEDSAIGKGWVEMVGNISM 347
Cdd:pfam19193   92 CLNGDDASSYAGLPWTQV-----DGSLK--YYSCGPGGCWGVNSNDDIYYRRYV-------GPSTCGGTGWTQVPGKLKM 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 195591795   348 VSVAANDQVFAVGAADRcLYHRSGVTSADPTGKKWRLIQCPMQISRTSSSL 398
Cdd:pfam19193  158 IEVGSDGSVFGVNSNGN-VYQRTGISSSNPTGTGWTQIPGSLSIKHVSYDL 207
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1165-1333 3.08e-15

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


Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 76.14  E-value: 3.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1165 WAIASNGDVLIRhgvcslnpRGDAWEHItsDQPLVGISVGPTGQVWTVARNGMVFFRYGISRQNPCGDAWQQVEapagVT 1244
Cdd:pfam19193   47 WGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVD----GS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1245 FKAISVGRAGIWALDNQQRLAVRKEISRTFPEGSHWQFLPNAanvpphtdqhcgFRSVSVGS--EVWAISLNGIICRRCG 1322
Cdd:pfam19193  113 LKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGK------------LKMIEVGSdgSVFGVNSNGNVYQRTG 180

                          170
                   ....*....|.
gi 195591795  1323 ITKENPAGVGW 1333
Cdd:pfam19193  181 ISSSNPTGTGW 191
PH1_TECPR1 cd13300
Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; ...
 639-767 5.83e-12

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.


Pssm-ID: 270112  Cd Length: 122  Bit Score: 64.03  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  639 VELSSWVKSADARYQRPGGEFE--DCIIELEwvssgSGTGTNSSENSRsgdsgtFTVLSPDGAATK-IQFPLSDITCVQ- 714
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKwaDCRVALE-----QGTGSDGRQDSI------FFVYYTYHGEKKyIQFFLSEITCVVp 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195591795  715 CCSEAGAPRIAIHAPHLPVNCSPVKLQFSSDSEMEDWLSHLSSVCSQINTLVG 767
Cdd:cd13300    70 VNNGGEKPSFAIYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122
DysFC smart00694
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1092-1125 1.56e-11

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.


Pssm-ID: 128935  Cd Length: 34  Bit Score: 59.92  E-value: 1.56e-11
                            10        20        30
                    ....*....|....*....|....*....|....
gi 195591795   1092 GWQYAIDFPANYHAHKKLTDCVRQRRWMKRCRLS 1125
Cdd:smart00694    1 GWQYSDNFWANYHKTEKMTDFVRRRRWVRRRRHK 34
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 64-125 3.06e-10

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.


Pssm-ID: 214777  Cd Length: 62  Bit Score: 57.15  E-value: 3.06e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195591795     64 PIRIREESYENE-RWLPIeGFSKTLLPTdRYRYSSADGSVERGVDKIRLPSMAWQWDGD-WHLD 125
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1021-1081 9.66e-08

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.


Pssm-ID: 214777  Cd Length: 62  Bit Score: 50.22  E-value: 9.66e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195591795   1021 DTHTYYVYENQ-RWNPIsGFTAKSLPTdRHMWSDATGRQKRSKEHTKLLSTHCEWISD-WAID 1081
Cdd:smart00693    2 IRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 966-1000 2.96e-05

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


Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 42.10  E-value: 2.96e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 195591795    966 MHWRQMGGHIKRIFNSGVDVVWGISCDNTGWVYNG 1000
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 1187-1223 1.38e-04

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


Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 40.17  E-value: 1.38e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 195591795   1187 DAWEHItsDQPLVGISVGPTGQVWTVARNGMVFFRYG 1223
Cdd:smart00706    1 GSWTQV--PGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 234-271 2.33e-04

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


Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 39.79  E-value: 2.33e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 195591795    234 RWTAVPtptgSELSQISVGPTGLVWAVLYNGRVIVRTG 271
Cdd:smart00706    2 SWTQVP----GELVQVSVGPSDTVWAVNSDGNIYRRTG 35
Pex24p pfam06398
Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, ...
 72-160 1.81e-03

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.


Pssm-ID: 399414 [Multi-domain]  Cd Length: 369  Bit Score: 42.41  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795    72 YENER-WLPIEGFSKTLLPTDRYRYSSADG-------SVERGVDKIRLPSMaWQWDG--DWHLDLELDG----------Q 131
Cdd:pfam06398  257 FENQRrWLLGIGWTSSLLSYERYDWTDEYRialneapPGVDHLEDFEPPEG-WRWVDnsKWRLDLTPDGwveerflttvN 335

                           90       100
                   ....*....|....*....|....*....
gi 195591795   132 PLPEDGWMYALDFPATYSAKKSWNSYVRR 160
Cdd:pfam06398  336 PDEDEGWVYDDNTWKEPSTEDGFSKYTRR 364
 
Name Accession Description Interval E-value
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 821-953 8.82e-38

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 137.77  E-value: 8.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   821 YNGMPCGTELEISGCVYDDADQIRFDLQSHstvkvqphrVEKHRVIAFHLNPRFNERTTVLNSMKESEWLDEIRNDKMAF 900
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG---------VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPF 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 195591795   901 APGATFSLKIRALQDHYLIIVNNAVYTDYKYRIDPESVTRLYVSGRIKLFNVL 953
Cdd:pfam00337   72 QPGQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 822-952 6.56e-34

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 126.55  E-value: 6.56e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795    822 NGMPCGTELEISGCVYDDADQIRFDLQSHSTvkvqphrvekhRVIAFHLNPRFNERTTVLNSMKESEWLDEIRNDKMAFA 901
Cdd:smart00908    2 GGLSPGSSITIRGIVLPDAKRFSINLQCGPN-----------ADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQ 70

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 195591795    902 PGATFSLKIRALQDHYLIIVNNAVYTDYKYRIDPESVTRLYVSGRIKLFNV 952
Cdd:smart00908   71 PGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 815-952 5.77e-29

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 112.73  E-value: 5.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  815 PYYNTLYNGMPCGTELEISGCVYDDADQIRFDLQSHSTVkvqphrvekhrvIAFHLNPRFNERTTVLNSMKESEWLDEIR 894
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGSSD------------IALHFNPRFDENVIVRNSFLNGNWGPEER 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 195591795  895 NDKMAFAPGATFSLKIRALQDHYLIIVNNAVYTDYKYRIDPESVTRLYVSGRIKLFNV 952
Cdd:cd00070    69 SGGFPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSV 126
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 816-952 4.18e-27

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 107.31  E-value: 4.18e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795    816 YYNTLYNGMPCGTELEISGCVYDDADQIRFDLQSHStvkvqphrvekhRVIAFHLNPRFNERTTVLNSMKESEWLDEIRN 895
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGG------------DDIALHFNPRFNENKIVCNSKLNGSWGSEERE 68

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 195591795    896 DKMAFAPGATFSLKIRALQDHYLIIVNNAVYTDYKYRIDPESVTRLYVSGRIKLFNV 952
Cdd:smart00276   69 GGFPFQPGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSV 125
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 210-398 7.98e-18

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


Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 83.84  E-value: 7.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   210 VWAITAHGRAMFRTGVSKTAPEGL---------------------RWTAVP-TPTGSELSQISVGPTGLVWAVLYNGRVI 267
Cdd:pfam19193   12 VWGVDSAGNVYYLTGSSWVRVPGRlkhvsvgpagvwgvnsnnkiyKYVGGSwVPVDGSLKQVDAGGDGQVWGVNSADDIY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   268 VRTGVTRDNLVGDSWLDVktpvaASSLRivHVSVGTDAVWCVTNDHHAWFRRGVkgeaagiSEDSAIGKGWVEMVGNISM 347
Cdd:pfam19193   92 CLNGDDASSYAGLPWTQV-----DGSLK--YYSCGPGGCWGVNSNDDIYYRRYV-------GPSTCGGTGWTQVPGKLKM 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 195591795   348 VSVAANDQVFAVGAADRcLYHRSGVTSADPTGKKWRLIQCPMQISRTSSSL 398
Cdd:pfam19193  158 IEVGSDGSVFGVNSNGN-VYQRTGISSSNPTGTGWTQIPGSLSIKHVSYDL 207
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1165-1333 3.08e-15

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


Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 76.14  E-value: 3.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1165 WAIASNGDVLIRhgvcslnpRGDAWEHItsDQPLVGISVGPTGQVWTVARNGMVFFRYGISRQNPCGDAWQQVEapagVT 1244
Cdd:pfam19193   47 WGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVD----GS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1245 FKAISVGRAGIWALDNQQRLAVRKEISRTFPEGSHWQFLPNAanvpphtdqhcgFRSVSVGS--EVWAISLNGIICRRCG 1322
Cdd:pfam19193  113 LKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGK------------LKMIEVGSdgSVFGVNSNGNVYQRTG 180

                          170
                   ....*....|.
gi 195591795  1323 ITKENPAGVGW 1333
Cdd:pfam19193  181 ISSSNPTGTGW 191
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 205-310 1.16e-13

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


Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 71.52  E-value: 1.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795   205 AGTLCVWAITAHGRAMFRTGVSKTAPEGLRWTAVPtptGSeLSQISVGPTGLVWAVLYNGRVIVRTGVTRDNLVGDSWLD 284
Cdd:pfam19193  118 CGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVP---GK-LKMIEVGSDGSVFGVNSNGNVYQRTGISSSNPTGTGWTQ 193

                           90       100
                   ....*....|....*....|....*.
gi 195591795   285 VktpvaASSLRIVHVSVGTDAVWCVT 310
Cdd:pfam19193  194 I-----PGSLSIKHVSYDLGRLWGVN 214
PH1_TECPR1 cd13300
Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; ...
 639-767 5.83e-12

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.


Pssm-ID: 270112  Cd Length: 122  Bit Score: 64.03  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  639 VELSSWVKSADARYQRPGGEFE--DCIIELEwvssgSGTGTNSSENSRsgdsgtFTVLSPDGAATK-IQFPLSDITCVQ- 714
Cdd:cd13300     1 VERSSWVKTGALQWWSDWKPHKwaDCRVALE-----QGTGSDGRQDSI------FFVYYTYHGEKKyIQFFLSEITCVVp 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195591795  715 CCSEAGAPRIAIHAPHLPVNCSPVKLQFSSDSEMEDWLSHLSSVCSQINTLVG 767
Cdd:cd13300    70 VNNGGEKPSFAIYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1165-1284 1.42e-11

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


Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 65.35  E-value: 1.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1165 WAIASNGDVLIRHGVCSLNPRGDAWEHItsDQPLVGISVGPTGqVWTVARNGMVFFRYGISRQNPCGDAWQQVEApagvT 1244
Cdd:pfam19193   82 WGVNSADDIYCLNGDDASSYAGLPWTQV--DGSLKYYSCGPGG-CWGVNSNDDIYYRRYVGPSTCGGTGWTQVPG----K 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 195591795  1245 FKAISVGRAG-IWALDNQQRLAVRKEISRTFPEGSHWQFLP 1284
Cdd:pfam19193  155 LKMIEVGSDGsVFGVNSNGNVYQRTGISSSNPTGTGWTQIP 195
DysFC smart00694
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1092-1125 1.56e-11

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.


Pssm-ID: 128935  Cd Length: 34  Bit Score: 59.92  E-value: 1.56e-11
                            10        20        30
                    ....*....|....*....|....*....|....
gi 195591795   1092 GWQYAIDFPANYHAHKKLTDCVRQRRWMKRCRLS 1125
Cdd:smart00694    1 GWQYSDNFWANYHKTEKMTDFVRRRRWVRRRRHK 34
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 64-125 3.06e-10

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.


Pssm-ID: 214777  Cd Length: 62  Bit Score: 57.15  E-value: 3.06e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195591795     64 PIRIREESYENE-RWLPIeGFSKTLLPTdRYRYSSADGSVERGVDKIRLPSMAWQWDGD-WHLD 125
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1165-1256 8.69e-10

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


Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 60.35  E-value: 8.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1165 WAIASNGDVLIRHGVCSLNPRGDAWEHItsDQPLVGISVGPTGQVWTVARNGMVFFRYGISRQNPCGDAWQQVeaPAGVT 1244
Cdd:pfam19193  124 WGVNSNDDIYYRRYVGPSTCGGTGWTQV--PGKLKMIEVGSDGSVFGVNSNGNVYQRTGISSSNPTGTGWTQI--PGSLS 199

                           90
                   ....*....|..
gi 195591795  1245 FKAISVGRAGIW 1256
Cdd:pfam19193  200 IKHVSYDLGRLW 211
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1021-1081 9.66e-08

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.


Pssm-ID: 214777  Cd Length: 62  Bit Score: 50.22  E-value: 9.66e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195591795   1021 DTHTYYVYENQ-RWNPIsGFTAKSLPTdRHMWSDATGRQKRSKEHTKLLSTHCEWISD-WAID 1081
Cdd:smart00693    2 IRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 1208-1237 2.00e-07

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.


Pssm-ID: 461921 [Multi-domain]  Cd Length: 30  Bit Score: 48.18  E-value: 2.00e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 195591795  1208 QVWTVARNGMVFFRYGISRQNPCGDAWQQV 1237
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1197-1334 5.84e-07

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


Pssm-ID: 465992 [Multi-domain]  Cd Length: 215  Bit Score: 51.87  E-value: 5.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1197 PLVGISVGPtGQVWTVARNGMVFFRYgisrqnpcGDAWQQVEAPAgvtfKAISVGRAGIWALDNQQRLAVRKEISrtfpe 1276
Cdd:pfam19193    1 SLKQIDAGQ-GQVWGVDSAGNVYYLT--------GSSWVRVPGRL----KHVSVGPAGVWGVNSNNKIYKYVGGS----- 62

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795  1277 gshWQFLPNAanvpphtdqhcgFRSVSVGSE--VWAISLNGIICRRCGITKENPAGVGWN 1334
Cdd:pfam19193   63 ---WVPVDGS------------LKQVDAGGDgqVWGVNSADDIYCLNGDDASSYAGLPWT 107
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 256-282 5.28e-06

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.


Pssm-ID: 461921 [Multi-domain]  Cd Length: 30  Bit Score: 44.33  E-value: 5.28e-06
                           10        20
                   ....*....|....*....|....*..
gi 195591795   256 LVWAVLYNGRVIVRTGVTRDNLVGDSW 282
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSW 27
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 1165-1192 5.71e-06

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.


Pssm-ID: 461921 [Multi-domain]  Cd Length: 30  Bit Score: 43.94  E-value: 5.71e-06
                           10        20
                   ....*....|....*....|....*...
gi 195591795  1165 WAIASNGDVLIRHGVCSLNPRGDAWEHI 1192
Cdd:pfam06462    3 WAVTSDGRVYFRTGVTPSNPTGTSWEHV 30
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 210-238 1.16e-05

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.


Pssm-ID: 461921 [Multi-domain]  Cd Length: 30  Bit Score: 43.17  E-value: 1.16e-05
                           10        20
                   ....*....|....*....|....*....
gi 195591795   210 VWAITAHGRAMFRTGVSKTAPEGLRWTAV 238
Cdd:pfam06462    2 VWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 966-1000 2.96e-05

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


Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 42.10  E-value: 2.96e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 195591795    966 MHWRQMGGHIKRIFNSGVDVVWGISCDNTGWVYNG 1000
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 1308-1333 3.37e-05

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.


Pssm-ID: 461921 [Multi-domain]  Cd Length: 30  Bit Score: 42.02  E-value: 3.37e-05
                           10        20
                   ....*....|....*....|....*.
gi 195591795  1308 VWAISLNGIICRRCGITKENPAGVGW 1333
Cdd:pfam06462    2 VWAVTSDGRVYFRTGVTPSNPTGTSW 27
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 1187-1223 1.38e-04

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


Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 40.17  E-value: 1.38e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 195591795   1187 DAWEHItsDQPLVGISVGPTGQVWTVARNGMVFFRYG 1223
Cdd:smart00706    1 GSWTQV--PGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 234-271 2.33e-04

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


Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 39.79  E-value: 2.33e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 195591795    234 RWTAVPtptgSELSQISVGPTGLVWAVLYNGRVIVRTG 271
Cdd:smart00706    2 SWTQVP----GELVQVSVGPSDTVWAVNSDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 280-320 1.13e-03

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


Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 37.86  E-value: 1.13e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 195591795    280 DSWLDVktpvaasSLRIVHVSVGT-DAVWCVTNDHHAWFRRG 320
Cdd:smart00706    1 GSWTQV-------PGELVQVSVGPsDTVWAVNSDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 338-371 1.21e-03

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


Pssm-ID: 214782 [Multi-domain]  Cd Length: 35  Bit Score: 37.48  E-value: 1.21e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 195591795    338 WVEMVGNISMVSVAANDQVFAVGaADRCLYHRSG 371
Cdd:smart00706    3 WTQVPGELVQVSVGPSDTVWAVN-SDGNIYRRTG 35
Pex24p pfam06398
Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, ...
 72-160 1.81e-03

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.


Pssm-ID: 399414 [Multi-domain]  Cd Length: 369  Bit Score: 42.41  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195591795    72 YENER-WLPIEGFSKTLLPTDRYRYSSADG-------SVERGVDKIRLPSMaWQWDG--DWHLDLELDG----------Q 131
Cdd:pfam06398  257 FENQRrWLLGIGWTSSLLSYERYDWTDEYRialneapPGVDHLEDFEPPEG-WRWVDnsKWRLDLTPDGwveerflttvN 335

                           90       100
                   ....*....|....*....|....*....
gi 195591795   132 PLPEDGWMYALDFPATYSAKKSWNSYVRR 160
Cdd:pfam06398  336 PDEDEGWVYDDNTWKEPSTEDGFSKYTRR 364
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 1255-1281 5.97e-03

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.


Pssm-ID: 461921 [Multi-domain]  Cd Length: 30  Bit Score: 35.47  E-value: 5.97e-03
                           10        20
                   ....*....|....*....|....*..
gi 195591795  1255 IWALDNQQRLAVRKEISRTFPEGSHWQ 1281
Cdd:pfam06462    2 VWAVTSDGRVYFRTGVTPSNPTGTSWE 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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