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Conserved domains on  [gi|193898752|gb|EDV97618|]
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GH16968 [Drosophila grimshawi]

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 1.08e-34

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: 128.91  E-value: 1.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   821 YNGMPCGSELEISGCVYDDADQIRFDLQCHskikalphrVEKYRVIAMHINPRFNERTTVLNSMMDSEWLEEIRNDRMVF 900
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG---------VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPF 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193898752   901 APGATFTVKIKALEHHYQIVVNHALYADYKYRVDPAAVTCLYVSGRVKLFSVV 953
Cdd:pfam00337   72 QPGQPFELTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Tectonin super family cl41172
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 210-396 3.16e-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: 85.00  E-value: 3.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   210 VWAITAHGRAMFRTG------------VTANAP---------EGLRWTAIS-TPTGSELSQISVGPTGLVWAVLYNGRVI 267
Cdd:pfam19193   12 VWGVDSAGNVYYLTGsswvrvpgrlkhVSVGPAgvwgvnsnnKIYKYVGGSwVPVDGSLKQVDAGGDGQVWGVNSADDIY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   268 VRTGITRDNLSGESWLDVkspvatssqsdtPRGLRilQISVGTDAVWCITNDHHAWFRRGIKGDAAGisedaaiGRGWVE 347
Cdd:pfam19193   92 CLNGDDASSYAGLPWTQV------------DGSLK--YYSCGPGGCWGVNSNDDIYYRRYVGPSTCG-------GTGWTQ 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 193898752   348 MVGNLSMISVAPNDQVFAIGAADrAIYYRSGVSAADPTGKKWLKIQCSM 396
Cdd:pfam19193  151 VPGKLKMIEVGSDGSVFGVNSNG-NVYQRTGISSSNPTGTGWTQIPGSL 198
Tectonin super family cl41172
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1164-1332 3.30e-14

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: 73.06  E-value: 3.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  1164 WAIASNGDVLIRhgvstlnpRGDNWEHIvsDQPLIGISVGPMGQVWAVARNGMIFYRYGISKQNPCGDAWQQVEaptgVT 1243
Cdd:pfam19193   47 WGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVD----GS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  1244 FKAVNVGRAGIWALDNQLRLAVRKEVTHTFPEGSHWQFLPNAanvpphtethcgFRAVSVGK--EVWAISLNGVICRRCG 1321
Cdd:pfam19193  113 LKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGK------------LKMIEVGSdgSVFGVNSNGNVYQRTG 180

                          170
                   ....*....|.
gi 193898752  1322 ITNENPAGAGW 1332
Cdd:pfam19193  181 ISSSNPTGTGW 191
DysFC smart00694
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1092-1125 2.17e-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: 59.53  E-value: 2.17e-11
                            10        20        30
                    ....*....|....*....|....*....|....
gi 193898752   1092 GWQYAIDFPATYHAHKKLTDCVRRRRWMKKCRLT 1125
Cdd:smart00694    1 GWQYSDNFWANYHKTEKMTDFVRRRRWVRRRRHK 34
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 64-125 6.85e-11

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: 59.08  E-value: 6.85e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193898752     64 PIRVKEESYENE-RWLPIeGFSKTLLPTdRYKYSNVDGSVERSVDKIRLPSMAWQWDGD-WHLD 125
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 644-764 7.75e-11

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: 60.95  E-value: 7.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  644 VEMTSWIKSADARYQH--PAGEYDDCSIELEwvSGNGSDTDSDSGTFSVLSSDGAATKIQFALSDITCVQCCSEPGA-PR 720
Cdd:cd13300     1 VERSSWVKTGALQWWSdwKPHKWADCRVALE--QGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGEkPS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 193898752  721 LAIHAVHLPINCSPVKLQFTSDSEMEDWLSHLSSVCSQINMLMG 764
Cdd:cd13300    79 FAIYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1025-1081 6.40e-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: 50.60  E-value: 6.40e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 193898752   1025 YYVYENQ-RWNPIsGFTAKSLPTdRHMWSDASGRQKRSKEHTKLLSTHCEWISD-WAID 1081
Cdd:smart00693    6 EEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 966-1000 4.45e-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: 39.02  E-value: 4.45e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 193898752    966 MHWRQMGGHVKRVYSSGVDVVWGISCDNTAWAYNG 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 1.08e-34

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: 128.91  E-value: 1.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   821 YNGMPCGSELEISGCVYDDADQIRFDLQCHskikalphrVEKYRVIAMHINPRFNERTTVLNSMMDSEWLEEIRNDRMVF 900
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG---------VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPF 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193898752   901 APGATFTVKIKALEHHYQIVVNHALYADYKYRVDPAAVTCLYVSGRVKLFSVV 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 2.06e-33

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: 125.40  E-value: 2.06e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752    822 NGMPCGSELEISGCVYDDADQIRFDLQCHSkikalphrvekYRVIAMHINPRFNERTTVLNSMMDSEWLEEIRNDRMVFA 901
Cdd:smart00908    2 GGLSPGSSITIRGIVLPDAKRFSINLQCGP-----------NADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQ 70

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 193898752    902 PGATFTVKIKALEHHYQIVVNHALYADYKYRVDPAAVTCLYVSGRVKLFSV 952
Cdd:smart00908   71 PGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 815-953 5.13e-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: 5.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  815 PYYNTLYNGMPCGSELEISGCVYDDADQIRFDLQCHSkikalphrvekyRVIAMHINPRFNERTTVLNSMMDSEWLEEIR 894
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGS------------SDIALHFNPRFDENVIVRNSFLNGNWGPEER 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 193898752  895 NDRMVFAPGATFTVKIKALEHHYQIVVNHALYADYKYRVDPAAVTCLYVSGRVKLFSVV 953
Cdd:cd00070    69 SGGFPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 210-396 3.16e-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: 85.00  E-value: 3.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   210 VWAITAHGRAMFRTG------------VTANAP---------EGLRWTAIS-TPTGSELSQISVGPTGLVWAVLYNGRVI 267
Cdd:pfam19193   12 VWGVDSAGNVYYLTGsswvrvpgrlkhVSVGPAgvwgvnsnnKIYKYVGGSwVPVDGSLKQVDAGGDGQVWGVNSADDIY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   268 VRTGITRDNLSGESWLDVkspvatssqsdtPRGLRilQISVGTDAVWCITNDHHAWFRRGIKGDAAGisedaaiGRGWVE 347
Cdd:pfam19193   92 CLNGDDASSYAGLPWTQV------------DGSLK--YYSCGPGGCWGVNSNDDIYYRRYVGPSTCG-------GTGWTQ 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 193898752   348 MVGNLSMISVAPNDQVFAIGAADrAIYYRSGVSAADPTGKKWLKIQCSM 396
Cdd:pfam19193  151 VPGKLKMIEVGSDGSVFGVNSNG-NVYQRTGISSSNPTGTGWTQIPGSL 198
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1164-1332 3.30e-14

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: 73.06  E-value: 3.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  1164 WAIASNGDVLIRhgvstlnpRGDNWEHIvsDQPLIGISVGPMGQVWAVARNGMIFYRYGISKQNPCGDAWQQVEaptgVT 1243
Cdd:pfam19193   47 WGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVD----GS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  1244 FKAVNVGRAGIWALDNQLRLAVRKEVTHTFPEGSHWQFLPNAanvpphtethcgFRAVSVGK--EVWAISLNGVICRRCG 1321
Cdd:pfam19193  113 LKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGK------------LKMIEVGSdgSVFGVNSNGNVYQRTG 180

                          170
                   ....*....|.
gi 193898752  1322 ITNENPAGAGW 1332
Cdd:pfam19193  181 ISSSNPTGTGW 191
DysFC smart00694
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1092-1125 2.17e-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: 59.53  E-value: 2.17e-11
                            10        20        30
                    ....*....|....*....|....*....|....
gi 193898752   1092 GWQYAIDFPATYHAHKKLTDCVRRRRWMKKCRLT 1125
Cdd:smart00694    1 GWQYSDNFWANYHKTEKMTDFVRRRRWVRRRRHK 34
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 64-125 6.85e-11

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: 59.08  E-value: 6.85e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193898752     64 PIRVKEESYENE-RWLPIeGFSKTLLPTdRYKYSNVDGSVERSVDKIRLPSMAWQWDGD-WHLD 125
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
PH1_TECPR1 cd13300
Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; ...
 644-764 7.75e-11

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: 60.95  E-value: 7.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  644 VEMTSWIKSADARYQH--PAGEYDDCSIELEwvSGNGSDTDSDSGTFSVLSSDGAATKIQFALSDITCVQCCSEPGA-PR 720
Cdd:cd13300     1 VERSSWVKTGALQWWSdwKPHKWADCRVALE--QGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGEkPS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 193898752  721 LAIHAVHLPINCSPVKLQFTSDSEMEDWLSHLSSVCSQINMLMG 764
Cdd:cd13300    79 FAIYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1025-1081 6.40e-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: 50.60  E-value: 6.40e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 193898752   1025 YYVYENQ-RWNPIsGFTAKSLPTdRHMWSDASGRQKRSKEHTKLLSTHCEWISD-WAID 1081
Cdd:smart00693    6 EEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 1188-1222 1.39e-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: 1.39e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 193898752   1188 WEHIvsDQPLIGISVGPMGQVWAVARNGMIFYRYG 1222
Cdd:smart00706    3 WTQV--PGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 345-378 2.62e-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: 39.40  E-value: 2.62e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 193898752    345 WVEMVGNLSMISVAPNDQVFAIGaADRAIYYRSG 378
Cdd:smart00706    3 WTQVPGELVQVSVGPSDTVWAVN-SDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 966-1000 4.45e-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: 39.02  E-value: 4.45e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 193898752    966 MHWRQMGGHVKRVYSSGVDVVWGISCDNTAWAYNG 1000
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
Pex24p pfam06398
Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, ...
 64-160 2.23e-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: 42.02  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752    64 PIRVKEESYENER-WLPIEGFSKTLLPTDRY-------KYSNVDGSVERSVDKIRLPSMaWQWDG--DWHLDLELDG--- 130
Cdd:pfam06398  249 PVRFTVEIFENQRrWLLGIGWTSSLLSYERYdwtdeyrIALNEAPPGVDHLEDFEPPEG-WRWVDnsKWRLDLTPDGwve 327

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 193898752   131 -------QQLPEDGWMYALDFPASYSAKKSWNSYVRR 160
Cdd:pfam06398  328 erflttvNPDEDEGWVYDDNTWKEPSTEDGFSKYTRR 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 1.08e-34

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: 128.91  E-value: 1.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   821 YNGMPCGSELEISGCVYDDADQIRFDLQCHskikalphrVEKYRVIAMHINPRFNERTTVLNSMMDSEWLEEIRNDRMVF 900
Cdd:pfam00337    1 PGGLQPGSSLTIKGIVLPDAQRFSINLQTG---------VGPSDDIALHFNPRFDENVIVRNSRQNGQWGQEEREGGFPF 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 193898752   901 APGATFTVKIKALEHHYQIVVNHALYADYKYRVDPAAVTCLYVSGRVKLFSVV 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 2.06e-33

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: 125.40  E-value: 2.06e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752    822 NGMPCGSELEISGCVYDDADQIRFDLQCHSkikalphrvekYRVIAMHINPRFNERTTVLNSMMDSEWLEEIRNDRMVFA 901
Cdd:smart00908    2 GGLSPGSSITIRGIVLPDAKRFSINLQCGP-----------NADIALHFNPRFDEGTIVRNSKQNGKWGKEERSGGFPFQ 70

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 193898752    902 PGATFTVKIKALEHHYQIVVNHALYADYKYRVDPAAVTCLYVSGRVKLFSV 952
Cdd:smart00908   71 PGQPFELEILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSV 121
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 815-953 5.13e-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: 5.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  815 PYYNTLYNGMPCGSELEISGCVYDDADQIRFDLQCHSkikalphrvekyRVIAMHINPRFNERTTVLNSMMDSEWLEEIR 894
Cdd:cd00070     1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLGTGS------------SDIALHFNPRFDENVIVRNSFLNGNWGPEER 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 193898752  895 NDRMVFAPGATFTVKIKALEHHYQIVVNHALYADYKYRVDPAAVTCLYVSGRVKLFSVV 953
Cdd:cd00070    69 SGGFPFQPGQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 816-954 2.58e-28

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 110.78  E-value: 2.58e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752    816 YYNTLYNGMPCGSELEISGCVYDDADQIRFDLQCHSKikalphrvekyrVIAMHINPRFNERTTVLNSMMDSEWLEEIRN 895
Cdd:smart00276    1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLLTGGD------------DIALHFNPRFNENKIVCNSKLNGSWGSEERE 68

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 193898752    896 DRMVFAPGATFTVKIKALEHHYQIVVNHALYADYKYRVDPAAVTCLYVSGRVKLFSVVY 954
Cdd:smart00276   69 GGFPFQPGQPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 210-396 3.16e-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: 85.00  E-value: 3.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   210 VWAITAHGRAMFRTG------------VTANAP---------EGLRWTAIS-TPTGSELSQISVGPTGLVWAVLYNGRVI 267
Cdd:pfam19193   12 VWGVDSAGNVYYLTGsswvrvpgrlkhVSVGPAgvwgvnsnnKIYKYVGGSwVPVDGSLKQVDAGGDGQVWGVNSADDIY 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752   268 VRTGITRDNLSGESWLDVkspvatssqsdtPRGLRilQISVGTDAVWCITNDHHAWFRRGIKGDAAGisedaaiGRGWVE 347
Cdd:pfam19193   92 CLNGDDASSYAGLPWTQV------------DGSLK--YYSCGPGGCWGVNSNDDIYYRRYVGPSTCG-------GTGWTQ 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 193898752   348 MVGNLSMISVAPNDQVFAIGAADrAIYYRSGVSAADPTGKKWLKIQCSM 396
Cdd:pfam19193  151 VPGKLKMIEVGSDGSVFGVNSNG-NVYQRTGISSSNPTGTGWTQIPGSL 198
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1164-1332 3.30e-14

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: 73.06  E-value: 3.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  1164 WAIASNGDVLIRhgvstlnpRGDNWEHIvsDQPLIGISVGPMGQVWAVARNGMIFYRYGISKQNPCGDAWQQVEaptgVT 1243
Cdd:pfam19193   47 WGVNSNNKIYKY--------VGGSWVPV--DGSLKQVDAGGDGQVWGVNSADDIYCLNGDDASSYAGLPWTQVD----GS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  1244 FKAVNVGRAGIWALDNQLRLAVRKEVTHTFPEGSHWQFLPNAanvpphtethcgFRAVSVGK--EVWAISLNGVICRRCG 1321
Cdd:pfam19193  113 LKYYSCGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVPGK------------LKMIEVGSdgSVFGVNSNGNVYQRTG 180

                          170
                   ....*....|.
gi 193898752  1322 ITNENPAGAGW 1332
Cdd:pfam19193  181 ISSSNPTGTGW 191
DysFC smart00694
Dysferlin domain, C-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1092-1125 2.17e-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: 59.53  E-value: 2.17e-11
                            10        20        30
                    ....*....|....*....|....*....|....
gi 193898752   1092 GWQYAIDFPATYHAHKKLTDCVRRRRWMKKCRLT 1125
Cdd:smart00694    1 GWQYSDNFWANYHKTEKMTDFVRRRRWVRRRRHK 34
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 64-125 6.85e-11

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: 59.08  E-value: 6.85e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193898752     64 PIRVKEESYENE-RWLPIeGFSKTLLPTdRYKYSNVDGSVERSVDKIRLPSMAWQWDGD-WHLD 125
Cdd:smart00693    1 PIRFTEEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
PH1_TECPR1 cd13300
Tectonin beta-propeller repeat-containing protein 1 Pleckstrin homology (PH) domain, repeat 1; ...
 644-764 7.75e-11

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: 60.95  E-value: 7.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  644 VEMTSWIKSADARYQH--PAGEYDDCSIELEwvSGNGSDTDSDSGTFSVLSSDGAATKIQFALSDITCVQCCSEPGA-PR 720
Cdd:cd13300     1 VERSSWVKTGALQWWSdwKPHKWADCRVALE--QGTGSDGRQDSIFFVYYTYHGEKKYIQFFLSEITCVVPVNNGGEkPS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 193898752  721 LAIHAVHLPINCSPVKLQFTSDSEMEDWLSHLSSVCSQINMLMG 764
Cdd:cd13300    79 FAIYTPKRTKQRWPIRLAANTEQELEDWLSLLSMSCCEVRGIQG 122
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 205-282 1.14e-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: 62.66  E-value: 1.14e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193898752   205 AGTLCVWAITAHGRAMFRTGVTANAPEGLRWTAIStptGSeLSQISVGPTGLVWAVLYNGRVIVRTGITRDNLSGESW 282
Cdd:pfam19193  118 CGPGGCWGVNSNDDIYYRRYVGPSTCGGTGWTQVP---GK-LKMIEVGSDGSVFGVNSNGNVYQRTGISSSNPTGTGW 191
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1164-1242 2.61e-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: 61.89  E-value: 2.61e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193898752  1164 WAIASNGDVLIRHGVSTLNPRGDNWEHIvsDQPLIGISVGPMGQVWAVARNGMIFYRYGISKQNPCGDAWQQVEAPTGV 1242
Cdd:pfam19193  124 WGVNSNDDIYYRRYVGPSTCGGTGWTQV--PGKLKMIEVGSDGSVFGVNSNGNVYQRTGISSSNPTGTGWTQIPGSLSI 200
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 1207-1236 2.91e-08

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: 50.49  E-value: 2.91e-08
                           10        20        30
                   ....*....|....*....|....*....|
gi 193898752  1207 QVWAVARNGMIFYRYGISKQNPCGDAWQQV 1236
Cdd:pfam06462    1 QVWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30
DysFN smart00693
Dysferlin domain, N-terminal region; Domain of unknown function present in yeast peroxisomal ...
 1025-1081 6.40e-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: 50.60  E-value: 6.40e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 193898752   1025 YYVYENQ-RWNPIsGFTAKSLPTdRHMWSDASGRQKRSKEHTKLLSTHCEWISD-WAID 1081
Cdd:smart00693    6 EEMYENQrRWLGG-GWKTTLLPY-RPKFSDASGGKECLPKENLLPPPGWEWEDDnWSLD 62
Tectonin pfam19193
Tectonin domain; This entry represents proteins homologous to tectonin. This protein adopts a ...
 1196-1345 1.75e-06

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: 50.33  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752  1196 PLIGISVGPmGQVWAVARNGMIFYRYgiskqnpcGDAWQQVEAPtgvtFKAVNVGRAGIWALDnqlrlavRKEVTHTFpE 1275
Cdd:pfam19193    1 SLKQIDAGQ-GQVWGVDSAGNVYYLT--------GSSWVRVPGR----LKHVSVGPAGVWGVN-------SNNKIYKY-V 59

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193898752  1276 GSHWQFLPNAanvpphtethcgFRAVSVG--KEVWAISLNGVICRRCGITNENPAGAGWNlGISGQWKHLSV 1345
Cdd:pfam19193   60 GGSWVPVDGS------------LKQVDAGgdGQVWGVNSADDIYCLNGDDASSYAGLPWT-QVDGSLKYYSC 118
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 1164-1191 2.82e-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: 45.10  E-value: 2.82e-06
                           10        20
                   ....*....|....*....|....*...
gi 193898752  1164 WAIASNGDVLIRHGVSTLNPRGDNWEHI 1191
Cdd:pfam06462    3 WAVTSDGRVYFRTGVTPSNPTGTSWEHV 30
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 256-282 3.23e-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: 44.71  E-value: 3.23e-06
                           10        20
                   ....*....|....*....|....*..
gi 193898752   256 LVWAVLYNGRVIVRTGITRDNLSGESW 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 ...
 210-238 5.65e-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: 5.65e-06
                           10        20
                   ....*....|....*....|....*....
gi 193898752   210 VWAITAHGRAMFRTGVTANAPEGLRWTAI 238
Cdd:pfam06462    2 VWAVTSDGRVYFRTGVTPSNPTGTSWEHV 30
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 1307-1332 1.34e-04

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: 40.09  E-value: 1.34e-04
                           10        20
                   ....*....|....*....|....*.
gi 193898752  1307 VWAISLNGVICRRCGITNENPAGAGW 1332
Cdd:pfam06462    2 VWAVTSDGRVYFRTGVTPSNPTGTSW 27
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 1188-1222 1.39e-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: 1.39e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 193898752   1188 WEHIvsDQPLIGISVGPMGQVWAVARNGMIFYRYG 1222
Cdd:smart00706    3 WTQV--PGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 345-378 2.62e-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: 39.40  E-value: 2.62e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 193898752    345 WVEMVGNLSMISVAPNDQVFAIGaADRAIYYRSG 378
Cdd:smart00706    3 WTQVPGELVQVSVGPSDTVWAVN-SDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 234-271 3.12e-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: 39.40  E-value: 3.12e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 193898752    234 RWTAIStptgSELSQISVGPTGLVWAVLYNGRVIVRTG 271
Cdd:smart00706    2 SWTQVP----GELVQVSVGPSDTVWAVNSDGNIYRRTG 35
TECPR smart00706
Beta propeller repeats in Physarum polycephalum tectonins, Limulus lectin L-6 and animal ...
 966-1000 4.45e-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: 39.02  E-value: 4.45e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 193898752    966 MHWRQMGGHVKRVYSSGVDVVWGISCDNTAWAYNG 1000
Cdd:smart00706    1 GSWTQVPGELVQVSVGPSDTVWAVNSDGNIYRRTG 35
Pex24p pfam06398
Integral peroxisomal membrane peroxin; Peroxisomes play diverse roles in the cell, ...
 64-160 2.23e-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: 42.02  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193898752    64 PIRVKEESYENER-WLPIEGFSKTLLPTDRY-------KYSNVDGSVERSVDKIRLPSMaWQWDG--DWHLDLELDG--- 130
Cdd:pfam06398  249 PVRFTVEIFENQRrWLLGIGWTSSLLSYERYdwtdeyrIALNEAPPGVDHLEDFEPPEG-WRWVDnsKWRLDLTPDGwve 327

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 193898752   131 -------QQLPEDGWMYALDFPASYSAKKSWNSYVRR 160
Cdd:pfam06398  328 erflttvNPDEDEGWVYDDNTWKEPSTEDGFSKYTRR 364
Hyd_WA pfam06462
Propeller; Tectonins I and II are two dominant proteins in the nuclei and nuclear matrix from ...
 1254-1280 8.92e-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: 35.08  E-value: 8.92e-03
                           10        20
                   ....*....|....*....|....*..
gi 193898752  1254 IWALDNQLRLAVRKEVTHTFPEGSHWQ 1280
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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