PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454 1027 PKGLIEIKVPKAPGEKLGISIRGGNKGHPGNPLDRGDEGIFISKVNEVGAAARDGRLRVGQRILEVNSQSMLGSRHREAV 1106
Cdd:cd06701      1 PPGLQELTIVKEPGEKLGISIRGGAKGHAGNPLDPTDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAV 80

                           90
                   ....*....|....*...
gi 1752404454 1107 MALRGCGDMLGILVCDGF 1124
Cdd:cd06701     81 RILRSVGDTLTLLVCDGY 98

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  809 EKITLKLVKDSNGLGFSIAGGKGSPPFKGTDDSIFISRISEGGAADRTGALSVGDKVLKINNVEMAEARHETAVALLTKS 888
Cdd:cd06703      1 ETITTTLIRDGKGLGFSIAGGKGSTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSS 80

                           90
                   ....*....|..
gi 1752404454  889 KE-IDLVIMRET 899
Cdd:cd06703     81 SPtITLVVEREA 92

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  935 EEVFLKRTRGPLGLSIVGGIDHSSHPFGGDEPGIFISKIVPNGSAASTNLRVGDRLLVVNNKEMKGATHQFAVNTLLSNS 1014
Cdd:cd06702      1 EEIHLVKAGGPLGLSIVGGSDHSSHPFGVDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPG 80

                   ....*....
gi 1752404454 1015 EHIQLVVRH 1023
Cdd:cd06702     81 QEIKLLVRH 89

PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454 1027 PKGLIEIKVPKAPGEKLGISIRGGNKGHPGNPLDRGDEGIFISKVNEVGAAARDGRLRVGQRILEVNSQSMLGSRHREAV 1106
Cdd:cd06701      1 PPGLQELTIVKEPGEKLGISIRGGAKGHAGNPLDPTDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAV 80

                           90
                   ....*....|....*...
gi 1752404454 1107 MALRGCGDMLGILVCDGF 1124
Cdd:cd06701     81 RILRSVGDTLTLLVCDGY 98

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  809 EKITLKLVKDSNGLGFSIAGGKGSPPFKGTDDSIFISRISEGGAADRTGALSVGDKVLKINNVEMAEARHETAVALLTKS 888
Cdd:cd06703      1 ETITTTLIRDGKGLGFSIAGGKGSTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSS 80

                           90
                   ....*....|..
gi 1752404454  889 KE-IDLVIMRET 899
Cdd:cd06703     81 SPtITLVVEREA 92

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  935 EEVFLKRTRGPLGLSIVGGIDHSSHPFGGDEPGIFISKIVPNGSAASTNLRVGDRLLVVNNKEMKGATHQFAVNTLLSNS 1014
Cdd:cd06702      1 EEIHLVKAGGPLGLSIVGGSDHSSHPFGVDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPG 80

                   ....*....
gi 1752404454 1015 EHIQLVVRH 1023
Cdd:cd06702     81 QEIKLLVRH 89

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454   657 EKMVINFSRDGSGLGISIAGGKGstpykgNDEGIFISRVVEGGVAAKNGLTLGDKILAVNSANLENADHLEAVEALKAAG 736
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKD------EGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAG 74

                    ....*....
gi 1752404454   737 NNIHMVVTR 745
Cdd:smart00228   75 GKVTLTVLR 83

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454   809 EKITLKLVKDSNGLGFSIAGGKGSPPFkgtddsIFISRISEGGAADRTGaLSVGDKVLKINNVEMAEARHETAVALLTKS 888
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEGGG------VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKA 73

                            90
                    ....*....|
gi 1752404454   889 KE-IDLVIMR 897
Cdd:smart00228   74 GGkVTLTVLR 83

PDZ domain; PDZ domains are found in diverse signaling proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  812 TLKLVKDSNG-LGFSIAGGKGSPpfkgtDDSIFISRISEGGAADRTGaLSVGDKVLKINNVEMAEARHETAVALLTKSK- 889
Cdd:pfam00595    1 QVTLEKDGRGgLGFSLKGGSDQG-----DPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGg 74

                   ....*..
gi 1752404454  890 EIDLVIM 896
Cdd:pfam00595   75 KVTLTIL 81

PDZ domain; PDZ domains are found in diverse signaling proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  940 KRTRGPLGLSIVGGIDHSshpfggdEPGIFISKIVPNGSAASTNLRVGDRLLVVNNKEMKGATHQFAVNTLLSNSEHIQL 1019
Cdd:pfam00595    6 KDGRGGLGFSLKGGSDQG-------DPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTL 78

                   ...
gi 1752404454 1020 VVR 1022
Cdd:pfam00595   79 TIL 81

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  128 LHDLRHLTLNDVSLESLPqDIGSMSNLIAMELRENLLKVLPDsLSFLVKLETLDLGSNELEELpETLGALPNLSELWLDC 207
Cdd:cd21340      1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  208 NQLTIlppeIGNLGNLTCLdvSENNL--QCLPDEigglQSLTDLTLSQNCLeklpegigkLKDLSILKIDQNRLITLTPa 285
Cdd:cd21340     78 NRISV----VEGLENLTNL--EELHIenQRLPPG----EKLTFDPRSLAAL---------SNSLRVLNISGNNIDSLEP- 137

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752404454  286 IGSCENMQELILTENLLQEIpptigslrhlnnfnvdrNRLTQLpaqIGKCTRLGVLSLRDNRLLRLP 352
Cdd:cd21340    138 LAPLRNLEQLDASNNQISDL-----------------EELLDL---LSSWPSLRELDLTGNPVCKKP 184

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  942 TRGPLGLSIVG---------GIDHSShpfggdepGIFISKIVPNGSAASTNLRVGDRLLVVNNKEMKGATH-QFAVNTLL 1011
Cdd:TIGR02037  232 KRGWLGVTIQEvtsdlakslGLEKQR--------GALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADlRRAIGTLK 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454 1012 SNSEHIQLVVRHDPPPKglIEIKVPKAPGEKLgisirGGNKGHPGN-------------PLDRGDEGIFISKVNEVGAAA 1078
Cdd:TIGR02037  304 PGKKVTLGILRKGKEKT--ITVTLGASPEEQA-----SSSNPFLGLtvanlspeirkelRLKGDVKGVVVTKVVSGSPAA 376

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1752404454 1079 RDGrLRVGQRILEVNSQSMLGSRHREAVMALRGCGDMLGILV 1120
Cdd:TIGR02037  377 RAG-LQPGDVILSVNQQPVSSVAELRKVLARAKKGGRVALLI 417

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752404454  838 TDDSIFISRISEGGAADRTGaLSVGDKVLKINNVEMAEARHETAVALL--TKSKEIDLVIMR----ETMEIE 903
Cdd:COG0793     69 EDGKVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLLrgKAGTKVTLTIKRpgegEPITVT 139

PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454 1027 PKGLIEIKVPKAPGEKLGISIRGGNKGHPGNPLDRGDEGIFISKVNEVGAAARDGRLRVGQRILEVNSQSMLGSRHREAV 1106
Cdd:cd06701      1 PPGLQELTIVKEPGEKLGISIRGGAKGHAGNPLDPTDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAV 80

                           90
                   ....*....|....*...
gi 1752404454 1107 MALRGCGDMLGILVCDGF 1124
Cdd:cd06701     81 RILRSVGDTLTLLVCDGY 98

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  809 EKITLKLVKDSNGLGFSIAGGKGSPPFKGTDDSIFISRISEGGAADRTGALSVGDKVLKINNVEMAEARHETAVALLTKS 888
Cdd:cd06703      1 ETITTTLIRDGKGLGFSIAGGKGSTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSS 80

                           90
                   ....*....|..
gi 1752404454  889 KE-IDLVIMRET 899
Cdd:cd06703     81 SPtITLVVEREA 92

Leucine-rich repeat (LRR) protein [Transcription];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454   59 LTNLRILGLSDNELERLPAEIGNFMNLLELDVSRNDIMEIPDNIKFCKALTIVDFSGNPLSRLPPGFTQLHDLRHLTLND 138
Cdd:COG4886      3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  139 VSLESLPQDIGSMSNLIAMELRENllkvlpDSLSFLVKLETLDLGSNELEELPETLGALPNLSELWLDCNQLTILPPEIG 218
Cdd:COG4886     83 SLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  219 NLGNLTCLDVSENNLQCLPDEIGGLQSLTDLTLSQNCLEKLPEGIGKLKdlsilkidqnrlitltpaigsceNMQELILT 298
Cdd:COG4886    157 NLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLT-----------------------NLEELDLS 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  299 ENLLQEIPPTIGSLRHLNNFNVDRNRLTQLPaQIGKCTRLGVLSLRDNRLLRLPPeLGQLRELHVLDVCGNRLDWLpiQL 378
Cdd:COG4886    214 GNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDL--KL 289

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752404454  379 ANCNLKALWLSENQSQPMLNFQTEEIGPQRLKVLTCFLLPQKGPSEGIDYDNFQDNLNIGALDTDAVNFEG 449
Cdd:COG4886    290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLS 360

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  935 EEVFLKRTRGPLGLSIVGGIDHSSHPFGGDEPGIFISKIVPNGSAASTNLRVGDRLLVVNNKEMKGATHQFAVNTLLSNS 1014
Cdd:cd06702      1 EEIHLVKAGGPLGLSIVGGSDHSSHPFGVDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPG 80

                   ....*....
gi 1752404454 1015 EHIQLVVRH 1023
Cdd:cd06702     81 QEIKLLVRH 89

PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  811 ITLKLVKDSNGLGFSIAGGKGSPPFKGTDDSIFISRISEGGAADRTGaLSVGDKVLKINNVEMAEARHETAVALLTKS-K 889
Cdd:cd06704      1 LTITIERQTGGLGISIAGGKGSTPYKGDDEGIFISRVTEGGPAAKAG-VRVGDKLLEVNGVDLVDADHHEAVEALKNSgN 79

                   ....*...
gi 1752404454  890 EIDLVIMR 897
Cdd:cd06704     80 TVTMVVLR 87

leucine-rich repeat receptor-like protein kinase; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454   56 FFRLTNLRILGLSDNELErlpaeignfmnlleldvsrndiMEIPDNI-KFCKALTIVDFSGNPLS-RLPPGFTQLHDLRH 133
Cdd:PLN00113    89 IFRLPYIQTINLSNNQLS----------------------GPIPDDIfTTSSSLRYLNLSNNNFTgSIPRGSIPNLETLD 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  134 LTLNDVSLEsLPQDIGSMSNLIAMELREN-LLKVLPDSLSFLVKLETLDLGSNELE-ELPETLGALPNLSELWLDCNQLT 211
Cdd:PLN00113   147 LSNNMLSGE-IPNDIGSFSSLKVLDLGGNvLVGKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLS 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  212 -ILPPEIGNLGNLTCLDVSENNLQ-CLPDEIGGLQSLTDLTLSQNCLE-KLPEGIGKLKDLSILKIDQNRLITLTPA-IG 287
Cdd:PLN00113   226 gEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSGEIPElVI 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  288 SCENMQEL-ILTENLLQEIPPTIGSLRHLNNFNVDRNRLT-QLPAQIGKCTRLGVLSLRDNRLL-RLPPELGQLRELHVL 364
Cdd:PLN00113   306 QLQNLEILhLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKL 385

                          330       340
                   ....*....|....*....|....*....
gi 1752404454  365 DVCGNRLD-WLPIQLANCN-LKALWLSEN 391
Cdd:PLN00113   386 ILFSNSLEgEIPKSLGACRsLRRVRLQDN 414

leucine-rich repeat receptor-like protein kinase; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454   14 HVEYIDKRHCNLPG-VPDDVYRYARTLEELRLDANQIR-DLPRHFfrLTNLRILGLSDNELE-RLPAEIGNFMNLLELDV 90
Cdd:PLN00113    94 YIQTINLSNNQLSGpIPDDIFTTSSSLRYLNLSNNNFTgSIPRGS--IPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDL 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454   91 SRNDIM-------------------------------------------------EIPDNIKFCKALTIVDFSGNPLS-R 120
Cdd:PLN00113   172 GGNVLVgkipnsltnltslefltlasnqlvgqiprelgqmkslkwiylgynnlsgEIPYEIGGLTSLNHLDLVYNNLTgP 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  121 LPPGFTQLHDLRHLTLNDVSLE-SLPQDIGSMSNLIAMELRENLLK-VLPDSLSFLVKLETLDLGSNELE-ELPETLGAL 197
Cdd:PLN00113   252 IPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSL 331

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  198 PNLSELWLDCNQLT-ILPPEIGNLGNLTCLDVSENNLQC-LPDEIGGLQSLTDLTLSQNCLE------------------ 257
Cdd:PLN00113   332 PRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTGeIPEGLCSSGNLFKLILFSNSLEgeipkslgacrslrrvrl 411

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752404454  258 -------KLPEGIGKLK-----DLS-------------------ILKIDQNRLITLTPAIGSCENMQELILTENLLQE-I 305
Cdd:PLN00113   412 qdnsfsgELPSEFTKLPlvyflDISnnnlqgrinsrkwdmpslqMLSLARNKFFGGLPDSFGSKRLENLDLSRNQFSGaV 491

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752404454  306 PPTIGSLRHLNNFNVDRNRLT-QLPAQIGKCTRLGVLSLRDNRLL-RLPPELGQLRELHVLDVCGNRL 371
Cdd:PLN00113   492 PRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQL 559