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 62472958 1331 PPGFQEVLLSKAEGERLGMHIKGGLNGQRGNPADPSDEGVFVSKINSVGAARRDGRLKVGMRLLEVNGHSLLGASHQDAV 1410
Cdd:cd06701    1 PPGLQELTIVKEPGEKLGISIRGGAKGHAGNPLDPTDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAV 80

                         90
                 ....*....|....*...
gi 62472958 1411 NVLRNAGNEIQLVVCKGY 1428
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 62472958  927 QLHTTLIRDqiGQGLGFSIAGGKGSPPFKDDCDGIFISRITEGGLAYRDGKIMVGDRVMAINGNDMTEAHHDAAVACLTE 1006
Cdd:cd06703    2 TITTTLIRD--GKGLGFSIAGGKGSTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTS 79

                         90
                 ....*....|...
gi 62472958 1007 PQRFVRLVLQREY 1019
Cdd:cd06703   80 SSPTITLVVEREA 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 62472958 1238 EEVVLPKNQGSLGFSIIGGTDHSCVPFGTREPGIFISHIVPGGIASKCGkLRMGDRILKVNEADVSKATHQDAVLELLKP 1317
Cdd:cd06702    1 EEIHLVKAGGPLGLSIVGGSDHSSHPFGVDEPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVSALLSP 79

                         90
                 ....*....|
gi 62472958 1318 GDEIKLTIQH 1327
Cdd:cd06702   80 GQEIKLLVRH 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 62472958 1331 PPGFQEVLLSKAEGERLGMHIKGGLNGQRGNPADPSDEGVFVSKINSVGAARRDGRLKVGMRLLEVNGHSLLGASHQDAV 1410
Cdd:cd06701    1 PPGLQELTIVKEPGEKLGISIRGGAKGHAGNPLDPTDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAV 80

                         90
                 ....*....|....*...
gi 62472958 1411 NVLRNAGNEIQLVVCKGY 1428
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 62472958  927 QLHTTLIRDqiGQGLGFSIAGGKGSPPFKDDCDGIFISRITEGGLAYRDGKIMVGDRVMAINGNDMTEAHHDAAVACLTE 1006
Cdd:cd06703    2 TITTTLIRD--GKGLGFSIAGGKGSTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTS 79

                         90
                 ....*....|...
gi 62472958 1007 PQRFVRLVLQREY 1019
Cdd:cd06703   80 SSPTITLVVEREA 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 62472958 1238 EEVVLPKNQGSLGFSIIGGTDHSCVPFGTREPGIFISHIVPGGIASKCGkLRMGDRILKVNEADVSKATHQDAVLELLKP 1317
Cdd:cd06702    1 EEIHLVKAGGPLGLSIVGGSDHSSHPFGVDEPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVSALLSP 79

                         90
                 ....*....|
gi 62472958 1318 GDEIKLTIQH 1327
Cdd:cd06702   80 GQEIKLLVRH 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 62472958     728 EQYEIHIERTAAGLGLSIAGGKGstpfkgDDDGIFISRVTEAGPADLAGLKVGDKVIKVNGIVVVDADHYQAVQVLKACG 807
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKD------EGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAG 74

                    ....*....
gi 62472958     808 AVLVLVVQR 816
Cdd:smart00228   75 GKVTLTVLR 83

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 62472958  128 LKNLTVLGLNDMSLTTLPaDFGSLTQLESLELRENLLKHLpETISQLTKLKRLDLGDNEIEDLPPyLGYLPGLHELWLDH 207
Cdd:cd21340    1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  208 NQLQRLppE-LGLLTKLTYLDVSENRL---EEL---PNEISGL-VSLTDLDLAQNLLEALpDGIAKLSRLTILKLDQNRL 279
Cdd:cd21340   78 NRISVV--EgLENLTNLEELHIENQRLppgEKLtfdPRSLAALsNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQI 154

                        170       180
                 ....*....|....*....|....
gi 62472958  280 QRLND---TLGNCENMQELILTEN 300
Cdd:cd21340  155 SDLEElldLLSSWPSLRELDLTGN 178

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958    731 EIHIER-TAAGLGLSIAGGKGstpfkGDDDGIFISRVTEAGPADLAGLKVGDKVIKVNGIVVVDADHYQAVQVLKACGAV 809
Cdd:pfam00595    1 QVTLEKdGRGGLGFSLKGGSD-----QGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                   ....*.
gi 62472958    810 LVLVVQ 815
Cdd:pfam00595   76 VTLTIL 81

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 62472958    1335 QEVLLSKaEGERLGMHIKGGlngqrgnpaDPSDEGVFVSKINSVGAARRDGrLKVGMRLLEVNGHSLLGASHQDAVNVLR 1414
Cdd:smart00228    3 RLVELEK-GGGGLGFSLVGG---------KDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLK 71

                            90
                    ....*....|...
gi 62472958    1415 NAGNEIQLVVCKG 1427
Cdd:smart00228   72 KAGGKVTLTVLRG 84

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958    930 TTLIRDQIGQGLGFSIAGGKGsppfkDDCDGIFISRITEGGLAYRDGkIMVGDRVMAINGNDMTEAHHDAAVACLTEPQR 1009
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSD-----QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGG 74

                   ....*..
gi 62472958   1010 FVRLVLQ 1016
Cdd:pfam00595   75 KVTLTIL 81

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  727 LEQYEIHIERTAAGLGLSIAGgkgstpfkgDDDGIFISRVTEAGPADLAGLKVGDKVIKVNGIVVVDADHYQAVQVLK-A 805
Cdd:COG0793   48 YEDFQESTSGEFGGLGAELGE---------EDGKVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAGLTLDDAVKLLRgK 118

                         90
                 ....*....|..
gi 62472958  806 CGAVLVLVVQRE 817
Cdd:COG0793  119 AGTKVTLTIKRP 130

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958 1247 GSLGFSIIGGTDHSCVPFGTREP-GIFISHIVPGGIASKCGkLRMGDRILKVNEADVSKATHQDAVLELLKPGDEIKLTI 1325
Cdd:COG0265  178 GWLGVTIQPVTPELAEALGLPEPeGVLVARVEPGSPAAKAG-LRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTV 256

                 ...
gi 62472958 1326 QHD 1328
Cdd:COG0265  257 LRG 259

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
                   ....*....|....*....|....*....|....*....|
gi 62472958    760 GIFISRVTEAGPADLAGLKVGDKVIKVNGIVVVDADHYQA 799
Cdd:TIGR02037  258 GALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRR 297

serine endoprotease DegS;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 62472958   747 GGKGSTPFKGDDD------GIFISRVTEAGPADLAGLKVGDKVIKVNG 788
Cdd:PRK10898  261 GGREIAPLHAQGGgidqlqGIVVNEVSPDGPAAKAGIQVNDLIISVNN 308

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 62472958 1331 PPGFQEVLLSKAEGERLGMHIKGGLNGQRGNPADPSDEGVFVSKINSVGAARRDGRLKVGMRLLEVNGHSLLGASHQDAV 1410
Cdd:cd06701    1 PPGLQELTIVKEPGEKLGISIRGGAKGHAGNPLDPTDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAV 80

                         90
                 ....*....|....*...
gi 62472958 1411 NVLRNAGNEIQLVVCKGY 1428
Cdd:cd06701   81 RILRSVGDTLTLLVCDGY 98

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958   30 EEILRYSRTLEELFLDANHIRDLPKNFFRLHRLRKLGLSDNEIGRLPPDIQNFENLVELDVSRNDipdipdDIKHLQSLQ 109
Cdd:COG4886   43 LSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE------ELSNLTNLE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  110 VADFSSNPIPKLPSGFSQLKNLTVLGLNDMSLTTLPADFGSLTQLESLELRENLLKHLPETISQLTKLKRLDLGDNEIED 189
Cdd:COG4886  117 SLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  190 LPPYLGYLPGLHELWLDHNQLQRLPPELGLLTKLTYLDVSENRLEELPnEISGLVSLTDLDLAQNLLEALPDgIAKLSRL 269
Cdd:COG4886  197 LPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNL 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  270 TILKLDQNRLQRLNDTLGNCENMQELILTENFLSELPASIGQMTKLNNLNVDRNALEYLPLEIGQCANLGVLSLRDNKLK 349
Cdd:COG4886  275 KTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLL 354

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 62472958  350 KLPPELGNCTVLHVLDVSGNQLLYLPYSLVNLQLKAVWLSENQSQPLLTFQPDTDAE 406
Cdd:COG4886  355 LLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAV 411

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958   52 LPKNFFRLHRLRKLGLSDNEigrlppDIQNFENLVELDVSRNDIPDIPDDIKHLQSLQVADFSSNPIPKLPSGFSQLKNL 131
Cdd:COG4886   88 GLTDLGDLTNLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  132 TVLGLNDMSLTTLPADFGSLTQLESLELRENLLKHLPETISQLTKLKRLDLGDNEIEDLPPYLGYLPGLHELWLDHNQLQ 211
Cdd:COG4886  162 KSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLT 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  212 RLpPELGLLTKLTYLDVSENRLEELPnEISGLVSLTDLDLAQNLLEALPDGIAKLSRLTILKLDQNRLQRLNDTLGNCEN 291
Cdd:COG4886  242 DL-PELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLL 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  292 MQELILTENFLSELPASIGQMTKLNNLNVDRNALEYLPLEIGQCANLGVLSLRDNKLKKLPPELGNCTVLHVLDVSGNQL 371
Cdd:COG4886  320 LTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAG 399

                        330
                 ....*....|....*
gi 62472958  372 LYLPYSLVNLQLKAV 386
Cdd:COG4886  400 VLLLTLALLDAVNTE 414

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 62472958  730 YEIHIERTAAGLGLSIAGGKGSTPFKGDDDGIFISRVTEAGPADLAGLKVGDKVIKVNGIVVVDADHYQAVQVLKACGAV 809
Cdd:cd06704    1 LTITIERQTGGLGISIAGGKGSTPYKGDDEGIFISRVTEGGPAAKAGVRVGDKLLEVNGVDLVDADHHEAVEALKNSGNT 80

                 ....*..
gi 62472958  810 LVLVVQR 816
Cdd:cd06704   81 VTMVVLR 87

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  127 QLKNLTVLGLNDMSLTTLPADFGSLTQLESLELRENLLKHLPETISQLTKLKRLDLGDNEIEDLPPYLGYLPGLHELWLD 206
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  207 HNQLQRLPPELGLLTKLTYLDVSENrleelpNEISGLVSLTDLDLAQNLLEALPDGIAKLSRLTILKLDQNRLQRLNDTL 286
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958  287 GNCENMQELILTENFLSELPASIGQMTKLNNLNVDRNALEYLPLEIGQCANLGVLSLRDNKLKKLPPELGNCTVLHVLDV 366
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDL 235

                        250       260
                 ....*....|....*....|....*..
gi 62472958  367 SGNQLLYLPySLVNL-QLKAVWLSENQ 392
Cdd:COG4886  236 SNNQLTDLP-ELGNLtNLEELDLSNNQ 261

leucine-rich repeat receptor-like protein kinase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958    27 QVPEEILRYSrTLEELFLDANHIR-DLPKNFFRLHRLRKLGLSDNEI-GRLPPDIQNFENLVELDVSRNDIP-DIPDDIK 103
Cdd:PLN00113  227 EIPYEIGGLT-SLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIFSLQKLISLDLSDNSLSgEIPELVI 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958   104 HLQSLQVAD-FSSNPIPKLPSGFSQLKNLTVLGLNDMSLT-TLPADFGSLTQLESLELREN-LLKHLPETISQLTKLKRL 180
Cdd:PLN00113  306 QLQNLEILHlFSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNnLTGEIPEGLCSSGNLFKL 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958   181 DLGDNEIED-LPPYLGYLPGLHELWLDHNQLQ-RLPPELGLLTKLTYLDVSENRLE------------------------ 234
Cdd:PLN00113  386 ILFSNSLEGeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQgrinsrkwdmpslqmlslarnkff 465

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472958   235 -ELPnEISGLVSLTDLDLAQNLL-EALPDGIAKLSRLTILKLDQNRLQ-RLNDTLGNCENMQELILTENFLS-ELPASIG 310
Cdd:PLN00113  466 gGLP-DSFGSKRLENLDLSRNQFsGAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQLSgQIPASFS 544

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62472958   311 QMTKLNNLNVDRNALE-YLPLEIGQCANLGVLSLRDNKLKKLPPELGNCTVLHVLDVSGNQLL 372
Cdd:PLN00113  545 EMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLHGSLPSTGAFLAINASAVAGNIDL 607