canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains 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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568945118   31 GFNVAGG--GKEGIFVRELREDSPAAKSLSLQEGDQLLSA-RVFFENFKYEDALRLLQ 85
Cdd:cd00136    13 GFSIRGGkdGGGGIFVSRVEPGGPAARDGRLRVGDRILEVnGVSLEGLTHEEAVELLK 70

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains 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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568945118   31 GFNVAGG--GKEGIFVRELREDSPAAKSLSLQEGDQLLSA-RVFFENFKYEDALRLLQ 85
Cdd:cd00136    13 GFSIRGGkdGGGGIFVSRVEPGGPAARDGRLRVGDRILEVnGVSLEGLTHEEAVELLK 70

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 568945118     17 VEIIVETEAQTGVSGFNVAGGGKE--GIFVRELREDSPAAKSlSLQEGDQLLS-ARVFFENFKYEDALRLLQCAEPyKVS 93
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEggGVVVSSVVPGSPAAKA-GLRVGDVILEvNGTSVEGLTHLEAVDLLKKAGG-KVT 78

                    ....*
gi 568945118     94 FCLKR 98
Cdd:smart00228   79 LTVLR 83

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945118  433 PEVKAPKGPEVKLPKVPEVKL-PKVPEAAIPDVQLPEVQLPKMSDMKLPKIPEMVVPDVRLPEVQLPKVPEMKVPEMKLP 511
Cdd:NF033839  177 PDTKPSPQPEGKKPSVPDINQeKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVE 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945118  512 kvPEMAVPDVhLPDVQLPKVPEMKLPEMKLPKVPEMAVPDVRLPEVQLPKVSEVKLPKM-PEMAVPDVHlPELQLPKMSE 590
Cdd:NF033839  257 --IENTVHKI-FADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPePETPKPEVK-PQLEKPKPEV 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945118  591 VKLPKMPEMAVPdvrlPEVQLPKVSEMKLPKMPEMTM-PDIRLPEVQLPKVPDIKLPEMKlPEIKLPKVPDMAVPDVPLP 669
Cdd:NF033839  333 KPQPEKPKPEVK----PQLETPKPEVKPQPEKPKPEVkPQPEKPKPEVKPQPETPKPEVK-PQPEKPKPEVKPQPEKPKP 407

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568945118  670 ELQ-LPKVSDIRLPEMQVSQVPEVQ-LPKMPEMKLSKVPEVQRKSAGAEQAK 719
Cdd:NF033839  408 EVKpQPEKPKPEVKPQPEKPKPEVKpQPEKPKPEVKPQPEKPKPEVKPQPET 459

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains 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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568945118   31 GFNVAGG--GKEGIFVRELREDSPAAKSLSLQEGDQLLSA-RVFFENFKYEDALRLLQ 85
Cdd:cd00136    13 GFSIRGGkdGGGGIFVSRVEPGGPAARDGRLRVGDRILEVnGVSLEGLTHEEAVELLK 70

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 568945118     17 VEIIVETEAQTGVSGFNVAGGGKE--GIFVRELREDSPAAKSlSLQEGDQLLS-ARVFFENFKYEDALRLLQCAEPyKVS 93
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEggGVVVSSVVPGSPAAKA-GLRVGDVILEvNGTSVEGLTHLEAVDLLKKAGG-KVT 78

                    ....*
gi 568945118     94 FCLKR 98
Cdd:smart00228   79 LTVLR 83

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945118   433 PEVKAPKGPEVKLPKVPEVKLPKVPEAAIPDVqlPEVQLPKMSDMKLPKIPEMVVPDVrlPEVQLPKVPE---MKVPEMK 509
Cdd:pfam02389   30 PEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKV--PEPCCPKVPEPCYPKVPEPCSPKV--PEPCHPKAPEpchPKVPEPC 105

                           90
                   ....*....|....*
gi 568945118   510 LPKVPEMAVPDVHLP 524
Cdd:pfam02389  106 YPKAPEPCQPKVPEP 120

PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins , and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. 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 ZO 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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568945118   31 GFNVAGGGKEGIFVRELREDSPAAKSlSLQEGDQLLSAR-VFFENFKYEDALRLL 84
Cdd:cd06729    14 GLRLAGGNDVGIFVAGVQEGSPAEKQ-GLQEGDQILKVNgVDFRNLTREEAVLFL 67

PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. 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 SYNJ2BP-like family 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568945118   18 EIIVETEAQTGVsGFNVAGG-------GKEGIFVRELREDSPAAKSLSLQEGDQLLSAR-VFFENFKYEDALRL 83
Cdd:cd06709     1 EEITLKRGPSGL-GFNIVGGtdqpyipNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINgQSLENLTHQDAVEL 73

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945118   468 EVQLPKMSDMKLPKIPEMVVP-DVRLPEVQLPKVPE---MKVPEMKLPKVPEMAVPDVhlPDVQLPKVPE---MKLPEMK 540
Cdd:pfam02389    4 QVKQPCQPPPQEPCVPTTKEPcHSKVPEPCNPKVPEpccPKVPEPCCPKVPEPCCPKV--PEPCCPKVPEpcyPKVPEPC 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 568945118   541 LPKVPEMAVPdvRLPEVQLPKVSEVKLPKMPEMAVPDVHLP 581
Cdd:pfam02389   82 SPKVPEPCHP--KAPEPCHPKVPEPCYPKAPEPCQPKVPEP 120

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945118   594 PKMPEMAVPDVRLPevQLPKVSEMKLPKMPEMTMPdiRLPEVQLPKVPDIKLPemKLPEIKLPKVPDMAVPDVPLP-ELQ 672
Cdd:pfam02389   11 PPPQEPCVPTTKEP--CHSKVPEPCNPKVPEPCCP--KVPEPCCPKVPEPCCP--KVPEPCCPKVPEPCYPKVPEPcSPK 84

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 568945118   673 LPKVSDIRLPEMQVSQVPEVQLPKMPEMKLSKVPE 707
Cdd:pfam02389   85 VPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPE 119

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. 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 PTPN13 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 568945118   15 ELVEIIVETEAQTGVsGFNVAGGGK-----EGIFVRELREDSPAAKSLSLQEGDQLLSAR-VFFENFKYEDALRLLQCAe 88
Cdd:cd06694     1 EIVIVTLKKDPQKGL-GFTIVGGENsgsldLGIFVKSIIPGGPADKDGRIKPGDRIIAINgQSLEGKTHHAAVEIIQNA- 78

                  ....*.
gi 568945118   89 PYKVSF 94
Cdd:cd06694    79 PDKVEL 84

PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form domain-swapping dimers; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins , and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. 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 ZO 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
                  ....*....|....*....|....*....|....*....|....
gi 568945118   42 IFVRELREDSPAAKSLSLQEGDQLLSAR-VFFENFKYEDALRLL 84
Cdd:cd06728    22 IFVKEITPDSLAAKDGNLQEGDIILKINgTPVENLSLSEAKKLI 65

PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). 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 PTPN13-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 568945118   18 EIIVETEAQTGVSGFNVAGGGKE-----GIFVRELREDSPAAKSLSLQEGDQLLSA-RVFFENFKYEDALRLLQCAePYK 91
Cdd:cd06792     2 VFEVELSKKDGSLGISVTGGINTsvrhgGIYVKSLVPGGAAEQDGRIQKGDRLLEVnGVSLEGVTHKQAVECLKNA-GQV 80

                  ....*..
gi 568945118   92 VSFCLKR 98
Cdd:cd06792    81 VTLVLER 87

PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the first PDZ domain of the canonical isoform of PDZD7- isoform 1. 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 PDZD7-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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568945118   31 GFNVAGGGKEG--IFVRELREDSPAAKSlSLQEGDQLLSAR-VFFENFKYEDALRLLQ 85
Cdd:cd10833    15 GFSVRGGSEHGlgIFVSKVEEGSAAERA-GLCVGDKITEVNgVSLENITMSSAVKVLT 71

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945118   31 GFNVAGG--------GKEGIFVRELREDSPAAKSLSLQEGDQLLSAR-VFFENFKYEDALRLLQCAEP 89
Cdd:cd06703    15 GFSIAGGkgstpfrdGDEGIFISRITEGGAADRDGKLQVGDRVLSINgVDVTEARHDQAVALLTSSSP 82