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 392889341    7 ILSVGLKKASNGeFGLQVMDG---IRGPVISFVSPGS-ASAHIFRAGDVIMAVNDRQVTDMKT--VQDSFEAAGNVVWIE 80
Cdd:smart00228  2 PRLVELEKGGGG-LGFSLVGGkdeGGGVVVSSVVPGSpAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKAGGKVTLT 80

                  ....
gi 392889341   81 FYRP 84
Cdd:smart00228 81 VLRG 84

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 392889341    7 ILSVGLKKASNGeFGLQVMDG---IRGPVISFVSPGS-ASAHIFRAGDVIMAVNDRQVTDMKT--VQDSFEAAGNVVWIE 80
Cdd:smart00228  2 PRLVELEKGGGG-LGFSLVGGkdeGGGVVVSSVVPGSpAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKAGGKVTLT 80

                  ....
gi 392889341   81 FYRP 84
Cdd:smart00228 81 VLRG 84

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 392889341 10 VGLKKASNGEFGLQVMDGI---RGPVISFVSPGSASAH--IFRAGDVIMAVNDRQVTDM 63
Cdd:cd00136   2 VTLEKDPGGGLGFSIRGGKdggGGIFVSRVEPGGPAARdgRLRVGDRILEVNGVSLEGL 60

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392889341   26 DGIRGPVISFVSPGSASAHI-FRAGDVIMAVNDRQVTDMKTVQDSFEAAGN--VVWIEFYR 83
Cdd:TIGR02037 359 GDVKGVVVTKVVSGSPAARAgLQPGDVILSVNQQPVSSVAELRKVLARAKKggRVALLILR 419

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 392889341    7 ILSVGLKKASNGeFGLQVMDG---IRGPVISFVSPGS-ASAHIFRAGDVIMAVNDRQVTDMKT--VQDSFEAAGNVVWIE 80
Cdd:smart00228  2 PRLVELEKGGGG-LGFSLVGGkdeGGGVVVSSVVPGSpAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKAGGKVTLT 80

                  ....
gi 392889341   81 FYRP 84
Cdd:smart00228 81 VLRG 84

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 392889341 10 VGLKKASNGEFGLQVMDGI---RGPVISFVSPGSASAH--IFRAGDVIMAVNDRQVTDM 63
Cdd:cd00136   2 VTLEKDPGGGLGFSIRGGKdggGGIFVSRVEPGGPAARdgRLRVGDRILEVNGVSLEGL 60

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392889341   9 SVGLKKASNGEFGLQVMDG----IRGPVISFVSPGS-ASAHIFRAGDVIMAVNDRQVTDM 63
Cdd:pfam00595  1 QVTLEKDGRGGLGFSLKGGsdqgDPGIFVSEVLPGGaAEAGGLKVGDRILSINGQDVENM 60

Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 392889341  20 FGLQVMDGIRGPVISFVSPGSAsAHI--FRAGDVIMAVNDRQVT 61
Cdd:COG3975  485 LGLRVSADGGGLVVTSVLWGSP-AYKagLSAGDELLAIDGLRVT 527

circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do) and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for combining with other DegP monomers to form a stable oligomer structure. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegP family PDZ domain 1 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 392889341 25 MDGIRGPVISFVSPGSASAHI-FRAGDVIMAVNDRQVTDMK 64
Cdd:cd10839  21 LKEPKGALVAQVLPDSPAAKAgLKAGDVILSLNGKPITSSA 61

PDZ domain of neuronal nitric oxide synthase (nNOS), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of nNOS, and related domains. nNOS produces a key signaling molecule, nitric oxide (NO), which has diverse functions throughout the body and acts as a neurotransmitter and intracellular signaling molecule in the central and peripheral nervous system. nNOS is concentrated at synaptic junctions in the brain and motor endplates in skeletal muscle. The PDZ domain of neuronal nitric oxide synthase (nNOS) interacts with the PDZ domain of alpha1-syntrophin (in muscle cells) and with the second PDZ domain of Disks large homolog 4 (Dlg4, also known as PSD-95), and nitric oxide synthase 1 adaptor protein NOS1AP in neurons. Dlg4 binds NMDA receptors, and nNOS, forming a complex in neurons. NOS1AP competes with Dgl4 for the nNOS PDZ domain and prevents the coupling of nNos activation with NMDA receptor-mediated calcium influx. 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 nNOS-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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392889341   7 ILSVGLKKASNGEFGLQVMD-GIRGPVI--SFVSPGSA-SAHIFRAGDVIMAVNDRQVTDM 63
Cdd:cd06708    2 VISVRLFKRKVGGLGFLVKQrVCKPPVIisDLIRGGAAeQSGLVQVGDIILAVNGRPLVDV 62

PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. 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 Zasp52-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
                ....*....|....*....|....*....|....*....|....*
gi 392889341 36 VSPGS-ASAHIFRAGDVIMAVNDRQVTDM--KTVQDSFEAAGNVV 77
Cdd:cd23068  32 VNPGSpADKAGLRRGDVILRINGTDTSNLthKQAQDLIKRAGNDL 76

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 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 PDLIM-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
                ....*....|....*....|....*....|....
gi 392889341 32 VISFVSPGS--ASAHIfRAGDVIMAVNDRQVTDM 63
Cdd:cd06753  25 TISRVTPGGkaAQANL-RPGDVILAINGESTEGM 57