GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806485   74 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSD-QILQESE 152
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806485  153 DFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQ 210
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPVV 138

envelope glycoprotein D; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806485 199 IGYGYLHRIPTQPPSYHKKPPGTPPPSALPLGAPPPDALPPGPTPEDSPSLETGSRQSDYMEALLQAP----GSSMEDPL 274
Cdd:PHA03264 243 VDYWFMRHGGVVPPYFEESKGYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPagrdGAAGGEPK 322

                         90       100
                 ....*....|....*....|....*....
gi 578806485 275 PGPGSPSHSAPDPDGLPHFMETPLQPPPP 303
Cdd:PHA03264 323 PGPPRPAPDADRPEGWPSLEAITFPPPTP 351

GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806485   74 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSD-QILQESE 152
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806485  153 DFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQ 210
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPVV 138

GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806485   26 QVQENSPAQQAGLEPYFDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASV 105
Cdd:pfam04495  49 DVHENSPAAKAGLQPYSDYIIGTPKGLLKGEDD-LYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGL 127

circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. 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 HhoA-like PDZ domain 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        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806485  26 QVQENSPAQQAGLEPyFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF---NMKTMRVR 85
Cdd:cd10838   39 QVLPNSPAARAGLRR-GDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLrgdRRQTLAVK 100

envelope glycoprotein D; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806485 199 IGYGYLHRIPTQPPSYHKKPPGTPPPSALPLGAPPPDALPPGPTPEDSPSLETGSRQSDYMEALLQAP----GSSMEDPL 274
Cdd:PHA03264 243 VDYWFMRHGGVVPPYFEESKGYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPagrdGAAGGEPK 322

                         90       100
                 ....*....|....*....|....*....
gi 578806485 275 PGPGSPSHSAPDPDGLPHFMETPLQPPPP 303
Cdd:PHA03264 323 PGPPRPAPDADRPEGWPSLEAITFPPPTP 351

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806485    12 SVDSGMHPARSVF-QQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEV 76
Cdd:smart00228  17 SLVGGKDEGGGVVvSSVVPGSPAAKAGLRVG-DVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTV 81

GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806485   74 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSD-QILQESE 152
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578806485  153 DFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQ 210
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPVV 138

GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806485   26 QVQENSPAQQAGLEPYFDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASV 105
Cdd:pfam04495  49 DVHENSPAAKAGLQPYSDYIIGTPKGLLKGEDD-LYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGL 127

circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. 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 HhoA-like PDZ domain 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        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806485  26 QVQENSPAQQAGLEPyFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF---NMKTMRVR 85
Cdd:cd10838   39 QVLPNSPAARAGLRR-GDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLrgdRRQTLAVK 100

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806485  19 PARSVFQQVQENSPAQQAGLEPYfDFIITIGHSRLNKENdtLKALLK-ANVEKPVKLEVFNMKtmRVREVEVVP 91
Cdd:COG3975  493 GGGLVVTSVLWGSPAYKAGLSAG-DELLAIDGLRVTADN--LDDALAaYKPGDPIELLVFRRD--ELRTVTVTL 561

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with its associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in 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 beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806485 123 VEPSSPAALAGLRPyTDYVV-GSDQILQESEDFFTLIESHEGKPLKLMVynSKSDSCREVTVTP 185
Cdd:cd23081    6 VVANSPAAEAGLKP-GDRILkIDGQKVRTWEDIVRIVRENPGKPLTLKI--ERDGKILTVTVTP 66

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806485  29 ENSPAQQAGLEPYFDFIITIGHSRLNKENDT-LKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASV 105
Cdd:COG5233  196 QDKPPAYALLSPDEDYIDGSSDGQPLEIGELdLEDVNESPVNLPLSLYYYNPIDDQERAKTERDGVHKGIVGILGCQV 273

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 578806485   16 GMHPARSVF-QQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF-NMKTMRVR-------E 86
Cdd:TIGR02037 252 GLEKQRGALvAQVLPGSPAEKAGLKAG-DVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILrKGKEKTITvtlgaspE 330

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578806485   87 VEVVPSNMWggQGLLGASVRFCSFRRASEQVWH----VLDVEPSSPAALAGLRP 136
Cdd:TIGR02037 331 EQASSSNPF--LGLTVANLSPEIRKELRLKGDVkgvvVTKVVSGSPAARAGLQP 382

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806485 120 VLDVEPSSPAALAGLRPYtdyvvgsDQILQ-------ESEDFFTLIESHE-GKPLKLMVY-NSKSdscREVTVTP 185
Cdd:COG0265  205 VARVEPGSPAAKAGLRPG-------DVILAvdgkpvtSARDLQRLLASLKpGDTVTLTVLrGGKE---LTVTVTL 269

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578806485    12 SVDSGMHPARSVF-QQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEV 76
Cdd:smart00228  17 SLVGGKDEGGGVVvSSVVPGSPAAKAGLRVG-DVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTV 81