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Conserved domains on  [gi|530400001|ref|XP_005268811|]
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glutamate receptor-interacting protein 1 isoform X6 [Homo sapiens]

Protein Classification

PDZ domain-containing protein( domain architecture ID 10097540)

PDZ (PSD-95, Dlg, and ZO-1/2) domain-containing protein is involved in protein-protein interactions and may play a role in scaffolding supramolecular complexes

CATH:  2.30.42.10
Gene Ontology:  GO:0005515
SCOP:  4001790

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
153-236 6.42e-20

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 84.93  E-value: 6.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  153 EVTLHKEGNT-FGFVIRGGahddRNKSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEA 231
Cdd:cd00992     3 TVTLRKDPGGgLGFSLRGG----KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                  ....*
gi 530400001  232 ALLIE 236
Cdd:cd00992    78 TLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
672-753 8.99e-19

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 81.84  E-value: 8.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  672 IYTVEL-KRYGGPLGITISGTEEPFDPIIISSLTKGGLAERtGAIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTL 750
Cdd:cd00992     1 VRTVTLrKDPGGGLGFSLRGGKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                  ...
gi 530400001  751 KIK 753
Cdd:cd00992    80 TVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
54-134 6.81e-18

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 79.15  E-value: 6.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   54 VVELMKKEGTTLGLTVSGGIDKDGKPRVSNLRQGGIAARSdQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEV 133
Cdd:cd00992     3 TVTLRKDPGGGLGFSLRGGKDSGGGIFVSRVEPGGPAERG-GLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLTV 81

                  .
gi 530400001  134 E 134
Cdd:cd00992    82 R 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
572-656 1.47e-16

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 75.30  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  572 TFHVKLPKKHNVELGITISSPSSRKPGdpLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLV 651
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGKDSGGG--IFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                  ....*
gi 530400001  652 KLKIR 656
Cdd:cd00992    78 TLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1003-1083 8.55e-16

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 73.37  E-value: 8.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001 1003 LHKVTLYKDSDmEDFGFSVADGLLEK-GVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDL 1081
Cdd:cd00992     1 VRTVTLRKDPG-GGLGFSLRGGKDSGgGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                  ..
gi 530400001 1082 VI 1083
Cdd:cd00992    80 TV 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
471-559 3.80e-15

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 71.44  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  471 TTEVVLTADPVTGFGIQLQGSVfateTLSSPPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRDSSi 550
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGK----DSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSG- 74

                  ....*....
gi 530400001  551 tSKVTLEIE 559
Cdd:cd00992    75 -DEVTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
251-334 1.18e-14

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 69.90  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  251 PLLVEVAKTPGASLGVALTTSmCCNKQVIVIDKIKSASIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVK 330
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGG-KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVT 78

                  ....
gi 530400001  331 LEIL 334
Cdd:cd00992    79 LTVR 82
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
153-236 6.42e-20

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 84.93  E-value: 6.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  153 EVTLHKEGNT-FGFVIRGGahddRNKSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEA 231
Cdd:cd00992     3 TVTLRKDPGGgLGFSLRGG----KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                  ....*
gi 530400001  232 ALLIE 236
Cdd:cd00992    78 TLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
150-238 2.14e-19

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 83.58  E-value: 2.14e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    150 RTVEVTLHKEGNTFGFVIRGGahddRNKSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQ 229
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGG----KDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGG 75

                    ....*....
gi 530400001    230 EAALLIEYD 238
Cdd:smart00228   76 KVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
672-753 8.99e-19

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 81.84  E-value: 8.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  672 IYTVEL-KRYGGPLGITISGTEEPFDPIIISSLTKGGLAERtGAIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTL 750
Cdd:cd00992     1 VRTVTLrKDPGGGLGFSLRGGKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                  ...
gi 530400001  751 KIK 753
Cdd:cd00992    80 TVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
54-134 6.81e-18

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 79.15  E-value: 6.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   54 VVELMKKEGTTLGLTVSGGIDKDGKPRVSNLRQGGIAARSdQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEV 133
Cdd:cd00992     3 TVTLRKDPGGGLGFSLRGGKDSGGGIFVSRVEPGGPAERG-GLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLTV 81

                  .
gi 530400001  134 E 134
Cdd:cd00992    82 R 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
671-753 1.05e-17

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 78.96  E-value: 1.05e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    671 IIYTVELKRYGGPLGITISGTEEPFDPIIISSLTKGGLAERTGaIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTL 750
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79

                    ...
gi 530400001    751 KIK 753
Cdd:smart00228   80 TVL 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
572-656 1.47e-16

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 75.30  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  572 TFHVKLPKKHNVELGITISSPSSRKPGdpLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLV 651
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGKDSGGG--IFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                  ....*
gi 530400001  652 KLKIR 656
Cdd:cd00992    78 TLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1003-1083 8.55e-16

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 73.37  E-value: 8.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001 1003 LHKVTLYKDSDmEDFGFSVADGLLEK-GVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDL 1081
Cdd:cd00992     1 VRTVTLRKDPG-GGLGFSLRGGKDSGgGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                  ..
gi 530400001 1082 VI 1083
Cdd:cd00992    80 TV 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
471-559 3.80e-15

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 71.44  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  471 TTEVVLTADPVTGFGIQLQGSVfateTLSSPPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRDSSi 550
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGK----DSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSG- 74

                  ....*....
gi 530400001  551 tSKVTLEIE 559
Cdd:cd00992    75 -DEVTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
251-334 1.18e-14

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 69.90  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  251 PLLVEVAKTPGASLGVALTTSmCCNKQVIVIDKIKSASIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVK 330
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGG-KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVT 78

                  ....
gi 530400001  331 LEIL 334
Cdd:cd00992    79 LTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
54-135 5.36e-14

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 68.17  E-value: 5.36e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001     54 VVELMKKEGTtLGLTVSGGIDKDGKPRVSNLRQGGIAARsDQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEV 133
Cdd:smart00228    4 LVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTV 81

                    ..
gi 530400001    134 EY 135
Cdd:smart00228   82 LR 83
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1002-1087 2.04e-13

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 66.63  E-value: 2.04e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   1002 ELHKVTLYKDSdmEDFGFSVADGLLE-KGVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLD 1080
Cdd:smart00228    1 EPRLVELEKGG--GGLGFSLVGGKDEgGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*..
gi 530400001   1081 LVISRNP 1087
Cdd:smart00228   79 LTVLRGG 85
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
572-658 3.69e-13

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 65.86  E-value: 3.69e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    572 TFHVKLPKKHNvELGITISSpsSRKPGDPLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLV 651
Cdd:smart00228    2 PRLVELEKGGG-GLGFSLVG--GKDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                    ....*..
gi 530400001    652 KLKIRKD 658
Cdd:smart00228   78 TLTVLRG 84
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
153-236 2.85e-12

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 63.07  E-value: 2.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   153 EVTLHKEGNT-FGFVIRGGahdDRNKSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEA 231
Cdd:pfam00595    1 QVTLEKDGRGgLGFSLKGG---SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKV 76

                   ....*
gi 530400001   232 ALLIE 236
Cdd:pfam00595   77 TLTIL 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
470-559 3.35e-12

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 63.17  E-value: 3.35e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    470 ETTEVVLTADPvTGFGIQLQGSVFAtetlSSPPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRDSS 549
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLVGGKDE----GGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAG 74
                            90
                    ....*....|
gi 530400001    550 itSKVTLEIE 559
Cdd:smart00228   75 --GKVTLTVL 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
251-335 6.43e-12

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 62.40  E-value: 6.43e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    251 PLLVEVAKTPGaSLGVALTTSMCcNKQVIVIDKIKSASIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVK 330
Cdd:smart00228    2 PRLVELEKGGG-GLGFSLVGGKD-EGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*
gi 530400001    331 LEILP 335
Cdd:smart00228   79 LTVLR 83
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
674-753 9.20e-12

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 61.91  E-value: 9.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   674 TVELKRYG-GPLGITISG-TEEPFDPIIISSLTKGGLAERTGaIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTLK 751
Cdd:pfam00595    1 QVTLEKDGrGGLGFSLKGgSDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   ..
gi 530400001   752 IK 753
Cdd:pfam00595   80 IL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
55-134 2.22e-09

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 54.98  E-value: 2.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    55 VELMKKEGTTLGLTVSGGIDKDGKP-RVSNLRQGGIAARsDQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEV 133
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSDQGDPGiFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTI 80

                   .
gi 530400001   134 E 134
Cdd:pfam00595   81 L 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
575-656 1.19e-08

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 53.05  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   575 VKLPKKHNVELGITISSPSSrKPGDPLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLVKLK 654
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSD-QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   ..
gi 530400001   655 IR 656
Cdd:pfam00595   80 IL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
473-559 1.49e-08

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 52.67  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   473 EVVLTADPVTGFGIQLQGSvfaTETLSSPPLISYIEADSPAERcGVLQIGDRVMAINGIPTEDSTFEEASQLLRDSSitS 552
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGG---SDQGDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSG--G 74

                   ....*..
gi 530400001   553 KVTLEIE 559
Cdd:pfam00595   75 KVTLTIL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1005-1083 1.24e-06

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 47.28  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  1005 KVTLYKDSDmEDFGFSVADG--LLEKGVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDLV 1082
Cdd:pfam00595    1 QVTLEKDGR-GGLGFSLKGGsdQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   .
gi 530400001  1083 I 1083
Cdd:pfam00595   80 I 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
253-334 1.38e-06

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 47.28  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   253 LVEVAKTPGASLGVALTTSMCCNKQVIVIDKIKSASIADRcGALHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVKLE 332
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSDQGDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   ..
gi 530400001   333 IL 334
Cdd:pfam00595   80 IL 81
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
54-236 1.79e-06

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]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 51.84  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    54 VVELMKKEGTT----LGLTVsGGIDKD-------GKPR---VSNLRQGGIAARSDqLDVGDYIKAVNGINLAKFRH-DEI 118
Cdd:TIGR02037  221 VVDQLIEGGKVkrgwLGVTI-QEVTSDlakslglEKQRgalVAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADlRRA 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   119 ISLLKnVGERVVLEVEYELPPVSVqgSSVIFRTVEVTLHKEGNTFGFVIR------GGAHDDRNKSRPVVITCVRPGGPA 192
Cdd:TIGR02037  299 IGTLK-PGKKVTLGILRKGKEKTI--TVTLGASPEEQASSSNPFLGLTVAnlspeiRKELRLKGDVKGVVVTKVVSGSPA 375
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 530400001   193 DREGtIKPGDRLLSVDGIRLlgTTHAEAMSILKQCGQ--EAALLIE 236
Cdd:TIGR02037  376 ARAG-LQPGDVILSVNQQPV--SSVAELRKVLARAKKggRVALLIL 418
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
482-559 2.29e-06

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 51.18  E-value: 2.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400001  482 TGFGIQLQgsvfatETLSSPPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRdSSITSKVTLEIE 559
Cdd:COG0793   100 GGIGIELQ------MEDIGGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIR-GKPGTKVTLTIL 169
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
58-134 8.89e-04

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 43.09  E-value: 8.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400001   58 MKKEGTTLGLTVsgGIDKDGKPRVSNLRQGGIAARSdQLDVGDYIKAVNGINLAKFRHDEIISLLKN-VGERVVLEVE 134
Cdd:COG0793    95 TSGEFGGIGIEL--QMEDIGGVKVVSPIDGSPAAKA-GIKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTIL 169
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
690-816 2.17e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 41.65  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  690 GTEEPFDPIIISSLTKGGLAERTGaIHIGDRILAINSSSLKGKPLSEAIHLLQ-MAGETVTLKIKKQTDAQSASSPKK-- 766
Cdd:PLN00049   96 GSDGPPAGLVVVAPAPGGPAARAG-IRPGDVILAIDGTSTEGLSLYEAADRLQgPEGSSVELTLRRGPETRLVTLTREkv 174
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530400001  767 --FPISSHLSDLGDVEEDsSPAQKPGKLSDMYPSTVPSVDSAVDSWDGSAID 816
Cdd:PLN00049  175 slNPVKSRLCEVPGPGAG-SPKIGYIKLTTFNQNASSAVKEAIETLRANGVD 225
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
477-559 2.22e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 41.65  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  477 TADPVTGFGIQLQgsvFATETLSSPPLISYIEA--DSPAERCGVLQiGDRVMAINGIPTEDSTFEEASQLLRdSSITSKV 554
Cdd:PLN00049   80 TKGAVTGVGLEVG---YPTGSDGPPAGLVVVAPapGGPAARAGIRP-GDVILAIDGTSTEGLSLYEAADRLQ-GPEGSSV 154

                  ....*
gi 530400001  555 TLEIE 559
Cdd:PLN00049  155 ELTLR 159
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
265-335 3.19e-03

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 41.16  E-value: 3.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400001  265 GVALTTSMCCNKQVIVIDKIKSaSIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTTD-QVKLEILP 335
Cdd:COG0793   101 GIGIELQMEDIGGVKVVSPIDG-SPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRGKPGtKVTLTILR 170
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
170-225 4.04e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 40.88  E-value: 4.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530400001  170 GAHDDRNKSRPVVITCVrPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILK 225
Cdd:PLN00049   94 PTGSDGPPAGLVVVAPA-PGGPAARAG-IRPGDVILAIDGTSTEGLSLYEAADRLQ 147
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
153-236 6.42e-20

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 84.93  E-value: 6.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  153 EVTLHKEGNT-FGFVIRGGahddRNKSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEA 231
Cdd:cd00992     3 TVTLRKDPGGgLGFSLRGG----KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                  ....*
gi 530400001  232 ALLIE 236
Cdd:cd00992    78 TLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
150-238 2.14e-19

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 83.58  E-value: 2.14e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    150 RTVEVTLHKEGNTFGFVIRGGahddRNKSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQ 229
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGG----KDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGG 75

                    ....*....
gi 530400001    230 EAALLIEYD 238
Cdd:smart00228   76 KVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
672-753 8.99e-19

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 81.84  E-value: 8.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  672 IYTVEL-KRYGGPLGITISGTEEPFDPIIISSLTKGGLAERtGAIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTL 750
Cdd:cd00992     1 VRTVTLrKDPGGGLGFSLRGGKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                  ...
gi 530400001  751 KIK 753
Cdd:cd00992    80 TVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
54-134 6.81e-18

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 79.15  E-value: 6.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   54 VVELMKKEGTTLGLTVSGGIDKDGKPRVSNLRQGGIAARSdQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEV 133
Cdd:cd00992     3 TVTLRKDPGGGLGFSLRGGKDSGGGIFVSRVEPGGPAERG-GLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLTV 81

                  .
gi 530400001  134 E 134
Cdd:cd00992    82 R 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
671-753 1.05e-17

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 78.96  E-value: 1.05e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    671 IIYTVELKRYGGPLGITISGTEEPFDPIIISSLTKGGLAERTGaIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTL 750
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79

                    ...
gi 530400001    751 KIK 753
Cdd:smart00228   80 TVL 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
572-656 1.47e-16

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 75.30  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  572 TFHVKLPKKHNVELGITISSPSSRKPGdpLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLV 651
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGKDSGGG--IFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                  ....*
gi 530400001  652 KLKIR 656
Cdd:cd00992    78 TLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1003-1083 8.55e-16

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 73.37  E-value: 8.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001 1003 LHKVTLYKDSDmEDFGFSVADGLLEK-GVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDL 1081
Cdd:cd00992     1 VRTVTLRKDPG-GGLGFSLRGGKDSGgGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                  ..
gi 530400001 1082 VI 1083
Cdd:cd00992    80 TV 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
471-559 3.80e-15

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 71.44  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  471 TTEVVLTADPVTGFGIQLQGSVfateTLSSPPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRDSSi 550
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGK----DSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSG- 74

                  ....*....
gi 530400001  551 tSKVTLEIE 559
Cdd:cd00992    75 -DEVTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
251-334 1.18e-14

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 69.90  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  251 PLLVEVAKTPGASLGVALTTSmCCNKQVIVIDKIKSASIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVK 330
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGG-KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVT 78

                  ....
gi 530400001  331 LEIL 334
Cdd:cd00992    79 LTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
54-135 5.36e-14

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 68.17  E-value: 5.36e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001     54 VVELMKKEGTtLGLTVSGGIDKDGKPRVSNLRQGGIAARsDQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEV 133
Cdd:smart00228    4 LVELEKGGGG-LGFSLVGGKDEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTV 81

                    ..
gi 530400001    134 EY 135
Cdd:smart00228   82 LR 83
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1002-1087 2.04e-13

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 66.63  E-value: 2.04e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   1002 ELHKVTLYKDSdmEDFGFSVADGLLE-KGVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLD 1080
Cdd:smart00228    1 EPRLVELEKGG--GGLGFSLVGGKDEgGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*..
gi 530400001   1081 LVISRNP 1087
Cdd:smart00228   79 LTVLRGG 85
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
572-658 3.69e-13

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 65.86  E-value: 3.69e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    572 TFHVKLPKKHNvELGITISSpsSRKPGDPLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLV 651
Cdd:smart00228    2 PRLVELEKGGG-GLGFSLVG--GKDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                    ....*..
gi 530400001    652 KLKIRKD 658
Cdd:smart00228   78 TLTVLRG 84
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
153-236 2.85e-12

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 63.07  E-value: 2.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   153 EVTLHKEGNT-FGFVIRGGahdDRNKSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEA 231
Cdd:pfam00595    1 QVTLEKDGRGgLGFSLKGG---SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKV 76

                   ....*
gi 530400001   232 ALLIE 236
Cdd:pfam00595   77 TLTIL 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
470-559 3.35e-12

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 63.17  E-value: 3.35e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    470 ETTEVVLTADPvTGFGIQLQGSVFAtetlSSPPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRDSS 549
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLVGGKDE----GGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAG 74
                            90
                    ....*....|
gi 530400001    550 itSKVTLEIE 559
Cdd:smart00228   75 --GKVTLTVL 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
251-335 6.43e-12

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.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 62.40  E-value: 6.43e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    251 PLLVEVAKTPGaSLGVALTTSMCcNKQVIVIDKIKSASIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVK 330
Cdd:smart00228    2 PRLVELEKGGG-GLGFSLVGGKD-EGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*
gi 530400001    331 LEILP 335
Cdd:smart00228   79 LTVLR 83
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
674-753 9.20e-12

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 61.91  E-value: 9.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   674 TVELKRYG-GPLGITISG-TEEPFDPIIISSLTKGGLAERTGaIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTLK 751
Cdd:pfam00595    1 QVTLEKDGrGGLGFSLKGgSDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   ..
gi 530400001   752 IK 753
Cdd:pfam00595   80 IL 81
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
682-753 3.50e-10

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 56.93  E-value: 3.50e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530400001  682 GPLGITISGTEEPFdpIIISSLTKGGLAERTGaIHIGDRILAINSSSLKGKPLSEAIHLLQ-MAGETVTLKIK 753
Cdd:cd00136     1 GGLGFSIRGGTEGG--VVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKkEVGEKVTLTVR 70
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
501-559 7.65e-10

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 56.16  E-value: 7.65e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530400001  501 PPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRDsSITSKVTLEIE 559
Cdd:cd00136    14 GVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKK-EVGEKVTLTVR 70
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
161-236 2.07e-09

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 54.62  E-value: 2.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530400001  161 NTFGFVIRGGAhddrnkSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILKQC-GQEAALLIE 236
Cdd:cd00136     1 GGLGFSIRGGT------EGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEvGEKVTLTVR 70
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
55-134 2.22e-09

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 54.98  E-value: 2.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    55 VELMKKEGTTLGLTVSGGIDKDGKP-RVSNLRQGGIAARsDQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEV 133
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSDQGDPGiFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTI 80

                   .
gi 530400001   134 E 134
Cdd:pfam00595   81 L 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
575-656 1.19e-08

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 53.05  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   575 VKLPKKHNVELGITISSPSSrKPGDPLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLVKLK 654
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSD-QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   ..
gi 530400001   655 IR 656
Cdd:pfam00595   80 IL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
473-559 1.49e-08

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 52.67  E-value: 1.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   473 EVVLTADPVTGFGIQLQGSvfaTETLSSPPLISYIEADSPAERcGVLQIGDRVMAINGIPTEDSTFEEASQLLRDSSitS 552
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGG---SDQGDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSG--G 74

                   ....*..
gi 530400001   553 KVTLEIE 559
Cdd:pfam00595   75 KVTLTIL 81
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
501-559 5.64e-08

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 51.08  E-value: 5.64e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530400001  501 PPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDstFEEASQLLRDSSiTSKVTLEIE 559
Cdd:cd00989    13 EPVIGEVVPGSPAAKAG-LKAGDRILAINGQKIKS--WEDLVDAVQENP-GKPLTLTVE 67
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
63-134 1.29e-07

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 49.61  E-value: 1.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530400001   63 TTLGLTVSGGIDKDGKprVSNLRQGGIAARSdQLDVGDYIKAVNGINLAKFRHDEIISLLKN-VGERVVLEVE 134
Cdd:cd00136     1 GGLGFSIRGGTEGGVV--VLSVEPGSPAERA-GLQAGDVILAVNGTDVKNLTLEDVAELLKKeVGEKVTLTVR 70
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
503-559 3.29e-07

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 47.91  E-value: 3.29e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400001   503 LISYIEADSPAERCGvLQIGDRVMAINGIPTEDstFEEASQLLRdSSITSKVTLEIE 559
Cdd:pfam17820    1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRS--LEDVARLLQ-GSAGESVTLTVR 53
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
584-656 6.24e-07

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 47.69  E-value: 6.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400001  584 ELGITISSpssrKPGDPLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDL-VKLKIR 656
Cdd:cd00136     2 GLGFSIRG----GTEGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEVGEkVTLTVR 70
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1005-1083 1.24e-06

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 47.28  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  1005 KVTLYKDSDmEDFGFSVADG--LLEKGVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDLV 1082
Cdd:pfam00595    1 QVTLEKDGR-GGLGFSLKGGsdQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   .
gi 530400001  1083 I 1083
Cdd:pfam00595   80 I 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
253-334 1.38e-06

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 47.28  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   253 LVEVAKTPGASLGVALTTSMCCNKQVIVIDKIKSASIADRcGALHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVKLE 332
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSDQGDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   ..
gi 530400001   333 IL 334
Cdd:pfam00595   80 IL 81
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
54-236 1.79e-06

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]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 51.84  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001    54 VVELMKKEGTT----LGLTVsGGIDKD-------GKPR---VSNLRQGGIAARSDqLDVGDYIKAVNGINLAKFRH-DEI 118
Cdd:TIGR02037  221 VVDQLIEGGKVkrgwLGVTI-QEVTSDlakslglEKQRgalVAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADlRRA 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   119 ISLLKnVGERVVLEVEYELPPVSVqgSSVIFRTVEVTLHKEGNTFGFVIR------GGAHDDRNKSRPVVITCVRPGGPA 192
Cdd:TIGR02037  299 IGTLK-PGKKVTLGILRKGKEKTI--TVTLGASPEEQASSSNPFLGLTVAnlspeiRKELRLKGDVKGVVVTKVVSGSPA 375
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 530400001   193 DREGtIKPGDRLLSVDGIRLlgTTHAEAMSILKQCGQ--EAALLIE 236
Cdd:TIGR02037  376 ARAG-LQPGDVILSVNQQPV--SSVAELRKVLARAKKggRVALLIL 418
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
182-234 2.12e-06

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 45.60  E-value: 2.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530400001   182 VITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAmsILKQCGQEAALL 234
Cdd:pfam17820    1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSLEDVAR--LLQGSAGESVTL 50
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
482-559 2.29e-06

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 51.18  E-value: 2.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400001  482 TGFGIQLQgsvfatETLSSPPLISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRdSSITSKVTLEIE 559
Cdd:COG0793   100 GGIGIELQ------MEDIGGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIR-GKPGTKVTLTIL 169
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
503-559 6.26e-06

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 45.29  E-value: 6.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400001  503 LISYIEADSPAERCGvLQIGDRVMAINGIPTEDSTFEEASQLLRdSSITSKVTLEIE 559
Cdd:cd00988    16 VITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLR-GKAGTKVRLTLK 70
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
680-756 8.23e-06

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 44.91  E-value: 8.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400001  680 YGGpLGITIsgTEEPfDPIIISSLTKGGLAERTGaIHIGDRILAINSSSLKGKPLSEAIHLLQ-MAGETVTLKIKKQT 756
Cdd:cd00988     1 FGG-IGLEL--KYDD-GGLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRgKAGTKVRLTLKRGD 73
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
263-334 1.02e-05

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 44.22  E-value: 1.02e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530400001  263 SLGVALTTSmccNKQVIVIDKIKSASIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTTDQ-VKLEIL 334
Cdd:cd00136     2 GLGFSIRGG---TEGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEVGEkVTLTVR 70
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
476-661 1.17e-05

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]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 49.14  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   476 LTADPVTGFGIQLQGSVFATEtlsspplisyIEADSPAERCGvLQIGDRVMAINGIPTEDstFEEASQLLRDSSITSKVT 555
Cdd:TIGR02037  243 VTSDLAKSLGLEKQRGALVAQ----------VLPGSPAEKAG-LKAGDVITSVNGKPISS--FADLRRAIGTLKPGKKVT 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   556 LEIEFDVAESVIpssgTFHVKLPKKHNVE-----LGITIS--SPSSRK----PGDP--LVISDIKKGSVAHRTGtLELGD 622
Cdd:TIGR02037  310 LGILRKGKEKTI----TVTLGASPEEQASssnpfLGLTVAnlSPEIRKelrlKGDVkgVVVTKVVSGSPAARAG-LQPGD 384
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 530400001   623 KLLAIDNIRLDNCS-MEDAVQILQQcEDLVKLKIRKDEDN 661
Cdd:TIGR02037  385 VILSVNQQPVSSVAeLRKVLARAKK-GGRVALLILRGGAT 423
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
181-225 4.25e-05

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 42.98  E-value: 4.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530400001  181 VVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILK 225
Cdd:cd00988    15 LVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLR 58
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
684-753 5.82e-05

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 42.61  E-value: 5.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400001  684 LGITISGteePFDPIIISSLTKGGLAERTGaIHIGDRILAINssslkGKPL---SEAIHLLQM-AGETVTLKIK 753
Cdd:cd00989     3 LGFVPGG---PPIEPVIGEVVPGSPAAKAG-LKAGDRILAIN-----GQKIkswEDLVDAVQEnPGKPLTLTVE 67
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
602-657 6.54e-05

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 41.36  E-value: 6.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400001   602 VISDIKKGSVAHRTGtLELGDKLLAIDNIRLDncSMEDAVQILQQCED-LVKLKIRK 657
Cdd:pfam17820    1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVR--SLEDVARLLQGSAGeSVTLTVRR 54
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
596-658 7.73e-05

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 42.22  E-value: 7.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400001  596 KPGDPLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDncSMEDAVQILQQ-CEDLVKLKIRKD 658
Cdd:cd00989     9 GPPIEPVIGEVVPGSPAAKAG-LKAGDRILAINGQKIK--SWEDLVDAVQEnPGKPLTLTVERN 69
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
503-559 1.05e-04

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 41.86  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400001  503 LISYIEADSPAERCGvLQIGDRVMAINGIPTEDstFEEASQLLRDSSITSKVTLEIE 559
Cdd:cd00987    27 LVASVDPGSPAAKAG-LKPGDVILAVNGKPVKS--VADLRRALAELKPGDKVTLTVL 80
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1017-1083 2.78e-04

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 40.37  E-value: 2.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400001 1017 FGFSVADGLlEKGVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLI-AESGNKLDLVI 1083
Cdd:cd00136     3 LGFSIRGGT-EGGVVVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLkKEVGEKVTLTV 69
Peptidase_M50 pfam02163
Peptidase family M50;
460-559 3.36e-04

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 44.02  E-value: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001   460 VGLAGQVVHtettevVLTADPVTGFGIQLQGsvfatETLSSPPLISYIEADSPAERCGvLQIGDRVMAINGIPTedSTFE 539
Cdd:pfam02163   64 IALAGPLAN------FILAIILFAVLLFLSG-----VPPPAPPVIGGVAPGSPAAKAG-LKPGDVILSINGKKI--TSWQ 129
                           90       100
                   ....*....|....*....|
gi 530400001   540 EASQLLRDsSITSKVTLEIE 559
Cdd:pfam02163  130 DLVEALAK-SPGKPITLTVE 148
PDZ_2 pfam13180
PDZ domain;
181-219 4.49e-04

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 39.95  E-value: 4.49e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 530400001   181 VVITCVRPGGPADREGtIKPGDRLLSVDGIRLLGTTHAE 219
Cdd:pfam13180    8 VVVVSVKSSGPAAKAG-LKAGDVILSIDGRKINDLTDLE 45
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
1029-1086 5.71e-04

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 39.52  E-value: 5.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530400001 1029 GVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDccLVVPLIAESGNK-LDLVISRN 1086
Cdd:cd00989    13 EPVIGEVVPGSPAAKAGLKAGDRILAINGQKIKSWE--DLVDAVQENPGKpLTLTVERN 69
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
65-134 6.15e-04

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 39.90  E-value: 6.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530400001   65 LGLTVSggiDKDGKPRVSNLRQGGIAARSDqLDVGDYIKAVNGINLAKFRHDEIISLLKN-VGERVVLEVE 134
Cdd:cd00988     4 IGLELK---YDDGGLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGkAGTKVRLTLK 70
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
58-134 8.89e-04

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 43.09  E-value: 8.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530400001   58 MKKEGTTLGLTVsgGIDKDGKPRVSNLRQGGIAARSdQLDVGDYIKAVNGINLAKFRHDEIISLLKN-VGERVVLEVE 134
Cdd:COG0793    95 TSGEFGGIGIEL--QMEDIGGVKVVSPIDGSPAAKA-GIKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTIL 169
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
279-353 1.10e-03

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 39.13  E-value: 1.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530400001  279 IVIDKIKSASIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTT-DQVKLEILPhhqtrlALKGPDHVKIQR 353
Cdd:cd00988    15 LVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGKAgTKVRLTLKR------GDGEPREVTLTR 83
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
180-247 1.80e-03

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 38.37  E-value: 1.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  180 PVVITCVRPGGPADREGtIKPGDRLLSVDGIRllgTTHAEAMS--ILKQCGQEAALLIEYDVSVMDSVAT 247
Cdd:cd00989    13 EPVIGEVVPGSPAAKAG-LKAGDRILAINGQK---IKSWEDLVdaVQENPGKPLTLTVERNGETITLTLT 78
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
699-754 1.82e-03

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 37.51  E-value: 1.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400001   699 IISSLTKGGLAERTGaIHIGDRILAINSSSLKGkpLSEAIHLLQ-MAGETVTLKIKK 754
Cdd:pfam17820    1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRS--LEDVARLLQgSAGESVTLTVRR 54
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
690-816 2.17e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 41.65  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  690 GTEEPFDPIIISSLTKGGLAERTGaIHIGDRILAINSSSLKGKPLSEAIHLLQ-MAGETVTLKIKKQTDAQSASSPKK-- 766
Cdd:PLN00049   96 GSDGPPAGLVVVAPAPGGPAARAG-IRPGDVILAIDGTSTEGLSLYEAADRLQgPEGSSVELTLRRGPETRLVTLTREkv 174
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530400001  767 --FPISSHLSDLGDVEEDsSPAQKPGKLSDMYPSTVPSVDSAVDSWDGSAID 816
Cdd:PLN00049  175 slNPVKSRLCEVPGPGAG-SPKIGYIKLTTFNQNASSAVKEAIETLRANGVD 225
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
477-559 2.22e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 41.65  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400001  477 TADPVTGFGIQLQgsvFATETLSSPPLISYIEA--DSPAERCGVLQiGDRVMAINGIPTEDSTFEEASQLLRdSSITSKV 554
Cdd:PLN00049   80 TKGAVTGVGLEVG---YPTGSDGPPAGLVVVAPapGGPAARAGIRP-GDVILAIDGTSTEGLSLYEAADRLQ-GPEGSSV 154

                  ....*
gi 530400001  555 TLEIE 559
Cdd:PLN00049  155 ELTLR 159
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
176-236 2.81e-03

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 38.00  E-value: 2.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530400001  176 NKSRPVVITCVRPGGPADREGtIKPGDRLLSVDGIRLlgTTHAEAMSILKQ--CGQEAALLIE 236
Cdd:cd00987    21 KDTKGVLVASVDPGSPAAKAG-LKPGDVILAVNGKPV--KSVADLRRALAElkPGDKVTLTVL 80
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
265-335 3.19e-03

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 41.16  E-value: 3.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400001  265 GVALTTSMCCNKQVIVIDKIKSaSIADRCGaLHVGDHILSIDGTSMEYCTLAEATQFLANTTD-QVKLEILP 335
Cdd:COG0793   101 GIGIELQMEDIGGVKVVSPIDG-SPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRGKPGtKVTLTILR 170
PDZ_glycyl_aminopeptidase cd00990
PDZ domain associated with archaeal and bacterial M61 glycyl-aminopeptidases. May be ...
504-558 3.62e-03

PDZ domain associated with archaeal and bacterial M61 glycyl-aminopeptidases. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand is presumed to form the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238490 [Multi-domain]  Cd Length: 80  Bit Score: 37.41  E-value: 3.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530400001  504 ISYIEADSPAERCGvLQIGDRVMAINGIptedsTFEEASQLLRDSSITSKVTLEI 558
Cdd:cd00990    16 VTFVRDDSPADKAG-LVAGDELVAVNGW-----RVDALQDRLKEYQAGDPVELTV 64
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
170-225 4.04e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 40.88  E-value: 4.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530400001  170 GAHDDRNKSRPVVITCVrPGGPADREGtIKPGDRLLSVDGIRLLGTTHAEAMSILK 225
Cdd:PLN00049   94 PTGSDGPPAGLVVVAPA-PGGPAARAG-IRPGDVILAIDGTSTEGLSLYEAADRLQ 147
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
1031-1064 5.54e-03

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 35.97  E-value: 5.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 530400001  1031 YVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFD 1064
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSLE 34
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
585-659 5.96e-03

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 36.82  E-value: 5.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530400001  585 LGITIsspssRKPGDPLVISDIKKGSVAHRTGtLELGDKLLAIDNIRLDNCSMEDAVQILQQCE-DLVKLKIRKDE 659
Cdd:cd00988     4 IGLEL-----KYDDGGLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGKAgTKVRLTLKRGD 73
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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