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Conserved domains on  [gi|1370451462|ref|XP_024304382|]
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inaD-like protein isoform X5 [Homo sapiens]

Protein Classification

L27_2 and PDZ_signaling domain-containing protein( domain architecture ID 13154871)

protein containing domains L27_2, CtpA, and PDZ_signaling

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. ...
1811-1895 1.93e-22

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: 93.02  E-value: 1.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1811 PKIITLEKG-SEGLGFSIVGGYGSphgDLPIYVKTVFAKGAAaDDGRLKRGDQILAVNGETLEGVTHEQAVAILKHQRGT 1889
Cdd:cd00992      1 VRTVTLRKDpGGGLGFSLRGGKDS---GGGIFVSRVEPGGPA-ERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                   ....*.
gi 1370451462 1890 VTLTVL 1895
Cdd:cd00992     77 VTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1688-1773 2.17e-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: 86.85  E-value: 2.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1688 PRTVEINRELSDALGISIAGGRGSplgDIPVFIAMIQASGVAARTqKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGR 1767
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGGKDS---GGGIFVSRVEPGGPAERG-GLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                   ....*.
gi 1370451462 1768 IILQVV 1773
Cdd:cd00992     77 VTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
246-325 2.90e-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: 86.47  E-value: 2.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  246 VEEVELI-NDGSGLGFGIVGGK--TSGVVVRTIVPGGLADRdGRLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRM 322
Cdd:cd00992      1 VRTVTLRkDPGGGLGFSLRGGKdsGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                   ...
gi 1370451462  323 LVA 325
Cdd:cd00992     80 TVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1066-1157 6.44e-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: 85.70  E-value: 6.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1066 PRIVEIFREPNVSLGISIVGGqtvikrlknGEELKGIFIKQVLEDSPAGKTNaLKTGDKILEVSGVDLQNASHSEAVEAI 1145
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGG---------KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELL 70
                           90
                   ....*....|..
gi 1370451462 1146 KNAGNPVVFIVQ 1157
Cdd:cd00992     71 KNSGDEVTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
135-218 4.96e-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: 80.30  E-value: 4.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  135 IDIERPSTGGLGFSVVALRSQNLGkvdIFVKDVQPGSVADRdQRLKENDQILAINHTPLdQNISHQQAIALLQQTTGSLR 214
Cdd:cd00992      4 VTLRKDPGGGLGFSLRGGKDSGGG---IFVSRVEPGGPAER-GGLRVGDRILEVNGVSV-EGLTHEEAVELLKNSGDEVT 78

                   ....
gi 1370451462  215 LIVA 218
Cdd:cd00992     79 LTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1545-1625 5.74e-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: 79.92  E-value: 5.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1545 IFPVDLQKKAGRGLGLSIVG-KRNGSGVFISDIVKGGAADLdGRLIQGDQILSVNGEDMRNASQETVATILKCAQGLVQL 1623
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGgKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                   ..
gi 1370451462 1624 EI 1625
Cdd:cd00992     80 TV 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1434-1533 8.29e-18

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: 79.73  E-value: 8.29e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1434 QEMIIEISKGRSGLGLSIVGGKDTPlfwrlgsprawsqhlNAIVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHE 1513
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEG---------------GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHL 64
                            90       100
                    ....*....|....*....|
gi 1370451462  1514 EAITALRQTPQKVRLVVYRD 1533
Cdd:smart00228   65 EAVDLLKKAGGKVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
366-450 1.26e-17

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: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  366 VELVRKDGQSLGIRIVGYVGtshtgEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFANHDVVEVLRNAGQVV 445
Cdd:cd00992      4 VTLRKDPGGGLGFSLRGGKD-----SGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                   ....*
gi 1370451462  446 HLTLV 450
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 ...
1236-1321 4.47e-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: 77.80  E-value: 4.47e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1236 ELHIIELEKDKNGLGLSLAGNKDrSRMSIFVVGINPEGPAAADGrMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVK 1315
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKD-EGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*.
gi 1370451462  1316 LVFIRN 1321
Cdd:smart00228   79 LTVLRG 84
L27_2 super family cl23017
L27_2; The L27_2 domain is a protein-protein interaction domain capable of organising scaffold ...
8-65 2.64e-15

L27_2; The L27_2 domain is a protein-protein interaction domain capable of organising scaffold proteins into supramolecular assemblies by formation of heteromeric L27_2 domain complexes. L27_2 domain-mediated protein assemblies have been shown to play essential roles in cellular processes including asymmetric cell division, establishment and maintenance of cell polarity, and clustering of receptors and ion channels. Members of this family form specific heterotetrameric complexes, in which each domain contains three alpha-helices. The two N-terminal helices of each L27_2 domain pack together to form a tight, four-helix bundle in the heterodimer, whilst the third helix of each L27_2 domain forms another four-helix bundle that assembles the two units of the heterodimer into a tetramer.


The actual alignment was detected with superfamily member pfam09045:

Pssm-ID: 312549  Cd Length: 58  Bit Score: 71.62  E-value: 2.64e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462    8 DKLQVLQVLDRLKMKLQEKGDTSQNEKLSMFYETLKSPLFNQILTLQQSIKQLKGQLN 65
Cdd:pfam09045    1 DKNRALQAAERLQAKLKERGDVANEDKLSLLKSVLQSPLFHQILALQKSLQHLKDQVN 58
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
683-772 2.71e-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: 67.02  E-value: 2.71e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   683 EVKIVELVKDCKGLGFSILDYQDPLDPtrsvIVIRSLVADGVAERSGgLLPGDRLVSVNEYCLDNTSLAEAVEILKAvPP 762
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEGGG----VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKK-AG 74
                            90
                    ....*....|
gi 1370451462   763 GLVHLGICKP 772
Cdd:smart00228   75 GKVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
570-634 7.08e-11

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: 59.89  E-value: 7.08e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462  570 LGVEV---DSFDGHHYISSIVSGGPVDtLGLLQPEDELLEVNGMQLYGKSRREAVSFLKEVPPPFTLV 634
Cdd:cd00992     14 LGFSLrggKDSGGGIFVSRVEPGGPAE-RGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLT 80
CtpA super family cl34043
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
391-513 2.26e-07

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


The actual alignment was detected with superfamily member COG0793:

Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 55.42  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  391 EASGIYVKSIIPGSAAYhNGHIQVNDKIVAVDGVNIQGFANHDVVEVLRN-AGQVVHLTLVRRKTSsstSPLEPPsdrgT 469
Cdd:COG0793    110 DIGGVKVVSPIDGSPAA-KAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTILRAGGG---KPFTVT----L 181
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370451462  470 VVEPLKPPALFLTGAVETETNVD-----------GEDEEIKERIDTLKNDNIQAL 513
Cdd:COG0793    182 TREEIELEDVAAKEKVEEGGKGRigyiripsfgeGTYEDLEKALDELKKQGAKGL 236
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1811-1895 1.93e-22

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: 93.02  E-value: 1.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1811 PKIITLEKG-SEGLGFSIVGGYGSphgDLPIYVKTVFAKGAAaDDGRLKRGDQILAVNGETLEGVTHEQAVAILKHQRGT 1889
Cdd:cd00992      1 VRTVTLRKDpGGGLGFSLRGGKDS---GGGIFVSRVEPGGPA-ERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                   ....*.
gi 1370451462 1890 VTLTVL 1895
Cdd:cd00992     77 VTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1811-1895 1.04e-20

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: 88.20  E-value: 1.04e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1811 PKIITLEKGSEGLGFSIVGGYGSPHGdlpIYVKTVFAKGAAADDGrLKRGDQILAVNGETLEGVTHEQAVAILKHQRGTV 1890
Cdd:smart00228    2 PRLVELEKGGGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                    ....*
gi 1370451462  1891 TLTVL 1895
Cdd:smart00228   78 TLTVL 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1688-1773 2.17e-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: 86.85  E-value: 2.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1688 PRTVEINRELSDALGISIAGGRGSplgDIPVFIAMIQASGVAARTqKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGR 1767
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGGKDS---GGGIFVSRVEPGGPAERG-GLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                   ....*.
gi 1370451462 1768 IILQVV 1773
Cdd:cd00992     77 VTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
246-325 2.90e-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: 86.47  E-value: 2.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  246 VEEVELI-NDGSGLGFGIVGGK--TSGVVVRTIVPGGLADRdGRLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRM 322
Cdd:cd00992      1 VRTVTLRkDPGGGLGFSLRGGKdsGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                   ...
gi 1370451462  323 LVA 325
Cdd:cd00992     80 TVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1066-1157 6.44e-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: 85.70  E-value: 6.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1066 PRIVEIFREPNVSLGISIVGGqtvikrlknGEELKGIFIKQVLEDSPAGKTNaLKTGDKILEVSGVDLQNASHSEAVEAI 1145
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGG---------KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELL 70
                           90
                   ....*....|..
gi 1370451462 1146 KNAGNPVVFIVQ 1157
Cdd:cd00992     71 KNSGDEVTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
248-328 6.60e-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: 82.81  E-value: 6.60e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   248 EVELINDGSGLGFGIVGGK--TSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRMLVA 325
Cdd:smart00228    4 LVELEKGGGGLGFSLVGGKdeGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82

                    ...
gi 1370451462   326 RDP 328
Cdd:smart00228   83 RGG 85
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
135-218 4.96e-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: 80.30  E-value: 4.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  135 IDIERPSTGGLGFSVVALRSQNLGkvdIFVKDVQPGSVADRdQRLKENDQILAINHTPLdQNISHQQAIALLQQTTGSLR 214
Cdd:cd00992      4 VTLRKDPGGGLGFSLRGGKDSGGG---IFVSRVEPGGPAER-GGLRVGDRILEVNGVSV-EGLTHEEAVELLKNSGDEVT 78

                   ....
gi 1370451462  215 LIVA 218
Cdd:cd00992     79 LTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1545-1625 5.74e-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: 79.92  E-value: 5.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1545 IFPVDLQKKAGRGLGLSIVG-KRNGSGVFISDIVKGGAADLdGRLIQGDQILSVNGEDMRNASQETVATILKCAQGLVQL 1623
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGgKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                   ..
gi 1370451462 1624 EI 1625
Cdd:cd00992     80 TV 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1434-1533 8.29e-18

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: 79.73  E-value: 8.29e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1434 QEMIIEISKGRSGLGLSIVGGKDTPlfwrlgsprawsqhlNAIVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHE 1513
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEG---------------GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHL 64
                            90       100
                    ....*....|....*....|
gi 1370451462  1514 EAITALRQTPQKVRLVVYRD 1533
Cdd:smart00228   65 EAVDLLKKAGGKVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
366-450 1.26e-17

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: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  366 VELVRKDGQSLGIRIVGYVGtshtgEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFANHDVVEVLRNAGQVV 445
Cdd:cd00992      4 VTLRKDPGGGLGFSLRGGKD-----SGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                   ....*
gi 1370451462  446 HLTLV 450
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 ...
1236-1321 4.47e-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: 77.80  E-value: 4.47e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1236 ELHIIELEKDKNGLGLSLAGNKDrSRMSIFVVGINPEGPAAADGrMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVK 1315
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKD-EGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*.
gi 1370451462  1316 LVFIRN 1321
Cdd:smart00228   79 LTVLRG 84
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
362-453 5.70e-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: 77.42  E-value: 5.70e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   362 ETYNVELvRKDGQSLGIRIVGYvgtshTGEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFANHDVVEVLRNA 441
Cdd:smart00228    1 EPRLVEL-EKGGGGLGFSLVGG-----KDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
                            90
                    ....*....|..
gi 1370451462   442 GQVVHLTLVRRK 453
Cdd:smart00228   74 GGKVTLTVLRGG 85
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1438-1530 5.71e-17

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: 77.22  E-value: 5.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1438 IEISKGRS-GLGLSIVGGKDtplfwrlgsprawsqHLNAIVIHEVYEEGAAARdGRLWAGDQILEVNGVDLRNSSHEEAI 1516
Cdd:cd00992      4 VTLRKDPGgGLGFSLRGGKD---------------SGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAV 67
                           90
                   ....*....|....
gi 1370451462 1517 TALRQTPQKVRLVV 1530
Cdd:cd00992     68 ELLKNSGDEVTLTV 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1066-1157 8.02e-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: 77.03  E-value: 8.02e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1066 PRIVEIFREPNvSLGISIVGGQtvikrlkngEELKGIFIKQVLEDSPAGKTNaLKTGDKILEVSGVDLQNASHSEAVEAI 1145
Cdd:smart00228    2 PRLVELEKGGG-GLGFSLVGGK---------DEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLL 70
                            90
                    ....*....|..
gi 1370451462  1146 KNAGNPVVFIVQ 1157
Cdd:smart00228   71 KKAGGKVTLTVL 82
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1814-1895 7.70e-16

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: 73.85  E-value: 7.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1814 ITLEK-GSEGLGFSIVGGygSPHGDLPIYVKTVFAKGAAADDGrLKRGDQILAVNGETLEGVTHEQAVAILKHQRGTVTL 1892
Cdd:pfam00595    2 VTLEKdGRGGLGFSLKGG--SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTL 78

                   ...
gi 1370451462 1893 TVL 1895
Cdd:pfam00595   79 TIL 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1237-1317 8.57e-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: 73.76  E-value: 8.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1237 LHIIELEKDKN-GLGLSLAGNKDrSRMSIFVVGINPEGPAAAdGRMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVK 1315
Cdd:cd00992      1 VRTVTLRKDPGgGLGFSLRGGKD-SGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVT 78

                   ..
gi 1370451462 1316 LV 1317
Cdd:cd00992     79 LT 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1544-1627 9.07e-16

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: 73.95  E-value: 9.07e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1544 EIFPVDLQKKAGrGLGLSIVG-KRNGSGVFISDIVKGGAADLDGrLIQGDQILSVNGEDMRNASQETVATILKCAQGLVQ 1622
Cdd:smart00228    1 EPRLVELEKGGG-GLGFSLVGgKDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*
gi 1370451462  1623 LEIGR 1627
Cdd:smart00228   79 LTVLR 83
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1687-1775 1.03e-15

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: 73.95  E-value: 1.03e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1687 EPRTVEINRElSDALGISIAGGRGSPLGdipVFIAMIQASGVAARTQkLKVGDRIVSINGQPLDGLSHADVVNLLKNAYG 1766
Cdd:smart00228    1 EPRLVELEKG-GGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGG 75

                    ....*....
gi 1370451462  1767 RIILQVVAD 1775
Cdd:smart00228   76 KVTLTVLRG 84
L27_2 pfam09045
L27_2; The L27_2 domain is a protein-protein interaction domain capable of organising scaffold ...
8-65 2.64e-15

L27_2; The L27_2 domain is a protein-protein interaction domain capable of organising scaffold proteins into supramolecular assemblies by formation of heteromeric L27_2 domain complexes. L27_2 domain-mediated protein assemblies have been shown to play essential roles in cellular processes including asymmetric cell division, establishment and maintenance of cell polarity, and clustering of receptors and ion channels. Members of this family form specific heterotetrameric complexes, in which each domain contains three alpha-helices. The two N-terminal helices of each L27_2 domain pack together to form a tight, four-helix bundle in the heterodimer, whilst the third helix of each L27_2 domain forms another four-helix bundle that assembles the two units of the heterodimer into a tetramer.


Pssm-ID: 312549  Cd Length: 58  Bit Score: 71.62  E-value: 2.64e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462    8 DKLQVLQVLDRLKMKLQEKGDTSQNEKLSMFYETLKSPLFNQILTLQQSIKQLKGQLN 65
Cdd:pfam09045    1 DKNRALQAAERLQAKLKERGDVANEDKLSLLKSVLQSPLFHQILALQKSLQHLKDQVN 58
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
131-221 1.35e-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: 70.49  E-value: 1.35e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   131 QIEYIDIERpSTGGLGFSVVALRSQNLGkvdIFVKDVQPGSVADRDQrLKENDQILAINHTPLdQNISHQQAIALLQQTT 210
Cdd:smart00228    1 EPRLVELEK-GGGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSV-EGLTHLEAVDLLKKAG 74
                            90
                    ....*....|.
gi 1370451462   211 GSLRLIVAREP 221
Cdd:smart00228   75 GKVTLTVLRGG 85
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1437-1530 1.64e-13

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: 67.31  E-value: 1.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1437 IIEISKGRSGLGLSIVGGKDtplfwrlgsprawsQHLNAIVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHEEAI 1516
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSD--------------QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAV 66
                           90
                   ....*....|....
gi 1370451462 1517 TALRQTPQKVRLVV 1530
Cdd:pfam00595   67 LALKGSGGKVTLTI 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
683-772 2.71e-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: 67.02  E-value: 2.71e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   683 EVKIVELVKDCKGLGFSILDYQDPLDPtrsvIVIRSLVADGVAERSGgLLPGDRLVSVNEYCLDNTSLAEAVEILKAvPP 762
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEGGG----VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKK-AG 74
                            90
                    ....*....|
gi 1370451462   763 GLVHLGICKP 772
Cdd:smart00228   75 GKVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
684-765 3.61e-13

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: 66.44  E-value: 3.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  684 VKIVELVKDC-KGLGFSILDYQDPLDPtrsvIVIRSLVADGVAERsGGLLPGDRLVSVNEYCLDNTSLAEAVEILKAVPP 762
Cdd:cd00992      1 VRTVTLRKDPgGGLGFSLRGGKDSGGG----IFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGD 75

                   ...
gi 1370451462  763 GLV 765
Cdd:cd00992     76 EVT 78
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
366-449 6.30e-13

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: 65.77  E-value: 6.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  366 VELVRKDGQSLGIRIVGYVGtshtGEASGIYVKSIIPGSAAyHNGHIQVNDKIVAVDGVNIQGFANHDVVEVLRNAGQVV 445
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSD----QGDPGIFVSEVLPGGAA-EAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKV 76

                   ....
gi 1370451462  446 HLTL 449
Cdd:pfam00595   77 TLTI 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1548-1625 7.97e-13

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: 65.38  E-value: 7.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1548 VDLQKKAGRGLGLSIVGKRNGS--GVFISDIVKGGAADLDGrlIQ-GDQILSVNGEDMRNASQETVATILKCAQGLVQLE 1624
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSDQGdpGIFVSEVLPGGAAEAGG--LKvGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   .
gi 1370451462 1625 I 1625
Cdd:pfam00595   80 I 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1069-1157 9.78e-13

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: 65.38  E-value: 9.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1069 VEIFREPNVSLGISIVGGQtvikrlknGEELKGIFIKQVLEDSPAgKTNALKTGDKILEVSGVDLQNASHSEAVEAIKNA 1148
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGS--------DQGDPGIFVSEVLPGGAA-EAGGLKVGDRILSINGQDVENMTHEEAVLALKGS 72

                   ....*....
gi 1370451462 1149 GNPVVFIVQ 1157
Cdd:pfam00595   73 GGKVTLTIL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1690-1772 5.44e-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: 5.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1690 TVEINRELSDALGISIAGGrgSPLGDIPVFIAMIQAsGVAARTQKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRII 1769
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGG--SDQGDPGIFVSEVLP-GGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVT 77

                   ...
gi 1370451462 1770 LQV 1772
Cdd:pfam00595   78 LTI 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
135-218 8.61e-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: 62.68  E-value: 8.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  135 IDIERPSTGGLGFSVVAlrSQNLGKVDIFVKDVQPGSVADRDQrLKENDQILAINHTPLDqNISHQQAIALLQQTTGSLR 214
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKG--GSDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVE-NMTHEEAVLALKGSGGKVT 77

                   ....
gi 1370451462  215 LIVA 218
Cdd:pfam00595   78 LTIL 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
570-634 7.08e-11

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: 59.89  E-value: 7.08e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462  570 LGVEV---DSFDGHHYISSIVSGGPVDtLGLLQPEDELLEVNGMQLYGKSRREAVSFLKEVPPPFTLV 634
Cdd:cd00992     14 LGFSLrggKDSGGGIFVSRVEPGGPAE-RGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLT 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
255-325 9.05e-11

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: 59.60  E-value: 9.05e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451462  255 GSGLGFGIVGG---KTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRMLVA 325
Cdd:pfam00595    9 RGGLGFSLKGGsdqGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1240-1317 1.10e-10

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: 59.22  E-value: 1.10e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451462 1240 IELEKDKNG-LGLSLAGNKDRSRMSIFVVGINPEGPAAADGrMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVKLV 1317
Cdd:pfam00595    2 VTLEKDGRGgLGFSLKGGSDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
563-638 2.63e-09

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: 55.46  E-value: 2.63e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451462   563 LPIHTLRLGVEV---DSFDGHHYISSIVSGGPVDTLGLlQPEDELLEVNGMQLYGKSRREAVSFLKEVPPPFTLVCCRR 638
Cdd:smart00228    7 LEKGGGGLGFSLvggKDEGGGVVVSSVVPGSPAAKAGL-RVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRG 84
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
391-513 2.26e-07

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: 55.42  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  391 EASGIYVKSIIPGSAAYhNGHIQVNDKIVAVDGVNIQGFANHDVVEVLRN-AGQVVHLTLVRRKTSsstSPLEPPsdrgT 469
Cdd:COG0793    110 DIGGVKVVSPIDGSPAA-KAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTILRAGGG---KPFTVT----L 181
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370451462  470 VVEPLKPPALFLTGAVETETNVD-----------GEDEEIKERIDTLKNDNIQAL 513
Cdd:COG0793    182 TREEIELEDVAAKEKVEEGGKGRigyiripsfgeGTYEDLEKALDELKKQGAKGL 236
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1533-1627 1.36e-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: 52.72  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1533 DEAH--YRDEENLEIFPVDLQKKAGrGLGLSIVgKRNGSGVFISDIVKGGAADLDGrlIQ-GDQILSVNGEDMRNASQET 1609
Cdd:COG0793     76 GDPHstYLDPEDAAEFRTDTSGEFG-GIGIELQ-MEDIGGVKVVSPIDGSPAAKAG--IKpGDVIIKIDGKSVGGVSLDE 151
                           90
                   ....*....|....*....
gi 1370451462 1610 VATILKCAQG-LVQLEIGR 1627
Cdd:COG0793    152 AVKLIRGKPGtKVTLTILR 170
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
11-68 3.71e-06

domain in receptor targeting proteins Lin-2 and Lin-7;


Pssm-ID: 197794  Cd Length: 53  Bit Score: 45.58  E-value: 3.71e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462    11 QVLQVLDRLKMKLQekgdtsQNEKLSMFYETLKSPLFNQILTLQQSIKQLKGQLNHIP 68
Cdd:smart00569    2 RLLELLEELQSLLS------PSEDLQELRRLLQSPHLQALLKIHDKVAETELDPPLPE 53
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
256-330 6.35e-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: 50.79  E-value: 6.35e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451462  256 SGLGFGIVGGKTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRN-CGNSVRMLVARDPAG 330
Cdd:COG0793    100 GGIGIELQMEDIGGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTILRAGGG 174
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
693-769 2.41e-05

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: 44.19  E-value: 2.41e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462  693 CKGLGFSILDYQDPLDPTrsvIVIRSLVADGVAERsGGLLPGDRLVSVNEYCLDNTSLAEAVEILKAvPPGLVHLGI 769
Cdd:pfam00595    9 RGGLGFSLKGGSDQGDPG---IFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKG-SGGKVTLTI 80
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
255-358 6.62e-05

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 47.42  E-value: 6.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  255 GSGLGFGI-VGGKTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRN-CGNSVRMLVARDPA-GD 331
Cdd:PLN00049    88 GLEVGYPTgSDGPPAGLVVVAPAPGGPAARAG-IRPGDVILAIDGTSTEGLSLYEAADRLQGpEGSSVELTLRRGPEtRL 166
                           90       100
                   ....*....|....*....|....*..
gi 1370451462  332 ISVTPPAPAALPVALPTVASKGPGSDS 358
Cdd:PLN00049   167 VTLTREKVSLNPVKSRLCEVPGPGAGS 193
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
1478-1605 9.10e-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: 47.22  E-value: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1478 IHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSH-EEAITALRqtP-QKVRLVVYRDEA---------HYRDEEN---- 1542
Cdd:TIGR02037  261 VAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADlRRAIGTLK--PgKKVTLGILRKGKektitvtlgASPEEQAsssn 337
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451462 1543 --LEIFPVDLQKKAGRGLGLsivgKRNGSGVFISDIVKGGAADLDGrLIQGDQILSVNGEDMRNA 1605
Cdd:TIGR02037  338 pfLGLTVANLSPEIRKELRL----KGDVKGVVVTKVVSGSPAARAG-LQPGDVILSVNQQPVSSV 397
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1434-1533 1.74e-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: 46.17  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1434 QEMIIEISKGRSGLGLSIVGGKDtplfwrlgsprawsqhlNAIVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHE 1513
Cdd:COG0793     89 AEFRTDTSGEFGGIGIELQMEDI-----------------GGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLD 150
                           90       100
                   ....*....|....*....|.
gi 1370451462 1514 EAITALRQTP-QKVRLVVYRD 1533
Cdd:COG0793    151 EAVKLIRGKPgTKVTLTILRA 171
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
381-455 1.25e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 43.19  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  381 VGYvGTSHTGEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVN------------IQGFANHDVVEVLRNAGQVVHLT 448
Cdd:PLN00049    91 VGY-PTGSDGPPAGLVVVAPAPGGPAARAG-IRPGDVILAIDGTSteglslyeaadrLQGPEGSSVELTLRRGPETRLVT 168

                   ....*..
gi 1370451462  449 LVRRKTS 455
Cdd:PLN00049   169 LTREKVS 175
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1840-1895 1.43e-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: 43.09  E-value: 1.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462 1840 IYVKTVFAKGAAADDGrLKRGDQILAVNGETLEGVTHEQAVAILKHQRGT-VTLTVL 1895
Cdd:COG0793    114 VKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRGKPGTkVTLTIL 169
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1811-1895 1.93e-22

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: 93.02  E-value: 1.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1811 PKIITLEKG-SEGLGFSIVGGYGSphgDLPIYVKTVFAKGAAaDDGRLKRGDQILAVNGETLEGVTHEQAVAILKHQRGT 1889
Cdd:cd00992      1 VRTVTLRKDpGGGLGFSLRGGKDS---GGGIFVSRVEPGGPA-ERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                   ....*.
gi 1370451462 1890 VTLTVL 1895
Cdd:cd00992     77 VTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1811-1895 1.04e-20

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: 88.20  E-value: 1.04e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1811 PKIITLEKGSEGLGFSIVGGYGSPHGdlpIYVKTVFAKGAAADDGrLKRGDQILAVNGETLEGVTHEQAVAILKHQRGTV 1890
Cdd:smart00228    2 PRLVELEKGGGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                    ....*
gi 1370451462  1891 TLTVL 1895
Cdd:smart00228   78 TLTVL 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1688-1773 2.17e-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: 86.85  E-value: 2.17e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1688 PRTVEINRELSDALGISIAGGRGSplgDIPVFIAMIQASGVAARTqKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGR 1767
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGGKDS---GGGIFVSRVEPGGPAERG-GLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDE 76

                   ....*.
gi 1370451462 1768 IILQVV 1773
Cdd:cd00992     77 VTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
246-325 2.90e-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: 86.47  E-value: 2.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  246 VEEVELI-NDGSGLGFGIVGGK--TSGVVVRTIVPGGLADRdGRLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRM 322
Cdd:cd00992      1 VRTVTLRkDPGGGLGFSLRGGKdsGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                   ...
gi 1370451462  323 LVA 325
Cdd:cd00992     80 TVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1066-1157 6.44e-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: 85.70  E-value: 6.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1066 PRIVEIFREPNVSLGISIVGGqtvikrlknGEELKGIFIKQVLEDSPAGKTNaLKTGDKILEVSGVDLQNASHSEAVEAI 1145
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGG---------KDSGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELL 70
                           90
                   ....*....|..
gi 1370451462 1146 KNAGNPVVFIVQ 1157
Cdd:cd00992     71 KNSGDEVTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
248-328 6.60e-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: 82.81  E-value: 6.60e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   248 EVELINDGSGLGFGIVGGK--TSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRMLVA 325
Cdd:smart00228    4 LVELEKGGGGLGFSLVGGKdeGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82

                    ...
gi 1370451462   326 RDP 328
Cdd:smart00228   83 RGG 85
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
135-218 4.96e-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: 80.30  E-value: 4.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  135 IDIERPSTGGLGFSVVALRSQNLGkvdIFVKDVQPGSVADRdQRLKENDQILAINHTPLdQNISHQQAIALLQQTTGSLR 214
Cdd:cd00992      4 VTLRKDPGGGLGFSLRGGKDSGGG---IFVSRVEPGGPAER-GGLRVGDRILEVNGVSV-EGLTHEEAVELLKNSGDEVT 78

                   ....
gi 1370451462  215 LIVA 218
Cdd:cd00992     79 LTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1545-1625 5.74e-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: 79.92  E-value: 5.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1545 IFPVDLQKKAGRGLGLSIVG-KRNGSGVFISDIVKGGAADLdGRLIQGDQILSVNGEDMRNASQETVATILKCAQGLVQL 1623
Cdd:cd00992      1 VRTVTLRKDPGGGLGFSLRGgKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTL 79

                   ..
gi 1370451462 1624 EI 1625
Cdd:cd00992     80 TV 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1434-1533 8.29e-18

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: 79.73  E-value: 8.29e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1434 QEMIIEISKGRSGLGLSIVGGKDTPlfwrlgsprawsqhlNAIVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHE 1513
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEG---------------GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHL 64
                            90       100
                    ....*....|....*....|
gi 1370451462  1514 EAITALRQTPQKVRLVVYRD 1533
Cdd:smart00228   65 EAVDLLKKAGGKVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
366-450 1.26e-17

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: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  366 VELVRKDGQSLGIRIVGYVGtshtgEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFANHDVVEVLRNAGQVV 445
Cdd:cd00992      4 VTLRKDPGGGLGFSLRGGKD-----SGGGIFVSRVEPGGPAERGG-LRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEV 77

                   ....*
gi 1370451462  446 HLTLV 450
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 ...
1236-1321 4.47e-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: 77.80  E-value: 4.47e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1236 ELHIIELEKDKNGLGLSLAGNKDrSRMSIFVVGINPEGPAAADGrMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVK 1315
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKD-EGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*.
gi 1370451462  1316 LVFIRN 1321
Cdd:smart00228   79 LTVLRG 84
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
362-453 5.70e-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: 77.42  E-value: 5.70e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   362 ETYNVELvRKDGQSLGIRIVGYvgtshTGEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFANHDVVEVLRNA 441
Cdd:smart00228    1 EPRLVEL-EKGGGGLGFSLVGG-----KDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
                            90
                    ....*....|..
gi 1370451462   442 GQVVHLTLVRRK 453
Cdd:smart00228   74 GGKVTLTVLRGG 85
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1438-1530 5.71e-17

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: 77.22  E-value: 5.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1438 IEISKGRS-GLGLSIVGGKDtplfwrlgsprawsqHLNAIVIHEVYEEGAAARdGRLWAGDQILEVNGVDLRNSSHEEAI 1516
Cdd:cd00992      4 VTLRKDPGgGLGFSLRGGKD---------------SGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAV 67
                           90
                   ....*....|....
gi 1370451462 1517 TALRQTPQKVRLVV 1530
Cdd:cd00992     68 ELLKNSGDEVTLTV 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1066-1157 8.02e-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: 77.03  E-value: 8.02e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1066 PRIVEIFREPNvSLGISIVGGQtvikrlkngEELKGIFIKQVLEDSPAGKTNaLKTGDKILEVSGVDLQNASHSEAVEAI 1145
Cdd:smart00228    2 PRLVELEKGGG-GLGFSLVGGK---------DEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLL 70
                            90
                    ....*....|..
gi 1370451462  1146 KNAGNPVVFIVQ 1157
Cdd:smart00228   71 KKAGGKVTLTVL 82
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1814-1895 7.70e-16

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: 73.85  E-value: 7.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1814 ITLEK-GSEGLGFSIVGGygSPHGDLPIYVKTVFAKGAAADDGrLKRGDQILAVNGETLEGVTHEQAVAILKHQRGTVTL 1892
Cdd:pfam00595    2 VTLEKdGRGGLGFSLKGG--SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTL 78

                   ...
gi 1370451462 1893 TVL 1895
Cdd:pfam00595   79 TIL 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
1237-1317 8.57e-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: 73.76  E-value: 8.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1237 LHIIELEKDKN-GLGLSLAGNKDrSRMSIFVVGINPEGPAAAdGRMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVK 1315
Cdd:cd00992      1 VRTVTLRKDPGgGLGFSLRGGKD-SGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVT 78

                   ..
gi 1370451462 1316 LV 1317
Cdd:cd00992     79 LT 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1544-1627 9.07e-16

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: 73.95  E-value: 9.07e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1544 EIFPVDLQKKAGrGLGLSIVG-KRNGSGVFISDIVKGGAADLDGrLIQGDQILSVNGEDMRNASQETVATILKCAQGLVQ 1622
Cdd:smart00228    1 EPRLVELEKGGG-GLGFSLVGgKDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                    ....*
gi 1370451462  1623 LEIGR 1627
Cdd:smart00228   79 LTVLR 83
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1687-1775 1.03e-15

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: 73.95  E-value: 1.03e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  1687 EPRTVEINRElSDALGISIAGGRGSPLGdipVFIAMIQASGVAARTQkLKVGDRIVSINGQPLDGLSHADVVNLLKNAYG 1766
Cdd:smart00228    1 EPRLVELEKG-GGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGG 75

                    ....*....
gi 1370451462  1767 RIILQVVAD 1775
Cdd:smart00228   76 KVTLTVLRG 84
L27_2 pfam09045
L27_2; The L27_2 domain is a protein-protein interaction domain capable of organising scaffold ...
8-65 2.64e-15

L27_2; The L27_2 domain is a protein-protein interaction domain capable of organising scaffold proteins into supramolecular assemblies by formation of heteromeric L27_2 domain complexes. L27_2 domain-mediated protein assemblies have been shown to play essential roles in cellular processes including asymmetric cell division, establishment and maintenance of cell polarity, and clustering of receptors and ion channels. Members of this family form specific heterotetrameric complexes, in which each domain contains three alpha-helices. The two N-terminal helices of each L27_2 domain pack together to form a tight, four-helix bundle in the heterodimer, whilst the third helix of each L27_2 domain forms another four-helix bundle that assembles the two units of the heterodimer into a tetramer.


Pssm-ID: 312549  Cd Length: 58  Bit Score: 71.62  E-value: 2.64e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462    8 DKLQVLQVLDRLKMKLQEKGDTSQNEKLSMFYETLKSPLFNQILTLQQSIKQLKGQLN 65
Cdd:pfam09045    1 DKNRALQAAERLQAKLKERGDVANEDKLSLLKSVLQSPLFHQILALQKSLQHLKDQVN 58
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
131-221 1.35e-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: 70.49  E-value: 1.35e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   131 QIEYIDIERpSTGGLGFSVVALRSQNLGkvdIFVKDVQPGSVADRDQrLKENDQILAINHTPLdQNISHQQAIALLQQTT 210
Cdd:smart00228    1 EPRLVELEK-GGGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSV-EGLTHLEAVDLLKKAG 74
                            90
                    ....*....|.
gi 1370451462   211 GSLRLIVAREP 221
Cdd:smart00228   75 GKVTLTVLRGG 85
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1437-1530 1.64e-13

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: 67.31  E-value: 1.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1437 IIEISKGRSGLGLSIVGGKDtplfwrlgsprawsQHLNAIVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHEEAI 1516
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSD--------------QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAV 66
                           90
                   ....*....|....
gi 1370451462 1517 TALRQTPQKVRLVV 1530
Cdd:pfam00595   67 LALKGSGGKVTLTI 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
683-772 2.71e-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: 67.02  E-value: 2.71e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462   683 EVKIVELVKDCKGLGFSILDYQDPLDPtrsvIVIRSLVADGVAERSGgLLPGDRLVSVNEYCLDNTSLAEAVEILKAvPP 762
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEGGG----VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKK-AG 74
                            90
                    ....*....|
gi 1370451462   763 GLVHLGICKP 772
Cdd:smart00228   75 GKVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
684-765 3.61e-13

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: 66.44  E-value: 3.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  684 VKIVELVKDC-KGLGFSILDYQDPLDPtrsvIVIRSLVADGVAERsGGLLPGDRLVSVNEYCLDNTSLAEAVEILKAVPP 762
Cdd:cd00992      1 VRTVTLRKDPgGGLGFSLRGGKDSGGG----IFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGD 75

                   ...
gi 1370451462  763 GLV 765
Cdd:cd00992     76 EVT 78
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
366-449 6.30e-13

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: 65.77  E-value: 6.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  366 VELVRKDGQSLGIRIVGYVGtshtGEASGIYVKSIIPGSAAyHNGHIQVNDKIVAVDGVNIQGFANHDVVEVLRNAGQVV 445
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSD----QGDPGIFVSEVLPGGAA-EAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKV 76

                   ....
gi 1370451462  446 HLTL 449
Cdd:pfam00595   77 TLTI 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1548-1625 7.97e-13

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: 65.38  E-value: 7.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1548 VDLQKKAGRGLGLSIVGKRNGS--GVFISDIVKGGAADLDGrlIQ-GDQILSVNGEDMRNASQETVATILKCAQGLVQLE 1624
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGSDQGdpGIFVSEVLPGGAAEAGG--LKvGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                   .
gi 1370451462 1625 I 1625
Cdd:pfam00595   80 I 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1069-1157 9.78e-13

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: 65.38  E-value: 9.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1069 VEIFREPNVSLGISIVGGQtvikrlknGEELKGIFIKQVLEDSPAgKTNALKTGDKILEVSGVDLQNASHSEAVEAIKNA 1148
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKGGS--------DQGDPGIFVSEVLPGGAA-EAGGLKVGDRILSINGQDVENMTHEEAVLALKGS 72

                   ....*....
gi 1370451462 1149 GNPVVFIVQ 1157
Cdd:pfam00595   73 GGKVTLTIL 81
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
256-324 1.56e-12

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: 64.25  E-value: 1.56e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  256 SGLGFGIVGGKTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRNC-GNSVRMLV 324
Cdd:cd00136      1 GGLGFSIRGGTEGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEvGEKVTLTV 69
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1690-1772 5.44e-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: 5.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1690 TVEINRELSDALGISIAGGrgSPLGDIPVFIAMIQAsGVAARTQKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRII 1769
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGG--SDQGDPGIFVSEVLP-GGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVT 77

                   ...
gi 1370451462 1770 LQV 1772
Cdd:pfam00595   78 LTI 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
135-218 8.61e-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: 62.68  E-value: 8.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  135 IDIERPSTGGLGFSVVAlrSQNLGKVDIFVKDVQPGSVADRDQrLKENDQILAINHTPLDqNISHQQAIALLQQTTGSLR 214
Cdd:pfam00595    2 VTLEKDGRGGLGFSLKG--GSDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVE-NMTHEEAVLALKGSGGKVT 77

                   ....
gi 1370451462  215 LIVA 218
Cdd:pfam00595   78 LTIL 81
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1822-1895 8.86e-12

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: 61.94  E-value: 8.86e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451462 1822 GLGFSIVGGygsphGDLPIYVKTVfAKGAAADDGRLKRGDQILAVNGETLEGVTHEQAVAILKHQRG-TVTLTVL 1895
Cdd:cd00136      2 GLGFSIRGG-----TEGGVVVLSV-EPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLKKEVGeKVTLTVR 70
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
570-634 7.08e-11

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: 59.89  E-value: 7.08e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462  570 LGVEV---DSFDGHHYISSIVSGGPVDtLGLLQPEDELLEVNGMQLYGKSRREAVSFLKEVPPPFTLV 634
Cdd:cd00992     14 LGFSLrggKDSGGGIFVSRVEPGGPAE-RGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLT 80
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
255-325 9.05e-11

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: 59.60  E-value: 9.05e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451462  255 GSGLGFGIVGG---KTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRMLVA 325
Cdd:pfam00595    9 RGGLGFSLKGGsdqGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
1240-1317 1.10e-10

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: 59.22  E-value: 1.10e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451462 1240 IELEKDKNG-LGLSLAGNKDRSRMSIFVVGINPEGPAAADGrMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVKLV 1317
Cdd:pfam00595    2 VTLEKDGRGgLGFSLKGGSDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
375-450 1.40e-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: 55.77  E-value: 1.40e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462  375 SLGIRIVGyvgtshtGEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFANHDVVEVLRNA-GQVVHLTLV 450
Cdd:cd00136      2 GLGFSIRG-------GTEGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEvGEKVTLTVR 70
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
563-638 2.63e-09

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: 55.46  E-value: 2.63e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451462   563 LPIHTLRLGVEV---DSFDGHHYISSIVSGGPVDTLGLlQPEDELLEVNGMQLYGKSRREAVSFLKEVPPPFTLVCCRR 638
Cdd:smart00228    7 LEKGGGGLGFSLvggKDEGGGVVVSSVVPGSPAAKAGL-RVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRG 84
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
255-335 2.46e-08

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: 53.00  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  255 GSGLGFGIVGGktsGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRN-CGNSVRMLVARDPAGDIS 333
Cdd:cd00988      3 GIGLELKYDDG---GLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGkAGTKVRLTLKRGDGEPRE 78

                   ..
gi 1370451462  334 VT 335
Cdd:cd00988     79 VT 80
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1556-1625 3.57e-08

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: 51.92  E-value: 3.57e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451462 1556 RGLGLSIVGKRNGsGVFISDIVKGGAADLDGrLIQGDQILSVNGEDMRNASQETVATILKCAQGL-VQLEI 1625
Cdd:cd00136      1 GGLGFSIRGGTEG-GVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEVGEkVTLTV 69
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1701-1773 8.04e-08

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: 50.77  E-value: 8.04e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451462 1701 LGISIAGGRGSPlgdipVFIAMIQASGVAARTqKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRII-LQVV 1773
Cdd:cd00136      3 LGFSIRGGTEGG-----VVVLSVEPGSPAERA-GLQAGDVILAVNGTDVKNLTLEDVAELLKKEVGEKVtLTVR 70
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1445-1531 1.64e-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: 50.00  E-value: 1.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1445 SGLGLSIVGGKDTPlfwrlgsprawsqhlnaIVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHEEAITALRQTP- 1523
Cdd:cd00136      1 GGLGFSIRGGTEGG-----------------VVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEVg 62

                   ....*...
gi 1370451462 1524 QKVRLVVY 1531
Cdd:cd00136     63 EKVTLTVR 70
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1078-1156 1.85e-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: 50.00  E-value: 1.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1078 SLGISIVGGqtvikrlkngeELKGIFIKQVLEDSPAGKtNALKTGDKILEVSGVDLQNASHSEAVEAIKNA-GNPVVFIV 1156
Cdd:cd00136      2 GLGFSIRGG-----------TEGGVVVLSVEPGSPAER-AGLQAGDVILAVNGTDVKNLTLEDVAELLKKEvGEKVTLTV 69
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
391-513 2.26e-07

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: 55.42  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  391 EASGIYVKSIIPGSAAYhNGHIQVNDKIVAVDGVNIQGFANHDVVEVLRN-AGQVVHLTLVRRKTSsstSPLEPPsdrgT 469
Cdd:COG0793    110 DIGGVKVVSPIDGSPAA-KAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTILRAGGG---KPFTVT----L 181
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370451462  470 VVEPLKPPALFLTGAVETETNVD-----------GEDEEIKERIDTLKNDNIQAL 513
Cdd:COG0793    182 TREEIELEDVAAKEKVEEGGKGRigyiripsfgeGTYEDLEKALDELKKQGAKGL 236
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
1718-1769 5.50e-07

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: 49.15  E-value: 5.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370451462 1718 VFIAMIQASGVAARTqKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRII 1769
Cdd:cd00988     15 LVITSVLPGSPAAKA-GIKAGDIIVAIDGEPVDGLSLEDVVKLLRGKAGTKV 65
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
396-451 1.08e-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: 47.14  E-value: 1.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462  396 YVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFanHDVVEVLR-NAGQVVHLTLVR 451
Cdd:pfam17820    1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSL--EDVARLLQgSAGESVTLTVRR 54
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
394-451 1.15e-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: 47.99  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451462  394 GIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFANHDVVEVLRN-AGQVVHLTLVR 451
Cdd:cd00988     14 GLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGkAGTKVRLTLKR 71
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1533-1627 1.36e-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: 52.72  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1533 DEAH--YRDEENLEIFPVDLQKKAGrGLGLSIVgKRNGSGVFISDIVKGGAADLDGrlIQ-GDQILSVNGEDMRNASQET 1609
Cdd:COG0793     76 GDPHstYLDPEDAAEFRTDTSGEFG-GIGIELQ-MEDIGGVKVVSPIDGSPAAKAG--IKpGDVIIKIDGKSVGGVSLDE 151
                           90
                   ....*....|....*....
gi 1370451462 1610 VATILKCAQG-LVQLEIGR 1627
Cdd:COG0793    152 AVKLIRGKPGtKVTLTILR 170
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
1557-1627 3.59e-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: 46.84  E-value: 3.59e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370451462 1557 GLGLSIvgKRNGSGVFISDIVKGGAADLDGrLIQGDQILSVNGEDMRNASQETVATILKCAQG-LVQLEIGR 1627
Cdd:cd00988      3 GIGLEL--KYDDGGLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGKAGtKVRLTLKR 71
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
11-68 3.71e-06

domain in receptor targeting proteins Lin-2 and Lin-7;


Pssm-ID: 197794  Cd Length: 53  Bit Score: 45.58  E-value: 3.71e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462    11 QVLQVLDRLKMKLQekgdtsQNEKLSMFYETLKSPLFNQILTLQQSIKQLKGQLNHIP 68
Cdd:smart00569    2 RLLELLEELQSLLS------PSEDLQELRRLLQSPHLQALLKIHDKVAETELDPPLPE 53
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
271-326 4.10e-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: 4.10e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462  271 VVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMtsEQVAQVLRNCGNS-VRMLVAR 326
Cdd:pfam17820    1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSL--EDVARLLQGSAGEsVTLTVRR 54
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
256-330 6.35e-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: 50.79  E-value: 6.35e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451462  256 SGLGFGIVGGKTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRN-CGNSVRMLVARDPAG 330
Cdd:COG0793    100 GGIGIELQMEDIGGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTILRAGGG 174
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
694-769 6.73e-06

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: 45.37  E-value: 6.73e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451462  694 KGLGFSILDYqdpldpTRSVIVIRSLVADGVAERsGGLLPGDRLVSVNEYCLDNTSLAEAVEILKAVPPGLVHLGI 769
Cdd:cd00136      1 GGLGFSIRGG------TEGGVVVLSVEPGSPAER-AGLQAGDVILAVNGTDVKNLTLEDVAELLKKEVGEKVTLTV 69
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
1840-1895 6.79e-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: 46.06  E-value: 6.79e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462 1840 IYVKTVFAKGAAADDGrLKRGDQILAVNGETLEGVTHEQAVAILKHQRGT-VTLTVL 1895
Cdd:cd00988     15 LVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGKAGTkVRLTLK 70
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
384-453 6.95e-06

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: 45.69  E-value: 6.95e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451462  384 VGTSHTGEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFAnhDVVEVLR-NAGQVVHLTLVRRK 453
Cdd:cd00989      3 LGFVPGGPPIEPVIGEVVPGSPAAKAG-LKAGDRILAINGQKIKSWE--DLVDAVQeNPGKPLTLTVERNG 70
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
143-211 1.61e-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: 1.61e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451462  143 GGLGFSVvalrsQNLGKVDIFVKDVQPGSVADRDQrLKENDQILAINHTPLdQNISHQQAIALLQQTTG 211
Cdd:cd00136      1 GGLGFSI-----RGGTEGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDV-KNLTLEDVAELLKKEVG 62
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
1247-1319 2.32e-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: 43.83  E-value: 2.32e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451462 1247 NGLGLSLAGNKDRSrmsIFVVGINPEGPAAADGrMRIGDELLEINNQILYGRSHQNASAIIKTAP-SKVKLVFI 1319
Cdd:cd00136      1 GGLGFSIRGGTEGG---VVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEVgEKVTLTVR 70
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
693-769 2.41e-05

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: 44.19  E-value: 2.41e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462  693 CKGLGFSILDYQDPLDPTrsvIVIRSLVADGVAERsGGLLPGDRLVSVNEYCLDNTSLAEAVEILKAvPPGLVHLGI 769
Cdd:pfam00595    9 RGGLGFSLKGGSDQGDPG---IFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKG-SGGKVTLTI 80
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
393-451 4.02e-05

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: 43.78  E-value: 4.02e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370451462  393 SGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVNIQGFAnhDVVEVLRN--AGQVVHLTLVR 451
Cdd:cd00987     24 KGVLVASVDPGSPAAKAG-LKPGDVILAVNGKPVKSVA--DLRRALAElkPGDKVTLTVLR 81
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
266-327 5.94e-05

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: 43.40  E-value: 5.94e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370451462  266 KTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQgmTSEQVAQVLRN--CGNSVRMLVARD 327
Cdd:cd00987     22 DTKGVLVASVDPGSPAAKAG-LKPGDVILAVNGKPVK--SVADLRRALAElkPGDKVTLTVLRG 82
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
255-358 6.62e-05

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 47.42  E-value: 6.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  255 GSGLGFGI-VGGKTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMTSEQVAQVLRN-CGNSVRMLVARDPA-GD 331
Cdd:PLN00049    88 GLEVGYPTgSDGPPAGLVVVAPAPGGPAARAG-IRPGDVILAIDGTSTEGLSLYEAADRLQGpEGSSVELTLRRGPEtRL 166
                           90       100
                   ....*....|....*....|....*..
gi 1370451462  332 ISVTPPAPAALPVALPTVASKGPGSDS 358
Cdd:PLN00049   167 VTLTREKVSLNPVKSRLCEVPGPGAGS 193
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
1476-1534 6.83e-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: 6.83e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1476 IVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHEEAITALRQTP-QKVRLVVYRDE 1534
Cdd:cd00988     15 LVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGKAgTKVRLTLKRGD 73
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
1478-1605 9.10e-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: 47.22  E-value: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1478 IHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSH-EEAITALRqtP-QKVRLVVYRDEA---------HYRDEEN---- 1542
Cdd:TIGR02037  261 VAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADlRRAIGTLK--PgKKVTLGILRKGKektitvtlgASPEEQAsssn 337
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370451462 1543 --LEIFPVDLQKKAGRGLGLsivgKRNGSGVFISDIVKGGAADLDGrLIQGDQILSVNGEDMRNA 1605
Cdd:TIGR02037  338 pfLGLTVANLSPEIRKELRL----KGDVKGVVVTKVVSGSPAARAG-LQPGDVILSVNQQPVSSV 397
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
1716-1769 1.39e-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: 41.84  E-value: 1.39e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370451462 1716 IPVFIAMIQASGVAARtQKLKVGDRIVSINGQPLDGLShaDVVNLLKNAYGRII 1769
Cdd:cd00989     12 IEPVIGEVVPGSPAAK-AGLKAGDRILAINGQKIKSWE--DLVDAVQENPGKPL 62
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
121-327 1.42e-04

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: 46.45  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  121 SVIQQMAQGRQIEYidierpstGGLGFSVVALRS---QNLGKVDI---FVKDVQPGSVADRdQRLKENDQILAINhtplD 194
Cdd:TIGR02037  220 NVVDQLIEGGKVKR--------GWLGVTIQEVTSdlaKSLGLEKQrgaLVAQVLPGSPAEK-AGLKAGDVITSVN----G 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  195 QNISHQqaiallqqttGSLRLIVAREPVHTKSSTSSSLNDTTLPETVCWGHVEEVELinDGSGLGFGIVG---------- 264
Cdd:TIGR02037  287 KPISSF----------ADLRRAIGTLKPGKKVTLGILRKGKEKTITVTLGASPEEQA--SSSNPFLGLTVanlspeirke 354
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451462  265 ----GKTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQgmTSEQVAQVLRNCGNS--VRMLVARD 327
Cdd:TIGR02037  355 lrlkGDVKGVVVTKVVSGSPAARAG-LQPGDVILSVNQQPVS--SVAELRKVLARAKKGgrVALLILRG 420
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1434-1533 1.74e-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: 46.17  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1434 QEMIIEISKGRSGLGLSIVGGKDtplfwrlgsprawsqhlNAIVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHE 1513
Cdd:COG0793     89 AEFRTDTSGEFGGIGIELQMEDI-----------------GGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLD 150
                           90       100
                   ....*....|....*....|.
gi 1370451462 1514 EAITALRQTP-QKVRLVVYRD 1533
Cdd:COG0793    151 EAVKLIRGKPgTKVTLTILRA 171
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
569-625 2.34e-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: 41.44  E-value: 2.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462  569 RLGVEVDSFDGHHYISSIVSGGPVDTLGlLQPEDELLEVNGMQLYGKSRREAVSFLK 625
Cdd:cd00988      3 GIGLELKYDDGGLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLR 58
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
1100-1152 3.30e-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: 41.06  E-value: 3.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1370451462 1100 KGIFIKQVLEDSPAGKTnALKTGDKILEVSGVDLQNASHSEAVEAIKN-AGNPV 1152
Cdd:cd00988     13 GGLVITSVLPGSPAAKA-GIKAGDIIVAIDGEPVDGLSLEDVVKLLRGkAGTKV 65
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
163-219 4.32e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 39.82  E-value: 4.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462  163 FVKDVQPGSVADRdQRLKENDQILAINHTPLDqniSHQQAIALLQQTTGS-LRLIVAR 219
Cdd:pfam17820    1 VVTAVVPGSPAER-AGLRVGDVILAVNGKPVR---SLEDVARLLQGSAGEsVTLTVRR 54
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
1476-1533 5.46e-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: 40.70  E-value: 5.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370451462 1476 IVIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSSHEEAITALRQTPQKVRLVVYRD 1533
Cdd:cd00987     26 VLVASVDPGSPAAKAG-LKPGDVILAVNGKPVKSVADLRRALAELKPGDKVTLTVLRG 82
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
1079-1157 5.96e-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: 40.70  E-value: 5.96e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370451462 1079 LGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTNaLKTGDKILEVSGVDLQNASHSEAVEAIKNAGNPVVFIVQ 1157
Cdd:cd00987      3 LGVTVQDLTPDLAEELGLKDTKGVLVASVDPGSPAAKAG-LKPGDVILAVNGKPVKSVADLRRALAELKPGDKVTLTVL 80
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
1822-1895 1.03e-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: 39.52  E-value: 1.03e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451462 1822 GLGFSIVGGYGSPhgdlpiYVKTVFAKGAAADDGrLKRGDQILAVNGETlegVTHEQAV--AILKHQRGTVTLTVL 1895
Cdd:cd00989      2 ILGFVPGGPPIEP------VIGEVVPGSPAAKAG-LKAGDRILAINGQK---IKSWEDLvdAVQENPGKPLTLTVE 67
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
381-455 1.25e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 43.19  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462  381 VGYvGTSHTGEASGIYVKSIIPGSAAYHNGhIQVNDKIVAVDGVN------------IQGFANHDVVEVLRNAGQVVHLT 448
Cdd:PLN00049    91 VGY-PTGSDGPPAGLVVVAPAPGGPAARAG-IRPGDVILAIDGTSteglslyeaadrLQGPEGSSVELTLRRGPETRLVT 168

                   ....*..
gi 1370451462  449 LVRRKTS 455
Cdd:PLN00049   169 LTREKVS 175
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1840-1895 1.43e-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: 43.09  E-value: 1.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462 1840 IYVKTVFAKGAAADDGrLKRGDQILAVNGETLEGVTHEQAVAILKHQRGT-VTLTVL 1895
Cdd:COG0793    114 VKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRGKPGTkVTLTIL 169
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
1841-1894 1.77e-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: 38.28  E-value: 1.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370451462 1841 YVKTVFAKGAAADDGrLKRGDQILAVNGETLEGVthEQAVAILKHQRGT-VTLTV 1894
Cdd:pfam17820    1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSL--EDVARLLQGSAGEsVTLTV 52
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
256-327 2.51e-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: 2.51e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370451462  256 SGLGFgIVGGKTSGVVVRTIVPGGLADRDGrLQTGDHILKIGGTNVQGMtSEQVAQVLRNCGNSVRMLVARD 327
Cdd:cd00989      1 AILGF-VPGGPPIEPVIGEVVPGSPAAKAG-LKAGDRILAINGQKIKSW-EDLVDAVQENPGKPLTLTVERN 69
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
1477-1532 3.10e-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: 3.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370451462 1477 VIHEVYEEGAAARDGrLWAGDQILEVNGVDLRNSshEEAITALRQ-TPQKVRLVVYR 1532
Cdd:pfam17820    1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSL--EDVARLLQGsAGESVTLTVRR 54
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
1248-1322 3.63e-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: 38.36  E-value: 3.63e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451462 1248 GLGLSLAGNKDRsrmsIFVVGINPEGPAAADGrMRIGDELLEINNQILYGRSHQNASAIIK-TAPSKVKLVFIRNE 1322
Cdd:cd00988      3 GIGLELKYDDGG----LVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRgKAGTKVRLTLKRGD 73
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
1719-1774 4.42e-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: 37.12  E-value: 4.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451462 1719 FIAMIQASGVAARtQKLKVGDRIVSINGQPLDGLshADVVNLLKNAYGRIILQVVA 1774
Cdd:pfam17820    1 VVTAVVPGSPAER-AGLRVGDVILAVNGKPVRSL--EDVARLLQGSAGESVTLTVR 53
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
1569-1764 4.89e-03

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: 41.44  E-value: 4.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1569 SGVFISDIVKGGAADLDGrLIQGDQILSVNGEDMRNASQ--ETVATiLKCAQGlVQLEIgrLRAGswtsarttsqnsqgs 1646
Cdd:TIGR02037  257 RGALVAQVLPGSPAEKAG-LKAGDVITSVNGKPISSFADlrRAIGT-LKPGKK-VTLGI--LRKG--------------- 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370451462 1647 qqsahsscHPSFAPVITGlqnlvgtkrvSDPSQKNSGTDMEPR------TVEINRELSDAlgisiAGGRGsplgdipVFI 1720
Cdd:TIGR02037  317 --------KEKTITVTLG----------ASPEEQASSSNPFLGltvanlSPEIRKELRLK-----GDVKG-------VVV 366
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1370451462 1721 AMIQASGVAARTqKLKVGDRIVSINGQPLDglSHADVVNLLKNA 1764
Cdd:TIGR02037  367 TKVVSGSPAARA-GLQPGDVILSVNQQPVS--SVAELRKVLARA 407
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
715-769 5.02e-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: 36.74  E-value: 5.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370451462  715 VIRSLVADGVAERsGGLLPGDRLVSVN-EYCldnTSLAEAVEILKAVPPGLVHLGI 769
Cdd:pfam17820    1 VVTAVVPGSPAER-AGLRVGDVILAVNgKPV---RSLEDVARLLQGSAGESVTLTV 52
 
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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