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Conserved domains on  [gi|296278259|ref|NP_001171716|]
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partitioning defective 3 homolog isoform 4 [Homo sapiens]

Protein Classification

partitioning defective 3 homolog( domain architecture ID 10572431)

partitioning defective 3 homolog is a PDZ (PSD-95, Dlg, and ZO-1/2) domain-containing protein that functions as an adapter protein involved in asymmetrical cell division and cell polarization processes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF3534 pfam12053
N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. ...
2-83 2.60e-49

N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 150 amino acids in length. This eukaryotic domain is found associated with pfam00595. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament.


:

Pssm-ID: 432291  Cd Length: 82  Bit Score: 169.06  E-value: 2.60e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259     2 KVTVCFGRTRVVVPCGDGHMKVFSLIQQAVTRYRKAIAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRLVAVFDE 81
Cdd:pfam12053    1 KVTVCFGRTRVVVPCGDGDLTVRDLIQQATQRYRKATEKDPGYWVKVHHLEYSDGGILDPDDILNDVVDDRDKLIAVYDE 80

                   ..
gi 296278259    82 QD 83
Cdd:pfam12053   81 QD 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
465-544 3.53e-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: 3.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  465 KKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAiQDGRLKAGDRLIEVNGVDLVGKSQEEVVSLLRSTKmeGTVSLLV 544
Cdd:cd00992     8 KDPGGGLGFSLRGGKDSGGG---IFVSRVEPGGPA-ERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG--DEVTLTV 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
588-681 5.92e-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: 5.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  588 TFEVPLNDSGSAGLGVSVKGNRSKenhaDLGIFVKSIINGGAASKdGRLRVNDQLIAVNGESLLGKTNQDAMETLRRSms 667
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGKDS----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNS-- 73
                          90
                  ....*....|....
gi 296278259  668 tegnkRGMIQLIVA 681
Cdd:cd00992    74 -----GDEVTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
272-347 5.14e-10

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: 57.19  E-value: 5.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278259  272 VKLVEVP-NDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEHENLfRENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:cd00992     1 VRTVTLRkDPGGGLGFSLR---GGKDSGGGIFVSRVEPGGPAERGGL-RVGDRILEVNGVSVEGLTHEEAVELLKNS 73
 
Name Accession Description Interval E-value
DUF3534 pfam12053
N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. ...
2-83 2.60e-49

N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 150 amino acids in length. This eukaryotic domain is found associated with pfam00595. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament.


Pssm-ID: 432291  Cd Length: 82  Bit Score: 169.06  E-value: 2.60e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259     2 KVTVCFGRTRVVVPCGDGHMKVFSLIQQAVTRYRKAIAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRLVAVFDE 81
Cdd:pfam12053    1 KVTVCFGRTRVVVPCGDGDLTVRDLIQQATQRYRKATEKDPGYWVKVHHLEYSDGGILDPDDILNDVVDDRDKLIAVYDE 80

                   ..
gi 296278259    82 QD 83
Cdd:pfam12053   81 QD 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
465-544 3.53e-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: 3.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  465 KKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAiQDGRLKAGDRLIEVNGVDLVGKSQEEVVSLLRSTKmeGTVSLLV 544
Cdd:cd00992     8 KDPGGGLGFSLRGGKDSGGG---IFVSRVEPGGPA-ERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG--DEVTLTV 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
458-547 1.61e-17

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 78.57  E-value: 1.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259    458 KRLNIQLKKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLVGKSQEEVVSLLRSTKme 537
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAG-- 74
                            90
                    ....*....|
gi 296278259    538 GTVSLLVFRQ 547
Cdd:smart00228   75 GKVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
588-681 5.92e-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: 5.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  588 TFEVPLNDSGSAGLGVSVKGNRSKenhaDLGIFVKSIINGGAASKdGRLRVNDQLIAVNGESLLGKTNQDAMETLRRSms 667
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGKDS----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNS-- 73
                          90
                  ....*....|....
gi 296278259  668 tegnkRGMIQLIVA 681
Cdd:cd00992    74 -----GDEVTLTVR 82
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
462-544 1.94e-14

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: 69.62  E-value: 1.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259   462 IQLKK-GTEGLGFSITSRDvtIGGSAPIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLVGKSQEEVVSLLRSTKmeGTV 540
Cdd:pfam00595    2 VTLEKdGRGGLGFSLKGGS--DQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSG--GKV 76

                   ....
gi 296278259   541 SLLV 544
Cdd:pfam00595   77 TLTI 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
597-683 6.23e-14

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 68.17  E-value: 6.23e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259    597 GSAGLGVSVKGNRSKENhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKTNQDAMETLRRSmstegnkRGMI 676
Cdd:smart00228   10 GGGGLGFSLVGGKDEGG----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKA-------GGKV 77

                    ....*..
gi 296278259    677 QLIVARR 683
Cdd:smart00228   78 TLTVLRG 84
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
590-681 8.71e-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: 59.22  E-value: 8.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259   590 EVPLNDSGSAGLGVSVKGNRSKENHadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKTNQDAMETLRrsmste 669
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSDQGDP---GIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALK------ 70
                           90
                   ....*....|..
gi 296278259   670 gNKRGMIQLIVA 681
Cdd:pfam00595   71 -GSGGKVTLTIL 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
272-347 5.14e-10

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: 57.19  E-value: 5.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278259  272 VKLVEVP-NDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEHENLfRENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:cd00992     1 VRTVTLRkDPGGGLGFSLR---GGKDSGGGIFVSRVEPGGPAERGGL-RVGDRILEVNGVSVEGLTHEEAVELLKNS 73
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
271-347 1.64e-07

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: 50.07  E-value: 1.64e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278259    271 MVKLVEVPNDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEHENLfRENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLV---GGKDEGGGVVVSSVVPGSPAAKAGL-RVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
449-547 2.54e-06

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 51.56  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  449 SGYNTKKIGKRLNIQLKKGTEGLGFSITSRDvtIGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLVGKSQEEVV 528
Cdd:COG0793    80 STYLDPEDAAEFRTDTSGEFGGIGIELQMED--IGG---VKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAV 153
                          90       100
                  ....*....|....*....|
gi 296278259  529 SLLRSTKmeGT-VSLLVFRQ 547
Cdd:COG0793   154 KLIRGKP--GTkVTLTILRA 171
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
281-347 3.02e-03

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: 38.03  E-value: 3.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278259   281 GGPLGIHVVpfSARGGRTLGLLVKRLEKGGKAEHENLfRENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:pfam00595    9 RGGLGFSLK--GGSDQGDPGIFVSEVLPGGAAEAGGL-KVGDRILSINGQDVENMTHEEAVLALKGS 72
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
489-649 5.94e-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: 40.67  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259   489 YVKNILPRGAAIQDGrLKAGDRLIEVNGVDLvgKSQEEVVSLLRSTKMEGTVSLLVFRQEdafHPRELNAEPSQmqiPKE 568
Cdd:TIGR02037  260 LVAQVLPGSPAEKAG-LKAGDVITSVNGKPI--SSFADLRRAIGTLKPGKKVTLGILRKG---KEKTITVTLGA---SPE 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259   569 TKAEdedivltpdGTREFLTFEV-PLNDSGSAGLGVSVKGNrskenhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNG 647
Cdd:TIGR02037  331 EQAS---------SSNPFLGLTVaNLSPEIRKELRLKGDVK---------GVVVTKVVSGSPAARAG-LQPGDVILSVNQ 391

                   ..
gi 296278259   648 ES 649
Cdd:TIGR02037  392 QP 393
 
Name Accession Description Interval E-value
DUF3534 pfam12053
N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. ...
2-83 2.60e-49

N-terminal of Par3 and HAL proteins; This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 150 amino acids in length. This eukaryotic domain is found associated with pfam00595. It has a conserved GILD sequence motif. Family members have been found to be essential for cell polarity establishment and maintenance such as Par3 (partitioning defective) and involved in conversion of histidine into ammonia (a crucial step for forming histamine in humans) such as Histidine ammonia lyase (HAL). This N-terminal domain is found to mediate oligomerization critical for the membrane localization of Par-3. It is also found to possess a self-association capacity via a front-to-back mode in Par-3 and HAL proteins. However, unlike the Par-3 N-terminal domain which self-assembles into a left-handed helical filament, the HAL N-terminal domain does not tend to form a helical filament but rather self-assembles into circular oligomeric particles. This has been suggested to be likely due to the absence of equivalent charged residues that are essential for the longitudinal packing of the Par-3 N-terminal domain filament.


Pssm-ID: 432291  Cd Length: 82  Bit Score: 169.06  E-value: 2.60e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259     2 KVTVCFGRTRVVVPCGDGHMKVFSLIQQAVTRYRKAIAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRLVAVFDE 81
Cdd:pfam12053    1 KVTVCFGRTRVVVPCGDGDLTVRDLIQQATQRYRKATEKDPGYWVKVHHLEYSDGGILDPDDILNDVVDDRDKLIAVYDE 80

                   ..
gi 296278259    82 QD 83
Cdd:pfam12053   81 QD 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
465-544 3.53e-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: 3.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  465 KKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAiQDGRLKAGDRLIEVNGVDLVGKSQEEVVSLLRSTKmeGTVSLLV 544
Cdd:cd00992     8 KDPGGGLGFSLRGGKDSGGG---IFVSRVEPGGPA-ERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG--DEVTLTV 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
458-547 1.61e-17

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 78.57  E-value: 1.61e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259    458 KRLNIQLKKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLVGKSQEEVVSLLRSTKme 537
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAG-- 74
                            90
                    ....*....|
gi 296278259    538 GTVSLLVFRQ 547
Cdd:smart00228   75 GKVTLTVLRG 84
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
588-681 5.92e-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: 5.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  588 TFEVPLNDSGSAGLGVSVKGNRSKenhaDLGIFVKSIINGGAASKdGRLRVNDQLIAVNGESLLGKTNQDAMETLRRSms 667
Cdd:cd00992     1 VRTVTLRKDPGGGLGFSLRGGKDS----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNS-- 73
                          90
                  ....*....|....
gi 296278259  668 tegnkRGMIQLIVA 681
Cdd:cd00992    74 -----GDEVTLTVR 82
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
462-544 1.94e-14

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: 69.62  E-value: 1.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259   462 IQLKK-GTEGLGFSITSRDvtIGGSAPIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLVGKSQEEVVSLLRSTKmeGTV 540
Cdd:pfam00595    2 VTLEKdGRGGLGFSLKGGS--DQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSG--GKV 76

                   ....
gi 296278259   541 SLLV 544
Cdd:pfam00595   77 TLTI 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
597-683 6.23e-14

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 68.17  E-value: 6.23e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259    597 GSAGLGVSVKGNRSKENhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKTNQDAMETLRRSmstegnkRGMI 676
Cdd:smart00228   10 GGGGLGFSLVGGKDEGG----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKA-------GGKV 77

                    ....*..
gi 296278259    677 QLIVARR 683
Cdd:smart00228   78 TLTVLRG 84
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
590-681 8.71e-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: 59.22  E-value: 8.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259   590 EVPLNDSGSAGLGVSVKGNRSKENHadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKTNQDAMETLRrsmste 669
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSDQGDP---GIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALK------ 70
                           90
                   ....*....|..
gi 296278259   670 gNKRGMIQLIVA 681
Cdd:pfam00595   71 -GSGGKVTLTIL 81
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
470-544 2.67e-10

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


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 57.32  E-value: 2.67e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296278259  470 GLGFSITSRDVTiggsaPIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLVGKSQEEVVSLLRsTKMEGTVSLLV 544
Cdd:cd00136     2 GLGFSIRGGTEG-----GVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLK-KEVGEKVTLTV 69
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
272-347 5.14e-10

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: 57.19  E-value: 5.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278259  272 VKLVEVP-NDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEHENLfRENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:cd00992     1 VRTVTLRkDPGGGLGFSLR---GGKDSGGGIFVSRVEPGGPAERGGL-RVGDRILEVNGVSVEGLTHEEAVELLKNS 73
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
600-669 1.80e-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: 52.31  E-value: 1.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  600 GLGVSVKGnrskenHADLGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKTNQDAMETLRRSMSTE 669
Cdd:cd00136     2 GLGFSIRG------GTEGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKEVGEK 64
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
271-347 1.64e-07

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: 50.07  E-value: 1.64e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278259    271 MVKLVEVPNDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEHENLfRENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLV---GGKDEGGGVVVSSVVPGSPAAKAGL-RVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
449-547 2.54e-06

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


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 51.56  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259  449 SGYNTKKIGKRLNIQLKKGTEGLGFSITSRDvtIGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLVGKSQEEVV 528
Cdd:COG0793    80 STYLDPEDAAEFRTDTSGEFGGIGIELQMED--IGG---VKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAV 153
                          90       100
                  ....*....|....*....|
gi 296278259  529 SLLRSTKmeGT-VSLLVFRQ 547
Cdd:COG0793   154 KLIRGKP--GTkVTLTILRA 171
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
599-663 4.53e-05

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


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 42.98  E-value: 4.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296278259  599 AGLGVSVKgnrsKENHadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKTNQDAMETLR 663
Cdd:cd00988     2 GGIGLELK----YDDG---GLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLR 58
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
469-546 7.91e-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: 42.60  E-value: 7.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296278259  469 EGLGFSITSRDvtiGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLVGKSQEEVVSLLRSTkmEGT-VSLLVFR 546
Cdd:cd00988     2 GGIGLELKYDD---GG---LVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGK--AGTkVRLTLKR 71
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
488-546 2.53e-03

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


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 38.39  E-value: 2.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 296278259  488 IYVKNILPRGAAiQDGRLKAGDRLIEVNGVDLvgKSQEEVVSLLRSTKMEGTVSLLVFR 546
Cdd:cd00987    26 VLVASVDPGSPA-AKAGLKPGDVILAVNGKPV--KSVADLRRALAELKPGDKVTLTVLR 81
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
281-347 3.02e-03

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: 38.03  E-value: 3.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278259   281 GGPLGIHVVpfSARGGRTLGLLVKRLEKGGKAEHENLfRENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:pfam00595    9 RGGLGFSLK--GGSDQGDPGIFVSEVLPGGAAEAGGL-KVGDRILSINGQDVENMTHEEAVLALKGS 72
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
282-352 3.45e-03

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: 37.28  E-value: 3.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296278259  282 GPLGihvvpFSARGGRTLGLLVKRLEKGGKAEHENLfRENDCIVRINDGDLRNRRFEQAQHMFRQAMRTPI 352
Cdd:cd00136     1 GGLG-----FSIRGGTEGGVVVLSVEPGSPAERAGL-QAGDVILAVNGTDVKNLTLEDVAELLKKEVGEKV 65
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
489-649 5.94e-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: 40.67  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259   489 YVKNILPRGAAIQDGrLKAGDRLIEVNGVDLvgKSQEEVVSLLRSTKMEGTVSLLVFRQEdafHPRELNAEPSQmqiPKE 568
Cdd:TIGR02037  260 LVAQVLPGSPAEKAG-LKAGDVITSVNGKPI--SSFADLRRAIGTLKPGKKVTLGILRKG---KEKTITVTLGA---SPE 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278259   569 TKAEdedivltpdGTREFLTFEV-PLNDSGSAGLGVSVKGNrskenhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNG 647
Cdd:TIGR02037  331 EQAS---------SSNPFLGLTVaNLSPEIRKELRLKGDVK---------GVVVTKVVSGSPAARAG-LQPGDVILSVNQ 391

                   ..
gi 296278259   648 ES 649
Cdd:TIGR02037  392 QP 393
 
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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