NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568957908|ref|XP_006531596|]
View 

partitioning defective 3 homolog isoform X15 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.07e-50

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: 171.37  E-value: 1.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908    2 KVTVCFGRTRVVVPCGDGRMKVFSLIQQAVTRYRKAVAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRLVAVFDE 81
Cdd:pfam12053   1 KVTVCFGRTRVVVPCGDGDLTVRDLIQQATQRYRKATEKDPGYWVKVHHLEYSDGGILDPDDILNDVVDDRDKLIAVYDE 80

                  ..
gi 568957908   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 1.70e-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: 77.61  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 465 KKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAiQDGRLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTKmeGTVSLLV 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 1.51e-14

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


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 69.13  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 588 TFEVPLNDSGSAGLGVSVKGNRSKenhaDLGIFVKSIINGGAASKdGRLRVNDQLIAVNGESLLGKANQEAMETLRRSms 667
Cdd:cd00992    1 VRTVTLRKDPGGGLGFSLRGGKDS----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNS-- 73
                         90
                 ....*....|....
gi 568957908 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 3.27e-09

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: 54.11  E-value: 3.27e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568957908 272 VKLVQVP-NDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEQENLfHENDCIVRINDGDLRNRRFEQAQHMFRQA 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 1.07e-50

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: 171.37  E-value: 1.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908    2 KVTVCFGRTRVVVPCGDGRMKVFSLIQQAVTRYRKAVAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRLVAVFDE 81
Cdd:pfam12053   1 KVTVCFGRTRVVVPCGDGDLTVRDLIQQATQRYRKATEKDPGYWVKVHHLEYSDGGILDPDDILNDVVDDRDKLIAVYDE 80

                  ..
gi 568957908   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 1.70e-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: 77.61  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 465 KKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAiQDGRLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTKmeGTVSLLV 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 4.84e-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: 76.26  E-value: 4.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908   458 KRLNIQLKKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTKme 537
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAG-- 74
                           90
                   ....*....|
gi 568957908   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 1.51e-14

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


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 69.13  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 588 TFEVPLNDSGSAGLGVSVKGNRSKenhaDLGIFVKSIINGGAASKdGRLRVNDQLIAVNGESLLGKANQEAMETLRRSms 667
Cdd:cd00992    1 VRTVTLRKDPGGGLGFSLRGGKDS----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNS-- 73
                         90
                 ....*....|....
gi 568957908 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 6.47e-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: 67.31  E-value: 6.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908  462 IQLKK-GTEGLGFSITSRDvtIGGSAPIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTKmeGTV 540
Cdd:pfam00595   2 VTLEKdGRGGLGFSLKGGS--DQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSG--GKV 76

                  ....
gi 568957908  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 6.11e-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: 64.71  E-value: 6.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908   597 GSAGLGVSVKGNRSKENhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKANQEAMETLRRSmstegnkRGMI 676
Cdd:smart00228  10 GGGGLGFSLVGGKDEGG----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKA-------GGKV 77

                   ....*..
gi 568957908   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 2.19e-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: 57.29  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908  590 EVPLNDSGSAGLGVSVKGNRSKENHadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKANQEAMETLRrsmste 669
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGDP---GIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALK------ 70
                          90
                  ....*....|..
gi 568957908  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 3.27e-09

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: 54.11  E-value: 3.27e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568957908 272 VKLVQVP-NDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEQENLfHENDCIVRINDGDLRNRRFEQAQHMFRQA 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 4.46e-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: 48.14  E-value: 4.46e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568957908   271 MVKLVQVPNDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEQENLfHENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLV---GGKDEGGGVVVSSVVPGSPAAKAGL-RVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
449-547 8.54e-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: 51.95  E-value: 8.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 449 SVYNTKKVGKRLNIQLKKGTEGLGFSITSRDvtIGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKSQEEVV 528
Cdd:COG0793   80 STYLDPEDAAEFRTDTSGEFGGIGIELQMED--IGG---VKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAV 153
                         90       100
                 ....*....|....*....|
gi 568957908 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 3.48e-04

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: 39.96  E-value: 3.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568957908  281 GGPLGIHVVpfSARGGRTLGLLVKRLEKGGKAEQENLfHENDCIVRINDGDLRNRRFEQAQHMFRQA 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 8.71e-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: 39.13  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908  489 YVKNILPRGAAIQDGrLKAGDRLIEVNGVDLagKSQEEVVSLLRSTKMEGTVSLLVFRQEeafHPREMNAEpsqMQTPKE 568
Cdd:TIGR02037 260 LVAQVLPGSPAEKAG-LKAGDVITSVNGKPI--SSFADLRRAIGTLKPGKKVTLGILRKG---KEKTITVT---LGASPE 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908  569 TKAEdedvvltpdGTREFLTFEV-PLNDSGSAGLGVSVKGNrskenhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNG 647
Cdd:TIGR02037 331 EQAS---------SSNPFLGLTVaNLSPEIRKELRLKGDVK---------GVVVTKVVSGSPAARAG-LQPGDVILSVNQ 391

                  ..
gi 568957908  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 1.07e-50

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: 171.37  E-value: 1.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908    2 KVTVCFGRTRVVVPCGDGRMKVFSLIQQAVTRYRKAVAKDPNYWIQVHRLEHGDGGILDLDDILCDVADDKDRLVAVFDE 81
Cdd:pfam12053   1 KVTVCFGRTRVVVPCGDGDLTVRDLIQQATQRYRKATEKDPGYWVKVHHLEYSDGGILDPDDILNDVVDDRDKLIAVYDE 80

                  ..
gi 568957908   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 1.70e-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: 77.61  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 465 KKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAiQDGRLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTKmeGTVSLLV 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 4.84e-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: 76.26  E-value: 4.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908   458 KRLNIQLKKGTEGLGFSITSRDVTIGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTKme 537
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLVGGKDEGGG---VVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAG-- 74
                           90
                   ....*....|
gi 568957908   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 1.51e-14

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


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 69.13  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 588 TFEVPLNDSGSAGLGVSVKGNRSKenhaDLGIFVKSIINGGAASKdGRLRVNDQLIAVNGESLLGKANQEAMETLRRSms 667
Cdd:cd00992    1 VRTVTLRKDPGGGLGFSLRGGKDS----GGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNS-- 73
                         90
                 ....*....|....
gi 568957908 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 6.47e-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: 67.31  E-value: 6.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908  462 IQLKK-GTEGLGFSITSRDvtIGGSAPIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTKmeGTV 540
Cdd:pfam00595   2 VTLEKdGRGGLGFSLKGGS--DQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSG--GKV 76

                  ....
gi 568957908  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 6.11e-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: 64.71  E-value: 6.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908   597 GSAGLGVSVKGNRSKENhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKANQEAMETLRRSmstegnkRGMI 676
Cdd:smart00228  10 GGGGLGFSLVGGKDEGG----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKA-------GGKV 77

                   ....*..
gi 568957908   677 QLIVARR 683
Cdd:smart00228  78 TLTVLRG 84
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
470-544 2.09e-10

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


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 56.93  E-value: 2.09e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568957908 470 GLGFSITSRDVTiggsaPIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKSQEEVVSLLRsTKMEGTVSLLV 544
Cdd:cd00136    2 GLGFSIRGGTEG-----GVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLK-KEVGEKVTLTV 69
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
590-681 2.19e-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: 57.29  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908  590 EVPLNDSGSAGLGVSVKGNRSKENHadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKANQEAMETLRrsmste 669
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGDP---GIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALK------ 70
                          90
                  ....*....|..
gi 568957908  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 3.27e-09

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: 54.11  E-value: 3.27e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568957908 272 VKLVQVP-NDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEQENLfHENDCIVRINDGDLRNRRFEQAQHMFRQA 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 3.73e-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: 3.73e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 600 GLGVSVKGnrskenHADLGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKANQEAMETLRRSMSTE 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 4.46e-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: 48.14  E-value: 4.46e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568957908   271 MVKLVQVPNDGGPLGIHVVpfsARGGRTLGLLVKRLEKGGKAEQENLfHENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:smart00228   1 EPRLVELEKGGGGLGFSLV---GGKDEGGGVVVSSVVPGSPAAKAGL-RVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
449-547 8.54e-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: 51.95  E-value: 8.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 449 SVYNTKKVGKRLNIQLKKGTEGLGFSITSRDvtIGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKSQEEVV 528
Cdd:COG0793   80 STYLDPEDAAEFRTDTSGEFGGIGIELQMED--IGG---VKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAV 153
                         90       100
                 ....*....|....*....|
gi 568957908 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 ...
469-549 3.85e-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: 3.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 469 EGLGFSITSRDvtiGGsapIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKSQEEVVSLLRSTkmEGT-VSLLVFRQ 547
Cdd:cd00988    2 GGIGLELKYDD---GG---LVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRGK--AGTkVRLTLKRG 72

                 ..
gi 568957908 548 EE 549
Cdd:cd00988   73 DG 74
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
282-352 1.83e-04

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


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 40.37  E-value: 1.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568957908 282 GPLGihvvpFSARGGRTLGLLVKRLEKGGKAEQENLfHENDCIVRINDGDLRNRRFEQAQHMFRQAMRARV 352
Cdd:cd00136    1 GGLG-----FSIRGGTEGGVVVLSVEPGSPAERAGL-QAGDVILAVNGTDVKNLTLEDVAELLKKEVGEKV 65
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
281-347 3.48e-04

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: 39.96  E-value: 3.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568957908  281 GGPLGIHVVpfSARGGRTLGLLVKRLEKGGKAEQENLfHENDCIVRINDGDLRNRRFEQAQHMFRQA 347
Cdd:pfam00595   9 RGGLGFSLK--GGSDQGDPGIFVSEVLPGGAAEAGGL-KVGDRILSINGQDVENMTHEEAVLALKGS 72
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
599-663 4.76e-04

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


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 39.52  E-value: 4.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568957908 599 AGLGVSVKGNRSkenhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNGESLLGKANQEAMETLR 663
Cdd:cd00988    2 GGIGLELKYDDG-------GLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLR 58
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
488-546 3.36e-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: 37.23  E-value: 3.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568957908 488 IYVKNILPRGAAiQDGRLKAGDRLIEVNGVDLagKSQEEVVSLLRSTKMEGTVSLLVFR 546
Cdd:cd00987   26 VLVASVDPGSPA-AKAGLKPGDVILAVNGKPV--KSVADLRRALAELKPGDKVTLTVLR 81
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
470-552 5.14e-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: 36.44  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908 470 GLGFSItsrdvtIGGSAPIYVKNILPRGAAIQDGrLKAGDRLIEVNGVDLagKSQEEVVSLLRStKMEGTVSLLVFRQEE 549
Cdd:cd00989    2 ILGFVP------GGPPIEPVIGEVVPGSPAAKAG-LKAGDRILAINGQKI--KSWEDLVDAVQE-NPGKPLTLTVERNGE 71

                 ...
gi 568957908 550 AFH 552
Cdd:cd00989   72 TIT 74
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
489-649 8.71e-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: 39.13  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908  489 YVKNILPRGAAIQDGrLKAGDRLIEVNGVDLagKSQEEVVSLLRSTKMEGTVSLLVFRQEeafHPREMNAEpsqMQTPKE 568
Cdd:TIGR02037 260 LVAQVLPGSPAEKAG-LKAGDVITSVNGKPI--SSFADLRRAIGTLKPGKKVTLGILRKG---KEKTITVT---LGASPE 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568957908  569 TKAEdedvvltpdGTREFLTFEV-PLNDSGSAGLGVSVKGNrskenhadlGIFVKSIINGGAASKDGrLRVNDQLIAVNG 647
Cdd:TIGR02037 331 EQAS---------SSNPFLGLTVaNLSPEIRKELRLKGDVK---------GVVVTKVVSGSPAARAG-LQPGDVILSVNQ 391

                  ..
gi 568957908  648 ES 649
Cdd:TIGR02037 392 QP 393
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
489-546 9.54e-03

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 34.81  E-value: 9.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568957908  489 YVKNILPRGAAIQDGrLKAGDRLIEVNGVDLAGKsqEEVVSLLRSTKmEGTVSLLVFR 546
Cdd:pfam17820   1 VVTAVVPGSPAERAG-LRVGDVILAVNGKPVRSL--EDVARLLQGSA-GESVTLTVRR 54
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH