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Conserved domains on  [gi|10439278|dbj|BAB15479|]
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unnamed protein product [Homo sapiens]

Protein Classification

PDZ domain-containing protein (domain architecture ID 10097540)

PDZ domain-containing protein similar to Homo sapiens Tax1-binding protein 3, glutamate receptor-interacting protein 1, gamma-2-syntrophin, cytohesin-interacting protein, syntenin-1, and synaptojanin-2-binding protein

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. ...
62-140 2.47e-23

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: 92.63  E-value: 2.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10439278  62 VELERGP-RGFGFSLRGGKEYNMGLFILRLAEDGPAIKdGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLR 140
Cdd:cd00992   4 VTLRKDPgGGLGFSLRGGKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLTVR 82
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
62-140 2.47e-23

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: 92.63  E-value: 2.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10439278  62 VELERGP-RGFGFSLRGGKEYNMGLFILRLAEDGPAIKdGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLR 140
Cdd:cd00992   4 VTLRKDPgGGLGFSLRGGKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
62-142 5.50e-22

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: 88.98  E-value: 5.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10439278     62 VELERGPRGFGFSLRGGKEYNMGLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKV-LLLLR 140
Cdd:smart00228   5 VELEKGGGGLGFSLVGGKDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVtLTVLR 83

                   ..
gi 10439278    141 PG 142
Cdd:smart00228  84 GG 85
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
66-140 6.33e-14

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


Pssm-ID: 334167 [Multi-domain]  Cd Length: 81  Bit Score: 66.53  E-value: 6.33e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10439278    66 RGPRGFGFSLRGGKE-YNMGLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLR 140
Cdd:pfam00595   7 DGPGGLGFSLKGGSDqGAKGIFVSEVLPGGAAEAAG-LQAGDRILSVNGVPIENLSHEEAVLALKGSGGKVTLLIL 81
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
78-144 8.67e-08

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: 53.49  E-value: 8.67e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10439278  78 GKEYNM----GLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQ-AGGNKV-LLLLRPGTG 144
Cdd:COG0793 103 GIELQMedigGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRgKPGTKVtLTILRAGGG 174
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
85-146 2.00e-05

C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]


Pssm-ID: 272970 [Multi-domain]  Cd Length: 334  Bit Score: 45.81  E-value: 2.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10439278    85 LFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQAG-GNKVLL-LLRPGTGLI 146
Cdd:TIGR00225  64 IVIVSPFEGSPAEKAG-IKPGDKIIKINGKSVAGMSLDDAVALIRGKkGTKVSLeILRAGKSKP 126
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
84-144 1.24e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 40.49  E-value: 1.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10439278   84 GLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQAG-GNKVLLLLRPGTG 144
Cdd:PLN00049 103 GLVVVAPAPGGPAARAG-IRPGDVILAIDGTSTEGLSLYEAADRLQGPeGSSVELTLRRGPE 163
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
62-140 2.47e-23

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: 92.63  E-value: 2.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10439278  62 VELERGP-RGFGFSLRGGKEYNMGLFILRLAEDGPAIKdGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLR 140
Cdd:cd00992   4 VTLRKDPgGGLGFSLRGGKDSGGGIFVSRVEPGGPAER-GGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLTVR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
62-142 5.50e-22

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: 88.98  E-value: 5.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10439278     62 VELERGPRGFGFSLRGGKEYNMGLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKV-LLLLR 140
Cdd:smart00228   5 VELEKGGGGLGFSLVGGKDEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVtLTVLR 83

                   ..
gi 10439278    141 PG 142
Cdd:smart00228  84 GG 85
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
66-140 6.33e-14

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


Pssm-ID: 334167 [Multi-domain]  Cd Length: 81  Bit Score: 66.53  E-value: 6.33e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 10439278    66 RGPRGFGFSLRGGKE-YNMGLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLR 140
Cdd:pfam00595   7 DGPGGLGFSLKGGSDqGAKGIFVSEVLPGGAAEAAG-LQAGDRILSVNGVPIENLSHEEAVLALKGSGGKVTLLIL 81
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
69-140 7.51e-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: 60.40  E-value: 7.51e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10439278  69 RGFGFSLRGGKeyNMGLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQA-GGNKVLLLLR 140
Cdd:cd00136   1 GGLGFSIRGGT--EGGVVVLSVEPGSPAERAG-LQAGDVILAVNGTDVKNLTLEDVAELLKKeVGEKVTLTVR 70
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
84-144 3.19e-09

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: 53.38  E-value: 3.19e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10439278  84 GLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQ-AGGNKVLLLLRPGTG 144
Cdd:cd00988  14 GLVITSVLPGSPAAKAG-IKAGDIIVAIDGEPVDGLSLEDVVKLLRgKAGTKVRLTLKRGDG 74
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
78-144 8.67e-08

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: 53.49  E-value: 8.67e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10439278  78 GKEYNM----GLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQ-AGGNKV-LLLLRPGTG 144
Cdd:COG0793 103 GIELQMedigGVKVVSPIDGSPAAKAG-IKPGDVIIKIDGKSVGGVSLDEAVKLIRgKPGTKVtLTILRAGGG 174
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
85-146 2.00e-05

C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]


Pssm-ID: 272970 [Multi-domain]  Cd Length: 334  Bit Score: 45.81  E-value: 2.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10439278    85 LFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQAG-GNKVLL-LLRPGTGLI 146
Cdd:TIGR00225  64 IVIVSPFEGSPAEKAG-IKPGDKIIKINGKSVAGMSLDDAVALIRGKkGTKVSLeILRAGKSKP 126
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
84-144 1.24e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 40.49  E-value: 1.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10439278   84 GLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITHTRAIELIQAG-GNKVLLLLRPGTG 144
Cdd:PLN00049 103 GLVVVAPAPGGPAARAG-IRPGDVILAIDGTSTEGLSLYEAADRLQGPeGSSVELTLRRGPE 163
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
90-145 3.07e-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: 36.06  E-value: 3.07e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 10439278  90 LAEDGPAIKDGrIHVGDQIVEINGEPtqgITHTRAI-ELIQAGGNKVLLL--LRPGTGL 145
Cdd:cd00989  19 VVPGSPAAKAG-LKAGDRILAINGQK---IKSWEDLvDAVQENPGKPLTLtvERNGETI 73
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
76-142 9.40e-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: 34.92  E-value: 9.40e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10439278  76 RGGKEYNMGLFILRLAEDGPAIKDGrIHVGDQIVEINGEPTQGITH-TRAIELIQAGGNKVLLLLRPG 142
Cdd:cd00987  17 ELGLKDTKGVLVASVDPGSPAAKAG-LKPGDVILAVNGKPVKSVADlRRALAELKPGDKVTLTVLRGG 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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