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Conserved domains on  [gi|21105855|ref|NP_631939|]
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cytohesin-interacting protein [Mus musculus]

Protein Classification

PDZ domain-containing protein (domain architecture ID 10097540)

PDZ domain-containing 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. ...
76-161 8.13e-19

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


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 79.92  E-value: 8.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21105855  76 KVVTVEKQDNGTFGFEIQTYRLQNQNIcssevctMICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRSSG 155
Cdd:cd00992   2 RTVTLRKDPGGGLGFSLRGGKDSGGGI-------FVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                ....*.
gi 21105855 156 NLLTIE 161
Cdd:cd00992  75 DEVTLT 80
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
76-161 8.13e-19

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


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 79.92  E-value: 8.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21105855  76 KVVTVEKQDNGTFGFEIQTYRLQNQNIcssevctMICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRSSG 155
Cdd:cd00992   2 RTVTLRKDPGGGLGFSLRGGKDSGGGI-------FVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                ....*.
gi 21105855 156 NLLTIE 161
Cdd:cd00992  75 DEVTLT 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
74-163 4.19e-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: 75.11  E-value: 4.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21105855     74 QRKVVTVEKQDNGtFGFEIQTYRLQNQNIcssevctMICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRS 153
Cdd:smart00228   1 EPRLVELEKGGGG-LGFSLVGGKDEGGGV-------VVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKK 72
                           90
                   ....*....|
gi 21105855    154 SGNLLTIETL 163
Cdd:smart00228  73 AGGKVTLTVL 82
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
78-163 8.18e-13

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 63.07  E-value: 8.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21105855    78 VTVEKQDNGTFGFEIQTYRLQNQNICSsevctmICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRSSGNL 157
Cdd:pfam00595   2 VTLEKDGRGGLGFSLKGGSDQGDPGIF------VSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                  ....*.
gi 21105855   158 LTIETL 163
Cdd:pfam00595  76 VTLTIL 81
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
116-163 7.36e-05

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: 44.24  E-value: 7.36e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21105855 116 EDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRS-SGNLLTIETL 163
Cdd:COG0793 121 DGSPAAKAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTIL 169
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
76-161 8.13e-19

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


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 79.92  E-value: 8.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21105855  76 KVVTVEKQDNGTFGFEIQTYRLQNQNIcssevctMICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRSSG 155
Cdd:cd00992   2 RTVTLRKDPGGGLGFSLRGGKDSGGGI-------FVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                ....*.
gi 21105855 156 NLLTIE 161
Cdd:cd00992  75 DEVTLT 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
74-163 4.19e-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: 75.11  E-value: 4.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21105855     74 QRKVVTVEKQDNGtFGFEIQTYRLQNQNIcssevctMICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRS 153
Cdd:smart00228   1 EPRLVELEKGGGG-LGFSLVGGKDEGGGV-------VVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKK 72
                           90
                   ....*....|
gi 21105855    154 SGNLLTIETL 163
Cdd:smart00228  73 AGGKVTLTVL 82
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
78-163 8.18e-13

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 63.07  E-value: 8.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21105855    78 VTVEKQDNGTFGFEIQTYRLQNQNICSsevctmICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRSSGNL 157
Cdd:pfam00595   2 VTLEKDGRGGLGFSLKGGSDQGDPGIF------VSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                  ....*.
gi 21105855   158 LTIETL 163
Cdd:pfam00595  76 VTLTIL 81
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
111-161 1.96e-07

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


Pssm-ID: 407688 [Multi-domain]  Cd Length: 54  Bit Score: 47.15  E-value: 1.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21105855   111 ICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFThkQVVDLIRSSGN---LLTIE 161
Cdd:pfam17820   2 VTSVVPGSPAERAGLRVGDVILSVNGEPVRSLA--DVARLLQGAGGesvTLTVR 53
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
110-152 3.30e-07

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


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 46.91  E-value: 3.30e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 21105855 110 MICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIR 152
Cdd:cd00136  16 VVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLK 58
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
108-166 8.53e-07

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


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 46.45  E-value: 8.53e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21105855 108 CTMICKVQEDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIR-SSGNLLTIETLNGT 166
Cdd:cd00988  14 GLVITSVLPGSPAAKAGIKAGDIIVAIDGEPVDGLSLEDVVKLLRgKAGTKVRLTLKRGD 73
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
113-161 1.13e-05

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


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 42.99  E-value: 1.13e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21105855 113 KVQEDSPAHCAGLQVGDIFANVNGVSTEGFThkQVVDLIRSSGN---LLTIE 161
Cdd:cd00989  18 EVVPGSPAAKAGLKAGDRILAINGQKIKSWE--DLVDAVQENPGkplTLTVE 67
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
116-163 7.36e-05

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: 44.24  E-value: 7.36e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21105855 116 EDSPAHCAGLQVGDIFANVNGVSTEGFTHKQVVDLIRS-SGNLLTIETL 163
Cdd:COG0793 121 DGSPAAKAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRGkPGTKVTLTIL 169
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
110-137 5.07e-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: 35.69  E-value: 5.07e-03
                        10        20
                ....*....|....*....|....*...
gi 21105855 110 MICKVQEDSPAHCAGLQVGDIFANVNGV 137
Cdd:cd00987  27 LVASVDPGSPAAKAGLKPGDVILAVNGK 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
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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