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Conserved domains on  [gi|187607187|ref|NP_001120354|]
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protein TAMALIN [Xenopus tropicalis]

Protein Classification

PDZ domain-containing protein( domain architecture ID 10097540)

PDZ (PSD-95, Dlg, and ZO-1/2) domain-containing protein is involved in protein-protein interactions and may play a role in scaffolding supramolecular complexes

CATH:  2.30.42.10
Gene Ontology:  GO:0005515
SCOP:  4001790

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. ...
78-163 2.25e-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: 81.46  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187  78 KILTLQKEDSESFGFEIQTYGLHhqdknavEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKVSG 157
Cdd:cd00992    2 RTVTLRKDPGGGLGFSLRGGKDS-------GGGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                 ....*.
gi 187607187 158 NTIRLE 163
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. ...
78-163 2.25e-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: 81.46  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187  78 KILTLQKEDSESFGFEIQTYGLHhqdknavEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKVSG 157
Cdd:cd00992    2 RTVTLRKDPGGGLGFSLRGGKDS-------GGGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                 ....*.
gi 187607187 158 NTIRLE 163
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 ...
76-168 4.13e-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: 4.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187    76 QRKILTLQKeDSESFGFEIQTYGlhhqdknAVEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKV 155
Cdd:smart00228   1 EPRLVELEK-GGGGLGFSLVGGK-------DEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKK 72
                           90
                   ....*....|...
gi 187607187   156 SGNTIRLETVYGS 168
Cdd:smart00228  73 AGGKVTLTVLRGG 85
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
80-163 1.95e-12

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 61.91  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187   80 LTLQKEDSESFGFEIQtyglhhQDKNAVEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKVSGNT 159
Cdd:pfam00595   2 VTLEKDGRGGLGFSLK------GGSDQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                  ....
gi 187607187  160 IRLE 163
Cdd:pfam00595  76 VTLT 79
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
82-173 2.90e-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: 48.48  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187  82 LQKEDSESFG----FEIQTYGLHHQDKNAVemFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIK-VS 156
Cdd:COG0793   83 LDPEDAAEFRtdtsGEFGGIGIELQMEDIG--GVKVVSPIDGSPAAKAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRgKP 160
                         90
                 ....*....|....*..
gi 187607187 157 GNTIRLEtvygsaIRRA 173
Cdd:COG0793  161 GTKVTLT------ILRA 171
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
95-185 1.24e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 43.36  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187   95 QTYGLHHQdKNAvemftFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRH-RDIVELIKVsGNTIRLETVYGSAIRra 173
Cdd:TIGR02037 249 KSLGLEKQ-RGA-----LVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADlRRAIGTLKP-GKKVTLGILRKGKEK-- 319
                          90
                  ....*....|..
gi 187607187  174 ELEARIQYLKQT 185
Cdd:TIGR02037 320 TITVTLGASPEE 331
 
Name Accession Description Interval E-value
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
78-163 2.25e-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: 81.46  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187  78 KILTLQKEDSESFGFEIQTYGLHhqdknavEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKVSG 157
Cdd:cd00992    2 RTVTLRKDPGGGLGFSLRGGKDS-------GGGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSG 74

                 ....*.
gi 187607187 158 NTIRLE 163
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 ...
76-168 4.13e-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: 4.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187    76 QRKILTLQKeDSESFGFEIQTYGlhhqdknAVEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKV 155
Cdd:smart00228   1 EPRLVELEK-GGGGLGFSLVGGK-------DEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKK 72
                           90
                   ....*....|...
gi 187607187   156 SGNTIRLETVYGS 168
Cdd:smart00228  73 AGGKVTLTVLRGG 85
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
80-163 1.95e-12

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 61.91  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187   80 LTLQKEDSESFGFEIQtyglhhQDKNAVEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKVSGNT 159
Cdd:pfam00595   2 VTLEKDGRGGLGFSLK------GGSDQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                  ....
gi 187607187  160 IRLE 163
Cdd:pfam00595  76 VTLT 79
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
89-165 5.15e-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: 55.00  E-value: 5.15e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187607187  89 SFGFEIQTYGlhhqdknavEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIK-VSGNTIRLETV 165
Cdd:cd00136    2 GLGFSIRGGT---------EGGVVVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVAELLKkEVGEKVTLTVR 70
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
112-165 1.96e-07

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 47.14  E-value: 1.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 187607187  112 FVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVrhRDIVELIKVSGNTIRLETV 165
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSL--EDVARLLQGSAGESVTLTV 52
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
112-183 2.05e-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: 47.99  E-value: 2.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187607187 112 FVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKVSGNT-IRLEtvygsaIRRAELEARIQYLK 183
Cdd:cd00988   16 VITSVLPGSPAAKAGIKAGDIIVAIDGEPVDGLSLEDVVKLLRGKAGTkVRLT------LKRGDGEPREVTLT 82
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
82-173 2.90e-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: 48.48  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187  82 LQKEDSESFG----FEIQTYGLHHQDKNAVemFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIK-VS 156
Cdd:COG0793   83 LDPEDAAEFRtdtsGEFGGIGIELQMEDIG--GVKVVSPIDGSPAAKAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRgKP 160
                         90
                 ....*....|....*..
gi 187607187 157 GNTIRLEtvygsaIRRA 173
Cdd:COG0793  161 GTKVTLT------ILRA 171
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
112-163 3.77e-06

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: 44.55  E-value: 3.77e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187607187 112 FVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRH-RDIVELIKVsGNTIRLE 163
Cdd:cd00987   27 LVASVDPGSPAAKAGLKPGDVILAVNGKPVKSVADlRRALAELKP-GDKVTLT 78
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
95-185 1.24e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 43.36  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607187   95 QTYGLHHQdKNAvemftFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRH-RDIVELIKVsGNTIRLETVYGSAIRra 173
Cdd:TIGR02037 249 KSLGLEKQ-RGA-----LVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADlRRAIGTLKP-GKKVTLGILRKGKEK-- 319
                          90
                  ....*....|..
gi 187607187  174 ELEARIQYLKQT 185
Cdd:TIGR02037 320 TITVTLGASPEE 331
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
116-158 1.84e-04

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


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 39.52  E-value: 1.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 187607187 116 VQDGSPAQLCGLKVGDIIAGVNGLNMDGVrhRDIVELIKVSGN 158
Cdd:cd00989   19 VVPGSPAAKAGLKAGDRILAINGQKIKSW--EDLVDAVQENPG 59
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
112-163 3.97e-03

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223343 [Multi-domain]  Cd Length: 347  Bit Score: 38.72  E-value: 3.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 187607187 112 FVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVR-HRDIVELIKVsGNTIRLE 163
Cdd:COG0265  273 VVLGVLPGSPAAKAGIKAGDIITAVNGKPVASLSdLVAAVASNRP-GDEVALK 324
 
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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