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Conserved domains on  [gi|161078240|ref|NP_001097763|]
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uncharacterized protein Dmel_CG31342, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 589-785 3.00e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240  589 PITSRSSPTRVANTNTTQPVTNG--SPALPRRRLASPATAQPVTPNA----AGRATPQLTRGLTELVISSRPSRRDFHYL 662
Cdd:PHA03247 2725 PAAARQASPALPAAPAPPAVPAGpaTPGGPARPARPPTTAGPPAPAPpaapAAGPPRRLTRPAVASLSESRESLPSPWDP 2804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240  663 KLLNTPLKTKTSHKSTSAANNNIEQSTPSSSNSTQVTPTQRNNTSIVTGDS----QEQRRRSSS-------TSDAQAPLQ 731
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapgGDVRRRPPSrspaakpAAPARPPVR 2884

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161078240  732 RVPQPATQRNANNNEFTPsrNGAFRMQPPPQGTPPSSTNPAQQSPNKRLTLREQ 785
Cdd:PHA03247 2885 RLARPAVSRSTESFALPP--DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 879-969 1.17e-03

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


The actual alignment was detected with superfamily member cd06794:

Pssm-ID: 483948 [Multi-domain]  Cd Length: 78  Bit Score: 38.44  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240 879 PFGRAYAIRRDREGqCLGLI-RDGNtstIVDVVPNSLAARHGLppktqscdgnsLTFWMLTEINGRSLnLFFKDFEIRDR 957
Cdd:cd06794    2 PFERTITMHKDSTG-HVGFVfKNGK---ITSIVKDSSAARNGL-----------LTDHQLCEVNGQNV-IGLKDKEIADI 65

                         90
                 ....*....|..
gi 161078240 958 LNSVGRDISILV 969
Cdd:cd06794   66 LATAGRVVTITI 77
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 838-866 1.34e-03

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


The actual alignment was detected with superfamily member cd06684:

Pssm-ID: 483948 [Multi-domain]  Cd Length: 87  Bit Score: 38.77  E-value: 1.34e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 161078240 838 ALHIGDQLLSIAGVSI--SSAAEANKIIRNT 866
Cdd:cd06684   46 ALHVGDHILSIDGTSVehCSLAEATQLLASN 76
 
Name Accession Description Interval E-value
PHA03247 PHA03247
large tegument protein UL36; Provisional
 589-785 3.00e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240  589 PITSRSSPTRVANTNTTQPVTNG--SPALPRRRLASPATAQPVTPNA----AGRATPQLTRGLTELVISSRPSRRDFHYL 662
Cdd:PHA03247 2725 PAAARQASPALPAAPAPPAVPAGpaTPGGPARPARPPTTAGPPAPAPpaapAAGPPRRLTRPAVASLSESRESLPSPWDP 2804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240  663 KLLNTPLKTKTSHKSTSAANNNIEQSTPSSSNSTQVTPTQRNNTSIVTGDS----QEQRRRSSS-------TSDAQAPLQ 731
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapgGDVRRRPPSrspaakpAAPARPPVR 2884

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161078240  732 RVPQPATQRNANNNEFTPsrNGAFRMQPPPQGTPPSSTNPAQQSPNKRLTLREQ 785
Cdd:PHA03247 2885 RLARPAVSRSTESFALPP--DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
PDZ2_syntenin-like cd06794
PDZ domain 2 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 879-969 1.17e-03

PDZ domain 2 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of syntenin-1, syntenin-2, and related domains. Syntenins are implicated in various cellular processes such as trafficking, signaling, and cancer metastasis. They bind to signaling and adhesion molecules, such as syndecans, neurexins, ephrin B, and phospholipid PIP2. Through its tandem PDZ domains (PDZ1 and PDZ2) syntenin links syndecans to other cell surface receptors and kinases, such as E-cadherin and ephrin-B, establishing signaling crosstalk. During syndecan binding, syntenin PDZ2 serves as a high-affinity domain, and PDZ1, also necessary for binding, acts as a complementary, low-affinity domain; this is also the case for syntenin binding to proto-oncogene c-Src. The syntenin PDZ domain-PIP2 interaction controls Arf6-mediated syndecan recycling through endosomal compartments; both PDZ1 and PDZ2 interact with PIP2. Different binding partners and downstream regulators of syntenin1 PDZ domains, such as to proto-oncogene c-Src, mitogen-activated protein kinase (MAPK), and focal adhesion kinase (FAK), have been identified that promote the progression and invasion of a variety of cancers, such as melanoma, glioblastoma multiforme, and breast cancer. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntenin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467256 [Multi-domain]  Cd Length: 78  Bit Score: 38.44  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240 879 PFGRAYAIRRDREGqCLGLI-RDGNtstIVDVVPNSLAARHGLppktqscdgnsLTFWMLTEINGRSLnLFFKDFEIRDR 957
Cdd:cd06794    2 PFERTITMHKDSTG-HVGFVfKNGK---ITSIVKDSSAARNGL-----------LTDHQLCEVNGQNV-IGLKDKEIADI 65

                         90
                 ....*....|..
gi 161078240 958 LNSVGRDISILV 969
Cdd:cd06794   66 LATAGRVVTITI 77
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 838-866 1.34e-03

PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467172 [Multi-domain]  Cd Length: 87  Bit Score: 38.77  E-value: 1.34e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 161078240 838 ALHIGDQLLSIAGVSI--SSAAEANKIIRNT 866
Cdd:cd06684   46 ALHVGDHILSIDGTSVehCSLAEATQLLASN 76
 
Name Accession Description Interval E-value
PHA03247 PHA03247
large tegument protein UL36; Provisional
 589-785 3.00e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240  589 PITSRSSPTRVANTNTTQPVTNG--SPALPRRRLASPATAQPVTPNA----AGRATPQLTRGLTELVISSRPSRRDFHYL 662
Cdd:PHA03247 2725 PAAARQASPALPAAPAPPAVPAGpaTPGGPARPARPPTTAGPPAPAPpaapAAGPPRRLTRPAVASLSESRESLPSPWDP 2804

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240  663 KLLNTPLKTKTSHKSTSAANNNIEQSTPSSSNSTQVTPTQRNNTSIVTGDS----QEQRRRSSS-------TSDAQAPLQ 731
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapgGDVRRRPPSrspaakpAAPARPPVR 2884

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 161078240  732 RVPQPATQRNANNNEFTPsrNGAFRMQPPPQGTPPSSTNPAQQSPNKRLTLREQ 785
Cdd:PHA03247 2885 RLARPAVSRSTESFALPP--DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
PDZ2_syntenin-like cd06794
PDZ domain 2 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 879-969 1.17e-03

PDZ domain 2 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of syntenin-1, syntenin-2, and related domains. Syntenins are implicated in various cellular processes such as trafficking, signaling, and cancer metastasis. They bind to signaling and adhesion molecules, such as syndecans, neurexins, ephrin B, and phospholipid PIP2. Through its tandem PDZ domains (PDZ1 and PDZ2) syntenin links syndecans to other cell surface receptors and kinases, such as E-cadherin and ephrin-B, establishing signaling crosstalk. During syndecan binding, syntenin PDZ2 serves as a high-affinity domain, and PDZ1, also necessary for binding, acts as a complementary, low-affinity domain; this is also the case for syntenin binding to proto-oncogene c-Src. The syntenin PDZ domain-PIP2 interaction controls Arf6-mediated syndecan recycling through endosomal compartments; both PDZ1 and PDZ2 interact with PIP2. Different binding partners and downstream regulators of syntenin1 PDZ domains, such as to proto-oncogene c-Src, mitogen-activated protein kinase (MAPK), and focal adhesion kinase (FAK), have been identified that promote the progression and invasion of a variety of cancers, such as melanoma, glioblastoma multiforme, and breast cancer. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntenin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467256 [Multi-domain]  Cd Length: 78  Bit Score: 38.44  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078240 879 PFGRAYAIRRDREGqCLGLI-RDGNtstIVDVVPNSLAARHGLppktqscdgnsLTFWMLTEINGRSLnLFFKDFEIRDR 957
Cdd:cd06794    2 PFERTITMHKDSTG-HVGFVfKNGK---ITSIVKDSSAARNGL-----------LTDHQLCEVNGQNV-IGLKDKEIADI 65

                         90
                 ....*....|..
gi 161078240 958 LNSVGRDISILV 969
Cdd:cd06794   66 LATAGRVVTITI 77
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 838-866 1.34e-03

PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467172 [Multi-domain]  Cd Length: 87  Bit Score: 38.77  E-value: 1.34e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 161078240 838 ALHIGDQLLSIAGVSI--SSAAEANKIIRNT 866
Cdd:cd06684   46 ALHVGDHILSIDGTSVehCSLAEATQLLASN 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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