NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958674160|ref|XP_038947290|]
View 

uncharacterized protein KIAA1614 homolog isoform X5 [Rattus norvegicus]

Protein Classification

DUF4685 and PDZ_signaling domain-containing protein( domain architecture ID 11238999)

DUF4685 and PDZ_signaling domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DUF4685 pfam15737
Domain of unknown function (DUF4685); This domain family is found in eukaryotes, and is ...
 1-98 1.51e-37

Domain of unknown function (DUF4685); This domain family is found in eukaryotes, and is typically between 106 and 131 amino acids in length. There are two conserved sequence motifs: SGE and VRF.


:

Pssm-ID: 464834 [Multi-domain]  Cd Length: 117  Bit Score: 136.44  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160   1 MKAKTQPLRASHDIVPIIAQGSRNGQRSPAPDVRTTSASRESLqngnlNDPSSVEssnGQWPKQGMPLSHVRFEDESARE 80
Cdd:pfam15737  27 MKARTGPLRADHDIVPTVAQGSRDGQGSPAPKPRATSACRDSL-----SDSSSGE---GQGPRRGMSPSRVRFEDESARD 98

                          90
                  ....*....|....*...
gi 1958674160  81 AEFRYLDRLQQRQRQVLS 98
Cdd:pfam15737  99 AELRYWERLQQRQQQVLS 116
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 742-821 1.02e-14

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 cd06718:

Pssm-ID: 483948 [Multi-domain]  Cd Length: 84  Bit Score: 69.90  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160 742 LQRPPEGTFGFCVAYGSGR-RDSGLYVQDMADlDTAKLYSGLLGVGDEILEMNGAKVAGLGLAHINELLVRVESLSIRVL 820
Cdd:cd06718     5 LIKPPGKPLGFYIRDGNGVeRVPGIFISRLVL-GSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTRLIITVK 83


                  .
gi 1958674160 821 R 821
Cdd:cd06718    84 P 84
 
Name Accession Description Interval E-value
DUF4685 pfam15737
Domain of unknown function (DUF4685); This domain family is found in eukaryotes, and is ...
 1-98 1.51e-37

Domain of unknown function (DUF4685); This domain family is found in eukaryotes, and is typically between 106 and 131 amino acids in length. There are two conserved sequence motifs: SGE and VRF.


Pssm-ID: 464834 [Multi-domain]  Cd Length: 117  Bit Score: 136.44  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160   1 MKAKTQPLRASHDIVPIIAQGSRNGQRSPAPDVRTTSASRESLqngnlNDPSSVEssnGQWPKQGMPLSHVRFEDESARE 80
Cdd:pfam15737  27 MKARTGPLRADHDIVPTVAQGSRDGQGSPAPKPRATSACRDSL-----SDSSSGE---GQGPRRGMSPSRVRFEDESARD 98

                          90
                  ....*....|....*...
gi 1958674160  81 AEFRYLDRLQQRQRQVLS 98
Cdd:pfam15737  99 AELRYWERLQQRQQQVLS 116
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 742-821 1.02e-14

PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. 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 Par6-like family 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: 467202 [Multi-domain]  Cd Length: 84  Bit Score: 69.90  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160 742 LQRPPEGTFGFCVAYGSGR-RDSGLYVQDMADlDTAKLYSGLLGVGDEILEMNGAKVAGLGLAHINELLVRVESLSIRVL 820
Cdd:cd06718     5 LIKPPGKPLGFYIRDGNGVeRVPGIFISRLVL-GSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTRLIITVK 83


                  .
gi 1958674160 821 R 821
Cdd:cd06718    84 P 84
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 739-802 1.18e-03

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 38.42  E-value: 1.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674160 739 QLQLQRPPEGTFGFCVAYGSGRRDSGLYVQDMADLDTAKLysGLLGVGDEILEMNGAKVAGLGL 802
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGDPGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTH 62
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 740-822 3.64e-03

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: 37.36  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160  740 LQLQRPPEGtFGFCVAyGSGRRDSGLYVQD-----MADLDtaklysGLLgVGDEILEMNGAKVAGLGLAHINELLVRV-E 813
Cdd:smart00228   5 VELEKGGGG-LGFSLV-GGKDEGGGVVVSSvvpgsPAAKA------GLR-VGDVILEVNGTSVEGLTHLEAVDLLKKAgG 75


                   ....*....
gi 1958674160  814 SLSIRVLRQ 822
Cdd:smart00228  76 KVTLTVLRG 84
 
Name Accession Description Interval E-value
DUF4685 pfam15737
Domain of unknown function (DUF4685); This domain family is found in eukaryotes, and is ...
 1-98 1.51e-37

Domain of unknown function (DUF4685); This domain family is found in eukaryotes, and is typically between 106 and 131 amino acids in length. There are two conserved sequence motifs: SGE and VRF.


Pssm-ID: 464834 [Multi-domain]  Cd Length: 117  Bit Score: 136.44  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160   1 MKAKTQPLRASHDIVPIIAQGSRNGQRSPAPDVRTTSASRESLqngnlNDPSSVEssnGQWPKQGMPLSHVRFEDESARE 80
Cdd:pfam15737  27 MKARTGPLRADHDIVPTVAQGSRDGQGSPAPKPRATSACRDSL-----SDSSSGE---GQGPRRGMSPSRVRFEDESARD 98

                          90
                  ....*....|....*...
gi 1958674160  81 AEFRYLDRLQQRQRQVLS 98
Cdd:pfam15737  99 AELRYWERLQQRQQQVLS 116
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 742-821 1.02e-14

PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. 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 Par6-like family 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: 467202 [Multi-domain]  Cd Length: 84  Bit Score: 69.90  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160 742 LQRPPEGTFGFCVAYGSGR-RDSGLYVQDMADlDTAKLYSGLLGVGDEILEMNGAKVAGLGLAHINELLVRVESLSIRVL 820
Cdd:cd06718     5 LIKPPGKPLGFYIRDGNGVeRVPGIFISRLVL-GSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTRLIITVK 83


                  .
gi 1958674160 821 R 821
Cdd:cd06718    84 P 84
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 742-800 3.44e-06

PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. 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 MAGI family PDZ5 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: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 45.65  E-value: 3.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958674160 742 LQRPPEGtFGFCVAYGSGRRDSGLYVQDMADLDTAKLySGLLGVGDEILEMNGAKVAGL 800
Cdd:cd06735     6 LERGPKG-FGFSIRGGREYNNMPLYVLRLAEDGPAQR-DGRLRVGDQILEINGESTQGM 62
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 742-809 4.84e-06

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.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 45.23  E-value: 4.84e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958674160 742 LQRPPEGTFGFCVAYGSGRrDSGLYVQDM-----ADLDtaklysGLLGVGDEILEMNGAKVAGLGLAHINELL 809
Cdd:cd00136     4 LEKDPGGGLGFSIRGGKDG-GGGIFVSRVepggpAARD------GRLRVGDRILEVNGVSLEGLTHEEAVELL 69
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 739-800 2.00e-05

PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. 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 PTPN13-like family 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: 467273 [Multi-domain]  Cd Length: 80  Bit Score: 43.49  E-value: 2.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958674160 739 QLQLQRPPEGTFGFCVAygSGRRDSGLYVQDMADLDTAKLySGLLGVGDEILEMNGAKVAGL 800
Cdd:cd23060     1 QIELEKPANGGLGFSLV--GGEGGSGIFVKSISPGGVADR-DGRLQVGDRLLQVNGESVIGL 59
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 739-802 1.18e-03

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 38.42  E-value: 1.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674160 739 QLQLQRPPEGTFGFCVAYGSGRRDSGLYVQDMADLDTAKLysGLLGVGDEILEMNGAKVAGLGL 802
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGDPGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTH 62
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 780-809 1.50e-03

PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. 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 MPP1-like family 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: 467208 [Multi-domain]  Cd Length: 80  Bit Score: 38.02  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958674160 780 SGLLGVGDEILEMNGAKVAGLGLAHINELL 809
Cdd:cd06726    38 SGLLHVGDEILEINGIPVSGKTVDELQKLL 67
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 740-822 3.64e-03

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: 37.36  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160  740 LQLQRPPEGtFGFCVAyGSGRRDSGLYVQD-----MADLDtaklysGLLgVGDEILEMNGAKVAGLGLAHINELLVRV-E 813
Cdd:smart00228   5 VELEKGGGG-LGFSLV-GGKDEGGGVVVSSvvpgsPAAKA------GLR-VGDVILEVNGTSVEGLTHLEAVDLLKKAgG 75


                   ....*....
gi 1958674160  814 SLSIRVLRQ 822
Cdd:smart00228  76 KVTLTVLRG 84
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 739-821 4.24e-03

PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 11 of MUPP1, PDZ domain 9 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. 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 MUPP1-like family PDZ11 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: 467162 [Multi-domain]  Cd Length: 87  Bit Score: 36.88  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160 739 QLQLQRPPEGTFGFCVAygsGRR-DSGLYVQDM-----ADLDtaklysGLLGVGDEILEMNGAKVAGLGLAHINELLVRV 812
Cdd:cd06674     5 TVELQKKPGRGLGLSIV---GKRnDTGVFVSDIvkggaADAD------GRLMQGDQILSVNGEDVRNASQEAAAALLKCA 75

                          90
                  ....*....|
gi 1958674160 813 E-SLSIRVLR 821
Cdd:cd06674    76 QgKVRLEVGR 85
PDZ0_MAGI-1_3-like cd06730
PDZ domain 0 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 742-809 5.86e-03

PDZ domain 0 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 0 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. 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 MAGI family PDZ0 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: 467212 [Multi-domain]  Cd Length: 85  Bit Score: 36.41  E-value: 5.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674160 742 LQRPPEGTFGFCVAYGSgrrDSGL--YVQDMAdLDTAKLYSGLLGVGDEILEMNGAKVAGLGLAHINELL 809
Cdd:cd06730     7 VSRGPDGELNLEIRGGA---ENGQfpYLGEVK-EDKVVYKSGKLHPGELLLEVNGTPVSGLTLRDVLAVI 72
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 739-812 9.36e-03

PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2)and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. 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 LNX family PDZ4 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: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 36.17  E-value: 9.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958674160 739 QLQLQRPPEGTFGFCV--AYGSGRRDSGLYVQDMAdLDTAKLYSGLLGVGDEILEMNGAKVAGLGLAHINELLVRV 812
Cdd:cd06680     2 DITLRRSSSGSLGFSIvgGYEESHGNQPFFVKSIV-PGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQ 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH