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Conserved domains on  [gi|71983519|ref|NP_001022007|]
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Protein shank [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 429-529 3.74e-47

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. 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 SHANK-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: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 163.15  E-value: 3.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 429 HETNIARILVIPRGVKGFGFILRGAKHVAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHD 508
Cdd:cd06746   1 DSIIDPRTVVLQKGDKGFGFVLRGAKAVGPILEFTPTPAFPALQYLESVDPGGVADKAGLKKGDFLLEINGEDVVKASHE 80

                        90       100
                ....*....|....*....|.
gi 71983519 509 EVVEFIQQAGDTITLKVITVD 529
Cdd:cd06746  81 QVVNLIRQSGNTLVLKVVTVT 101
FERM_F0_SHANK cd17091
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ...
 8-91 6.31e-40

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains proteins, SHANK1, SHANK2, and SHANK3; SHANK proteins (SHANK1, SHANK2, and SHANK3) are core components of the postsynaptic density (PSD) of excitatory synapses. They act as scaffolding molecules that cluster neurotransmitter receptors as well as cell adhesion molecules attaching them to the actin cytoskeleton. They play important roles in proper excitatory synapse and circuit function. Mutations in SHANK genes, especially in SHANK3 and SHANK2, may lead to neuropsychiatric disorders, such as autism spectrum disorder (ASD). SHANK proteins contain an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also termed DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold.


:

Pssm-ID: 340611  Cd Length: 84  Bit Score: 141.98  E-value: 6.31e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   8 VNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDCVPYLEL 87
Cdd:cd17091   1 IVLRISIPDLNLQKCLKFNPDDTVWDAKQQVLEKLAKDLKDALNYGLFLPPTNGKAGKFLDEERLLREYPLDGPVGYLEF 80


                ....
gi 71983519  88 KYKK 91
Cdd:cd17091  81 KYKR 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-336 2.06e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  95 KMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDF 174
Cdd:COG0666   3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 175 RNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLyynMLTADSND-QVAEILLREAADIGVTDMHGNHEIHQ 253
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL---HLAAYNGNlEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 254 ACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVSHIVGNPGVADVVQ 333
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239


                ...
gi 71983519 334 AHN 336
Cdd:COG0666 240 EAG 242
 
Name Accession Description Interval E-value
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 429-529 3.74e-47

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. 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 SHANK-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: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 163.15  E-value: 3.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 429 HETNIARILVIPRGVKGFGFILRGAKHVAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHD 508
Cdd:cd06746   1 DSIIDPRTVVLQKGDKGFGFVLRGAKAVGPILEFTPTPAFPALQYLESVDPGGVADKAGLKKGDFLLEINGEDVVKASHE 80

                        90       100
                ....*....|....*....|.
gi 71983519 509 EVVEFIQQAGDTITLKVITVD 529
Cdd:cd06746  81 QVVNLIRQSGNTLVLKVVTVT 101
FERM_F0_SHANK cd17091
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ...
 8-91 6.31e-40

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains proteins, SHANK1, SHANK2, and SHANK3; SHANK proteins (SHANK1, SHANK2, and SHANK3) are core components of the postsynaptic density (PSD) of excitatory synapses. They act as scaffolding molecules that cluster neurotransmitter receptors as well as cell adhesion molecules attaching them to the actin cytoskeleton. They play important roles in proper excitatory synapse and circuit function. Mutations in SHANK genes, especially in SHANK3 and SHANK2, may lead to neuropsychiatric disorders, such as autism spectrum disorder (ASD). SHANK proteins contain an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also termed DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold.


Pssm-ID: 340611  Cd Length: 84  Bit Score: 141.98  E-value: 6.31e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   8 VNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDCVPYLEL 87
Cdd:cd17091   1 IVLRISIPDLNLQKCLKFNPDDTVWDAKQQVLEKLAKDLKDALNYGLFLPPTNGKAGKFLDEERLLREYPLDGPVGYLEF 80


                ....
gi 71983519  88 KYKK 91
Cdd:cd17091  81 KYKR 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-336 2.06e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  95 KMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDF 174
Cdd:COG0666   3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 175 RNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLyynMLTADSND-QVAEILLREAADIGVTDMHGNHEIHQ 253
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL---HLAAYNGNlEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 254 ACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVSHIVGNPGVADVVQ 333
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239


                ...
gi 71983519 334 AHN 336
Cdd:COG0666 240 EAG 242
PHA03095 PHA03095
ankyrin-like protein; Provisional
 116-317 3.03e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  116 FMDYVQQKNNEKVEK-MCSQGLDANFHDAQGETPLTLAAGIPNNRA-VIVSLIGGGAHVDFRNSEGQTAMHkaAFLSS-- 191
Cdd:PHA03095  87 LHLYLYNATTLDVIKlLIKAGADVNAKDKVGRTPLHVYLSGFNINPkVIRLLLRKGADVNALDLYGMTPLA--VLLKSrn 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  192 --FENVKTLIELGASPNYRDPIGLTPLYYNMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTK--HVEHLL 267
Cdd:PHA03095 165 anVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLL 244

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 71983519  268 YFGGQIDAENVNGNSPLHVCAV-NNRPECARvLLFRGADHLAVNKQGQTAL 317
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPL 294
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 435-526 6.02e-15

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: 70.87  E-value: 6.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519    435 RILVIPRGVKGFGFILRGAKHVAMPLnfeptaqvpalqFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:smart00228   3 RLVELEKGGGGLGFSLVGGKDEGGGV------------VVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                           90
                   ....*....|..
gi 71983519    515 QQAGDTITLKVI 526
Cdd:smart00228  71 KKAGGKVTLTVL 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-209 4.29e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   116 FMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGipNNRAVIVS-LIgggAHVDFRN-SEGQTAMHKAAFLSSFE 193
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAK--NGHLEIVKlLL---EHADVNLkDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 71983519   194 NVKTLIELGASPNYRD 209
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 435-526 1.60e-08

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 52.67  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   435 RILVIPRGVKGFGFILRGakhvaMPLNFEPTAQVpalqffEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKG-----GSDQGDPGIFV------SEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLAL 69

                          90
                  ....*....|..
gi 71983519   515 QQAGDTITLKVI 526
Cdd:pfam00595  70 KGSGGKVTLTIL 81
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 483-532 3.09e-05

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 47.17  E-value: 3.09e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71983519 483 AVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQ-QAGDTITLKVITVDVAD 532
Cdd:COG0793  84 AEKAGIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLTIKRPGEGE 134
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 279-305 1.49e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.49e-03
                           10        20
                   ....*....|....*....|....*..
gi 71983519    279 NGNSPLHVCAVNNRPECARVLLFRGAD 305
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
FERM_f0 pfam16511
N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The ...
 9-91 2.02e-03

N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The fold is an ubiquitin-like fold joined to the f1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components, No binding partner has yet been found for it.


Pssm-ID: 465152  Cd Length: 81  Bit Score: 38.02  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519     9 NLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDcvpYLELK 88
Cdd:pfam16511   2 SLKISIVGSNVTKTMQFDPSTTVYDACRLIREKIPEGGLNASEYGLFLADEDPKKGRWLEPGRTLEYYDLRN---GDELE 78


                  ...
gi 71983519    89 YKK 91
Cdd:pfam16511  79 YKK 81
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 146-319 5.25e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 5.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 146 ETPLTLAAGiPNNRAVIVSLIGGgAHVDF--RNSEGQTAMHKAAFLSSFENVKTLIElgASPNY-RDPI------GLTPL 216
Cdd:cd22192  18 ESPLLLAAK-ENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLME--AAPELvNEPMtsdlyqGETAL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 217 YynMLTADSNDQVAEILLREAADIgVTDmhgnheihQACKNGLTKHVEHLLYFggqidaenvnGNSPLHVCAVNNRPECA 296
Cdd:cd22192  94 H--IAVVNQNLNLVRELIARGADV-VSP--------RATGTFFRPGPKNLIYY----------GEHPLSFAACVGNEEIV 152

                       170       180
                ....*....|....*....|...
gi 71983519 297 RVLLFRGADHLAVNKQGQTALHV 319
Cdd:cd22192 153 RLLIEHGADIRAQDSLGNTVLHI 175
 
Name Accession Description Interval E-value
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 429-529 3.74e-47

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. 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 SHANK-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: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 163.15  E-value: 3.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 429 HETNIARILVIPRGVKGFGFILRGAKHVAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHD 508
Cdd:cd06746   1 DSIIDPRTVVLQKGDKGFGFVLRGAKAVGPILEFTPTPAFPALQYLESVDPGGVADKAGLKKGDFLLEINGEDVVKASHE 80

                        90       100
                ....*....|....*....|.
gi 71983519 509 EVVEFIQQAGDTITLKVITVD 529
Cdd:cd06746  81 QVVNLIRQSGNTLVLKVVTVT 101
FERM_F0_SHANK cd17091
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ...
 8-91 6.31e-40

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains proteins, SHANK1, SHANK2, and SHANK3; SHANK proteins (SHANK1, SHANK2, and SHANK3) are core components of the postsynaptic density (PSD) of excitatory synapses. They act as scaffolding molecules that cluster neurotransmitter receptors as well as cell adhesion molecules attaching them to the actin cytoskeleton. They play important roles in proper excitatory synapse and circuit function. Mutations in SHANK genes, especially in SHANK3 and SHANK2, may lead to neuropsychiatric disorders, such as autism spectrum disorder (ASD). SHANK proteins contain an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also termed DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold.


Pssm-ID: 340611  Cd Length: 84  Bit Score: 141.98  E-value: 6.31e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   8 VNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDCVPYLEL 87
Cdd:cd17091   1 IVLRISIPDLNLQKCLKFNPDDTVWDAKQQVLEKLAKDLKDALNYGLFLPPTNGKAGKFLDEERLLREYPLDGPVGYLEF 80


                ....
gi 71983519  88 KYKK 91
Cdd:cd17091  81 KYKR 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-336 2.06e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  95 KMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDF 174
Cdd:COG0666   3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 175 RNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLyynMLTADSND-QVAEILLREAADIGVTDMHGNHEIHQ 253
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL---HLAAYNGNlEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 254 ACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVSHIVGNPGVADVVQ 333
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239


                ...
gi 71983519 334 AHN 336
Cdd:COG0666 240 EAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-318 7.30e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 7.30e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  95 KMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIpNNRAVIVSLIGGGAHVDF 174
Cdd:COG0666  37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN-GDLEIVKLLLEAGADVNA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 175 RNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLyynMLTADSND-QVAEILLREAADIGVTDMHGNHEIHQ 253
Cdd:COG0666 116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL---HLAAANGNlEIVKLLLEAGADVNARDNDGETPLHL 192

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983519 254 ACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALH 318
Cdd:COG0666 193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-317 1.58e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 1.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  95 KMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIpNNRAVIVSLIGGGAHVDF 174
Cdd:COG0666  70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN-GNLEIVKLLLEAGADVNA 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 175 RNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLyynMLTADSND-QVAEILLREAADIGVTDMHGNHEIHQ 253
Cdd:COG0666 149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL---HLAAENGHlEIVKLLLEAGADVNAKDNDGKTALDL 225

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983519 254 ACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTAL 317
Cdd:COG0666 226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
FERM_F0_SHANK3 cd17177
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ...
 7-91 3.56e-19

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains protein 3 (SHANK3); SHANK3, also termed proline-rich synapse-associated protein 2 (ProSAP2), is a postsynaptic density (PSD)-associated scaffolding protein at the excitatory synapse that interconnects neurotransmitter receptors and cell adhesion molecules by direct and indirect interactions with numerous other PSD-associated proteins. It is critical for synaptic plasticity and the trans-synaptic coupling between the reliability of presynaptic neurotransmitter release and postsynaptic responsiveness. It is a key component of a zinc-sensitive signaling system that regulates excitatory synaptic strength. Mutations in the SHANK3 synaptic scaffolding gene may lead to autism spectrum disorder and mental retardation, and the cause of human Phelan-McDermid syndrome (22q13.3 deletion syndrome) has been isolated to loss of function of one copy of the SHANK3 gene. SHANK3 contains an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also known as DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold.


Pssm-ID: 340697  Cd Length: 87  Bit Score: 82.99  E-value: 3.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   7 TVNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFT--DCVPY 84
Cdd:cd17177   1 ALVVRIGIPDLQQTKCLRLNPDAPVWASKQRILCTLNHSLKDVLNYGLFQPAFNGRAGKFLDEERLLREYPLPldTPVPY 80


                ....*..
gi 71983519  85 LELKYKK 91
Cdd:cd17177  81 LEFRYKR 87
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 436-525 1.14e-17

PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. 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 delphilin-like family PDZ2 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: 467226 [Multi-domain]  Cd Length: 75  Bit Score: 78.09  E-value: 1.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 436 ILVIPRGVKGFGFILRGAKHVamplnfeptaqvpalqFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQ 515
Cdd:cd06744   1 TVRVYRGNGSFGFTLRGHAPV----------------YIESVDPGSAAERAGLKPGDRILFLNGLDVRNCSHDKVVSLLQ 64

                        90
                ....*....|
gi 71983519 516 QAGDTITLKV 525
Cdd:cd06744  65 GSGSMPTLVV 74
PHA03095 PHA03095
ankyrin-like protein; Provisional
 116-317 3.03e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  116 FMDYVQQKNNEKVEK-MCSQGLDANFHDAQGETPLTLAAGIPNNRA-VIVSLIGGGAHVDFRNSEGQTAMHkaAFLSS-- 191
Cdd:PHA03095  87 LHLYLYNATTLDVIKlLIKAGADVNAKDKVGRTPLHVYLSGFNINPkVIRLLLRKGADVNALDLYGMTPLA--VLLKSrn 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  192 --FENVKTLIELGASPNYRDPIGLTPLYYNMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTK--HVEHLL 267
Cdd:PHA03095 165 anVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLL 244

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 71983519  268 YFGGQIDAENVNGNSPLHVCAV-NNRPECARvLLFRGADHLAVNKQGQTAL 317
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 116-319 4.03e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 4.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  116 FMDYVQQKNNEKVEKM---CSQGLDANFHDAQGETPLT--LAAGIPNNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLS 190
Cdd:PHA03095  15 LYDYLLNASNVTVEEVrrlLAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  191 SFENV-KTLIELGASPNYRDPIGLTPLYYNMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKN-GLT-KHVEHLL 267
Cdd:PHA03095  95 TTLDViKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSrNANvELLRLLI 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71983519  268 YFGGQIDAENVNGNSPLHVCAVNNRP--ECARVLLFRGADHLAVNKQGQTALHV 319
Cdd:PHA03095 175 DAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHS 228
FERM_F0_SHANK1 cd17175
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ...
 10-90 5.91e-17

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains protein 1 (SHANK1); SHANK1, also termed somatostatin receptor-interacting protein, or SSTR-interacting protein (SSTRIP), is a postsynaptic density (PSD)-associated scaffolding proteins at the excitatory synapse that interconnects neurotransmitter receptors and cell adhesion molecules by direct and indirect interactions with numerous other PSD-associated proteins. Mutations in the SHANK1 synaptic scaffolding gene may lead to autism spectrum disorder and mental retardation. SHANK1 contains an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also termed DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold.


Pssm-ID: 340695  Cd Length: 89  Bit Score: 76.96  E-value: 5.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  10 LQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYP--FTDCVPYLEL 87
Cdd:cd17175   6 FRIGIPDLHQTKCLRFNPDATIWVAKQQVLCTLNESLKDVLNYGLFQPATNGRDAKFLEEERLLREYPqsFEKGVPYLEF 85


                ...
gi 71983519  88 KYK 90
Cdd:cd17175  86 RYK 88
FERM_F0_SHANK2 cd17176
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ...
 6-91 1.34e-16

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in SH3 and multiple ankyrin repeat domains protein 2 (SHANK2); SHANK2, also termed cortactin-binding protein 1 (CortBP1), or proline-rich synapse-associated protein 1, is a postsynaptic density (PSD)-associated scaffolding proteins at the excitatory synapse that interconnects neurotransmitter receptors and cell adhesion molecules by direct and indirect interactions with numerous other PSD-associated proteins. It is strongly expressed in the cerebellum. Moreover, SHANK2 acts as a component of the albumin endocytic pathway in podocytes, and regulates renal albumin endocytosis. It also associates with and regulates Na+/H+ exchanger 3 (NHE3) and is involved in the fine regulation of transepithelial salt and water transport through affecting NHE3 expression and activity. Mutations in the SHANK2 synaptic scaffolding gene may lead to autism spectrum disorder and mental retardation. SHANK2 contains an N-terminal F0 domain of FERM (Band 4.1, ezrin, radixin, moesin), six ankyrin (ANK) repeats, one SH3 (Src homology 3) domain, one PDZ (PSD-95, Dlg, and ZO-1/2, also termed DHR or GLGF) domain, and a C-terminal SAM (sterile alpha motif) domain. This family corresponds to the F0 domain that adopts a ubiquitin-like fold.


Pssm-ID: 340696  Cd Length: 88  Bit Score: 75.79  E-value: 1.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   6 DTVNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDY--PFTDCVP 83
Cdd:cd17176   1 NTLVIRIIIPDLQQTKCIRFNPDATVWVAKQRILCTLNQSLKDVLNYGLFQPASNGRDGKFLDEERLLREYpqPVNKGVP 80


                ....*...
gi 71983519  84 YLELKYKK 91
Cdd:cd17176  81 SLEFRYKK 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 128-320 2.98e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.57  E-value: 2.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  128 VEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFEN-VKTLIELGASPN 206
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDiVITLLELGANVN 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  207 YRDPIGLTPLYYNMLTadSNDQVAEILLREAADIGVTDMHGNHEIHQA-CKNGLTKHVEHLLYFGGQIDAENVNGNSPLH 285
Cdd:PHA02876 370 ARDYCDKTPIHYAAVR--NNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 71983519  286 -VCAVNNRPECARVLLFRGADHLAVNKQGQTALHVS 320
Cdd:PHA02876 448 yACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIA 483
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 435-526 1.29e-15

PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. 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 NHERF-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: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 72.47  E-value: 1.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGFILRGAKHVAmplnfeptaqvpaLQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:cd06768   1 RLCHLVKGPEGYGFNLHAEKGRP-------------GHFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQVVEKI 67

                        90
                ....*....|..
gi 71983519 515 QQAGDTITLKVI 526
Cdd:cd06768  68 KASGNQVTLLVV 79
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 435-526 6.02e-15

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: 70.87  E-value: 6.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519    435 RILVIPRGVKGFGFILRGAKHVAMPLnfeptaqvpalqFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:smart00228   3 RLVELEKGGGGLGFSLVGGKDEGGGV------------VVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                           90
                   ....*....|..
gi 71983519    515 QQAGDTITLKVI 526
Cdd:smart00228  71 KKAGGKVTLTVL 82
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 435-527 2.07e-14

PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. 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 SNX27-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: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 69.74  E-value: 2.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGFILRGAKHVAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:cd23070   1 RVVTIVKSETGFGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLEGGAADKAGVRKGDRILEVNGVNVEGATHKQVVDLI 80

                        90
                ....*....|...
gi 71983519 515 QQAGDTITLKVIT 527
Cdd:cd23070  81 KSGGDELTLTVIS 93
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 435-525 2.71e-13

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: 66.03  E-value: 2.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGFILRGAKHVAMPLnfeptaqvpalqFFEGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEF 513
Cdd:cd00136   1 TVTLEKDPGGGLGFSIRGGKDGGGGI------------FVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTHEEAVEL 68

                        90
                ....*....|..
gi 71983519 514 IQQAGDTITLKV 525
Cdd:cd00136  69 LKSAGGEVTLTV 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-209 4.29e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   116 FMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGipNNRAVIVS-LIgggAHVDFRN-SEGQTAMHKAAFLSSFE 193
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAK--NGHLEIVKlLL---EHADVNLkDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 71983519   194 NVKTLIELGASPNYRD 209
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 435-526 5.38e-12

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. 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 rhophilin-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: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 62.22  E-value: 5.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGFILRGAKHVamplnfeptaQVpalqffEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:cd06712   2 RTVHLTKEEGGFGFTLRGDSPV----------QV------ASVDPGSCAAEAGLKEGDYIVSVGGVDCKWSKHSEVVKLL 65

                        90
                ....*....|...
gi 71983519 515 QQAG-DTITLKVI 526
Cdd:cd06712  66 KSAGeEGLELQVV 78
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 157-320 6.99e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 6.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  157 NNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFEN-----VKTLIELGASPNYRDPIGLTPLYYNMLTADSNDQVAE 231
Cdd:PHA03100  46 RNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  232 ILLREAADIGVTDMHGNHEIHQACKNG---------LTKH---------VEHLLYFGGQIDAENVNGNSPLHVCAVNNRP 293
Cdd:PHA03100 126 YLLDNGANVNIKNSDGENLLHLYLESNkidlkilklLIDKgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNP 205

                        170       180
                 ....*....|....*....|....*..
gi 71983519  294 ECARVLLFRGADHLAVNKQGQTALHVS 320
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
251-329 7.69e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 7.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   251 IHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLfrgaDHLAVNKQ--GQTALHVSHIVGNPGV 328
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKdnGRTALHYAARSGHLEI 76


                  .
gi 71983519   329 A 329
Cdd:pfam12796  77 V 77
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 116-332 1.33e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  116 FMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGG----------------------GAHVD 173
Cdd:PHA02874  39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtsilpipciekdmiktildcGIDVN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  174 FRNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLYynMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQ 253
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH--IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983519  254 ACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPecARVLLFRGADHLAVNKQGQTALHvsHIVGNPGVADVV 332
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLH--HAINPPCDIDII 271
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 435-514 4.57e-11

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. 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 RGS12-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: 467194 [Multi-domain]  Cd Length: 76  Bit Score: 59.57  E-value: 4.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGFILRGakhvamplnfeptaQVPALqfFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:cd06710   1 RTVEIARGRAGYGFTISG--------------QAPCV--LSCVVRGSPADVAGLKAGDQILAVNGINVSKASHEDVVKLI 64
PDZ_MYO18-like cd06747
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ...
 440-525 4.91e-11

PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). 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 MYO18-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: 467229 [Multi-domain]  Cd Length: 90  Bit Score: 60.02  E-value: 4.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 440 PRGvkGFGFILRgaKHVAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGD 519
Cdd:cd06747   8 PTG--DFGFSLR--RGTIVERGPDDGQELKRTVHFAEPGAGTKNLATGLLPGDRLIEVNGVNVENASRDEIIEMIRKSGD 83


                ....*.
gi 71983519 520 TITLKV 525
Cdd:cd06747  84 TVTLKV 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 80-318 7.85e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 7.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   80 DCVPYLELKYKKRVYKMLNLDEKQLKAMH--------TKGQLKKFMDY-------VQQKNNEKVEKMCSQGLDANFHDAQ 144
Cdd:PHA02876  98 DCDIILDIKYASIILNKHKLDEACIHILKeaisgndiHYDKINESIEYmklikerIQQDELLIAEMLLEGGADVNAKDIY 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  145 GETPLTLAAGIPNNRAVIVsLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDpigltplyYNMLTAD 224
Cdd:PHA02876 178 CITPIHYAAERGNAKMVNL-LLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND--------LSLLKAI 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  225 SNDQVAEILLREAADIGVT--DMHGNHEIHQACKN-GLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNN-RPECARVLL 300
Cdd:PHA02876 249 RNEDLETSLLLYDAGFSVNsiDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLI 328

                        250
                 ....*....|....*...
gi 71983519  301 FRGADHLAVNKQGQTALH 318
Cdd:PHA02876 329 MLGADVNAADRLYITPLH 346
Ank_2 pfam12796
Ankyrin repeats (3 copies);
183-305 1.20e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   183 MHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLyynmltadsndqvaeillreaadigvtdmhgnheiHQACKNGLTKH 262
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL-----------------------------------HLAAKNGHLEI 45

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 71983519   263 VEHLLYFgGQIDAENvNGNSPLHVCAVNNRPECARVLLFRGAD 305
Cdd:pfam12796  46 VKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 92-320 3.17e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 3.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   92 RVYKMLNLDEKQ--LKAM----HTKGQLKK--------FMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPN 157
Cdd:PHA02878   3 KLYKSMYTDNYEtiLKYIeyidHTENYSTSaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  158 NRAvIVSLIGGGAHVDFRNSEG--QTAMH-------KAAFLSSFEN----------------------VKTLIELGASPN 206
Cdd:PHA02878  83 KLG-MKEMIRSINKCSVFYTLVaiKDAFNnrnveifKIILTNRYKNiqtidlvyidkkskddiieaeiTKLLLSYGADIN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  207 YRDP-IGLTPLYYnmLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLH 285
Cdd:PHA02878 162 MKDRhKGNTALHY--ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 71983519  286 --VCAVNNRpECARVLLFRGADhlaVNKQ----GQTALHVS 320
Cdd:PHA02878 240 isVGYCKDY-DILKLLLEHGVD---VNAKsyilGLTALHSS 276
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 438-523 3.66e-10

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: 57.20  E-value: 3.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 438 VIPRGVKGFGFILRGAKHVA-MPLnfeptaqvpalqFFEGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQ 515
Cdd:cd06735   5 ELERGPKGFGFSIRGGREYNnMPL------------YVLRLAEDGPAQRDGrLRVGDQILEINGESTQGMTHAQAIELIR 72


                ....*...
gi 71983519 516 QAGDTITL 523
Cdd:cd06735  73 SGGSVVRL 80
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 436-525 4.14e-09

PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. 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 syntrophin-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: 467262 [Multi-domain]  Cd Length: 83  Bit Score: 54.12  E-value: 4.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 436 ILVIPRGVKGFGFILRGAKHVAMPlnfeptaqVPALQFFEG--VDMSGMavragLRPGDYLLEIDGIDVRRCSHDEVVEF 513
Cdd:cd06801   3 VRVVKQDVGGLGISIKGGAEHKMP--------ILISKIFKGqaADQTGQ-----LFVGDAILSVNGENLEDATHDEAVQA 69

                        90
                ....*....|..
gi 71983519 514 IQQAGDTITLKV 525
Cdd:cd06801  70 LKNAGDEVTLTV 81
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 477-526 4.62e-09

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. 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 tamalin-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: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 54.17  E-value: 4.62e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71983519 477 VDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06713  42 VHEDSPAYLAGLTAGDVILSVNGVSVEGASHQEIVELIRSSGNTLRLETL 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 104-378 7.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 7.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  104 LKAMHTKGQLKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDFRNSEGQTAM 183
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPI 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  184 HKAAFLSSFENVKTLIELGAS-PNYRDPIGlTPLYYNMLTADSNDQVaEILLREAADIGVTDMHGNHEIHQACKNGLTKH 262
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADiEALSQKIG-TALHFALCGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNCKLD 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  263 V-EHLLYFGGQIDAENVNGNSPLHVCAvnNRPECARVLLFRGA---DHLAVNKQ-GQTALHVSHIVGNPGVADVVQaHNP 337
Cdd:PHA02876 458 ViEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAelrDSRVLHKSlNDNMFSFRYIIAHICIQDFIR-HDI 534

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 71983519  338 KSSVpyrgtpqySTRRRLSSTITRRRSMSQSSICSQDVYRT 378
Cdd:PHA02876 535 RNEV--------NPLKRVPTRFTSLRESFKEIIQSDDTFKR 567
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 130-325 1.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  130 KMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVsLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIELGASPN--- 206
Cdd:PHA02875  20 RLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKL-LMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdvf 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  207 YRDpiGLTPLYynMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHV 286
Cdd:PHA02875  99 YKD--GMTPLH--LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 71983519  287 CAVNNRPECARVLLFRGADHLAVNKQGQTALHVSHIVGN 325
Cdd:PHA02875 175 AMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENN 213
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 435-526 1.60e-08

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 52.67  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   435 RILVIPRGVKGFGFILRGakhvaMPLNFEPTAQVpalqffEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKG-----GSDQGDPGIFV------SEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLAL 69

                          90
                  ....*....|..
gi 71983519   515 QQAGDTITLKVI 526
Cdd:pfam00595  70 KGSGGKVTLTIL 81
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 124-240 2.64e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  124 NNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVS-----------------LIGGGAHVDFRNSEGQTAMHKA 186
Cdd:PHA03100 120 SYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLHYA 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71983519  187 AFLSSFENVKTLIELGASPNYRDPIGLTPLYYNMLTadSNDQVAEILLREAADI 240
Cdd:PHA03100 200 VYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN--NNKEIFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
157-244 2.81e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   157 NNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIElGASPNYRDpIGLTPLYYnmltADSNDQ--VAEILL 234
Cdd:pfam12796   8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHY----AARSGHleIVKLLL 81

                          90
                  ....*....|
gi 71983519   235 REAADIGVTD 244
Cdd:pfam12796  82 EKGADINVKD 91
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 473-525 3.75e-08

PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. 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 Dlg5-like 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: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 51.56  E-value: 3.75e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71983519 473 FFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06767  28 FVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 120-305 4.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 4.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  120 VQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAGIPNNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLI 199
Cdd:PHA02875  43 MKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  200 ELGASPNYRDPIGLTPLYYNMLTADSNdqVAEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVN 279
Cdd:PHA02875 123 ARGADPDIPNTDKFSPLHLAVMMGDIK--GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200

                        170       180
                 ....*....|....*....|....*..
gi 71983519  280 GNSPLHVCAV-NNRPECARVLLFRGAD 305
Cdd:PHA02875 201 GCVAALCYAIeNNKIDIVRLFIKRGAD 227
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 483-526 5.25e-08

PDZ domain 4 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 4 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 PDZ4 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: 467216 [Multi-domain]  Cd Length: 84  Bit Score: 51.08  E-value: 5.25e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 71983519 483 AVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06734  39 ADRCGqLKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIV 83
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 435-525 7.81e-08

PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two 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 Dlg-like 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: 467257 [Multi-domain]  Cd Length: 91  Bit Score: 50.82  E-value: 7.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGF-ILRGAKHVAMPLNFePTAQVPAlqffegvDMSGMavragLRPGDYLLEIDGIDVRRCSHDEVVEF 513
Cdd:cd06795   3 RKIVLHKGSTGLGFnIVGGEDGEGIFISF-ILAGGPA-------DLSGE-----LRRGDQILSVNGVDLRNATHEQAAAA 69

                        90
                ....*....|..
gi 71983519 514 IQQAGDTITLKV 525
Cdd:cd06795  70 LKNAGQTVTIIA 81
PHA03095 PHA03095
ankyrin-like protein; Provisional
 135-290 2.48e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  135 GLDANFHDAQGETPLtlAAGIPNNRA---VIVSLIGGGAHVDFRNSEGQTAMHKaaFLSSF----ENVKTLIELGASPNY 207
Cdd:PHA03095 142 GADVNALDLYGMTPL--AVLLKSRNAnveLLRLLIDAGADVYAVDDRFRSLLHH--HLQSFkpraRIVRELIRAGCDPAA 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  208 RDPIGLTPLYYNMLTADSNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPL--- 284
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLslm 297

                        170
                 ....*....|
gi 71983519  285 ----HVCAVN 290
Cdd:PHA03095 298 vrnnNGRAVR 307
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 483-525 3.01e-07

circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 49.02  E-value: 3.01e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 71983519 483 AVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQ-QAGDTITLKV 525
Cdd:cd06782  27 AEKAGIKPGDVIVAVDGESVRGMSLDEVVKLLRgPKGTKVKLTI 70
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 112-256 5.53e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  112 QLKKFMDYVQQKNN-EKVEKMCSQGLDANFHDAQGETPLTLAAGiPNNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLS 190
Cdd:PHA02874 123 ELKTFLHYAIKKGDlESIKMLFEYGADVNIEDDNGCYPIHIAIK-HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  191 SFENVKTLIELG-------------------------------ASPNYRDPIGLTPLYYNMLTADSNDqVAEILLREAAD 239
Cdd:PHA02874 202 DYACIKLLIDHGnhimnkckngftplhnaiihnrsaiellinnASINDQDIDGSTPLHHAINPPCDID-IIDILLYHKAD 280

                        170
                 ....*....|....*..
gi 71983519  240 IGVTDMHGNHEIHQACK 256
Cdd:PHA02874 281 ISIKDNKGENPIDTAFK 297
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 446-525 6.45e-07

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 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 PDLIM-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: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 47.91  E-value: 6.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 446 FGFILRGAKHVAMPLNFEPtaqvpalqffegVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06753  10 WGFRLQGGKDFNQPLTISR------------VTPGGKAAQANLRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTL 77
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 431-532 7.54e-07

PDZ domain 4 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 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: 467174 [Multi-domain]  Cd Length: 99  Bit Score: 48.50  E-value: 7.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 431 TNIARILVIPRGVKGFGFILRGAKHVAMPLnFEPtaqvPALQFfegVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDE 509
Cdd:cd06686   5 TETTEVILRGDPLKGFGIQLQGGVFATETL-SSP----PLISF---IEPDSPAERCGvLQVGDRVLSINGIPTEDRTLEE 76

                        90       100
                ....*....|....*....|...
gi 71983519 510 VVEFIQQAGDTITLKvITVDVAD 532
Cdd:cd06686  77 ANQLLRDSASKVTLE-IEFDVAE 98
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 441-528 8.22e-07

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. 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 harmonin family PDZ1 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: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 47.64  E-value: 8.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 441 RGVKGFGFILRGAKHVAMPLnfeptaqvpalqFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAgDT 520
Cdd:cd06737  10 RGPESLGFSVRGGLEHGCGL------------FVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINLIKTK-KT 76


                ....*...
gi 71983519 521 ITLKVITV 528
Cdd:cd06737  77 VSLKVRHV 84
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 488-525 1.05e-06

PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 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 7 of MUPP1 and PDZ domain 6 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 PDZ7 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: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 47.70  E-value: 1.05e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 71983519 488 LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06671  55 LKTGDRILEVNGVDLRNATHEEAVEAIRNAGNPVVFLV 92
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 481-525 1.18e-06

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. 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 Scribble-like 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: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 47.25  E-value: 1.18e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 71983519 481 GMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06702  43 GAAAKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPGQEIKLLV 87
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 446-525 1.59e-06

PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. 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 Zasp52-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: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 46.75  E-value: 1.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 446 FGFILRGAKHVAMPLnfeptaqvpalqFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd23068  13 WGFRLQGGADFGQPL------------SIQKVNPGSPADKAGLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTV 80
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 146-320 1.63e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  146 ETPLTLAAGIPNNRAVIVSL-IGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIELGASPNyrdpigLTPLyynmltAD 224
Cdd:PHA02874  34 ETTTPLIDAIRSGDAKIVELfIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS------ILPI------PC 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  225 SNDQVAEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGA 304
Cdd:PHA02874 102 IEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                        170
                 ....*....|....*.
gi 71983519  305 DHLAVNKQGQTALHVS 320
Cdd:PHA02874 182 YANVKDNNGESPLHNA 197
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 446-525 1.74e-06

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the 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 SYNPO2-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: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 46.53  E-value: 1.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 446 FGFILRGAKHVAMPLnfeptaQVPAlqffegVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd10820  10 WGFRLQGGSEQKKPL------QVAK------IRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLI 77
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 441-526 2.21e-06

PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. 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 SYNJ2BP-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: 467193 [Multi-domain]  Cd Length: 86  Bit Score: 46.52  E-value: 2.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 441 RGVKGFGFILRGAkhVAMPLNFEPTAQvpalqFFEGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGD 519
Cdd:cd06709   7 RGPSGLGFNIVGG--TDQPYIPNDSGI-----YVAKIKEDGAAAIDGrLQEGDKILEINGQSLENLTHQDAVELFRNAGE 79


                ....*..
gi 71983519 520 TITLKVI 526
Cdd:cd06709  80 DVKLKVQ 86
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 445-525 2.74e-06

PDZ domain 2 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 PDZ2 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: 467169 [Multi-domain]  Cd Length: 89  Bit Score: 46.46  E-value: 2.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 445 GFGFILRGAKHVAMPLNFEPTAQvpalqffeGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITL 523
Cdd:cd06681  13 SFGFVIRGGAHEDRNKSRPLTVT--------HVRPGGPADREGtIKPGDRLLSVDGISLHGATHAEAMSILKQCGQEATL 84


                ..
gi 71983519 524 KV 525
Cdd:cd06681  85 LI 86
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 91-310 2.90e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   91 KRVYKMLNLDEKQLK-AMHTKGQ-----LKKFMDYVQQKNNEKVEKMCSQGLDANFHDAQGETPLTLAAgiPNNRAVIVS 164
Cdd:PLN03192 466 KTLSQLLRLKTSTLIeAMQTRQEdnvviLKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVAS--TGNAALLEE 543

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  165 LIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLYyNMLTADSNdQVAEILLREAAdigVTD 244
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALW-NAISAKHH-KIFRILYHFAS---ISD 618

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983519  245 MH-GNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVN 310
Cdd:PLN03192 619 PHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PDZ_MAST cd06705
PDZ domain of the microtubule-associated serine-threonine (MAST) protein kinase family; PDZ ...
 437-526 3.56e-06

PDZ domain of the microtubule-associated serine-threonine (MAST) protein kinase family; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinases, including MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain; MAST family member MASTL is a shorter protein lacking the PDZ domain. The PDZ domain gives the MAST family the capacity to scaffold its own kinase activity. These kinases are implicated in the inhibition of neurite outgrowth and regeneration in cultured cells. Their binding partners include microtubules, beta2-syntrophin, TNF receptor-associated factor 6 (TRAF6), cAMP-regulated phosphoprotein (ARPP-16), and PTEN. This family also includes Caenorhabditis elegans KIN-4 MAST kinase, a key longevity factor acting through binding PTEN phosphatase, and Drosophila Drop out which regulates dynein-dependent transport during embryonic development. 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 MAST-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: 467189 [Multi-domain]  Cd Length: 93  Bit Score: 46.08  E-value: 3.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 437 LVIPRGVKGFGFILRGAK------------HVAMplnfeptaqvpalqffeGVDMSGMAVRAGLRPGDYLLEIDGIDVRR 504
Cdd:cd06705   5 IVIKKGPRGFGFTLRAIRvyigdsdvytvhHLVT-----------------AVEEGSPAYEAGLRPGDLITHVNGEPVQG 67

                        90       100
                ....*....|....*....|..
gi 71983519 505 CSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06705  68 LLHTQVVQLILKGGNKVSIRAT 89
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 473-525 4.57e-06

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 44.83  E-value: 4.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71983519   473 FFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRrcSHDEVVEFIQQAGDT-ITLKV 525
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVR--SLEDVARLLQGSAGEsVTLTV 52
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 481-526 5.20e-06

PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. 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 Scribble-like family PDZ1 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: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 45.73  E-value: 5.20e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71983519 481 GMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06704  41 GPAAKAGVRVGDKLLEVNGVDLVDADHHEAVEALKNSGNTVTMVVL 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 180-325 5.89e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 5.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  180 QTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLYYNMLTADSndQVAEILLREAADIGVTDMHGNHEIHQACKNGL 259
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDS--EAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983519  260 TKHVEHLLYFGGQI-DAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVSHIVGN 325
Cdd:PHA02875  81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 435-525 6.46e-06

PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. 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 Lin-7-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: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 45.12  E-value: 6.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGFILRGAKHVAMPLnfeptaqvpalqFFEGVDMSGMAVR-AGLRPGDYLLEIDGIDVRRCSHDEVVEF 513
Cdd:cd06796   3 RVVELPKTEEGLGFNVMGGKEQNSPI------------YISRIIPGGVADRhGGLKRGDQLLSVNGVSVEGEHHEKAVEL 70

                        90
                ....*....|..
gi 71983519 514 IQQAGDTITLKV 525
Cdd:cd06796  71 LKAAQGSVKLVV 82
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 483-525 8.66e-06

PDZ domain 5 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 domain PDZ5 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: 467170 [Multi-domain]  Cd Length: 85  Bit Score: 45.03  E-value: 8.66e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 71983519 483 AVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06682  40 AHRTGtLEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKI 83
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-301 9.21e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 9.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  118 DYVQQKNNEKVEKMCSQGLDANFHDA-QGETPLTLAAGIPNNRaVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVK 196
Cdd:PHA02878 140 SKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQR-LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVH 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  197 TLIELGASPNYRDPIGLTPLYYNMLTADSNDqVAEILLREAADI-------GVTDMHGNheIHQACKNGLtkhvehLLYF 269
Cdd:PHA02878 219 ILLENGASTDARDKCGNTPLHISVGYCKDYD-ILKLLLEHGVDVnaksyilGLTALHSS--IKSERKLKL------LLEY 289

                        170       180       190
                 ....*....|....*....|....*....|....
gi 71983519  270 GGQIDAENVNGNSPLHVcAVNNRP--ECARVLLF 301
Cdd:PHA02878 290 GADINSLNSYKLTPLSS-AVKQYLciNIGRILIS 322
PHA02946 PHA02946
ankyin-like protein; Provisional
 84-286 1.11e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   84 YLELkYKKRVYKMLNLDEKQLKAMHTKGQLKKFMDYVQQKNNEK--VEKMCSQGLDANFHDAQGETPLTLAAGIPNNRaV 161
Cdd:PHA02946  10 YLSL-YAKYNSKNLDVFRNMLQAIEPSGNYHILHAYCGIKGLDErfVEELLHRGYSPNETDDDGNYPLHIASKINNNR-I 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  162 IVSLIGGGAHVDFRNSEGQTAMHkaaFLSS-----FENVKTLIELGASPNYR-DPIGLTPLyynMLTADSNDQVAEILLR 235
Cdd:PHA02946  88 VAMLLTHGADPNACDKQHKTPLY---YLSGtddevIERINLLVQYGAKINNSvDEEGCGPL---LACTDPSERVFKKIMS 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71983519  236 EAADIGVTDMHGNHEIHQ--ACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHV 286
Cdd:PHA02946 162 IGFEARIVDKFGKNHIHRhlMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
PDZ_ARHGEF11-12-like cd23069
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 435-525 1.36e-05

PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGEF11, ARHGEF12, and related domains. This subfamily includes the GEFs (guanine exchange factors) ARHGEF11 (Rho guanine nucleotide exchange factor 11, known as PDZ-RhoGEF) and ARHGEF12 (Rho guanine nucleotide exchange factor 12, also known as leukemia-associated RhoGEF). GEFs activate Rho GTPases by promoting GTP binding. ARHGEF11/12 are regulators of G protein signaling (RGS) domain-containing GEFs; the RGS domain mediates their binding to and activation of Galpha (and Gq also in the case of ARHGEF12), in response to G-protein coupled receptor activation. ARHGEF11 and 12 are involved in serum-signaling, and regulate Yes-Associated Protein (YAP1)-dependent transcription. The ARHGEF12 PDZ domain binds plexin-B1 and the receptor tyrosine kinase insulin-like growth factor receptor (IGF-R1) beta-subunit. ARHGEF12 also interacts with glutamate receptor delta-1(GluD1), a postsynaptic organizer of inhibitory synapses in cortical pyramidal neurons. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGEF11-12-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: 467282 [Multi-domain]  Cd Length: 76  Bit Score: 43.92  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGFILRGAKHVamplnfeptaqvpalqFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFI 514
Cdd:cd23069   2 RCVVIQRDENGYGLTVSGDNPV----------------FVQSVKEGGAAYRAGVQEGDRIIKVNGTLVTHSNHLEVVKLI 65

                        90
                ....*....|.
gi 71983519 515 qQAGDTITLKV 525
Cdd:cd23069  66 -KSGSYVALTL 75
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 215-300 1.85e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  215 PLYYNMLT------ADSNDQV-AEILLREAADIGVTDMHGNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVC 287
Cdd:PTZ00322  76 PVVAHMLTvelcqlAASGDAVgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155

                         90
                 ....*....|...
gi 71983519  288 AVNNRPECARVLL 300
Cdd:PTZ00322 156 EENGFREVVQLLS 168
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 488-525 2.06e-05

PDZ domain 4 of protein tyrosine 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 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. 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 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: 467182 [Multi-domain]  Cd Length: 85  Bit Score: 43.83  E-value: 2.06e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 71983519 488 LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06696  45 LRPGDRLIMVNGVDVTNMSHTEAVSLLRAAPKEVTLVL 82
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 477-526 2.22e-05

PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. 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 PDZRN4-like family PDZ1 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: 467199 [Multi-domain]  Cd Length: 92  Bit Score: 43.92  E-value: 2.22e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71983519 477 VDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06715  42 VENGPAADEGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKEPIVVQVL 91
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 483-553 2.58e-05

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with its associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains 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. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467638 [Multi-domain]  Cd Length: 83  Bit Score: 43.33  E-value: 2.58e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983519 483 AVRAGLRPGDYLLEIDGIDVRrcSHDEVVEFIQQ-AGDTITLKVitvdvadmSRGGTIVHR---PPTDTHDAHGV 553
Cdd:cd23081  12 AAEAGLKPGDRILKIDGQKVR--TWEDIVRIVREnPGKPLTLKI--------ERDGKILTVtvtPELVEVEGKGV 76
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 483-532 3.09e-05

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 47.17  E-value: 3.09e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71983519 483 AVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQ-QAGDTITLKVITVDVAD 532
Cdd:COG0793  84 AEKAGIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLTIKRPGEGE 134
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 441-518 3.49e-05

PDZ domain 3 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 3 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 PDZ3 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: 467215 [Multi-domain]  Cd Length: 85  Bit Score: 42.98  E-value: 3.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 441 RGVKGFGF-ILRGAkhvamplnfEPTAQVPALQFFEGvdmsGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAG 518
Cdd:cd06733   8 RQETGFGFrILGGT---------EEGSQVSIGAIVPG----GAADLDGrLRTGDELLSVDGVNVVGASHHKVVDLMGNAA 74
FERM_F0_TLN cd17089
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin and ...
 8-92 4.21e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain, found in Talin and similar proteins; Talin is a cytoskeletal protein that activates integrins and couples them to cytoskeletal actin. Talin consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain that is joined to the F1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components; no binding partner has yet been found for it.


Pssm-ID: 340609  Cd Length: 84  Bit Score: 43.01  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   8 VNLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALP-QAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDcvpYLE 86
Cdd:cd17089   1 LSLKIHIVKSGIVKTMQFDPSMTVYDACRLIREKIPEAAQgQASDYGLFLPDEDPKKGRWLEPDRTLEYYDLRN---GDE 77


                ....*.
gi 71983519  87 LKYKKR 92
Cdd:cd17089  78 LEYKKK 83
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 444-523 4.35e-05

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 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 PTPN13 family PDZ1 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: 467180 [Multi-domain]  Cd Length: 92  Bit Score: 43.15  E-value: 4.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 444 KGFGFILRGAkhvamplnfEPTAQVPALQFFEGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTIT 522
Cdd:cd06694  13 KGLGFTIVGG---------ENSGSLDLGIFVKSIIPGGPADKDGrIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVE 83


                .
gi 71983519 523 L 523
Cdd:cd06694  84 L 84
PDZ2_MAGI-1_3-like cd06732
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 487-516 6.75e-05

PDZ domain 2 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 2 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 PDZ2 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: 467214 [Multi-domain]  Cd Length: 82  Bit Score: 42.16  E-value: 6.75e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 71983519 487 GLRPGDYLLEIDGIDVRRCSHDEVVEFIQQ 516
Cdd:cd06732  39 GLQEGDLIVEINGQNVQNLSHAQVVDVLKE 68
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 481-526 7.31e-05

PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). 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: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 42.23  E-value: 7.31e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71983519 481 GMAVRAGL-RPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06799  34 GAADRSGLiHVGDELREVNGISVEGKDPEEVIQILANSQGPITFKLI 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
181-218 8.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 8.10e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 71983519   181 TAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLYY 218
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank_2 pfam12796
Ankyrin repeats (3 copies);
284-347 8.84e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 8.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983519   284 LHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVSHIVGNPGVADVVQAHNPKSSVPYRGTP 347
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 473-525 1.20e-04

PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. 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 Scribble-like 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: 467185 [Multi-domain]  Cd Length: 98  Bit Score: 41.83  E-value: 1.20e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 71983519 473 FFEGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06701  41 FISKINPDGAAARDGrLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTLLV 94
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 437-525 1.57e-04

PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. 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 INAD-like family PDZ1 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: 467276 [Multi-domain]  Cd Length: 87  Bit Score: 41.35  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 437 LVIPRGVK-GFGF-ILRGAkhvampLNFEPTAQVPALqFFEGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEF 513
Cdd:cd23063   2 VVIEKTEKkSFGIcIVRGE------VKVSPNTKTTGI-FIKGIIPDSPAHKCGrLKVGDRILSVNGNDVRNSTEQAAIDL 74

                        90
                ....*....|..
gi 71983519 514 IQQAGDTITLKV 525
Cdd:cd23063  75 IKEADFKIVLEI 86
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 483-553 1.62e-04

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 45.08  E-value: 1.62e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71983519 483 AVRAGLRPGDYLLEIDGIDVRrcSHDEVVEFIQQ-AGDTITLKVitvdvadmSRGGTIVH---RPPTDTHDAHGV 553
Cdd:COG0750 141 AAKAGLQPGDRIVAINGQPVT--SWDDLVDIIRAsPGKPLTLTV--------ERDGEELTltvTPRLVEEDGVGR 205
PDZ_DEPTOR-like cd23067
PDZ domain of DEP domain-containing mTOR-interacting protein (DEPTOR), and related domains; ...
 445-526 1.84e-04

PDZ domain of DEP domain-containing mTOR-interacting protein (DEPTOR), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of DEPTOR, and related domains. DEPTOR (also known as DEP domain-containing protein 6, DEP6) is a regulatory protein of mTOR signaling; it is a negative regulator of both the mTORC1 and mTORC2 signaling pathways. DEPTOR's PDZ domain binds to mTOR's FAT domain to suppress mTOR's kinase activity. The DEPTOR PDZ domain also binds lysine-specific demethylase 4A (KDM4A), leucine-rich repeat containing 4 (LRRC4), p38gamma, and major intrinsically disordered Notch2-binding receptor 1 (MINAR1, also known as Ubtor). DEPTOR also interacts with salt-inducible kinase 3 (SIK3). 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 DEPTOR-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: 467280 [Multi-domain]  Cd Length: 75  Bit Score: 40.86  E-value: 1.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 445 GFGFILRGAKHVamplnfeptaqvpalqFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLK 524
Cdd:cd23067  10 GWGFVVRGSKPC----------------HIQAVDPSGPAAAAGMKVCQFIVSVNGLNVLHMDHRTVSNLILTGPRTIVME 73


                ..
gi 71983519 525 VI 526
Cdd:cd23067  74 VM 75
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 481-525 2.06e-04

PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of TAX1BP3, and related domains. TAX1BP3 (also known as glutaminase-interacting protein 3, tax interaction protein 1, TIP-1, tax-interacting protein 1) may regulate a number of protein-protein interactions by competing for PDZ domain binding sites. TAX1BP3 binds beta-catenin and may act as an inhibitor of the Wnt signaling pathway. It competes with LIN7A (also known as Lin-7A or LIN-7A) for inward rectifier potassium channel 4 (KCNJ4) binding, and thereby promotes KCNJ4 internalization. It may play a role in the Rho signaling pathway, and in the activation of CDC42 by the viral protein HPV16 E6. Binding partners of the TAX1BP3 PDZ domain include beta-catenin, KCNJ4, glutaminase liver isoform (GLS2), rho guanine nucleotide exchange factor 16 (ARHGEF16), rhotekin, and CDK5 regulatory subunit-associated protein 3 (also known as LAPZ). 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 TAX1BP3-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: 467265 [Multi-domain]  Cd Length: 94  Bit Score: 41.17  E-value: 2.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 71983519 481 GMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd10822  48 GPAEKAGLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKPVLRMLV 92
Ank_5 pfam13857
Ankyrin repeats (many copies);
266-319 2.21e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71983519   266 LLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHV 319
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 481-526 2.25e-04

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: 40.71  E-value: 2.25e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71983519 481 GMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06726  33 GMAHRSGlLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLI 79
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 476-537 2.63e-04

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


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 43.98  E-value: 2.63e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71983519 476 GVDMSGMAVRAGLRPGDYLLEIDGIDVRrcSHDEVVEFIQ--QAGDTITLKVItvdvadmsRGG 537
Cdd:COG0265 207 RVEPGSPAAKAGLRPGDVILAVDGKPVT--SARDLQRLLAslKPGDTVTLTVL--------RGG 260
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 483-526 3.38e-04

permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 40.35  E-value: 3.38e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71983519 483 AVRAGLRPGDYLLEIDGIDVRrcSHDEVVEFIQQ--AGDTITLKVI 526
Cdd:cd06779  38 AAKAGLKEGDVILSVNGKPVT--SFNDLRAALDTkkPGDSLNLTIL 81
Ank_4 pfam13637
Ankyrin repeats (many copies);
280-318 3.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.79e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 71983519   280 GNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALH 318
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALH 39
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 279-311 4.17e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 4.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 71983519   279 NGNSPLHVCAV-NNRPECARVLLFRGADHLAVNK 311
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 439-525 4.24e-04

PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS3, and related domains. RGS3 down-regulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. It downregulates G-protein-mediated release of inositol phosphates and activation of MAP kinases. In Eph/ephrin signaling, RGS3 binds via its PDZ domain to the cytoplasmic C terminus of Eph receptor tyrosine kinase EphB. 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 RGS3-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: 467195 [Multi-domain]  Cd Length: 77  Bit Score: 39.68  E-value: 4.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 439 IPRGVKGFGFILRGakhvamplNFEPTAQvpalqffeGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAG 518
Cdd:cd06711   5 IQRGKDGFGFTICD--------DSPVRVQ--------AVDPGGPAEQAGLQQGDTVLQINGQPVERSKCVELAHAIRNCP 68


                ....*..
gi 71983519 519 DTITLKV 525
Cdd:cd06711  69 SEIILLV 75
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 473-527 5.07e-04

PDZ domain 3 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 3 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 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: 467167 [Multi-domain]  Cd Length: 88  Bit Score: 39.93  E-value: 5.07e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71983519 473 FFEGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGD--TITLKVIT 527
Cdd:cd06679  31 YVTNVQPDGCLGRDGrIKKGDVLLSINGISLTNLSHSEAVAVLKASAAssSIVLKVLE 88
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 483-526 5.11e-04

PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). 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 FRMPD1,3,4-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: 467250 [Multi-domain]  Cd Length: 75  Bit Score: 39.54  E-value: 5.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71983519 483 AVRAG------LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06769  26 SVTPGgpsegkLLPGDQILKINNEPVEDLPRERVIDLIRECKDSIVLTVL 75
Peptidase_M50 pfam02163
Peptidase family M50;
434-550 6.35e-04

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 42.86  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   434 ARILVIPRGVkGFGFILRGAkhVAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRrcSHDEVVEF 513
Cdd:pfam02163  60 QRLAIALAGP-LANFILAII--LFAVLLFLSGVPPPAPPVIGGVAPGSPAAKAGLKPGDVILSINGKKIT--SWQDLVEA 134

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 71983519   514 IQQ-AGDTITLKVItvdvadmsRGGTIVHRPPTDTHDA 550
Cdd:pfam02163 135 LAKsPGKPITLTVE--------RGGQTLTVTITPKSSE 164
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 481-525 6.96e-04

PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 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 PDZ10 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: 467161 [Multi-domain]  Cd Length: 86  Bit Score: 39.58  E-value: 6.96e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71983519 481 GMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06673  39 GAAAKDGrLWAGDQILEVNGEDLRKATHDEAINVLRQTPQKVRLLV 84
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 477-515 7.96e-04

PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the second PDZ domain of the canonical isoform of PDZD7- isoform 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 PDZD7-like family PDZ2 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: 467270 [Multi-domain]  Cd Length: 85  Bit Score: 39.29  E-value: 7.96e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 71983519 477 VDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQ 515
Cdd:cd10834  34 VDPGGLAEQNGIKVGDQILAVNGVSFEDITHSKAVEVLK 72
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 483-533 8.26e-04

circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 39.61  E-value: 8.26e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71983519 483 AVRAGLRPGDYLLEIDGIDVRrcSHDEVVEFIQQA--GDTITLKV--------ITVDVADM 533
Cdd:cd10838  46 AARAGLRRGDVIQAVDGQPVT--TADDVQRIVEQAgvGEELELTVlrgdrrqtLAVKPGDL 104
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 250-334 9.23e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 9.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  250 EIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLLFRGADHLAVNKQGQTALHVShivGNPGVA 329
Cdd:PTZ00322  85 ELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA---EENGFR 161


                 ....*
gi 71983519  330 DVVQA 334
Cdd:PTZ00322 162 EVVQL 166
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 488-523 1.01e-03

PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). 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 PDZ2 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: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 39.12  E-value: 1.01e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 71983519 488 LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITL 523
Cdd:cd06792  48 IQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTL 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
247-300 1.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71983519   247 GNHEIHQACKNGLTKHVEHLLYFGGQIDAENVNGNSPLHVCAVNNRPECARVLL 300
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 481-525 1.18e-03

PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. 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 Par3 family PDZ2 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: 467271 [Multi-domain]  Cd Length: 93  Bit Score: 39.16  E-value: 1.18e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 71983519 481 GMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQA--GDTITLKV 525
Cdd:cd23058  43 GAAIQDGrLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTklGGTVSLVV 90
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 481-525 1.27e-03

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. 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 Scribble-like family PDZ2 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: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 38.78  E-value: 1.27e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71983519 481 GMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06703  43 GAADRDGkLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITLVV 88
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 481-525 1.38e-03

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and 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 PDZ2 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: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 38.42  E-value: 1.38e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71983519 481 GMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06667  33 GVADRDGrLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRLVV 78
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 436-526 1.38e-03

PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 13 of MUPP1. 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. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ13 domain is therefore absent from PATJ. 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). 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 PDZ13 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: 467164 [Multi-domain]  Cd Length: 83  Bit Score: 38.48  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 436 ILVIPRGVKGFGFIL---RGAKHVAMPLnfeptaqvpalqFFEGVDMSGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVV 511
Cdd:cd06676   1 TITLERGSDGLGFSIvggFGSPHGDLPI------------YVKTVFEKGAAAEDGrLKRGDQILAVNGESLEGVTHEEAV 68

                        90
                ....*....|....*
gi 71983519 512 EFIQQAGDTITLKVI 526
Cdd:cd06676  69 NILKKTKGTVTLTVL 83
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 279-305 1.49e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.49e-03
                           10        20
                   ....*....|....*....|....*..
gi 71983519    279 NGNSPLHVCAVNNRPECARVLLFRGAD 305
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
175-216 1.76e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 71983519   175 RNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPL 216
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
FERM_f0 pfam16511
N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The ...
 9-91 2.02e-03

N-terminal or F0 domain of Talin-head FERM; FERM_f0 forms a stable globular structure. The fold is an ubiquitin-like fold joined to the f1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components, No binding partner has yet been found for it.


Pssm-ID: 465152  Cd Length: 81  Bit Score: 38.02  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519     9 NLQIFVPELNVRKFLAVTQNDFIWDVKRKLLATLPQALPQAFNYGLFLPPCDGRAGKFLLEDRTIRDYPFTDcvpYLELK 88
Cdd:pfam16511   2 SLKISIVGSNVTKTMQFDPSTTVYDACRLIREKIPEGGLNASEYGLFLADEDPKKGRWLEPGRTLEYYDLRN---GDELE 78


                  ...
gi 71983519    89 YKK 91
Cdd:pfam16511  79 YKK 81
PDZ_MAST2 cd23074
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 2; PDZ (PSD-95 ...
 437-523 2.35e-03

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 2; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST2 (also known as microtubule-associated serine/threonine kinase-205 kD, MAST205) , and related domains. MAST2 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain. MAST2 may function to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Binding partners of MAST2 include beta2-syntrophin, TNF receptor-associated factor 6 (TRAF6), cAMP-regulated phosphoprotein (ARPP-16), Na+/H+ exchanger NHE3 (SLC9A3) and PTEN. MAST2 is also associated with microtubules of the spermatid manchette. 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 MAST2 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: 467287 [Multi-domain]  Cd Length: 93  Bit Score: 38.07  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 437 LVIPRGVKGFGFILRgakhvAMPLNFEPTAQVPALQFFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQ 516
Cdd:cd23074   5 IIIHRAGKKYGFTLR-----AIRVYMGDSDVYTVHHMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELILK 79


                ....*..
gi 71983519 517 AGDTITL 523
Cdd:cd23074  80 SGNKVSI 86
PHA02798 PHA02798
ankyrin-like protein; Provisional
 87-250 2.74e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519   87 LKYKKRVYKMLNLDEkqlkamhTKGQLKKFMDYVQQKN--NEKVEKMCSQGLDANFHDAQGETPL-TLAAGIPNNRA--- 160
Cdd:PHA02798  18 LSTVKLLIKSCNPNE-------IVNEYSIFQKYLQRDSpsTDIVKLFINLGANVNGLDNEYSTPLcTILSNIKDYKHmld 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519  161 VIVSLIGGGAHVDFRNSEGQT---AMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPLYYNMLTADSND-QVAEILLRE 236
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDiEIIKLLLEK 170

                        170
                 ....*....|....
gi 71983519  237 AADIgvtDMHGNHE 250
Cdd:PHA02798 171 GVDI---NTHNNKE 181
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 473-525 2.96e-03

PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. 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 PDZD11-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: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 37.68  E-value: 2.96e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 71983519 473 FFEGVDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAgDTITLKV 525
Cdd:cd06752  28 FISKVIPDSDAHRLGLKEGDQILSVNGVDFEDIEHSEAVKVLKTA-REIQMRV 79
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 165-235 3.10e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 3.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71983519  165 LIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLIELGASPNYRDPIGLTPlyynMLTADSND--QVAEILLR 235
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP----LELAEENGfrEVVQLLSR 169
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 279-305 3.15e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|....*..
gi 71983519   279 NGNSPLHVCAVNNRPECARVLLFRGAD 305
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 486-525 3.29e-03

PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. 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 Dlg5-like 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: 467247 [Multi-domain]  Cd Length: 81  Bit Score: 37.37  E-value: 3.29e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 71983519 486 AGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06766  41 DGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 481-526 3.35e-03

PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of afadin (AFDN, also known as ALL1-fused gene from chromosome 6 protein (AF6) and MLLT4), and related domains. AFDN belongs to the adhesion system, probably together with the E-cadherin-catenin system, that plays a role in the organization of homotypic, interneuronal, and heterotypic cell-cell adherens junctions. The AFDN PDZ domain interaction partners include poliovirus receptor-related protein PRR2/nectin, the junctional adhesion molecule (JAM), the breakpoint-cluster-region protein (BCR), connexin36 (Cx36), and a subset of Eph-related receptor tyrosine kinases; it can also bind low molecular weight ligands, in competition with a natural peptide ligand. Other AFDN-binding proteins have been identified. 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 AFDN 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: 467251 [Multi-domain]  Cd Length: 89  Bit Score: 37.65  E-value: 3.35e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71983519 481 GMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06789  41 GAADLDGrLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTLEVA 87
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 480-525 3.41e-03

PDZ domain 2 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 2 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 PDZ2 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: 467166 [Multi-domain]  Cd Length: 82  Bit Score: 37.23  E-value: 3.41e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71983519 480 SGMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06678  34 GGLAARDGrLKSDDRVLAINGQDLRHGTPEQAAQIIQASGERVHFVV 80
PDZ_ARHGAP21_23-like cd06756
PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 435-526 3.62e-03

PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGAP21, ARHGAP23, and related domains. This subfamily includes the GAPs (GTPase activating proteins): ARHGAP21 (Rho GTPase-activating protein 21; also known as Rho GTPase-activating protein 10, Rho-type GTPase-activating protein 21) and ARHGAP23 (Rho GTPase-activating protein 23; also known as Rho-type GTPase-activating protein 23). GAPs deactivate Rho GTPases by accelerating GTP hydrolysis. ARHGAP21/23 interact with a planar cell polarity (PCP) protein Pk1 to regulate a lateral signaling pathway in migrating cells. The ARHGAP21 PDZ domain binds claudin-2. 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 ARHGAP21-23-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: 467238 [Multi-domain]  Cd Length: 109  Bit Score: 38.21  E-value: 3.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 435 RILVIPRGVKGFGFILR--------------------GAKHVAMPLNFEPTAQVpalqFFEGVDMSGMAVRAGLRPGDYL 494
Cdd:cd06756   2 KTVTLQRTSQGFGFTLRhfivyppesavheslkdeenGNRGGKQRSRLEPMDTI----FVKQVKEGGPAHQAGLCTGDRI 77

                        90       100       110
                ....*....|....*....|....*....|..
gi 71983519 495 LEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06756  78 VKVNGESVIGKTYSQVIALIQNSDSTLELSVM 109
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 488-525 3.68e-03

PDZ domain 1 of protein tyrosine 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 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. 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 family PDZ1 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: 467285 [Multi-domain]  Cd Length: 92  Bit Score: 37.47  E-value: 3.68e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 71983519 488 LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd23072  49 LKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVV 86
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 481-525 3.70e-03

PDZ domain 6 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 PDZ6 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: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 37.28  E-value: 3.70e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 71983519 481 GMAVRAG-LRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06683  38 GLAERTGaIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTLKI 83
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 487-526 4.13e-03

PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. 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 GOPC-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: 467261 [Multi-domain]  Cd Length: 83  Bit Score: 37.35  E-value: 4.13e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 71983519 487 GLRPGDYLLEIDGIDVRRCSHDEVVEFI-QQAGDtITLKVI 526
Cdd:cd06800  43 GLYVGDAILSVNGIDLRDAKHKEAVTILsQQRGE-ITLEVV 82
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-199 5.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 5.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71983519   147 TPLTLAAgIPNNRAVIVSLIGGGAHVDFRNSEGQTAMHKAAFLSSFENVKTLI 199
Cdd:pfam13637   3 TALHAAA-ASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 146-319 5.25e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 5.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 146 ETPLTLAAGiPNNRAVIVSLIGGgAHVDF--RNSEGQTAMHKAAFLSSFENVKTLIElgASPNY-RDPI------GLTPL 216
Cdd:cd22192  18 ESPLLLAAK-ENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLME--AAPELvNEPMtsdlyqGETAL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983519 217 YynMLTADSNDQVAEILLREAADIgVTDmhgnheihQACKNGLTKHVEHLLYFggqidaenvnGNSPLHVCAVNNRPECA 296
Cdd:cd22192  94 H--IAVVNQNLNLVRELIARGADV-VSP--------RATGTFFRPGPKNLIYY----------GEHPLSFAACVGNEEIV 152

                       170       180
                ....*....|....*....|...
gi 71983519 297 RVLLFRGADHLAVNKQGQTALHV 319
Cdd:cd22192 153 RLLIEHGADIRAQDSLGNTVLHI 175
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 474-526 7.73e-03

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. 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 SIPA1-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: 467227 [Multi-domain]  Cd Length: 73  Bit Score: 36.10  E-value: 7.73e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71983519 474 FEG----VDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGdTITLKVI 526
Cdd:cd06745  18 YEGfvteVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSV-KVKVTVI 73
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 481-526 7.83e-03

PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP5, Drosophila Stardust, and related domains. MPP5 (also known as MAGUK p55 subfamily member 1, protein associated with Lin-7 1 or PALS1) and Drosophila Stardust are membrane-associated guanylate kinase (MAGUK)-like proteins that serve as signaling and scaffolding proteins, linking different proteins critical to the formation and maintenance of tight junctions (TJ) and apical-basal polarity. Apical-basal polarity determinants cluster in complexes; in particular, the Crumbs complex (Crb, MPP5, and PATJ) and the PAR/aPKC-complex (PAR-3, PAR-6, aPKC) determine the apical plasma membrane domain. Within the Crumbs complex, Crb is stabilized in the plasma membrane by MPP5, which in turn recruits PATJ and Lin-7 to the complex. MPP5 also links the Crumbs complex with the PAR/aPKC-complex. The Drosophila homolog of the Crumbs complex is the (CRB)-Stardust (Sdt)-Discs Lost (Dlt) complex. MPP5 also acts as an interaction partner for SARS-CoV envelope protein E, which results in delayed formation of TJs and dysregulation of cell polarity. 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 MPP5-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: 467259 [Multi-domain]  Cd Length: 79  Bit Score: 36.17  E-value: 7.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71983519 481 GMAVRAGL-RPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKVI 526
Cdd:cd06798  32 GAAEKSGLlHEGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFLLI 78
PDZ2_APBA1_3-like cd06793
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ...
 481-524 7.87e-03

PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking, and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2) which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins, APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). 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 APBA1,3-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: 467255 [Multi-domain]  Cd Length: 78  Bit Score: 36.22  E-value: 7.87e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 71983519 481 GMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLK 524
Cdd:cd06793  32 GIAERGGVRVGHRIIEINGQSVVATPHEKIVQLLSNSVGEIHMK 75
PDZ1_L-delphilin-like cd06743
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 477-517 8.91e-03

PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. 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 delphilin-like family PDZ1 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: 467225 [Multi-domain]  Cd Length: 76  Bit Score: 36.10  E-value: 8.91e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 71983519 477 VDMSGMAVRAGLRPGDYLLEIDGIDVRRCSHDEVVEFIQQA 517
Cdd:cd06743  26 VEEGSSAHAAGLQPGDQILELDGQDVSSLSCEAIIALARRC 66
PDZ1_GRIP1-2-like cd06687
PDZ domain 1 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 476-525 9.53e-03

PDZ domain 1 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 PDZ1 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: 467175 [Multi-domain]  Cd Length: 83  Bit Score: 36.23  E-value: 9.53e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983519 476 GVDMSGMAVRAGLRP------------GDYLLEIDGIDVRRCSHDEVVEFIQQAGDTITLKV 525
Cdd:cd06687  20 GIDKDGKPRVSNLRPggiaarsdqlnvGDYIKSVNGIRTTKLRHDEIISLLKNVGERVVLEV 81
 
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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