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Conserved domains on  [gi|55770895|ref|NP_001006600|]
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erbin isoform 7 [Homo sapiens]

Protein Classification

leucine-rich repeat and PDZ domain-containing protein( domain architecture ID 11469328)

leucine-rich repeat and PDZ domain-containing protein may play a role in signaling or cell differentiation; similar to human erbin that acts as an adapter for the receptor ERBB2

CATH:  2.30.42.10
Gene Ontology:  GO:0005515
PubMed:  11751054|30712672|11158544|11283303
SCOP:  4001790

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 1212-1298 1.24e-52

PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion complex. 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 densin and erbin-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: 467231 [Multi-domain]  Cd Length: 87  Bit Score: 178.67  E-value: 1.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT 1291
Cdd:cd06749    1 IRVRIEKNPGLGFSISGGIGSQGNPFRPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVNIEHGQAVSLLKSFQNT 80


                 ....*..
gi 55770895 1292 VELIIVR 1298
Cdd:cd06749   81 VDLVVER 87
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
67-419 3.96e-45

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 168.96  E-value: 3.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   67 NCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLN 146
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  147 DAFLEFLPANFGRLTKLQILELRENqlkmlpKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFI 226
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  227 GSLKQLTYLDVSKNNIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDC 306
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  307 SFNEVEALPsSIGQLTNLRTFAADHNYLQQLPPEiGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFS 386
Cdd:COG4886  236 SNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPL-ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLEL 313

                        330       340       350
                 ....*....|....*....|....*....|...
gi 55770895  387 FTKLQQLTAMWLSDNQSKPLIPLQKETDSETQK 419
Cdd:COG4886  314 LILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
 
Name Accession Description Interval E-value
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 1212-1298 1.24e-52

PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion complex. 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 densin and erbin-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: 467231 [Multi-domain]  Cd Length: 87  Bit Score: 178.67  E-value: 1.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT 1291
Cdd:cd06749    1 IRVRIEKNPGLGFSISGGIGSQGNPFRPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVNIEHGQAVSLLKSFQNT 80


                 ....*..
gi 55770895 1292 VELIIVR 1298
Cdd:cd06749   81 VDLVVER 87
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
67-419 3.96e-45

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 168.96  E-value: 3.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   67 NCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLN 146
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  147 DAFLEFLPANFGRLTKLQILELRENqlkmlpKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFI 226
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  227 GSLKQLTYLDVSKNNIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDC 306
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  307 SFNEVEALPsSIGQLTNLRTFAADHNYLQQLPPEiGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFS 386
Cdd:COG4886  236 SNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPL-ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLEL 313

                        330       340       350
                 ....*....|....*....|....*....|...
gi 55770895  387 FTKLQQLTAMWLSDNQSKPLIPLQKETDSETQK 419
Cdd:COG4886  314 LILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 18-408 1.10e-22

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 105.32  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    18 RGEEETVTTLDYSHCSLE-QVPKEIFTFEkTLEELYLDANQIE-ELPKQLFNCQSLHKLSLPDNDLT-TLPASIANLINL 94
Cdd:PLN00113  136 RGSIPNLETLDLSNNMLSgEIPNDIGSFS-SLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSL 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    95 RELDVSKNGIQ-EFPENIKNCKVLTIVEASVNPIS-KLPDGFSQLLNLTQLYL-NDAFLEFLPANFGRLTKLQILELREN 171
Cdd:PLN00113  215 KWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLyQNKLSGPIPPSIFSLQKLISLDLSDN 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   172 QLK-MLPKTMNRLTQLERLDLGSNEFT-EVPEVLEQLSGLKEFWMDANRLTF-IPGFIGSLKQLTYLDVSKNNIE-MVEE 247
Cdd:PLN00113  295 SLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKFSGeIPKNLGKHNNLTVLDLSTNNLTgEIPE 374

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   248 GISTCENLQDLLLSSNSLQ-QLPETIGSLKNITTLKIDEN-------------QLMYLPD----SIGGLI--------SV 301
Cdd:PLN00113  375 GLCSSGNLFKLILFSNSLEgEIPKSLGACRSLRRVRLQDNsfsgelpseftklPLVYFLDisnnNLQGRInsrkwdmpSL 454

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   302 EELDCSFNEVEA-LPSSIGQlTNLRTFAADHNYLQQ-LPPEIGSWKNITVLFLHSNKLE-TLPEEMGDMQKLKVINLSDN 378
Cdd:PLN00113  455 QMLSLARNKFFGgLPDSFGS-KRLENLDLSRNQFSGaVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHN 533

                         410       420       430
                  ....*....|....*....|....*....|.
gi 55770895   379 RLK-NLPFSFTKLQQLTAMWLSDNQSKPLIP 408
Cdd:PLN00113  534 QLSgQIPASFSEMPVLSQLDLSQNQLSGEIP 564
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1210-1298 1.94e-16

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 75.49  E-value: 1.94e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    1210 EKIRVRVEKDPE-LGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPASK-LLQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:smart00228    1 EPRLVELEKGGGgLGFSLVGG--------KDEGGGVVVSSVVPGSPAAKaGLRVGDVILEVNGTSVEGLTHLEAVDLLKK 72

                            90
                    ....*....|.
gi 55770895    1288 FQNTVELIIVR 1298
Cdd:smart00228   73 AGGKVTLTVLR 83
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 137-355 6.46e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 75.21  E-value: 6.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  137 LLNLTQLYLNDAFLEFLPaNFGRLTKLQILELRENQLKMLPKtMNRLTQLERLDLgSNeftevpevleqlsglkefwmda 216
Cdd:cd21340    1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYL-QN---------------------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  217 NRLTFIPGFiGSLKQLTYLDVSKNNIEMVeEGISTCENLQDLLLSSnslQQLPEtigslknittlkidENQLMYLPDSIG 296
Cdd:cd21340   56 NQIEKIENL-ENLVNLKKLYLGGNRISVV-EGLENLTNLEELHIEN---QRLPP--------------GEKLTFDPRSLA 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55770895  297 GL-ISVEELDCSFNEVEALpSSIGQLTNLRTFAADHNYLQ---QLPPEIGSWKNITVLFLHSN 355
Cdd:cd21340  117 ALsNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGN 178
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1213-1296 1.72e-11

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 61.14  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   1213 RVRVEKDP--ELGFSISGGVGGRgnpfrpdDDGIFVTRVQPEGPASK-LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQ 1289
Cdd:pfam00595    1 QVTLEKDGrgGLGFSLKGGSDQG-------DPGIFVSEVLPGGAAEAgGLKVGDRILSINGQDVENMTHEEAVLALKGSG 73


                   ....*..
gi 55770895   1290 NTVELII 1296
Cdd:pfam00595   74 GKVTLTI 80
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 1220-1299 1.74e-07

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: 54.88  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1220 PELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT-VELIIV 1297
Cdd:COG0793   49 EDFQESTSGEFGGLGAELGEEDGKVVVVSVIPGSPAEKAgIKPGDIILAIDGKSVAGLTLDDAVKLLRGKAGTkVTLTIK 128


                 ..
gi 55770895 1298 RE 1299
Cdd:COG0793  129 RP 130
LRR_8 pfam13855
Leucine rich repeat;
322-380 2.37e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.28  E-value: 2.37e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770895    322 TNLRTFAADHNYLQQLPPEI-GSWKNITVLFLHSNKLETL-PEEMGDMQKLKVINLSDNRL 380
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
 
Name Accession Description Interval E-value
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 1212-1298 1.24e-52

PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion complex. 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 densin and erbin-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: 467231 [Multi-domain]  Cd Length: 87  Bit Score: 178.67  E-value: 1.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT 1291
Cdd:cd06749    1 IRVRIEKNPGLGFSISGGIGSQGNPFRPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVNIEHGQAVSLLKSFQNT 80


                 ....*..
gi 55770895 1292 VELIIVR 1298
Cdd:cd06749   81 VDLVVER 87
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
67-419 3.96e-45

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 168.96  E-value: 3.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   67 NCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLN 146
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  147 DAFLEFLPANFGRLTKLQILELRENqlkmlpKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFI 226
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  227 GSLKQLTYLDVSKNNIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDC 306
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  307 SFNEVEALPsSIGQLTNLRTFAADHNYLQQLPPEiGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFS 386
Cdd:COG4886  236 SNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPL-ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLEL 313

                        330       340       350
                 ....*....|....*....|....*....|...
gi 55770895  387 FTKLQQLTAMWLSDNQSKPLIPLQKETDSETQK 419
Cdd:COG4886  314 LILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-453 5.30e-45

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 168.57  E-value: 5.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   76 LPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDafleflPA 155
Cdd:COG4886   34 LLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSG------NE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  156 NFGRLTKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFIGSLKQLTYL 235
Cdd:COG4886  108 ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKEL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  236 DVSKNNIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPdSIGGLISVEELDCSFNEVEALP 315
Cdd:COG4886  188 DLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLP 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  316 SSiGQLTNLRTFAADHNYLQQLPPEIGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTA 395
Cdd:COG4886  267 PL-ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLS 345

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895  396 MWLSDNQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPSLWEEQ 453
Cdd:COG4886  346 LLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLL 403
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
17-361 1.46e-42

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 161.64  E-value: 1.46e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   17 LRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANqieelpKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRE 96
Cdd:COG4886   67 LLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   97 LDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKML 176
Cdd:COG4886  141 LDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDL 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  177 PKTMNRLTQLERLDLGSNEFTEVPEvLEQLSGLKEFWMDANRLTFIPgFIGSLKQLTYLDVSKNNIEmvEEGISTCENLQ 256
Cdd:COG4886  221 PEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLT--DLKLKELELLL 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  257 DLLLSSNSLQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQLTNLRTFAADHNYLQQ 336
Cdd:COG4886  297 GLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLE 376

                        330       340
                 ....*....|....*....|....*
gi 55770895  337 LPPEIGSWKNITVLFLHSNKLETLP 361
Cdd:COG4886  377 ATLLTLALLLLTLLLLLLTTTAGVL 401
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
46-349 1.73e-40

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 155.48  E-value: 1.73e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   46 KTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTIVEASVN 125
Cdd:COG4886  113 TNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNN 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  126 PISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKMLPKtMNRLTQLERLDLGSNEFTEVPEvLEQ 205
Cdd:COG4886  193 QITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPP-LAN 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  206 LSGLKEFWMDANRLTFIPGFIGSLKQLTYLDVSKNNIEMVEEGISTCENLQDLLLSSNSLQQLPETIGSLKNITTLKIDE 285
Cdd:COG4886  271 LTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL 350

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55770895  286 NQLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQLTNLRTFAADHNYLQQLPPEIGSWKNITV 349
Cdd:COG4886  351 TLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
25-326 1.76e-38

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 149.70  E-value: 1.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   25 TTLDYSHCSLEQVPKEIFTFeKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGI 104
Cdd:COG4886  116 ESLDLSGNQLTDLPEELANL-TNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQI 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  105 QEFPENIKNCKVLTIVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPaNFGRLTKLQILELRENQLKMLPKTMNrLT 184
Cdd:COG4886  195 TDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPLAN-LT 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  185 QLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFIGSLKQLTYLDVSKNNIEMVEEGISTCENLQDLLLSSNS 264
Cdd:COG4886  273 NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTL 352

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55770895  265 LQQLPETIGSLKNITTLKIDENQLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQLTNLRT 326
Cdd:COG4886  353 LLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
181-402 2.13e-30

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 125.43  E-value: 2.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  181 NRLTQLERLDLGSNEFTEVPEVLEQLSGLKEFWMDANRLTFIPGFIGSLKQLTYLDVSKNNIEMVEEGISTCENLQDLLL 260
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  261 SSNSLQQLPETIGSLKNITTLKIDE-----------------NQLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQLTN 323
Cdd:COG4886   81 LLSLLLLGLTDLGDLTNLTELDLSGneelsnltnlesldlsgNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTN 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770895  324 LRTFAADHNYLQQLPPEIGSWKNITVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQ 402
Cdd:COG4886  161 LKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQ 239
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 18-408 1.10e-22

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 105.32  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    18 RGEEETVTTLDYSHCSLE-QVPKEIFTFEkTLEELYLDANQIE-ELPKQLFNCQSLHKLSLPDNDLT-TLPASIANLINL 94
Cdd:PLN00113  136 RGSIPNLETLDLSNNMLSgEIPNDIGSFS-SLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSL 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    95 RELDVSKNGIQ-EFPENIKNCKVLTIVEASVNPIS-KLPDGFSQLLNLTQLYL-NDAFLEFLPANFGRLTKLQILELREN 171
Cdd:PLN00113  215 KWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLyQNKLSGPIPPSIFSLQKLISLDLSDN 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   172 QLK-MLPKTMNRLTQLERLDLGSNEFT-EVPEVLEQLSGLKEFWMDANRLTF-IPGFIGSLKQLTYLDVSKNNIE-MVEE 247
Cdd:PLN00113  295 SLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKFSGeIPKNLGKHNNLTVLDLSTNNLTgEIPE 374

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   248 GISTCENLQDLLLSSNSLQ-QLPETIGSLKNITTLKIDEN-------------QLMYLPD----SIGGLI--------SV 301
Cdd:PLN00113  375 GLCSSGNLFKLILFSNSLEgEIPKSLGACRSLRRVRLQDNsfsgelpseftklPLVYFLDisnnNLQGRInsrkwdmpSL 454

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   302 EELDCSFNEVEA-LPSSIGQlTNLRTFAADHNYLQQ-LPPEIGSWKNITVLFLHSNKLE-TLPEEMGDMQKLKVINLSDN 378
Cdd:PLN00113  455 QMLSLARNKFFGgLPDSFGS-KRLENLDLSRNQFSGaVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHN 533

                         410       420       430
                  ....*....|....*....|....*....|.
gi 55770895   379 RLK-NLPFSFTKLQQLTAMWLSDNQSKPLIP 408
Cdd:PLN00113  534 QLSgQIPASFSEMPVLSQLDLSQNQLSGEIP 564
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1213-1297 1.14e-20

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: 87.21  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1213 RVRVEKDPE--LGFSISGGVGGrgnpfrpdDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTF 1288
Cdd:cd00136    1 TVTLEKDPGggLGFSIRGGKDG--------GGGIFVSRVEPGGPAARdgRLRVGDRILEVNGVSLEGLTHEEAVELLKSA 72


                 ....*....
gi 55770895 1289 QNTVELIIV 1297
Cdd:cd00136   73 GGEVTLTVR 81
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 48-401 1.40e-20

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 98.77  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    48 LEELYLDANQIE-ELPKQLFN-CQSLHKLSLPDNDLTTlPASIANLINLRELDVSKNGIQefpeniknckvltiveasvn 125
Cdd:PLN00113   95 IQTINLSNNQLSgPIPDDIFTtSSSLRYLNLSNNNFTG-SIPRGSIPNLETLDLSNNMLS-------------------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   126 piSKLPDGFSQLLNLTQLYLNDAFLE-FLPANFGRLTKLQILELRENQL-KMLPKTMNRLTQLERLDLGSNEFT-EVPEV 202
Cdd:PLN00113  154 --GEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLvGQIPRELGQMKSLKWIYLGYNNLSgEIPYE 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   203 LEQLSGLKEFWMDANRLTF-IPGFIGSLKQLTYLDVSKNNIE-MVEEGISTCENLQDLLLSSNSLQ-QLPETIGSLKNIT 279
Cdd:PLN00113  232 IGGLTSLNHLDLVYNNLTGpIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLE 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   280 TLKIDENQLM-YLPDSIGGLISVEELDCSFNEVEA-LPSSIGQLTNLRTFAADHNYLQ-QLPPEIGSWKNITVLFLHSNK 356
Cdd:PLN00113  312 ILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKFSGeIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNS 391

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 55770895   357 LET-LPEEMGDMQKLKVINLSDNRLK-NLPFSFTKLQQLTAMWLSDN 401
Cdd:PLN00113  392 LEGeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNN 438
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1222-1299 2.91e-20

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: 86.55  E-value: 2.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1222 LGFSISGGVGGrgNPFRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVRE 1299
Cdd:cd06703   14 LGFSIAGGKGS--TPFRDGDEGIFISRITEGGAADRdgKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITLVVERE 91
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1214-1298 5.73e-20

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: 85.41  E-value: 5.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPE-LGFSISGGVGGrgNPFRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT 1291
Cdd:cd06704    3 ITIERQTGgLGISIAGGKGS--TPYKGDDEGIFISRVTEGGPAAKAgVRVGDKLLEVNGVDLVDADHHEAVEALKNSGNT 80


                 ....*..
gi 55770895 1292 VELIIVR 1298
Cdd:cd06704   81 VTMVVLR 87
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
37-295 1.41e-18

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 91.68  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    37 VPKEIFTfektleeLYLDANQIEELPKQLFNcqSLHKLSLPDNDLTTLPASIANLInlRELDVSKNGIQEFPENIKNckV 116
Cdd:PRK15370  197 IPEQITT-------LILDNNELKSLPENLQG--NIKTLYANSNQLTSIPATLPDTI--QEMELSINRITELPERLPS--A 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   117 LTIVEASVNPISKLPDGfsqllnltqlylndaflefLPanfgrlTKLQILELRENQLKMLPKTMNrlTQLERLDLGSNEF 196
Cdd:PRK15370  264 LQSLDLFHNKISCLPEN-------------------LP------EELRYLSVYDNSIRTLPAHLP--SGITHLNVQSNSL 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   197 TEVPEVLEQlsGLKEFWMDANRLTFIPgfiGSL-KQLTYLDVSKNNIEMVEEGISTceNLQDLLLSSNSLQQLPETIGSL 275
Cdd:PRK15370  317 TALPETLPP--GLKTLEAGENALTSLP---ASLpPELQVLDVSKNQITVLPETLPP--TITTLDVSRNALTNLPENLPAA 389

                         250       260
                  ....*....|....*....|
gi 55770895   276 KNIttLKIDENQLMYLPDSI 295
Cdd:PRK15370  390 LQI--MQASRNNLVRLPESL 407
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 1222-1298 7.63e-18

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: 79.69  E-value: 7.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1222 LGFSISGGVG--GRGNPFRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd10822   15 LGFSIGGGIDqdPSKNPFSYTDKGIYVTRVSEGGPAEKAgLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKPVLRMLVTR 94
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1222-1297 1.10e-17

PDZ domain 2 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 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or 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. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. 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 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: 467207 [Multi-domain]  Cd Length: 85  Bit Score: 78.85  E-value: 1.10e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1222 LGFSISGGVGgrgNPFRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIV 1297
Cdd:cd06724   11 LGFSIAGGVG---NQHIPGDNGIYVTKIIEGGAAQKdgRLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYLKVA 85
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1209-1296 1.11e-16

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: 76.50  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1209 LEKIRVRVEKDPELGFSISGGVGG-RGNPFRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLL 1285
Cdd:cd06701    4 LQELTIVKEPGEKLGISIRGGAKGhAGNPLDPTDEGIFISKINPDGAAARdgRLKVGQRILEVNGQSLLGATHQEAVRIL 83

                         90
                 ....*....|.
gi 55770895 1286 KTFQNTVELII 1296
Cdd:cd06701   84 RSVGDTLTLLV 94
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1210-1298 1.94e-16

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 75.49  E-value: 1.94e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    1210 EKIRVRVEKDPE-LGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPASK-LLQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:smart00228    1 EPRLVELEKGGGgLGFSLVGG--------KDEGGGVVVSSVVPGSPAAKaGLRVGDVILEVNGTSVEGLTHLEAVDLLKK 72

                            90
                    ....*....|.
gi 55770895    1288 FQNTVELIIVR 1298
Cdd:smart00228   73 AGGKVTLTVLR 83
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 1222-1297 4.86e-16

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: 74.25  E-value: 4.86e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1222 LGFSISGGVGgrgNPFRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIV 1297
Cdd:cd06709   12 LGFNIVGGTD---QPYIPNDSGIYVAKIKEDGAAAIdgRLQEGDKILEINGQSLENLTHQDAVELFRNAGEDVKLKVQ 86
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1214-1298 1.92e-15

PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. 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 ZO 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: 467209 [Multi-domain]  Cd Length: 87  Bit Score: 72.69  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPELGFSIsgGV-GGRGNP-FRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT 1291
Cdd:cd06727    3 VTLHRAPGFGFGI--AVsGGRDNPhFQSGDTSIVISDVLKGGPAEGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKT 80


                 ....*..
gi 55770895 1292 VELIIVR 1298
Cdd:cd06727   81 ANITVKR 87
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 137-355 6.46e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 75.21  E-value: 6.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  137 LLNLTQLYLNDAFLEFLPaNFGRLTKLQILELRENQLKMLPKtMNRLTQLERLDLgSNeftevpevleqlsglkefwmda 216
Cdd:cd21340    1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYL-QN---------------------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  217 NRLTFIPGFiGSLKQLTYLDVSKNNIEMVeEGISTCENLQDLLLSSnslQQLPEtigslknittlkidENQLMYLPDSIG 296
Cdd:cd21340   56 NQIEKIENL-ENLVNLKKLYLGGNRISVV-EGLENLTNLEELHIEN---QRLPP--------------GEKLTFDPRSLA 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55770895  297 GL-ISVEELDCSFNEVEALpSSIGQLTNLRTFAADHNYLQ---QLPPEIGSWKNITVLFLHSN 355
Cdd:cd21340  117 ALsNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGN 178
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
24-266 8.09e-15

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 79.74  E-value: 8.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    24 VTTLDYSHCSLEQVPKeifTFEKTLEELYLDANQIEELPKQLfnCQSLHKLSLPDNDLTTLPASIANliNLRELDVSKNG 103
Cdd:PRK15370  222 IKTLYANSNQLTSIPA---TLPDTIQEMELSINRITELPERL--PSALQSLDLFHNKISCLPENLPE--ELRYLSVYDNS 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   104 IQEFPENIKNckvlTIVEASV--NPISKLPDGFSqlLNLTQLYLNDAFLEFLPANFGrlTKLQILELRENQLKMLPKTMN 181
Cdd:PRK15370  295 IRTLPAHLPS----GITHLNVqsNSLTALPETLP--PGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   182 rlTQLERLDLGSNEFTEVPEVLEqlSGLKEFWMDANRLT----FIPGFIGSLKQLTYLDVSKNNIEMveegiSTCENLQd 257
Cdd:PRK15370  367 --PTITTLDVSRNALTNLPENLP--AALQIMQASRNNLVrlpeSLPHFRGEGPQPTRIIVEYNPFSE-----RTIQNMQ- 436


                  ....*....
gi 55770895   258 LLLSSNSLQ 266
Cdd:PRK15370  437 RLMSSVGYQ 445
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
211-402 8.40e-14

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 76.27  E-value: 8.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   211 EFWMDANRLTFIPGFIGslKQLTYLDVSKNNIEMVEEGISTceNLQDLLLSSNSLQQLPETIGSlkNITTLKIDENQLMY 290
Cdd:PRK15370  182 ELRLKILGLTTIPACIP--EQITTLILDNNELKSLPENLQG--NIKTLYANSNQLTSIPATLPD--TIQEMELSINRITE 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   291 LPDSIGGliSVEELDCSFNEVEALPSSIGQltNLRTFAADHNYLQQLPPEIGSwkNITVLFLHSNKLETLPEEMGdmQKL 370
Cdd:PRK15370  256 LPERLPS--ALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLPS--GITHLNVQSNSLTALPETLP--PGL 327

                         170       180       190
                  ....*....|....*....|....*....|...
gi 55770895   371 KVINLSDNRLKNLPFSF-TKLQQLTamwLSDNQ 402
Cdd:PRK15370  328 KTLEAGENALTSLPASLpPELQVLD---VSKNQ 357
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 159-408 1.66e-13

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 75.65  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   159 RLTKLQILELRENQLK-MLPKTMNRLT-QLERLDLGSNEFT-EVPEvlEQLSGLKEFWMDANRLTF-IPGFIGSLKQLTY 234
Cdd:PLN00113   91 RLPYIQTINLSNNQLSgPIPDDIFTTSsSLRYLNLSNNNFTgSIPR--GSIPNLETLDLSNNMLSGeIPNDIGSFSSLKV 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   235 LDVSKNNIE-MVEEGISTCENLQDLLLSSNSLQ-QLPETIGSLKNITTLKIDENQLM-YLPDSIGGLISVEELDCSFNev 311
Cdd:PLN00113  169 LDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYN-- 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   312 ealpssigqltnlrtfaadhNYLQQLPPEIGSWKNITVLFLHSNKLE-TLPEEMGDMQKLKVINLSDNRLK-NLPFSFTK 389
Cdd:PLN00113  247 --------------------NLTGPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQ 306

                         250
                  ....*....|....*....
gi 55770895   390 LQQLTAMWLSDNQSKPLIP 408
Cdd:PLN00113  307 LQNLEILHLFSNNFTGKIP 325
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 1210-1296 6.32e-13

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: 65.88  E-value: 6.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1210 EKIRVRVEKDPE--LGFSISGGVGGRGNpfrpdDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLL 1285
Cdd:cd06694    1 EIVIVTLKKDPQkgLGFTIVGGENSGSL-----DLGIFVKSIIPGGPADKdgRIKPGDRIIAINGQSLEGKTHHAAVEII 75

                         90
                 ....*....|.
gi 55770895 1286 KTFQNTVELII 1296
Cdd:cd06694   76 QNAPDKVELII 86
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1211-1298 8.21e-13

PDZ domain 2 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 2 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 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: 467220 [Multi-domain]  Cd Length: 82  Bit Score: 65.03  E-value: 8.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1211 KIRVRVEKDPELGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQ 1289
Cdd:cd06738    4 KVFISLVGTRGLGCSISSG--------PTQKPGIFISNVKPGSLAEEVgLEVGDQIVEVNGTSFTNVDHKEAVMALKSSR 75


                 ....*....
gi 55770895 1290 NTveLIIVR 1298
Cdd:cd06738   76 HL--TITVR 82
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 1212-1297 2.16e-12

PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight junction (PATJ, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 12 of MUPP1, PDZ domain 10 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 PDZ12 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: 467163 [Multi-domain]  Cd Length: 86  Bit Score: 63.92  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPE--LGFSISGGVGgrgNPFrpDDDGIFVTRVQPEGPASKL--LQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd06675    1 RTVEIKRGPQdsLGISIAGGVG---SPL--GDVPVFIAMIQPNGVAAQTgkLKVGDRIVSINGQSTDGLTHSEAVNLLKN 75

                         90
                 ....*....|
gi 55770895 1288 FQNTVELIIV 1297
Cdd:cd06675   76 ASGTIILQVV 85
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1221-1287 5.20e-12

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: 62.72  E-value: 5.20e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1221 ELGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd06752   12 QLGFNIRGG--------KASGLGIFISKVIPDSDAHRLgLKEGDQILSVNGVDFEDIEHSEAVKVLKT 71
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1222-1298 1.38e-11

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: 61.89  E-value: 1.38e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1222 LGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06702   12 LGLSIVGGSDHSSHPFGVDEPGIFISKVIPDGAAAKSgLRIGDRILSVNGKDLRHATHQEAVSALLSPGQEIKLLVRH 89
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 1214-1296 1.46e-11

PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467273 [Multi-domain]  Cd Length: 80  Bit Score: 61.60  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDP--ELGFSISGGVGGRGnpfrpdddgIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQ 1289
Cdd:cd23060    2 IELEKPAngGLGFSLVGGEGGSG---------IFVKSISPGGVADRdgRLQVGDRLLQVNGESVIGLSHSKAVNILRKAK 72


                 ....*..
gi 55770895 1290 NTVELII 1296
Cdd:cd23060   73 GTVQLTV 79
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1222-1298 1.49e-11

PDZ domain 1 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 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or 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. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. 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 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: 467206 [Multi-domain]  Cd Length: 89  Bit Score: 61.56  E-value: 1.49e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770895 1222 LGFSISGGvggRGNPFRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06723   13 LGFSIAGG---TDNPHIGDDPSIYITKIIPGGAAAAdgRLRVNDIILRVNDVDVRNVTHSVAVEALKEAGSIVRLYVKR 88
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1213-1296 1.72e-11

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 61.14  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   1213 RVRVEKDP--ELGFSISGGVGGRgnpfrpdDDGIFVTRVQPEGPASK-LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQ 1289
Cdd:pfam00595    1 QVTLEKDGrgGLGFSLKGGSDQG-------DPGIFVSEVLPGGAAEAgGLKVGDRILSINGQDVENMTHEEAVLALKGSG 73


                   ....*..
gi 55770895   1290 NTVELII 1296
Cdd:pfam00595   74 GKVTLTI 80
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
65-288 3.73e-11

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 67.88  E-value: 3.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    65 LFNCQSLH--KLSLPDNDLTTLPASIANLinlRELDVSKNGIQEFPENIKNCKVLTIVEASVNPISKLPDGFSQLL---- 138
Cdd:PRK15387  216 LPDCLPAHitTLVIPDNNLTSLPALPPEL---RTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWifgn 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   139 ----------NLTQLYLNDAFLEFLPANFGRLTKL-----------------QILELRENQLKMLPKTMNRLTQLERLDl 191
Cdd:PRK15387  293 qltslpvlppGLQELSVSDNQLASLPALPSELCKLwaynnqltslptlpsglQELSVSDNQLASLPTLPSELYKLWAYN- 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   192 gsNEFTEVPEVLeqlSGLKEFWMDANRLTFIPGFIGSLKQLTYLDVSKNNIEMVEEGistcenLQDLLLSSNSLQQLPET 271
Cdd:PRK15387  372 --NRLTSLPALP---SGLKELIVSGNRLTSLPVLPSELKELMVSGNRLTSLPMLPSG------LLSLSVYRNQLTRLPES 440

                         250
                  ....*....|....*..
gi 55770895   272 IGSLKNITTLKIDENQL 288
Cdd:PRK15387  441 LIHLSSETTVNLEGNPL 457
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1213-1297 4.16e-11

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: 60.05  E-value: 4.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1213 RVRVEKDPE-LGFSIsggVGGRGNPFRpdDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQ 1289
Cdd:cd06676    1 TITLERGSDgLGFSI---VGGFGSPHG--DLPIYVKTVFEKGAAAEdgRLKRGDQILAVNGESLEGVTHEEAVNILKKTK 75


                 ....*...
gi 55770895 1290 NTVELIIV 1297
Cdd:cd06676   76 GTVTLTVL 83
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 1208-1298 6.93e-11

PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains, and is expressed at exceptionally high levels in the pancreas and certain cancer tissues such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. 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 PDZD2-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: 467239 [Multi-domain]  Cd Length: 88  Bit Score: 59.67  E-value: 6.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1208 KLEKIRVRVEKDpELGFSISGGVGGRGNPFrpdddGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLL 1285
Cdd:cd06758    1 RVWKMHLLKEKG-GLGIQITGGKGSKRGDI-----GIFVAGVEEGGSADRdgRLKKGDELLMINGQSLIGLSHQEAVAIL 74

                         90
                 ....*....|...
gi 55770895 1286 KTFQNTVELIIVR 1298
Cdd:cd06758   75 RSSASPVQLVIAS 87
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 1213-1296 7.75e-11

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: 60.03  E-value: 7.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1213 RVRVEKDPE--LGFSIsggVGGRGNPFRPDD----DGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSL 1284
Cdd:cd06671    4 RVELWREPGksLGISI---VGGRVMGSRLSNgeeiRGIFIKHVLEDSPAGRngTLKTGDRILEVNGVDLRNATHEEAVEA 80

                         90
                 ....*....|..
gi 55770895 1285 LKTFQNTVELII 1296
Cdd:cd06671   81 IRNAGNPVVFLV 92
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1222-1297 1.11e-10

PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2)and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 59.28  E-value: 1.11e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770895 1222 LGFSISGGVGG-RGNPfrpdddGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIV 1297
Cdd:cd06680   13 LGFSIVGGYEEsHGNQ------PFFVKSIVPGTPAYNdgRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTVV 85
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 19-240 1.69e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 65.64  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    19 GEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIE-ELPKQLFNCQSLHKLSLPDNDLT-TLPASIANLINLRE 96
Cdd:PLN00113  353 GKHNNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEgEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYF 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    97 LDVSKNGIQEFPENIK-NCKVLTIVEASVNPIS-KLPDGFSQlLNLTQLYLN-DAFLEFLPANFGRLTKLQILELRENQL 173
Cdd:PLN00113  433 LDISNNNLQGRINSRKwDMPSLQMLSLARNKFFgGLPDSFGS-KRLENLDLSrNQFSGAVPRKLGSLSELMQLKLSENKL 511

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   174 K-MLPKTMNRLTQLERLDLGSNEFT-EVPEVLEQLSGLKEFWMDANRLTF-IPGFIGSLKQLTYLDVSKN 240
Cdd:PLN00113  512 SgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSGeIPKNLGNVESLVQVNISHN 581
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1222-1297 2.15e-10

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: 58.52  E-value: 2.15e-10
                         10        20        30        40        50        60        70
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gi 55770895 1222 LGFSISGGvggrgnpfrPDDDGIFVTRVQPEGPA--SKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIV 1297
Cdd:cd06795   14 LGFNIVGG---------EDGEGIFISFILAGGPAdlSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIAQ 82
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1222-1300 2.40e-10

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: 58.17  E-value: 2.40e-10
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gi 55770895 1222 LGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPAS-KLLQPGDKIIQANGYSFINIEHGQAVSLLKTfqNTVELIIVREV 1300
Cdd:cd10834   15 LGFNIRGG--------SEYGLGIYVSKVDPGGLAEqNGIKVGDQILAVNGVSFEDITHSKAVEVLKS--QTHLMLTIKEV 84
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 97-291 2.54e-10

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 61.73  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   97 LDVSKNGIQEFpENIKNCKVLTIVEASVNPISKLPdGFSQLLNLTQLYLNDAFLEFLPaNFGRLTKLQILELRENQLKML 176
Cdd:cd21340    7 LYLNDKNITKI-DNLSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  177 pKTMNRLTQLE-------RLDLGsNEFTEVPEVLEQLSG-LKEFWMDANRLTFIpGFIGSLKQLTYLDVSKNNI---EMV 245
Cdd:cd21340   84 -EGLENLTNLEelhienqRLPPG-EKLTFDPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQIsdlEEL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55770895  246 EEGISTCENLQDLLLSSNSLQQLP----ETIGSLKNITTL---KIDENQLMYL 291
Cdd:cd21340  161 LDLLSSWPSLRELDLTGNPVCKKPkyrdKIILASKSLEVLdgkEITDTERQFL 213
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 1210-1298 4.94e-10

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: 57.22  E-value: 4.94e-10
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gi 55770895 1210 EKIRVRVEK-DPELGFSISGGVGGRgnpfrPDDDGIFVTRVQPEGPA--SKLLQPGDKIIQANGYSFINIEHGQAVSLLK 1286
Cdd:cd06792    1 DVFEVELSKkDGSLGISVTGGINTS-----VRHGGIYVKSLVPGGAAeqDGRIQKGDRLLEVNGVSLEGVTHKQAVECLK 75

                         90
                 ....*....|..
gi 55770895 1287 TFQNTVELIIVR 1298
Cdd:cd06792   76 NAGQVVTLVLER 87
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1211-1301 8.28e-10

PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. 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 whirlin 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: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 56.50  E-value: 8.28e-10
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1211 KIRVRVEKDPELGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKtfq 1289
Cdd:cd06741    3 KVNLVVEDGQSLGLMIRGG--------AEYGLGIYVTGVDPGSVAENAgLKVGDQILEVNGRSFLDITHDEAVKILK--- 71

                         90
                 ....*....|...
gi 55770895 1290 NTVELII-VREVS 1301
Cdd:cd06741   72 SSKHLIMtVKDVG 84
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1214-1287 8.68e-10

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: 56.49  E-value: 8.68e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1214 VRVEKDPE--LGFSISGGVGGRgnpfrPDDDGIFVTRVQPEG--PASKLLQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd06679    3 VTIKKEPSesLGISVAGGRGSR-----RGDLPIYVTNVQPDGclGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKA 75
PDZ3_PDZD2-PDZ1_hPro-IL-16-like cd06759
PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 ...
 1222-1286 1.25e-09

PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the first PDZ domain (PDZ1) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. 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 PDZD2-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: 467240 [Multi-domain]  Cd Length: 87  Bit Score: 56.13  E-value: 1.25e-09
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770895 1222 LGFSIsggVGGRGNPFRPDddGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLK 1286
Cdd:cd06759   14 LGFSI---VGGRDSPRGPM--GIYVKTIFPGGAAAEdgRLKEGDEILEVNGESLQGLTHQEAIQKFK 75
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1214-1298 1.56e-09

PDZ domain 1 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 1 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 first 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 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: 467269 [Multi-domain]  Cd Length: 84  Bit Score: 55.90  E-value: 1.56e-09
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPE--LGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLkTFQN 1290
Cdd:cd10833    4 VTVEKSPDgsLGFSVRGG--------SEHGLGIFVSKVEEGSAAERAgLCVGDKITEVNGVSLENITMSSAVKVL-TGSN 74


                 ....*...
gi 55770895 1291 TVELIIVR 1298
Cdd:cd10833   75 RLRMVVRR 82
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1223-1298 1.67e-09

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: 55.66  E-value: 1.67e-09
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1223 GFSISGGvggrgnpFRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06735   14 GFSIRGG-------REYNNMPLYVLRLAEDGPAQRdgRLRVGDQILEINGESTQGMTHAQAIELIRSGGSVVRLLLRR 84
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 1222-1297 1.97e-09

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: 55.86  E-value: 1.97e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1222 LGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKL--LQPGDKIIQANGYSFINIEHGQAVsllKTFQNTVELIIV 1297
Cdd:cd06715   14 LGFNIIGGRPCENNQEGSSSEGIYVSKIVENGPAADEggLQVHDRIIEVNGKDLSKATHEEAV---EAFRTAKEPIVV 88
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 51-240 2.12e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 59.03  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   51 LYLDANQIEELPKqLFNCQSLHKLSLPDNDLTTLPaSIANLINLRELDVSKNGIQEFpENIKNCKVLTIVEASVNPISKL 130
Cdd:cd21340    7 LYLNDKNITKIDN-LSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  131 pDGFSQLLNLTQLYL------NDAFLEFLPANFGRLTK-LQILELRENQLKMLpKTMNRLTQLERLDLGSNEFTEVPEVL 203
Cdd:cd21340   84 -EGLENLTNLEELHIenqrlpPGEKLTFDPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEELL 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 55770895  204 EQLSglkefwmdanrltfipgfigSLKQLTYLDVSKN 240
Cdd:cd21340  162 DLLS--------------------SWPSLRELDLTGN 178
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 1222-1298 3.44e-09

PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains. Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (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 STXBP4-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: 467179 [Multi-domain]  Cd Length: 88  Bit Score: 54.92  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1222 LGFSISGGVGGRGnpfrPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQ--NTVELIIV 1297
Cdd:cd06692   10 LGIKIIGGYRENT----GEEFGIFIKRILPGGLAATdgRLKEGDLILEVNGESLQGVTNERAVSILRSASasNHMSLLIA 85


                 .
gi 55770895 1298 R 1298
Cdd:cd06692   86 R 86
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
127-407 3.66e-09

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 61.33  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   127 ISKLPDGFSQllNLTQLYLNDAFLEFLPAnfgRLTKLQILELRENQLKMLPKTMNRLTQLErldLGSNEFTEVPEVLeql 206
Cdd:PRK15387  213 LTTLPDCLPA--HITTLVIPDNNLTSLPA---LPPELRTLEVSGNQLTSLPVLPPGLLELS---IFSNPLTHLPALP--- 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   207 SGLKEFWMDANRLTFIPGFIGSLKQLTyldVSKNNIEMVEegiSTCENLQDLLLSSNSLQQLPETIGSLKNittLKIDEN 286
Cdd:PRK15387  282 SGLCKLWIFGNQLTSLPVLPPGLQELS---VSDNQLASLP---ALPSELCKLWAYNNQLTSLPTLPSGLQE---LSVSDN 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   287 QLMYLPDSIGGLISVEELDCSFNEVEALPSSIGQL--------------TNLRTFAADHNYLQQLPPEIGSWKNITVlfl 352
Cdd:PRK15387  353 QLASLPTLPSELYKLWAYNNRLTSLPALPSGLKELivsgnrltslpvlpSELKELMVSGNRLTSLPMLPSGLLSLSV--- 429

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 55770895   353 HSNKLETLPEEMGDMQKLKVINLSDNrlknlPFSFTKLQQLTAMWLSDNQSKPLI 407
Cdd:PRK15387  430 YRNQLTRLPESLIHLSSETTVNLEGN-----PLSERTLQALREITSAPGYSGPII 479
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1215-1299 3.87e-09

PDZ domain 1 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 1 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 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: 467165 [Multi-domain]  Cd Length: 89  Bit Score: 54.94  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1215 RVEKDPELGFSIsggVGGRGNPFRpdddGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTV 1292
Cdd:cd06677   10 RSDPYEELGISI---VGGNDTPLI----NIVIQEVYRDGVIARdgRLLPGDQILEVNGVDISNVTHSQARSVLRQPCPVL 82


                 ....*..
gi 55770895 1293 ELIIVRE 1299
Cdd:cd06677   83 RLTVLRE 89
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1202-1298 7.37e-09

PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and 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 1 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 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: 467176 [Multi-domain]  Cd Length: 102  Bit Score: 54.56  E-value: 7.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1202 RHIEAKKLEKirvrvekdPE---LGFSIsggVGGRgNPFRpDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSF-IN 1275
Cdd:cd06689   13 RQVEYIELEK--------PEsggLGFSV---VGLK-SENR-GELGIFVQEIQPGSVAARdgRLKENDQILAINGQPLdQS 79

                         90       100
                 ....*....|....*....|...
gi 55770895 1276 IEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06689   80 ISHQQAIAILQQAKGSVELVVAR 102
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 1210-1296 1.54e-08

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: 53.26  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1210 EKIRVRVEKDPE--LGFSISGG-VGGRgnpfrpDDDGIFVTRVQPEGPA--SKLLQPGDKIIQANGYSFINIEHGQAVSL 1284
Cdd:cd23072    1 EITLVNLKKDAKygLGFQIVGGeKSGR------LDLGIFISSITPGGPAdlDGRLKPGDRLISVNDVSLEGLSHDAAVEI 74

                         90
                 ....*....|..
gi 55770895 1285 LKTFQNTVELII 1296
Cdd:cd23072   75 LQNAPEDVTLVV 86
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1212-1296 1.86e-08

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: 53.01  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPE-LGFSISGGVGGRGNPFRPdddgIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTF 1288
Cdd:cd06681    3 VEVTLEKEGNsFGFVIRGGAHEDRNKSRP----LTVTHVRPGGPADRegTIKPGDRLLSVDGISLHGATHAEAMSILKQC 78


                 ....*...
gi 55770895 1289 QNTVELII 1296
Cdd:cd06681   79 GQEATLLI 86
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1222-1286 2.21e-08

PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. 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 whirlin 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: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 52.37  E-value: 2.21e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55770895 1222 LGFSISGGVggrgnpfrPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLK 1286
Cdd:cd06740   15 LGFSIRGGA--------EHGVGIYVSLVEPGSLAEKEgLRVGDQILRVNDVSFEKVTHAEAVKILR 72
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1228-1297 3.67e-08

PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins , and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. 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 ZO 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: 467211 [Multi-domain]  Cd Length: 82  Bit Score: 51.80  E-value: 3.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55770895 1228 GGVGGR---GNpfrpdDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIV 1297
Cdd:cd06729   11 GSVGLRlagGN-----DVGIFVAGVQEGSPAEKQgLQEGDQILKVNGVDFRNLTREEAVLFLLDLPKGEEVTIL 79
PDZ1_DLG5-like cd06764
PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1205-1298 4.03e-08

PDZ domain 1 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 1 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 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: 467245 [Multi-domain]  Cd Length: 95  Bit Score: 52.02  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1205 EAKKLEKIRVRVEKDP-ELGFSIsggVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVS 1283
Cdd:cd06764    3 ETETVEFEKVRDDMDLkALGFDI---AGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQ 79

                         90
                 ....*....|....*
gi 55770895 1284 LLKTFQNTVELIIVR 1298
Cdd:cd06764   80 AVLNGGGVINMVVRR 94
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1211-1296 4.24e-08

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: 51.88  E-value: 4.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1211 KIRVRVEK-DPE-LGFSISGGVggrgnpfrPDDDGIFVTRVQPEGPAS-KLLQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd06737    2 LRLVRLDRrGPEsLGFSVRGGL--------EHGCGLFVSHVSPGSQADnKGLRVGDEIVRINGYSISQCTHEEVINLIKT 73


                 ....*....
gi 55770895 1288 FQnTVELII 1296
Cdd:cd06737   74 KK-TVSLKV 81
PDZ6_PDZD2-PDZ3_hPro-IL-16-like cd06762
PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 of human pro-interleukin-16 ...
 1222-1298 5.14e-08

PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 6 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the third PDZ domain (PDZ3) of human pro-interleukin-16 (isoform 1, also known as nPro-IL-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. 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 PDZD2-like 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: 467243 [Multi-domain]  Cd Length: 86  Bit Score: 51.49  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1222 LGFSISGGVGGRGNPfrpdddgIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQN-TVELIIVR 1298
Cdd:cd06762   14 LGFSLAGGSDLENKS-------ITVHRVFPSGLAAQegTIQKGDRILSINGKSLKGVTHGDALSVLKQARLpKVAVVVIR 86
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 1212-1286 6.26e-08

PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of DVL1-3, and related domains. The dishevelleds (DVL1, 2 and 3 in humans) act downstream of Frizzled (FZD) receptors in both the canonical and non-canonical WNT signaling pathway; they bind the cytoplasmic C-terminus of frizzled family members and transduce the Wnt signal to down-stream effectors. They bind to several proteins known to modulate Wnt signaling. Binding partners of the DVL1 PDZ domain include nucleoredoxin (NXN), Van Gogh-like (VANGL1), Wnt receptor RYK, Dapper 1 (DACT1), Frizzled7 (FZD7), transmembrane protein 88 (TMEM88), Daple (dishevelled-associating protein with a high frequency of leucines), also known as Ccdc88c), and cysteine-rich protein Idax. The DVL2 PDZ domain has been shown to bind the nuclear export signal sequence of the DVL2 protein. 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 DVL-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: 467201 [Multi-domain]  Cd Length: 87  Bit Score: 51.21  E-value: 6.26e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770895 1212 IRVRVEKDPELGFSISGGVGGRGnpfrpdDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLK 1286
Cdd:cd06717    2 VTLNMEKVNFLGISIVGQSNERG------DGGIYVGSIMKGGAVAAdgRIEPGDMILQVNDISFENMSNDDAVRVLR 72
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 1214-1296 7.20e-08

PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). 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 RapGEF2 and RapGEF6 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: 467237 [Multi-domain]  Cd Length: 83  Bit Score: 51.11  E-value: 7.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPELGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKtfqNTV 1292
Cdd:cd06755    6 TRPSRESPLHFSLLGG--------SEKGFGIFVSKVEKGSKAAEAgLKRGDQILEVNGQNFENITLKKALEILR---NNT 74


                 ....
gi 55770895 1293 ELII 1296
Cdd:cd06755   75 HLSI 78
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
 1210-1299 7.70e-08

PDZ domain 1 of 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 FRMPD2 (also known as PDZ domain-containing protein 4, and related domains. 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: 467284 [Multi-domain]  Cd Length: 92  Bit Score: 51.34  E-value: 7.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1210 EKIRVRVEKDPELGFsisGGVGGRGNPFRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd23071    1 EIVCVTLKRDPKRGF---GFVIVGGENTGKLDLGIFIASIIPGGPAEKdgRIKPGGRLISLNNISLEGVTFNTAVKILQN 77

                         90
                 ....*....|..
gi 55770895 1288 FQNTVELIIVRE 1299
Cdd:cd23071   78 SPDEVELIISQP 89
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 1223-1298 1.05e-07

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: 50.60  E-value: 1.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770895 1223 GFSISGGVGGrGNPfrpdddgIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd23068   14 GFRLQGGADF-GQP-------LSIQKVNPGSPADKAgLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 1220-1299 1.74e-07

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: 54.88  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1220 PELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT-VELIIV 1297
Cdd:COG0793   49 EDFQESTSGEFGGLGAELGEEDGKVVVVSVIPGSPAEKAgIKPGDIILAIDGKSVAGLTLDDAVKLLRGKAGTkVTLTIK 128


                 ..
gi 55770895 1298 RE 1299
Cdd:COG0793  129 RP 130
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 26-261 2.98e-07

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 55.27  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    26 TLDYSHCS-LEQVPKEIFTFEKtLEELYLD-ANQIEELPKQLfNCQSLHKLSLPD-NDLTTLPaSIANliNLRELDVSKN 102
Cdd:PLN03210  661 TLKLSDCSsLVELPSSIQYLNK-LEDLDMSrCENLEILPTGI-NLKSLYRLNLSGcSRLKSFP-DIST--NISWLDLDET 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   103 GIQEFPENIK--NCKVLTIVEASVNPISKLPDGFSQLL-----NLTQLYLND--AFLEfLPANFGRLTKLQILELRE-NQ 172
Cdd:PLN03210  736 AIEEFPSNLRleNLDELILCEMKSEKLWERVQPLTPLMtmlspSLTRLFLSDipSLVE-LPSSIQNLHKLEHLEIENcIN 814

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   173 LKMLPKTMNrLTQLERLDL-GSNEFTEVPEVLEQLSGLKefwMDANRLTFIPGFIGSLKQLTYLDVSK-NNIEMVEEGIS 250
Cdd:PLN03210  815 LETLPTGIN-LESLESLDLsGCSRLRTFPDISTNISDLN---LSRTGIEEVPWWIEKFSNLSFLDMNGcNNLQRVSLNIS 890

                         250
                  ....*....|.
gi 55770895   251 TCENLQDLLLS 261
Cdd:PLN03210  891 KLKHLETVDFS 901
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 1222-1298 3.22e-07

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: 49.23  E-value: 3.22e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770895 1222 LGFSISGGVggrgnpfrpDDDGIFVTRVQPEgPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06696   16 LGFTVTKGK---------DDNGCYIHDIVQD-PAKSdgRLRPGDRLIMVNGVDVTNMSHTEAVSLLRAAPKEVTLVLGR 84
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 1214-1297 3.47e-07

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: 48.97  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPE-LGFSISGGVGGRGNpfrpdddgiFVTRVQPEGPASK-LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT 1291
Cdd:cd06768    3 CHLVKGPEgYGFNLHAEKGRPGH---------FIREVDPGSPAERaGLKDGDRLVEVNGENVEGESHEQVVEKIKASGNQ 73


                 ....*.
gi 55770895 1292 VELIIV 1297
Cdd:cd06768   74 VTLLVV 79
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1214-1296 3.86e-07

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: 48.97  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPE-LGFSISGGvggrgnpfRPDDDGIFVTRVQPEGPASKL--LQPGDKIIQANGYSFINIEHGQAVSLLKTFQN 1290
Cdd:cd06796    5 VELPKTEEgLGFNVMGG--------KEQNSPIYISRIIPGGVADRHggLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQG 76


                 ....*.
gi 55770895 1291 TVELII 1296
Cdd:cd06796   77 SVKLVV 82
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 1222-1298 4.40e-07

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: 48.83  E-value: 4.40e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770895 1222 LGFSIsggVGGRGNPFrpddDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06673   15 LGLSI---VGGSDTLL----GAIIIHEVYEDGAAAKdgRLWAGDQILEVNGEDLRKATHDEAINVLRQTPQKVRLLVYR 86
PDZ7_GRIP1-2-like cd06685
PDZ domain 7 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1209-1298 6.00e-07

PDZ domain 7 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 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: 467173 [Multi-domain]  Cd Length: 85  Bit Score: 48.41  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1209 LEKIRVRVEKDP---ELGFSISGGVGGRGnpfrpdddgIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSL 1284
Cdd:cd06685    1 LELHKVTLYKDSdteDFGFSVSDGLYEKG---------VYVNAIRPGGPADLSgLQPYDRILQVNHVRTRDFDCCLVVPL 71

                         90
                 ....*....|....
gi 55770895 1285 LKTFQNTVELIIVR 1298
Cdd:cd06685   72 IAESGDKLELVVSR 85
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 48-131 9.51e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 51.33  E-value: 9.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   48 LEELYLDANQIEELPKQLFNCQSLHKLS-------LPDNDLTTLpASIANLINLRELDVSKNGIQEFPE---NIKNCKVL 117
Cdd:cd21340   92 LEELHIENQRLPPGEKLTFDPRSLAALSnslrvlnISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEElldLLSSWPSL 170

                         90
                 ....*....|....
gi 55770895  118 TIVEASVNPISKLP 131
Cdd:cd21340  171 RELDLTGNPVCKKP 184
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 1213-1270 1.28e-06

PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467202 [Multi-domain]  Cd Length: 84  Bit Score: 47.56  E-value: 1.28e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55770895 1213 RVRVEKDP--ELGFSISggvggRGNPFRPDDdGIFVTRVQPEGPASK--LLQPGDKIIQANG 1270
Cdd:cd06718    2 RVELIKPPgkPLGFYIR-----DGNGVERVP-GIFISRLVLGSLADStgLLAVGDEILEVNG 57
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
 1216-1285 1.46e-06

PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains. Human STXBP4 (also known as Synip) includes a single PDZ domain, a coiled-coil domain, and a WW domain (named for its two conserved tryptophans); Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). Human STXBP4 plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane: insulin induces the dissociation of the STXBP4 and STX4 complex liberating STX4 to interact with Vamp2, and to form the SNARE complex thereby promoting vesicle fusion. It may also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose. Human STXBP4 is also known to physically associate with a prominent isoform of TP63 (deltaNp63alpha 9) whose overexpression promotes squamous cell carcinoma development, and in doing so prevents degradation of this isoform by the Cdc20-APC/C complex, Itch, and RACK1. 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 STXBP4-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: 467184 [Multi-domain]  Cd Length: 89  Bit Score: 47.68  E-value: 1.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55770895 1216 VEKDPELGFSISGGVGgrgnpfRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLL 1285
Cdd:cd06698    7 VAKSTGLGLSIVGGIN------RPEGPMVFIQEVIPGGDCYKdgRLRPGDQLVSINKESLIGVTLEEAKSIL 72
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1248-1297 1.94e-06

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: 46.84  E-value: 1.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55770895 1248 RVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIV 1297
Cdd:cd06734   32 RIIPGSPADRcgQLKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIV 83
PDZ7_PDZD2-PDZ4_hPro-IL-16-like cd06763
PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 ...
 1212-1296 2.51e-06

PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers 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 PDZD2-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: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 46.84  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPE-LGFSISGGVGG-RGNpfRPdddgIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd06763    2 VTVELEKGSAgLGFSLEGGKGSpLGD--RP----LTIKRIFKGGAAEQsgVLQVGDEILQINGTSLQGLTRFEAWNIIKS 75

                         90
                 ....*....|
gi 55770895 1288 FQN-TVELII 1296
Cdd:cd06763   76 LPEgPVTLLI 85
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1214-1294 2.66e-06

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: 46.41  E-value: 2.66e-06
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPE--LGFSISGGvggRGNPFrPdddgIFVTRVQPEGPASK--LLQPGDKIIQANGysfINIE---HGQAVSLLK 1286
Cdd:cd06801    3 VRVVKQDVggLGISIKGG---AEHKM-P----ILISKIFKGQAADQtgQLFVGDAILSVNG---ENLEdatHDEAVQALK 71


                 ....*...
gi 55770895 1287 TFQNTVEL 1294
Cdd:cd06801   72 NAGDEVTL 79
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1214-1296 3.30e-06

PDZ domain 9 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 9 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 PDZ9 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 PDZ9 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: 467263 [Multi-domain]  Cd Length: 79  Bit Score: 46.19  E-value: 3.30e-06
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPE-LGFSISGGvggrgnpfrPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQN 1290
Cdd:cd10817    2 VELPKDQGgLGIAISEE---------DTENGIVIKSLTEGGPAAKdgRLKVGDQILAVDDESVVGCPYEKAISLLKTAKG 72


                 ....*.
gi 55770895 1291 TVELII 1296
Cdd:cd10817   73 TVKLTV 78
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 1211-1298 3.45e-06

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: 46.48  E-value: 3.45e-06
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1211 KIRVRVEKDPE-LGFSISGgvggRGNPFrPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLK- 1286
Cdd:cd23058    5 KLHIQLKKGPEgLGFSITS----RDNPT-GGSGPIYIKNILPKGAAIQdgRLKAGDRLLEVNGVDVTGKTQEEVVSLLRs 79

                         90
                 ....*....|...
gi 55770895 1287 -TFQNTVELIIVR 1298
Cdd:cd23058   80 tKLGGTVSLVVSR 92
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 1212-1298 5.49e-06

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: 45.83  E-value: 5.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPE--LGFSISGGvGGRGNPfrpdddgIFVTRVQPEGPASKL--LQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd06800    1 RKVLLSKEPHegLGISITGG-KEHGVP-------ILISEIHEGQPADRCggLYVGDAILSVNGIDLRDAKHKEAVTILSQ 72

                         90
                 ....*....|.
gi 55770895 1288 FQNTVELIIVR 1298
Cdd:cd06800   73 QRGEITLEVVY 83
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 1214-1298 8.22e-06

PDZ domain 3 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 3 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. 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). 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). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 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: 467181 [Multi-domain]  Cd Length: 90  Bit Score: 45.33  E-value: 8.22e-06
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEK-DPELGFSISGGvgGRGNPFRPDDDGIFVTRVQPEGPA--SKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQN 1290
Cdd:cd06695    4 VKLTKgSSGLGFSFLGG--ENNSPEDPFSGLVRIKKLFPGQPAaeSGLIQEGDVILAVNGEPLKGLSYQEVLSLLRGAPP 81


                 ....*...
gi 55770895 1291 TVELIIVR 1298
Cdd:cd06695   82 EVTLLLCR 89
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 1209-1294 1.02e-05

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: 44.97  E-value: 1.02e-05
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gi 55770895 1209 LEKIRVRVEK-DPELGFSIsggVGGRGNpfRPDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLL 1285
Cdd:cd06789    1 PEIITVTLKKvGNGMGLSI---VAAKGA--GQDKLGIYIKSVVKGGAADLdgRLQAGDQLLSVDGHSLVGLSQERAAELM 75


                 ....*....
gi 55770895 1286 KTFQNTVEL 1294
Cdd:cd06789   76 TKTGSVVTL 84
PLN03150 PLN03150
hypothetical protein; Provisional
 267-342 1.06e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 49.81  E-value: 1.06e-05
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gi 55770895   267 QLPETIGSLKNITTLKIDENQLM-YLPDSIGGLISVEELDCSFNEVE-ALPSSIGQLTNLRTFAADHNYLQ-QLPPEIG 342
Cdd:PLN03150  433 FIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAALG 511
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 48-200 1.07e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 47.86  E-value: 1.07e-05
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gi 55770895   48 LEELYLDANQIEELPkQLFNCQSLHKLSLPDNDLTTLpASIANLINLRELDVSKngiQEFPENIKnckvLTIVEASVNPI 127
Cdd:cd21340   48 LTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV-EGLENLTNLEELHIEN---QRLPPGEK----LTFDPRSLAAL 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770895  128 SK-LpdgfsQLLNLTQLYLNDafleflPANFGRLTKLQILELRENQLKMLPK---TMNRLTQLERLDLGSNEFTEVP 200
Cdd:cd21340  119 SNsL-----RVLNISGNNIDS------LEPLAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGNPVCKKP 184
PLN03150 PLN03150
hypothetical protein; Provisional
 152-229 1.08e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 49.81  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   152 FLPANFGRLTKLQILELRENQLK-MLPKTMNRLTQLERLDLGSNEFT-EVPEVLEQLSGLKEFWMDANRLT-FIPGFIGS 228
Cdd:PLN03150  433 FIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAALGG 512


                  .
gi 55770895   229 L 229
Cdd:PLN03150  513 R 513
PDZ_neurabin-like cd06790
PDZ domain of neurabin-1 and neurabin-2, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1214-1298 1.30e-05

PDZ domain of neurabin-1 and neurabin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of neurabin-1 (also known as protein phosphatase 1 regulatory subunit 9A) and neurabin-2 (also known as spinophilin, and protein phosphatase 1 regulatory subunit 9B), and related domains. Neurabin-1 and neurabin-2 are neuronal scaffolding proteins that play important roles in the regulation of synaptic transmission through their ability to interact with and target protein phosphatase 1 (PP1) to dendritic spines where PP1 dephosphorylates and inactivates glutamate receptors. Neurabin-2 interacts with multiple other synaptic proteins, including synaptic signaling and scaffolding proteins (e.g., GluN1 and SAPAP3) and cytoskeletal proteins (e.g., neurofilament medium polypeptide, NF-M). Neurabin-1 and neurabin-2 also binds F-actin. Other binding partners of neurabin-1 include adenosine A1 receptor (A1R), SAD-1 kinase and 70 kDa ribosomal protein S6 kinase (p70-S6K). This PDZ domain is immediately C-terminal to the PP1 binding 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 neurabin-like PDZ 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: 467252 [Multi-domain]  Cd Length: 90  Bit Score: 44.72  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPE-LGFSISG-GVGGRGNPfrpDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQ 1289
Cdd:cd06790    5 VELEKGSEgLGISIIGmGVGADAGL---EKLGIFVKTVTEGGAAQRdgRIQVNDQIVEVDGISLVGVTQAFAASVLRNTS 81


                 ....*....
gi 55770895 1290 NTVELIIVR 1298
Cdd:cd06790   82 GTVRFLIGR 90
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 1214-1296 1.78e-05

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: 44.43  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDPE--LGFSISGG-VGGRGNPFRpddDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTF 1288
Cdd:cd23063    2 VVIEKTEKksFGICIVRGeVKVSPNTKT---TGIFIKGIIPDSPAHKcgRLKVGDRILSVNGNDVRNSTEQAAIDLIKEA 78


                 ....*...
gi 55770895 1289 QNTVELII 1296
Cdd:cd23063   79 DFKIVLEI 86
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1213-1292 2.17e-05

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: 43.85  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1213 RVRVEK-DPELGFSISGGVGGrgnpfrpdddGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQN 1290
Cdd:cd06767    5 HVSIEKgSEPLGISIVSGENG----------GIFVSSVTEGSLAHQAgLEYGDQLLEVNGINLRNATEQQAALILRQCGD 74


                 ..
gi 55770895 1291 TV 1292
Cdd:cd06767   75 TI 76
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1210-1298 2.32e-05

PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and 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 3 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 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: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 44.15  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1210 EKIRVRVEKDPE-LGFSISGGVGGRGNPfrpDDDGIFVTRVQPeGPASKL---LQPGDKIIQANGYSFINIEHGQAVSLL 1285
Cdd:cd06791    1 ETFEVELVKDEQgLGITIAGYVGEKASG---ELSGIFVKSIIP-GSAADQdgrIQVNDQIIAVDGVNLQGFTNQEAVEVL 76

                         90
                 ....*....|...
gi 55770895 1286 KTFQNTVELIIVR 1298
Cdd:cd06791   77 RNTGQVVHLTLAR 89
LRR_8 pfam13855
Leucine rich repeat;
322-380 2.37e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.28  E-value: 2.37e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770895    322 TNLRTFAADHNYLQQLPPEI-GSWKNITVLFLHSNKLETL-PEEMGDMQKLKVINLSDNRL 380
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 1245-1298 2.68e-05

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: 44.12  E-value: 2.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 55770895 1245 FVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06746   45 YLESVDPGGVADKAgLKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVLKVVT 99
LRR_8 pfam13855
Leucine rich repeat;
346-402 2.94e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.90  E-value: 2.94e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 55770895    346 NITVLFLHSNKLETLPEEM-GDMQKLKVINLSDNRLKNL-PFSFTKLQQLTAMWLSDNQ 402
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNR 60
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 48-209 2.97e-05

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 47.74  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   48 LEELYLDANQI-----EELPKQLFNCQSLHKLSLPDNDLTtlPASIANLinlreldvskngIQEFPENiKNCKVLTIVEA 122
Cdd:cd00116  139 LEKLVLGRNRLegascEALAKALRANRDLKELNLANNGIG--DAGIRAL------------AEGLKAN-CNLEVLDLNNN 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  123 SVNP--ISKLPDGFSQLLNLTQLYLNDAFL------EFLPANFGRLTKLQILELRENQL-----KMLPKTMNRLTQLERL 189
Cdd:cd00116  204 GLTDegASALAETLASLKSLEVLNLGDNNLtdagaaALASALLSPNISLLTLSLSCNDItddgaKDLAEVLAEKESLLEL 283

                        170       180
                 ....*....|....*....|
gi 55770895  190 DLGSNEFTEVPEVLEQLSGL 209
Cdd:cd00116  284 DLRGNKFGEEGAQLLAESLL 303
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
246-408 3.35e-05

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 48.23  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   246 EEGISTCEN-----LQDLLLSSNSLQQLPETIGSLKnitTLKIDENQLMYLPDSIGGLISVEELDCSFNEVEALPSSI-- 318
Cdd:PRK15387  210 ESGLTTLPDclpahITTLVIPDNNLTSLPALPPELR---TLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLck 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   319 -----GQLTN-------LRTFAADHNYLQQLPpeiGSWKNITVLFLHSNKLETLPEEMGDMQKLKVinlSDNRLKNLPfs 386
Cdd:PRK15387  287 lwifgNQLTSlpvlppgLQELSVSDNQLASLP---ALPSELCKLWAYNNQLTSLPTLPSGLQELSV---SDNQLASLP-- 358

                         170       180
                  ....*....|....*....|....
gi 55770895   387 fTKLQQLTAMWLSDNQ--SKPLIP 408
Cdd:PRK15387  359 -TLPSELYKLWAYNNRltSLPALP 381
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1241-1301 4.56e-05

PDZ domain 2 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 2 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 PSZ2 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: 467246 [Multi-domain]  Cd Length: 77  Bit Score: 43.10  E-value: 4.56e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55770895 1241 DDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVREVS 1301
Cdd:cd06765   15 ENGVFISRIVPGSPAAKegSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 1231-1302 5.99e-05

circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do), and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for the identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for the combining with other DegP monomers to form a stable oligomer structure. 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 DegP family PDZ domain 2 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: 467631 [Multi-domain]  Cd Length: 83  Bit Score: 42.61  E-value: 5.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55770895 1231 GGRGNPFRPDDD--GIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVslLKTFQNTVELIIVREVSS 1302
Cdd:cd23084    5 GATVSNVTDEDGgkGVVVTEVDPGSPAAQSgLKKGDVIIGVNRQPVKSIAELRKV--LKSKPSAVLLQIKRGDSS 77
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 130-314 6.34e-05

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 46.58  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  130 LPDGFSQLLNLTQLYLND-AFLEFLPANFGRLTK---LQILELRENQL-----KMLPKTMNRLT-QLERLDLGSNEFTEv 199
Cdd:cd00116   73 LLQGLTKGCGLQELDLSDnALGPDGCGVLESLLRsssLQELKLNNNGLgdrglRLLAKGLKDLPpALEKLVLGRNRLEG- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  200 pEVLEQLSGLkefwmdanrltFIpgFIGSLKQLtylDVSKNNIEmvEEGI-STCE------NLQDLLLSSNSL-----QQ 267
Cdd:cd00116  152 -ASCEALAKA-----------LR--ANRDLKEL---NLANNGIG--DAGIrALAEglkancNLEVLDLNNNGLtdegaSA 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55770895  268 LPETIGSLKNITTLKIDENQL------MYLPDSIGGLISVEELDCSFNEVEAL 314
Cdd:cd00116  213 LAETLASLKSLEVLNLGDNNLtdagaaALASALLSPNISLLTLSLSCNDITDD 265
PDZ_ARHGEF11-12-like cd23069
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1214-1286 7.16e-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: 42.38  E-value: 7.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55770895 1214 VRVEKDPE-LGFSISGgvggrgnpfrpdDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLK 1286
Cdd:cd23069    4 VVIQRDENgYGLTVSG------------DNPVFVQSVKEGGAAYRAgVQEGDRIIKVNGTLVTHSNHLEVVKLIK 66
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1212-1298 1.05e-04

PDZ domain 1 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 1 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 PDZ1 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: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 42.20  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPE-LGFSISGGvggrgnpfrpDDDGIF--VTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLlk 1286
Cdd:cd06731    2 IRTSLKKSARgFGFTIIGG----------DEPDEFlqIKSVVPDGPAALdgKLRTGDVLVSVNDTCVLGYTHADVVKL-- 69

                         90
                 ....*....|....*..
gi 55770895 1287 tFQN-----TVELIIVR 1298
Cdd:cd06731   70 -FQSipigqSVNLEVCR 85
PDZ1_GRIP1-2-like cd06687
PDZ domain 1 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1222-1294 1.08e-04

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: 42.01  E-value: 1.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55770895 1222 LGFSISGGVGGRGNPFrpdddgifVTRVQPEGPA--SKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVEL 1294
Cdd:cd06687   13 LGLTVSGGIDKDGKPR--------VSNLRPGGIAarSDQLNVGDYIKSVNGIRTTKLRHDEIISLLKNVGERVVL 79
PLN03150 PLN03150
hypothetical protein; Provisional
 130-203 1.16e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 46.35  E-value: 1.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770895   130 LPDGFSQLLNLTQLYLNDAFLE-FLPANFGRLTKLQILELRENQLK-MLPKTMNRLTQLERLDLGSNEFT-EVPEVL 203
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAAL 510
PDZ8_MUPP1-PDZ7_PATJ-PDZ2_INAD-like cd06672
PDZ domain 8 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 7 of protein-associated tight ...
 1213-1298 1.33e-04

PDZ domain 8 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 7 of protein-associated tight junction (PATJ), PDZ domain 2 of Drosophila melanogaster 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 8 of MUPP1, PDZ domain 7 of PATJ, and PDZ domain 2 of Drosophila melanogaster INAD, 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. 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. 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 PDZ8 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: 467160 [Multi-domain]  Cd Length: 84  Bit Score: 41.90  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1213 RVRVEKDPE-LGFSISGgvggrgNPFRpDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQ 1289
Cdd:cd06672    3 LIELEKGSSgLGLSLAG------NKDR-SRMSVFVVGIDPDGAAGKdgRIQVGDELLEINGQVLYGRSHLNASAIIKSAP 75


                 ....*....
gi 55770895 1290 NTVELIIVR 1298
Cdd:cd06672   76 SKVKIVFLR 84
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 19-242 1.58e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 45.94  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   19 GEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQI-----EELPKQLFNCQSLHKLSLPDNDLTTLPASI----- 88
Cdd:COG5238  153 GNAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIgdegiEELAEALTQNTTVTTLWLKRNPIGDEGAEIlaeal 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   89 ANLINLRELDVSKN-----GIQEFPENIKNCKVLTIVEASVNPISK-----LPDGFSQLLNLTQLYLND---------AF 149
Cdd:COG5238  233 KGNKSLTTLDLSNNqigdeGVIALAEALKNNTTVETLYLSGNQIGAegaiaLAKALQGNTTLTSLDLSVnrigdegaiAL 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  150 LEFLPANfgrlTKLQILELRENQL-----KMLPKTMNRLTQLERLDLGSNEFTEvpevlEQLSGLKEfwmdanrltfipg 224
Cdd:COG5238  313 AEGLQGN----KTLHTLNLAYNGIgaqgaIALAKALQENTTLHSLDLSDNQIGD-----EGAIALAK------------- 370

                        250
                 ....*....|....*...
gi 55770895  225 FIGSLKQLTYLDVSKNNI 242
Cdd:COG5238  371 YLEGNTTLRELNLGKNNI 388
LRR_8 pfam13855
Leucine rich repeat;
47-104 1.67e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 1.67e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895     47 TLEELYLDANQIEELPKQLF-NCQSLHKLSLPDNDLTTL-PASIANLINLRELDVSKNGI 104
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFkGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
231-288 1.98e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.59  E-value: 1.98e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    231 QLTYLDVSKNNIEMVEEGI-STCENLQDLLLSSNSLQQL-PETIGSLKNITTLKIDENQL 288
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PDZ_ARHGAP21_23-like cd06756
PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1218-1296 2.52e-04

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: 41.67  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1218 KDPELGfsisGGVGGRGNPFRPDDDgIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELII 1296
Cdd:cd06756   34 KDEENG----NRGGKQRSRLEPMDT-IFVKQVKEGGPAHQAgLCTGDRIVKVNGESVIGKTYSQVIALIQNSDSTLELSV 108
LRR_8 pfam13855
Leucine rich repeat;
139-196 2.68e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 2.68e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895    139 NLTQLYLNDAFLEFL-PANFGRLTKLQILELRENQLKML-PKTMNRLTQLERLDLGSNEF 196
Cdd:pfam13855    2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 1245-1298 2.91e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 39.82  E-value: 2.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 55770895   1245 FVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHgqAVSLLKTFQNT-VELIIVR 1298
Cdd:pfam17820    1 VVTAVVPGSPAERAgLRVGDVILAVNGKPVRSLED--VARLLQGSAGEsVTLTVRR 54
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 1236-1298 3.27e-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: 40.74  E-value: 3.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55770895 1236 PFRPDDDGIFVTRVQPEGPASK-LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06779   19 LGLPVNRGVLVAEVIPGSPAAKaGLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDSLNLTILR 82
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 1213-1297 4.13e-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: 40.31  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1213 RVRVEKDPELGFsisGGVGGRGNPfrpdddgIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTV 1292
Cdd:cd06769    1 TVEIQRDAVLGF---GFVAGSERP-------VVVRSVTPGGPSEGKLLPGDQILKINNEPVEDLPRERVIDLIRECKDSI 70


                 ....*
gi 55770895 1293 ELIIV 1297
Cdd:cd06769   71 VLTVL 75
PDZ3_PDZD7-like cd06751
PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1222-1286 4.70e-04

PDZ domain 3 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 3 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of the 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 and can also form homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the third 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 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: 467233 [Multi-domain]  Cd Length: 89  Bit Score: 40.50  E-value: 4.70e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770895 1222 LGFSISGGVGGRGNPFrpdddgIFVTRVQPEGPA--SKLLQPGDKIIQANGYSFINIEHGQAVSLLK 1286
Cdd:cd06751   13 LGISISGGIESKVQPV------VKIEKIFPGGAAalSGNLKAGYELVSVDGESLQQVTHQQAVDIIR 73
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
 1212-1298 4.76e-04

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. 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 PTPN3-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: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 40.37  E-value: 4.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPELGFSISGGVggrgnpfrpdDDG--IFVTRVQPEGPASKL---LQPGDKIIQANGYSFINIEHGQAVSLLK 1286
Cdd:cd06706    6 IRMKPDENGRFGFNVKGGV----------DQKmpVIVSRVAPGTPADLCiprLNEGDQVLLINGRDISEHTHDQVVMFIK 75

                         90
                 ....*....|....*
gi 55770895 1287 TF--QNTVELI-IVR 1298
Cdd:cd06706   76 ASreRHSGELVlLVR 90
PLN03150 PLN03150
hypothetical protein; Provisional
 314-380 5.45e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.42  E-value: 5.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770895   314 LPSSIGQLTNLRTFAADHNYLQ-QLPPEIGSWKNITVLFLHSNKLE-TLPEEMGDMQKLKVINLSDNRL 380
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSL 502
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 1243-1298 5.58e-04

PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Radil (also known as protein KIAA1849) and related domains. Radil is required for cell adhesion and migration of neural crest precursors during development. Radil is a component of a Rasip1-Radil-ARHGAP29 complex at endothelial cell-cell junctions. Rap1, via its effectors Radil and Rasip1 and their binding partner ArhGAP29, controls the endothelial barrier by decreasing Rho-mediated radial tension on cell-cell junctions. ArhGAP29 binds the Radil PDZ domain. The Radil PDZ domain also binds kinesin family protein 14 (KIF14); KIF14 negatively regulates Rap1-mediated inside-out integrin activation by tethering Radil on microtubules. 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 Radil-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: 467177 [Multi-domain]  Cd Length: 88  Bit Score: 40.35  E-value: 5.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1243 GIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06690   31 GIYIRTLVPDSPAARdgRLRLGDRILAVNGTSLVGADYQSAMDLIRTSGDKLRFLVAK 88
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 23-201 6.07e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 44.01  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   23 TVTTLDYS--HCSLEQVPK--EIFTFEKTLEELYLDANQIEE-----LPKQLFNCQSLHKLSLPDNDLT-----TLPASI 88
Cdd:COG5238  237 SLTTLDLSnnQIGDEGVIAlaEALKNNTTVETLYLSGNQIGAegaiaLAKALQGNTTLTSLDLSVNRIGdegaiALAEGL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   89 ANLINLRELDVSKNGIQE-----FPENIKNCKVLTIVEASVNPIS--------KLPDGFSQLLNLtqlylndafleflpa 155
Cdd:COG5238  317 QGNKTLHTLNLAYNGIGAqgaiaLAKALQENTTLHSLDLSDNQIGdegaialaKYLEGNTTLREL--------------- 381

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 55770895  156 NFGR--LTKLQILELrenqLKMLPKtmnrlTQLERLDLGSNEFTEVPE 201
Cdd:COG5238  382 NLGKnnIGKQGAEAL----IDALQT-----NRLHTLILDGNLIGAEAQ 420
PDZ4_MUPP1-like cd06668
PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1245-1298 6.25e-04

PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and 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 4 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 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: 467156 [Multi-domain]  Cd Length: 88  Bit Score: 39.97  E-value: 6.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 55770895 1245 FVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06668   33 YIRSILPEGPVGRngKLFSGDELLEVNGIQLLGLSHKEVVSILKELPPPVRLVCCR 88
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1213-1296 6.65e-04

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. 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 RIM-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: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 40.23  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1213 RVRVEKDPELGFSISGGVGGR---GNPFRPDDDGIFVTRVQPEGPASKL--LQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd06714    6 RIILQRDPKDGSVSGNGLGLKvvgGKMTESGRLGAYVTKVKPGSVADTVghLREGDEVLEWNGISLQGKTFEEVQDIISQ 85


                 ....*....
gi 55770895 1288 FQNTVELII 1296
Cdd:cd06714   86 SKGEVELVV 94
PLN03150 PLN03150
hypothetical protein; Provisional
 221-298 9.98e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 43.27  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895   221 FIPGFIGSLKQLTYLDVSKNNIE-MVEEGISTCENLQDLLLSSNSLQ-QLPETIGSLKNITTLKIDENQLM-YLPDSIGG 297
Cdd:PLN03150  433 FIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAALGG 512


                  .
gi 55770895   298 L 298
Cdd:PLN03150  513 R 513
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 1240-1298 1.09e-03

PDZ domain 2 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 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: 467200 [Multi-domain]  Cd Length: 88  Bit Score: 39.18  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770895 1240 DDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEhgQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06716   29 EDTGIYVSEVDPNSIAAKdgRIREGDQILQINGVDVQNRE--EAIALLSEEEKSITLLVAR 87
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 1212-1297 1.35e-03

PDZ domain 4 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 4 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 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: 467278 [Multi-domain]  Cd Length: 82  Bit Score: 39.04  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1212 IRVRVEKDPeLGFSISGGVGGRGNpfrpdddGIFVTRVQPEG--PASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFQ 1289
Cdd:cd23065    2 IELKTDKSP-LGVSVVGGKNHVTT-------GCIITHIYPNSivAADKRLKVFDQILDINGTKVHVMTTLKVHQLFHKTY 73


                 ....*...
gi 55770895 1290 NTVELIIV 1297
Cdd:cd23065   74 EKAVTLVV 81
LRR_8 pfam13855
Leucine rich repeat;
161-219 1.53e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 1.53e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770895    161 TKLQILELRENQLKMLPKTM-NRLTQLERLDLGSNEFTEV-PEVLEQLSGLKEFWMDANRL 219
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1214-1290 1.97e-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: 38.52  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1214 VRVEKDP-ELGFSISGGvggrgnpfrpDDDGIFVTRVQPEGPASKL--LQPGDKIIQANGYSFINIEHGQA-VSLLKTFQ 1289
Cdd:cd06766    5 VFLKKSQvELGIQLCGG----------NLHGIFVEDVEDDSPAKGPdgLVPGDLILEYNSVDMRNKTAEEAyLEMLKPAE 74


                 .
gi 55770895 1290 N 1290
Cdd:cd06766   75 T 75
LRR_8 pfam13855
Leucine rich repeat;
207-265 2.01e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 2.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770895    207 SGLKEFWMDANRLTFI-PGFIGSLKQLTYLDVSKNNIEMVEEG-ISTCENLQDLLLSSNSL 265
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 163-401 2.46e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 41.57  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  163 LQILELRENQL-----KMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLsglkefwmdanrltfiPGFIGSLKQLTYLDV 237
Cdd:cd00116   25 LQVLRLEGNTLgeeaaKALASALRPQPSLKELCLSLNETGRIPRGLQSL----------------LQGLTKGCGLQELDL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  238 SKNNIemveeGISTCENLQDLLLSSnslqqlpetigSLKNittLKIDENQL--MYLPDSIGGLISV----EELDCSFNEV 311
Cdd:cd00116   89 SDNAL-----GPDGCGVLESLLRSS-----------SLQE---LKLNNNGLgdRGLRLLAKGLKDLppalEKLVLGRNRL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895  312 -----EALPSSIGQLTNLRTFAADHNYLQQ-----LPPEIGSWKNITVLFLHSNKLEtlPEEMGDM-------QKLKVIN 374
Cdd:cd00116  150 egascEALAKALRANRDLKELNLANNGIGDagiraLAEGLKANCNLEVLDLNNNGLT--DEGASALaetlaslKSLEVLN 227

                        250       260       270
                 ....*....|....*....|....*....|...
gi 55770895  375 LSDNRLKNLPFS------FTKLQQLTAMWLSDN 401
Cdd:cd00116  228 LGDNNLTDAGAAalasalLSPNISLLTLSLSCN 260
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 1243-1299 2.59e-03

circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do) and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for combining with other DegP monomers to form a stable oligomer structure. 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 DegP family PDZ domain 1 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: 467630 [Multi-domain]  Cd Length: 91  Bit Score: 38.23  E-value: 2.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770895 1243 GIFVTRVQPEGPASKL-LQPGDKIIQANgysfiniehGQAVSLLKTFQN---------TVELIIVRE 1299
Cdd:cd10839   26 GALVAQVLPDSPAAKAgLKAGDVILSLN---------GKPITSSADLRNrvattkpgtKVELKILRD 83
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1214-1286 2.85e-03

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: 37.64  E-value: 2.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55770895 1214 VRVEK-DPELGFSISGGvggrgNPfrpdddgIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLK 1286
Cdd:cd06744    2 VRVYRgNGSFGFTLRGH-----AP-------VYIESVDPGSAAERAgLKPGDRILFLNGLDVRNCSHDKVVSLLQ 64
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1239-1299 3.03e-03

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: 40.90  E-value: 3.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55770895 1239 PDDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVRE 1299
Cdd:COG0265  198 PEPEGVLVARVEPGSPAAKAgLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRG 259
cpPDZ1_ScNma111-like cd06786
circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine ...
 1239-1277 3.33e-03

circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine protease Nma111p and related domains; First PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the HtrA-type protease Saccharomyces cerevisiae Nma111p (also known as Ynm3p), and related domains. Nma111p is a nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor Bir1p. Nma111p is composed of 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. 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 ScNma111-like PDZ1 domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation places both beta-strands A and B on the C-terminus.


Pssm-ID: 467625 [Multi-domain]  Cd Length: 89  Bit Score: 37.94  E-value: 3.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 55770895 1239 PDDDGIFVT-RVQPEGPASKLLQPGDKIIQANGY---SFINIE 1277
Cdd:cd06786   19 PSETGMLVAeTVLPEGPADGKLEEGDVLISVNGElitQFIRLE 61
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 1240-1297 3.37e-03

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: 37.75  E-value: 3.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 55770895 1240 DDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYsfiNIEHGQAVSLLKTFQNTVELIIV 1297
Cdd:cd06711   18 DDSPVRVQAVDPGGPAEQAgLQQGDTVLQINGQ---PVERSKCVELAHAIRNCPSEIIL 73
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 1240-1302 3.50e-03

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: 37.85  E-value: 3.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55770895 1240 DDDGIFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNT-VELIIVREVSS 1302
Cdd:cd06782   12 DDGYLVVVSPIPGGPAEKAgIKPGDVIVAVDGESVRGMSLDEVVKLLRGPKGTkVKLTIRRGGEG 76
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 1222-1287 5.47e-03

PDZ domain 3 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 3 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 Par-3 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 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: 467272 [Multi-domain]  Cd Length: 103  Bit Score: 37.65  E-value: 5.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55770895 1222 LGFSISGGVGGRGNPFRpDDDGIFVTRVQPEGPASK--LLQPGDKIIQANGYSFINIEHGQAVSLLKT 1287
Cdd:cd23059   18 LGVSVKGKTSKEDNGGK-ADLGIFIKSIIHGGAASKdgRLRVNDQLIAVNGESLLGLTNSEAMETLRR 84
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 1245-1297 6.19e-03

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: 37.22  E-value: 6.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55770895 1245 FVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIV 1297
Cdd:cd06713   38 YVCRVHEDSPAYLAgLTAGDVILSVNGVSVEGASHQEIVELIRSSGNTLRLETL 91
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 1222-1298 6.78e-03

PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 11 of MUPP1, PDZ domain 9 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ11 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467162 [Multi-domain]  Cd Length: 87  Bit Score: 36.88  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770895 1222 LGFSISGgvggrgnpfRPDDDGIFVTRVQPEGPAS---KLLQpGDKIIQANGYSFINIEHGQAVSLLKTFQNTVELIIVR 1298
Cdd:cd06674   16 LGLSIVG---------KRNDTGVFVSDIVKGGAADadgRLMQ-GDQILSVNGEDVRNASQEAAAALLKCAQGKVRLEVGR 85
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 1228-1297 8.63e-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: 36.49  E-value: 8.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770895 1228 GGVGGRGnpFRPDDDGiFVTRVQPEGPASKL-LQPGDKIIQANGYSFINIEHGQAVSLLKTFQnTVELIIV 1297
Cdd:cd06745    7 NGLGQLG--FHVNYEG-FVTEVERFGFAWQAgLRQGSRLVEICKVPVATLTHEQMIDLLRTSV-KVKVTVI 73
PDZ_2 pfam13180
PDZ domain;
1237-1271 8.73e-03

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 36.48  E-value: 8.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 55770895   1237 FRPDDDGIFVTRVQPEGPASK-LLQPGDKIIQANGY 1271
Cdd:pfam13180    1 FVDLEGGVVVVSVKSSGPAAKaGLKAGDVILSIDGR 36
 
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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