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Conserved domains on  [gi|1039746878|ref|XP_017171686|]
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disks large homolog 5 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDZ1_DLG5-like cd06764
PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 620-714 2.20e-59

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: 198.78  E-value: 2.20e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  620 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 699
Cdd:cd06764      1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                           90
                   ....*....|....*
gi 1039746878  700 LLNGEGAINMVVRRR 714
Cdd:cd06764     81 VLNGGGVINMVVRRR 95
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1356-1437 2.74e-48

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: 166.73  E-value: 2.74e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1356 EEPRHVKVQKGSEPLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1435
Cdd:cd06767      1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                   ..
gi 1039746878 1436 QY 1437
Cdd:cd06767     81 QY 82
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1512-1592 1.50e-47

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: 164.48  E-value: 1.50e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1512 DPRIVFIKKSQLDLGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLKV 1591
Cdd:cd06766      1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                   .
gi 1039746878 1592 Q 1592
Cdd:cd06766     81 Q 81
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 726-807 2.70e-41

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: 146.72  E-value: 2.70e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  726 HINLSGQKgsrpqDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 805
Cdd:cd06765      1 HINLSGQK-----DSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKV 75


                   ..
gi 1039746878  806 FP 807
Cdd:cd06765     76 FP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1744-1920 1.35e-40

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


:

Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 148.21  E-value: 1.35e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1744 QKVDCTSLRPVLLLG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1820
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1821 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSAKHIKEQRDPvylRDKVTQRHSKEQFETAQKIDQEYsRYFTGVV 1900
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 1039746878  1901 QGGALSSICTQILAMVSQEQ 1920
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1610-1672 3.04e-35

Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein that is located at sites of cell-cell contact and is involved in the maintenance of cell shape and polarity. Mutations in the DLG5 gene are associated with Crohn's disease (CD) and inflammatory bowel disease (IBD). DLG5 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG5 contains 4 PDZ domains as well as an N-terminal domain of unknown function. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212794  Cd Length: 63  Bit Score: 128.61  E-value: 3.04e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878 1610 YIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1672
Cdd:cd11860      1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
dbPDZ_assoc super family cl24984
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1437-1512 7.06e-31

Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote Dlg5, Disks large homolog 5, proteins, lying between the second pair of PDZ domains. The sequence is natively unstructured but may just be long extensions of the PDZs on these sequences in this position. The function is not known.


The actual alignment was detected with superfamily member pfam16610:

Pssm-ID: 465197  Cd Length: 81  Bit Score: 116.92  E-value: 7.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1437 YNPHIHQLNSHSRSSSHLDPAATpHSTLQGSSAGTPEHPSVIDPLMEQDEGPGTPPAKQSASST------RSVGDTTKKT 1510
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSN-HSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTTPATsphnsfRMPGDANKRV 79


                   ..
gi 1039746878 1511 PD 1512
Cdd:pfam16610   80 PE 81
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 129-213 6.23e-29

Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of this family regulate synaptic activity.


:

Pssm-ID: 461445  Cd Length: 85  Bit Score: 111.58  E-value: 6.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  129 KAPSPPPLLTEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 208
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 1039746878  209 HTNAL 213
Cdd:pfam04822   81 ISEAL 85
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 338-641 2.93e-16

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 85.49  E-value: 2.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  338 LEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQN----KDLQWEMELLQSELTELRSKqvk 413
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskelTELEAEIEELEERLEEAEEE--- 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  414 tAKESEKYKEERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAASEEMEALRQIKDTVTM 486
Cdd:TIGR02168  777 -LAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  487 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 566
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  567 DTRKQKNDVSRELKELnscvhrEQMECQLEKEARFRQ---LMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 641
Cdd:TIGR02168  919 ELREKLAQLELRLEGL------EVRIDNLQERLSEEYsltLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 204-389 6.89e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


The actual alignment was detected with superfamily member pfam13851:

Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 6.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  204 SLQNQHTNALKRCEEvaketdFYHTLHSRLLSDQTQLKDDVDMLRRengKLRRERNLLQQSWEDMKRLRE---EDQKEIG 280
Cdd:pfam13851    1 ELMKNHEKAFNEIKN------YYNDITRNNLELIKSLKEEIAELKK---KEERNEKLMSEIQQENKRLTEplqKAQEEVE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  281 DLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEkvamhnsdlsrLEQlgEENQRLQKQTEML--TQQ 358
Cdd:pfam13851   72 ELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEK-----------VER--ERDELYDKFEAAIqdVQQ 138

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039746878  359 RdtaIQLQHQcaLSLRRFETIHHELSKATAQ 389
Cdd:pfam13851  139 K---TGLKNL--LLEKKLQALGETLEKKEAQ 164
 
Name Accession Description Interval E-value
PDZ1_DLG5-like cd06764
PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 620-714 2.20e-59

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: 198.78  E-value: 2.20e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  620 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 699
Cdd:cd06764      1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                           90
                   ....*....|....*
gi 1039746878  700 LLNGEGAINMVVRRR 714
Cdd:cd06764     81 VLNGGGVINMVVRRR 95
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1356-1437 2.74e-48

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: 166.73  E-value: 2.74e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1356 EEPRHVKVQKGSEPLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1435
Cdd:cd06767      1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                   ..
gi 1039746878 1436 QY 1437
Cdd:cd06767     81 QY 82
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1512-1592 1.50e-47

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: 164.48  E-value: 1.50e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1512 DPRIVFIKKSQLDLGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLKV 1591
Cdd:cd06766      1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                   .
gi 1039746878 1592 Q 1592
Cdd:cd06766     81 Q 81
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 726-807 2.70e-41

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: 146.72  E-value: 2.70e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  726 HINLSGQKgsrpqDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 805
Cdd:cd06765      1 HINLSGQK-----DSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKV 75


                   ..
gi 1039746878  806 FP 807
Cdd:cd06765     76 FP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1744-1920 1.35e-40

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 148.21  E-value: 1.35e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1744 QKVDCTSLRPVLLLG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1820
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1821 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSAKHIKEQRDPvylRDKVTQRHSKEQFETAQKIDQEYsRYFTGVV 1900
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 1039746878  1901 QGGALSSICTQILAMVSQEQ 1920
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1610-1672 3.04e-35

Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein that is located at sites of cell-cell contact and is involved in the maintenance of cell shape and polarity. Mutations in the DLG5 gene are associated with Crohn's disease (CD) and inflammatory bowel disease (IBD). DLG5 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG5 contains 4 PDZ domains as well as an N-terminal domain of unknown function. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212794  Cd Length: 63  Bit Score: 128.61  E-value: 3.04e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878 1610 YIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1672
Cdd:cd11860      1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
dbPDZ_assoc pfam16610
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1437-1512 7.06e-31

Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote Dlg5, Disks large homolog 5, proteins, lying between the second pair of PDZ domains. The sequence is natively unstructured but may just be long extensions of the PDZs on these sequences in this position. The function is not known.


Pssm-ID: 465197  Cd Length: 81  Bit Score: 116.92  E-value: 7.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1437 YNPHIHQLNSHSRSSSHLDPAATpHSTLQGSSAGTPEHPSVIDPLMEQDEGPGTPPAKQSASST------RSVGDTTKKT 1510
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSN-HSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTTPATsphnsfRMPGDANKRV 79


                   ..
gi 1039746878 1511 PD 1512
Cdd:pfam16610   80 PE 81
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 129-213 6.23e-29

Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of this family regulate synaptic activity.


Pssm-ID: 461445  Cd Length: 85  Bit Score: 111.58  E-value: 6.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  129 KAPSPPPLLTEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 208
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 1039746878  209 HTNAL 213
Cdd:pfam04822   81 ISEAL 85
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1357-1439 7.58e-19

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: 82.81  E-value: 7.58e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1357 EPRHVKVQKGSEPLGISIVSG--EKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....*
gi 1039746878  1435 AQYNP 1439
Cdd:smart00228   81 VLRGG 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 338-641 2.93e-16

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 85.49  E-value: 2.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  338 LEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQN----KDLQWEMELLQSELTELRSKqvk 413
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskelTELEAEIEELEERLEEAEEE--- 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  414 tAKESEKYKEERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAASEEMEALRQIKDTVTM 486
Cdd:TIGR02168  777 -LAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  487 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 566
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  567 DTRKQKNDVSRELKELnscvhrEQMECQLEKEARFRQ---LMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 641
Cdd:TIGR02168  919 ELREKLAQLELRLEGL------EVRIDNLQERLSEEYsltLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
Guanylate_kin pfam00625
Guanylate kinase;
1750-1919 2.60e-15

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 75.88  E-value: 2.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1750 SLRPVLLLGPLL---DVVKEMLVNEAPGKFCRC---------PLEVMK-----ASQQAIERGVKDCLFVDYKRRSGHFDV 1812
Cdd:pfam00625    1 SRRPVVLSGPSGvgkSHIKKALLSEYPDKFGYSvphttrpprKGEVDGkdyyfVSKEEMERDISANEFLEYAQFSGNMYG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1813 TTVASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSakhIKEQRDPVYLRDKVTQRHSKEQFETAQKIDQEY 1892
Cdd:pfam00625   81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPS---LKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY 157

                          170       180
                   ....*....|....*....|....*..
gi 1039746878 1893 SryFTGVVQGGALSSICTQILAMVSQE 1919
Cdd:pfam00625  158 E--FDVIIVNDDLEEAYKKLKEALEAE 182
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 179-635 1.77e-12

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 72.83  E-value: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  179 RPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAK---ETDFYHTLHSRLLSDQTQLKDDvdmLRRENGKLR 255
Cdd:pfam05483   78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKaiqELQFENEKVSLKLEEEIQENKD---LIKENNATR 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  256 RERNLLQQ----SWEDMKRL---REEDQKEIGDLRAQQQQVLkhNGSSEILNKLYDTAMDKLEVVKKDYDA---LRKRYS 325
Cdd:pfam05483  155 HLCNLLKEtcarSAEKTKKYeyeREETRQVYMDLNNNIEKMI--LAFEELRVQAENARLEMHFKLKEDHEKiqhLEEEYK 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  326 EKVAMHNSDLSRLE-QLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMEL---LQ 401
Cdd:pfam05483  233 KEINDKEKQVSLLLiQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmsTQ 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  402 SELTELRSKQVKT----AKESEKYKEERDAVYSEYKLIMSERDQVISELDKL----QTEVELAESKLKSSTSEKKAASEE 473
Cdd:pfam05483  313 KALEEDLQIATKTicqlTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSE 392

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  474 MEALRQIKDtvtmdagraNKEVEIlrkqckalcQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDR 553
Cdd:pfam05483  393 LEEMTKFKN---------NKEVEL---------EELKKIL--------------AEDEKLLDEKKQFEKIAEELKGKEQE 440

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  554 AVSELAEALRSLDDTRKQ----KNDVSRELKELnscvhrEQMECQLEKEA-RFRQLMAHSSHDSaIDTDSMEWETE--VV 626
Cdd:pfam05483  441 LIFLLQAREKEIHDLEIQltaiKTSEEHYLKEV------EDLKTELEKEKlKNIELTAHCDKLL-LENKELTQEASdmTL 513


                   ....*....
gi 1039746878  627 EFERETEDI 635
Cdd:pfam05483  514 ELKKHQEDI 522
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
147-584 3.99e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 71.61  E-value: 3.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  147 ENLSIQLRLMTRERNELRKRLAFATHGATFDkrpyhrlNPDYERLKIQcvraMSDLQslqnqhtnalKRCEEVAKETDFY 226
Cdd:PRK02224   275 EELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEAR----REELE----------DRDEELRDRLEEC 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  227 HTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILnklYDTA 306
Cdd:PRK02224   334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD---LGNA 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  307 MDKLEVVKKDYDALRKRYSEKVAmhnsDLSRLEQLGEENQRLQKQTEMLTQQRDTAiQLQHQCALSLRRfetihHELSKA 386
Cdd:PRK02224   411 EDFLEELREERDELREREAELEA----TLRTARERVEEAEALLEAGKCPECGQPVE-GSPHVETIEEDR-----ERVEEL 480

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  387 TAQNKDLQWEMELLQSELTELrSKQVKTAKESEKYKEERDAV---YSEYKLIMSERDQVISEL----DKLQTEVELAESK 459
Cdd:PRK02224   481 EAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELreraAELEAEAEEKREA 559

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  460 LKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILrkqckALCQELKEALQEadVAKCRRDWAF---QERDKIVAE 536
Cdd:PRK02224   560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-----AAIADAEDEIER--LREKREALAElndERRERLAEK 632

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  537 RDSIRTLCDNL--------RRERDRAVSELAEALRSLDDTRKQKND-------VSRELKELNS 584
Cdd:PRK02224   633 RERKRELEAEFdearieeaREDKERAEEYLEQVEEKLDELREERDDlqaeigaVENELEELEE 695
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 741-803 6.35e-12

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: 63.17  E-value: 6.35e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878   741 GISL------ENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:smart00228   15 GFSLvggkdeGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1513-1594 1.01e-11

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: 62.40  E-value: 1.01e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1513 PRIVFIKKSQLDLGVHLCGG--NLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLK 1590
Cdd:smart00228    2 PRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....
gi 1039746878  1591 VQYR 1594
Cdd:smart00228   81 VLRG 84
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
231-510 3.05e-11

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 66.47  E-value: 3.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  231 SRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDM-------KRLREEDQKEIGDLRAQQQQVLkhngssEILNKLY 303
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELreeaqelREKRDELNEKVKELKEERDELN------EKLNELR 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  304 DTA------MDKLEVVKKDYDALRKRYsekvamhnsdlsrlEQLgEENQrlqkQTEMLTQQRDTAIQLQhqcalsLRRFE 377
Cdd:COG1340     92 EELdelrkeLAELNKAGGSIDKLRKEI--------------ERL-EWRQ----QTEVLSPEEEKELVEK------IKELE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  378 TIHHELSKATAQNKDLQW---EMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVE 454
Cdd:COG1340    147 KELEKAKKALEKNEKLKElraELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  455 LAESKLKSSTSEKKAASEEMEALRQIKdtvtmDAGRANKEVEILRKQCKALCQELK 510
Cdd:COG1340    227 ELHEEIIELQKELRELRKELKKLRKKQ-----RALKREKEKEELEEKAEEIFEKLK 277
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1366-1436 1.31e-10

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 59.22  E-value: 1.31e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1366 GSEPLGISIVSGEKG---GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1436
Cdd:pfam00595    8 GRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 622-715 3.27e-09

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: 55.46  E-value: 3.27e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878   622 ETEVVEFERETEDidlkaLGFDMAEGVNEpcfpgDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 700
Cdd:smart00228    1 EPRLVELEKGGGG-----LGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                            90
                    ....*....|....*
gi 1039746878   701 LNGEGAINMVVRRRK 715
Cdd:smart00228   71 KKAGGKVTLTVLRGG 85
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1607-1669 5.65e-09

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 53.70  E-value: 5.65e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  1607 DSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGvfgsWMAWQLDENaqkiQRGQIPSKYV 1669
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG----WWKGRLGRG----KEGLFPSNYV 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-485 6.60e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 6.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  147 ENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETdfy 226
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL--- 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  227 htlhSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQvlkhngsseiLNKLYDTA 306
Cdd:TIGR02168  757 ----TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------LNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  307 MDKLEVVKKDYDALRKRY----------SEKVAMHNSDLSRLEQLGEEnqrLQKQTEMLTQQRDtaiQLQHQCALSLRRF 376
Cdd:TIGR02168  823 RERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEE---LESELEALLNERA---SLEEALALLRSEL 896

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  377 ETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYS-EYKLIMSERDQVISELDKLQTEVEL 455
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKR 976

                          330       340       350
                   ....*....|....*....|....*....|
gi 1039746878  456 AESKLKSSTSEKKAASEEMEALRQIKDTVT 485
Cdd:TIGR02168  977 LENKIKELGPVNLAAIEEYEELKERYDFLT 1006
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 734-803 3.17e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 49.59  E-value: 3.17e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  734 GSRPQDSGISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:pfam00595   13 GFSLKGGSDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 741-792 4.59e-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: 54.11  E-value: 4.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  741 GISL---ENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 792
Cdd:COG0793     63 GAELgeeDGKVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLLR 116
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
158-428 9.95e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 9.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  158 RERNELRKRLAfaTHGATF--DKRPYH-RLnpdYERLKIQCVRAMSDL---QSLQN---------QH----TNALKRCEE 218
Cdd:COG4913    155 FDIRALKARLK--KQGVEFfdSFSAYLaRL---RRRLGIGSEKALRLLhktQSFKPigdlddfvrEYmleePDTFEAADA 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  219 VAKETDFYHTLHSRLLSDQTQlkddVDMLRRengkLRRERNLLQQSWEDMKRLRE--------EDQKEIGDLRAQQQQvl 290
Cdd:COG4913    230 LVEHFDDLERAHEALEDAREQ----IELLEP----IRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAELEE-- 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  291 khngsseiLNKLYDTAMDKLEVVKKDYDALRKRYSE-KVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRD----TAIQL 365
Cdd:COG4913    300 --------LRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRArleaLLAAL 371

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  366 QHQCALSLRRFETIHHELSKATAQNKDLQwemELLQSELTELRSKQVKTAKESEKYKEERDAV 428
Cdd:COG4913    372 GLPLPASAEEFAALRAEAAALLEALEEEL---EALEEALAEAEAALRDLRRELRELEAEIASL 431
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1514-1592 1.02e-05

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 45.35  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1514 RIVFIKKSQLDLGVHLCGGN---LHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLK 1590
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79


                   ..
gi 1039746878 1591 VQ 1592
Cdd:pfam00595   80 IL 81
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 640-712 4.18e-05

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 43.81  E-value: 4.18e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  640 LGFDMAEGVNEpcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 712
Cdd:pfam00595   12 LGFSLKGGSDQ----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 417-589 5.25e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 46.58  E-value: 5.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  417 ESEKYKEERDAVySEYKLIMSERDQVISELDKLQTEV-----ELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRA 491
Cdd:cd07596      2 EDQEFEEAKDYI-LKLEEQLKKLSKQAQRLVKRRRELgsalgEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  492 NKEVeilRKQCKALCQELKEALQEADVAKCrrdwAFQERDKIVAERDSIRTLCDNLRRERDRAVS-------ELAEALRS 564
Cdd:cd07596     81 EAQA---NQELVKLLEPLKEYLRYCQAVKE----TLDDRADALLTLQSLKKDLASKKAQLEKLKAapgikpaKVEELEEE 153

                          170       180
                   ....*....|....*....|....*
gi 1039746878  565 LDDTRKQKNDVSRELKELNSCVHRE 589
Cdd:cd07596    154 LEEAESALEEARKRYEEISERLKEE 178
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1370-1422 4.00e-04

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


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 44.37  E-value: 4.00e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1370 LGISIVS-----------GEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1422
Cdd:COG0265    180 LGVTIQPvtpelaealglPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSARDLQRLL 243
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 204-389 6.89e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 6.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  204 SLQNQHTNALKRCEEvaketdFYHTLHSRLLSDQTQLKDDVDMLRRengKLRRERNLLQQSWEDMKRLRE---EDQKEIG 280
Cdd:pfam13851    1 ELMKNHEKAFNEIKN------YYNDITRNNLELIKSLKEEIAELKK---KEERNEKLMSEIQQENKRLTEplqKAQEEVE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  281 DLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEkvamhnsdlsrLEQlgEENQRLQKQTEML--TQQ 358
Cdd:pfam13851   72 ELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEK-----------VER--ERDELYDKFEAAIqdVQQ 138

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039746878  359 RdtaIQLQHQcaLSLRRFETIHHELSKATAQ 389
Cdd:pfam13851  139 K---TGLKNL--LLEKKLQALGETLEKKEAQ 164
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
137-388 1.37e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  137 LTEQQANDTVENLSIQLRLMTRERNELRKRLAFAThgatfdKRPYHRLNPDYERLKiQCVRAMSDLQSLQNQHtnALKRC 216
Cdd:COG4717    298 ASLGKEAEELQALPALEELEEEELEELLAALGLPP------DLSPEELLELLDRIE-ELQELLREAEELEEEL--QLEEL 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  217 EE----------VAKETDFYHTL--HSRLLSDQTQLKDDVDMLRRENG------------KLRRERNLLQQSWEDMKRLR 272
Cdd:COG4717    369 EQeiaallaeagVEDEEELRAALeqAEEYQELKEELEELEEQLEELLGeleellealdeeELEEELEELEEELEELEEEL 448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  273 EEDQKEIGDLRAQQQQvLKHNGSSEILNKLYDTAMDKLEVVKKDYDALrkRYSEKVAMHNSDLSRLEQLGEENQRLQKQT 352
Cdd:COG4717    449 EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAAL--KLALELLEEAREEYREERLPPVLERASEYF 525

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1039746878  353 EMLTQQRDTAIQLQHQCALSLRRFETIH---HELSKATA 388
Cdd:COG4717    526 SRLTDGRYRLIRIDEDLSLKVDTEDGRTrpvEELSRGTR 564
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1535-1602 1.53e-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: 42.44  E-value: 1.53e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1535 HGVFVAEVEDDSPA-KGpdGLVPGDLILEYGSLDMRSrtVEDV--YVEMLKPKDSLRLKVqYRHEEFTRVK 1602
Cdd:COG0265    201 EGVLVARVEPGSPAaKA--GLRPGDVILAVDGKPVTS--ARDLqrLLASLKPGDTVTLTV-LRGGKELTVT 266
mukB PRK04863
chromosome partition protein MukB;
147-492 6.36e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 6.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  147 ENLSIQLRlmtRERNELRKRLAfathGATFDKRPYHRLNPDYERLKIQCVR---------AMSDLQSLQNQHTNALKRCE 217
Cdd:PRK04863   785 EKRIEQLR---AEREELAERYA----TLSFDVQKLQRLHQAFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHE 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  218 EVaketdfyhtlHSRLLSDQTQLKDDVDMLRrengKLRRERNLLqqswedmkrLREEDQKEIGDLRAQQQQ-------VL 290
Cdd:PRK04863   858 SQ----------EQQQRSQLEQAKEGLSALN----RLLPRLNLL---------ADETLADRVEEIREQLDEaeeakrfVQ 914

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  291 KHNGSSEILNKLYDTamdkLEVVKKDYDALRKRYSE------KVAMHNSDLSRLEQ-------------LGEE---NQRL 348
Cdd:PRK04863   915 QHGNALAQLEPIVSV----LQSDPEQFEQLKQDYQQaqqtqrDAKQQAFALTEVVQrrahfsyedaaemLAKNsdlNEKL 990

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  349 QKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHEL-SKATAQNKDLQwemELLQsELTELRSKQvkTAKESEKYKEERDA 427
Cdd:PRK04863   991 RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLkSSYDAKRQMLQ---ELKQ-ELQDLGVPA--DSGAEERARARRDE 1064

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  428 VYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVtMDAGRAN 492
Cdd:PRK04863  1065 LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDN 1128
 
Name Accession Description Interval E-value
PDZ1_DLG5-like cd06764
PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 620-714 2.20e-59

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: 198.78  E-value: 2.20e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  620 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 699
Cdd:cd06764      1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                           90
                   ....*....|....*
gi 1039746878  700 LLNGEGAINMVVRRR 714
Cdd:cd06764     81 VLNGGGVINMVVRRR 95
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1356-1437 2.74e-48

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: 166.73  E-value: 2.74e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1356 EEPRHVKVQKGSEPLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1435
Cdd:cd06767      1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                   ..
gi 1039746878 1436 QY 1437
Cdd:cd06767     81 QY 82
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1512-1592 1.50e-47

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: 164.48  E-value: 1.50e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1512 DPRIVFIKKSQLDLGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLKV 1591
Cdd:cd06766      1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                   .
gi 1039746878 1592 Q 1592
Cdd:cd06766     81 Q 81
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 726-807 2.70e-41

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: 146.72  E-value: 2.70e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  726 HINLSGQKgsrpqDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 805
Cdd:cd06765      1 HINLSGQK-----DSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKV 75


                   ..
gi 1039746878  806 FP 807
Cdd:cd06765     76 FP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1744-1920 1.35e-40

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 148.21  E-value: 1.35e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1744 QKVDCTSLRPVLLLG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1820
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1821 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSAKHIKEQRDPvylRDKVTQRHSKEQFETAQKIDQEYsRYFTGVV 1900
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 1039746878  1901 QGGALSSICTQILAMVSQEQ 1920
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1610-1672 3.04e-35

Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein that is located at sites of cell-cell contact and is involved in the maintenance of cell shape and polarity. Mutations in the DLG5 gene are associated with Crohn's disease (CD) and inflammatory bowel disease (IBD). DLG5 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG5 contains 4 PDZ domains as well as an N-terminal domain of unknown function. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212794  Cd Length: 63  Bit Score: 128.61  E-value: 3.04e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878 1610 YIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1672
Cdd:cd11860      1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
dbPDZ_assoc pfam16610
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1437-1512 7.06e-31

Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote Dlg5, Disks large homolog 5, proteins, lying between the second pair of PDZ domains. The sequence is natively unstructured but may just be long extensions of the PDZs on these sequences in this position. The function is not known.


Pssm-ID: 465197  Cd Length: 81  Bit Score: 116.92  E-value: 7.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1437 YNPHIHQLNSHSRSSSHLDPAATpHSTLQGSSAGTPEHPSVIDPLMEQDEGPGTPPAKQSASST------RSVGDTTKKT 1510
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSN-HSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTTPATsphnsfRMPGDANKRV 79


                   ..
gi 1039746878 1511 PD 1512
Cdd:pfam16610   80 PE 81
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 129-213 6.23e-29

Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of this family regulate synaptic activity.


Pssm-ID: 461445  Cd Length: 85  Bit Score: 111.58  E-value: 6.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  129 KAPSPPPLLTEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 208
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 1039746878  209 HTNAL 213
Cdd:pfam04822   81 ISEAL 85
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1357-1439 7.58e-19

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: 82.81  E-value: 7.58e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1357 EPRHVKVQKGSEPLGISIVSG--EKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....*
gi 1039746878  1435 AQYNP 1439
Cdd:smart00228   81 VLRGG 85
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1357-1439 8.52e-18

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: 80.09  E-value: 8.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1357 EPRHVKVQKGSEPLGISIVSGEKG-GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:cd06795      1 EPRKIVLHKGSTGLGFNIVGGEDGeGIFISFILAGGPADLSGeLRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTII 80


                   ....*
gi 1039746878 1435 AQYNP 1439
Cdd:cd06795     81 AQYKP 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 338-641 2.93e-16

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 85.49  E-value: 2.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  338 LEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQN----KDLQWEMELLQSELTELRSKqvk 413
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskelTELEAEIEELEERLEEAEEE--- 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  414 tAKESEKYKEERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAASEEMEALRQIKDTVTM 486
Cdd:TIGR02168  777 -LAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  487 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 566
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  567 DTRKQKNDVSRELKELnscvhrEQMECQLEKEARFRQ---LMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 641
Cdd:TIGR02168  919 ELREKLAQLELRLEGL------EVRIDNLQERLSEEYsltLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1360-1434 4.82e-16

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: 74.50  E-value: 4.82e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1360 HVKVQKGS-EPLGISIVSGE--KGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:cd00136      1 TVTLEKDPgGGLGFSIRGGKdgGGGIFVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLT 79
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 633-714 8.95e-16

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: 74.27  E-value: 8.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  633 EDIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGA 706
Cdd:cd06723      2 EEITLergnSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAaaDGRLRVNDIILRVNDVDVRNVTHSVAVEALKEAGSI 81


                   ....*...
gi 1039746878  707 INMVVRRR 714
Cdd:cd06723     82 VRLYVKRR 89
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1357-1436 1.14e-15

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: 73.58  E-value: 1.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1357 EPRHVKVQKGSEPLGISIVSGEKGGVYVSKVTLGSIAHQA-GLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1435
Cdd:cd06766      1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPdGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                   .
gi 1039746878 1436 Q 1436
Cdd:cd06766     81 Q 81
Guanylate_kin pfam00625
Guanylate kinase;
1750-1919 2.60e-15

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 75.88  E-value: 2.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1750 SLRPVLLLGPLL---DVVKEMLVNEAPGKFCRC---------PLEVMK-----ASQQAIERGVKDCLFVDYKRRSGHFDV 1812
Cdd:pfam00625    1 SRRPVVLSGPSGvgkSHIKKALLSEYPDKFGYSvphttrpprKGEVDGkdyyfVSKEEMERDISANEFLEYAQFSGNMYG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1813 TTVASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSakhIKEQRDPVYLRDKVTQRHSKEQFETAQKIDQEY 1892
Cdd:pfam00625   81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPS---LKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY 157

                          170       180
                   ....*....|....*....|....*..
gi 1039746878 1893 SryFTGVVQGGALSSICTQILAMVSQE 1919
Cdd:pfam00625  158 E--FDVIIVNDDLEEAYKKLKEALEAE 182
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 707-800 3.13e-15

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: 72.19  E-value: 3.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  707 INMVVRRRKSLGgkvvtplhINLSGqkgsrpqdsGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE 786
Cdd:cd00136      2 VTLEKDPGGGLG--------FSIRG---------GKDGGGGIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEE 64

                           90
                   ....*....|....
gi 1039746878  787 CESLLRSCQDSLTL 800
Cdd:cd00136     65 AVELLKSAGGEVTL 78
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 625-712 7.25e-15

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: 71.42  E-value: 7.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  625 VVEFERETEdidlKALGFDMAEGVNepcfpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd00136      1 TVTLEKDPG----GGLGFSIRGGKD-----GGGGIFVSRVEPGGPAarDGRLRVGDRILEVNGVSLEGLTHEEAVELLKS 71

                           90
                   ....*....|
gi 1039746878  703 GEGAINMVVR 712
Cdd:cd00136     72 AGGEVTLTVR 81
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 244-578 7.48e-15

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 80.88  E-value: 7.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  244 VDMLRRENGKLRRERNLLQQSWEDMKRLREEDQ----KEIGDLRAQQQQVLKhngssEIlnklyDTAMDKLEVVKKDYDA 319
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAERYQALLKEKREYEGyellKEKEALERQKEAIER-----QL-----ASLEEELEKLTEEISE 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  320 LRKRYSEKVAMHNSDLSRLEQLGEENQ-RLQKQTEMLTQQRDtaiQLQHQCALSLRRFEtihhelsKATAQNKDLQWEME 398
Cdd:TIGR02169  263 LEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIA---SLERSIAEKERELE-------DAEERLAKLEAEID 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  399 LLQSELTELRskqvktaKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALR 478
Cdd:TIGR02169  333 KLLAEIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  479 QIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSEL 558
Cdd:TIGR02169  406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485

                          330       340
                   ....*....|....*....|
gi 1039746878  559 AEALRSLDDTRKQKNDVSRE 578
Cdd:TIGR02169  486 SKLQRELAEAEAQARASEER 505
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1366-1433 3.20e-14

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: 69.66  E-value: 3.20e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1366 GSEPLGISIVSG--EKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITI 1433
Cdd:cd06738     11 GTRGLGCSISSGptQKPGIFISNVKPGSLAEEVGLEVGDQIVEVNGTSFTNVDHKEAVMAL-KSSRHLTI 79
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 183-550 5.01e-14

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 78.19  E-value: 5.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  183 RLNPDYERLKIQCVRAMSDLQSLQNqHTNALKRCEEVAKETdfyhtlHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQ 262
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEN-RLDELSQELSDASRK------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  263 QSWEDMKRLREEDQKEIGDLRAQQQQVlkhngsSEILNKLYDT-AMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQL 341
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKL------EEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  342 GEENQRLQKQTEMLTQQRDtaiqlqhqcALSLRRfETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKY 421
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRI---------DLKEQI-KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  422 KEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDtvtmdagrankeveiLRKQ 501
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED---------------VQAE 959

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  502 CKALCQELKE-------ALQEADVAKCRRDWAFQERDKIVAERDSIRTL---CDNLRRE 550
Cdd:TIGR02169  960 LQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERieeYEKKKRE 1018
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
 1610-1667 1.51e-13

Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212793  Cd Length: 62  Bit Score: 66.93  E-value: 1.51e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1610 YIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSK 1667
Cdd:cd11859      1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGTVGSWQAVRVGRNHQELERGVIPNK 58
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 297-609 2.34e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 2.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  297 EILNKLYDTA--MDKLEVV----KKDYDALRK------RYSE-KVAMHNSDLS----RLEQLGEENQRLQKQTEMLTQQR 359
Cdd:TIGR02168  176 ETERKLERTRenLDRLEDIlnelERQLKSLERqaekaeRYKElKAELRELELAllvlRLEELREELEELQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  360 DTAIQLQHQCALSLRRFETIHHELSKataqnkdlqwEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSER 439
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEE----------EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  440 DQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIK---------------------DTVTMDAGRANKEVEIL 498
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrleeleeqletlrskvAQLELQIASLNNEIERL 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  499 RKQCKALCQELKEALQEadVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRE 578
Cdd:TIGR02168  406 EARLERLEDRRERLQQE--IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1039746878  579 LKELNSCVHR-EQMECQLEKEARF-RQLMAHSS 609
Cdd:TIGR02168  484 LAQLQARLDSlERLQENLEGFSEGvKALLKNQS 516
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 634-702 1.56e-12

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: 64.98  E-value: 1.56e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  634 DIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd06724      1 EIKLvkgpKGLGFSIAGGVGNQHIPGDNGIYVTKIIEGGAAqkDGRLQVGDKLLAVNDVSLEEVTHEEAVAALKN 75
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 179-635 1.77e-12

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 72.83  E-value: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  179 RPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAK---ETDFYHTLHSRLLSDQTQLKDDvdmLRRENGKLR 255
Cdd:pfam05483   78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKaiqELQFENEKVSLKLEEEIQENKD---LIKENNATR 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  256 RERNLLQQ----SWEDMKRL---REEDQKEIGDLRAQQQQVLkhNGSSEILNKLYDTAMDKLEVVKKDYDA---LRKRYS 325
Cdd:pfam05483  155 HLCNLLKEtcarSAEKTKKYeyeREETRQVYMDLNNNIEKMI--LAFEELRVQAENARLEMHFKLKEDHEKiqhLEEEYK 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  326 EKVAMHNSDLSRLE-QLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMEL---LQ 401
Cdd:pfam05483  233 KEINDKEKQVSLLLiQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmsTQ 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  402 SELTELRSKQVKT----AKESEKYKEERDAVYSEYKLIMSERDQVISELDKL----QTEVELAESKLKSSTSEKKAASEE 473
Cdd:pfam05483  313 KALEEDLQIATKTicqlTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSE 392

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  474 MEALRQIKDtvtmdagraNKEVEIlrkqckalcQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDR 553
Cdd:pfam05483  393 LEEMTKFKN---------NKEVEL---------EELKKIL--------------AEDEKLLDEKKQFEKIAEELKGKEQE 440

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  554 AVSELAEALRSLDDTRKQ----KNDVSRELKELnscvhrEQMECQLEKEA-RFRQLMAHSSHDSaIDTDSMEWETE--VV 626
Cdd:pfam05483  441 LIFLLQAREKEIHDLEIQltaiKTSEEHYLKEV------EDLKTELEKEKlKNIELTAHCDKLL-LENKELTQEASdmTL 513


                   ....*....
gi 1039746878  627 EFERETEDI 635
Cdd:pfam05483  514 ELKKHQEDI 522
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
147-584 3.99e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 71.61  E-value: 3.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  147 ENLSIQLRLMTRERNELRKRLAFATHGATFDkrpyhrlNPDYERLKIQcvraMSDLQslqnqhtnalKRCEEVAKETDFY 226
Cdd:PRK02224   275 EELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEAR----REELE----------DRDEELRDRLEEC 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  227 HTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILnklYDTA 306
Cdd:PRK02224   334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD---LGNA 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  307 MDKLEVVKKDYDALRKRYSEKVAmhnsDLSRLEQLGEENQRLQKQTEMLTQQRDTAiQLQHQCALSLRRfetihHELSKA 386
Cdd:PRK02224   411 EDFLEELREERDELREREAELEA----TLRTARERVEEAEALLEAGKCPECGQPVE-GSPHVETIEEDR-----ERVEEL 480

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  387 TAQNKDLQWEMELLQSELTELrSKQVKTAKESEKYKEERDAV---YSEYKLIMSERDQVISEL----DKLQTEVELAESK 459
Cdd:PRK02224   481 EAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELreraAELEAEAEEKREA 559

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  460 LKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILrkqckALCQELKEALQEadVAKCRRDWAF---QERDKIVAE 536
Cdd:PRK02224   560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-----AAIADAEDEIER--LREKREALAElndERRERLAEK 632

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  537 RDSIRTLCDNL--------RRERDRAVSELAEALRSLDDTRKQKND-------VSRELKELNS 584
Cdd:PRK02224   633 RERKRELEAEFdearieeaREDKERAEEYLEQVEEKLDELREERDDlqaeigaVENELEELEE 695
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 753-800 5.01e-12

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: 63.41  E-value: 5.01e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039746878  753 VVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06681     37 VRPGGPADREGTIKPGDRLLSVDGISLHGATHAEAMSILKQCGQEATL 84
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1361-1436 5.93e-12

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: 63.43  E-value: 5.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1361 VKVQKGSEPLGISIVSG----------EKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1430
Cdd:cd06702      3 IHLVKAGGPLGLSIVGGsdhsshpfgvDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPGQE 82


                   ....*.
gi 1039746878 1431 ITILAQ 1436
Cdd:cd06702     83 IKLLVR 88
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 741-803 6.35e-12

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: 63.17  E-value: 6.35e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878   741 GISL------ENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:smart00228   15 GFSLvggkdeGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 248-582 7.55e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.86  E-value: 7.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  248 RRENGKLRRERNL--LQQSWEDMKRLREEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDALRKRyS 325
Cdd:TIGR02168  667 KTNSSILERRREIeeLEEKIEELEEKIAELEKALAELRKELEELEE---ELEQLRKELEELSRQISALRKDLARLEAE-V 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  326 EKVAmhnsdlSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCalsLRRFETIHHELSKATAQNKDLQWEMELLQSELT 405
Cdd:TIGR02168  743 EQLE------ERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  406 ELRSKQvkTAKESEKYKEERDAVYSEYKLIMSE------RDQVIS---ELDKLQTEVELAESKLKSSTSEKKAASEEMEA 476
Cdd:TIGR02168  814 LLNEEA--ANLRERLESLERRIAATERRLEDLEeqieelSEDIESlaaEIEELEELIEELESELEALLNERASLEEALAL 891

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  477 LRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDwAFQER----------------DKIVAERDSI 540
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-NLQERlseeysltleeaealeNKIEDDEEEA 970

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1039746878  541 RTLCDNLRRERDR-------AVSELAEALRSLDDTRKQKNDVSRELKEL 582
Cdd:TIGR02168  971 RRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1513-1594 1.01e-11

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: 62.40  E-value: 1.01e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  1513 PRIVFIKKSQLDLGVHLCGG--NLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLK 1590
Cdd:smart00228    2 PRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....
gi 1039746878  1591 VQYR 1594
Cdd:smart00228   81 VLRG 84
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
231-636 1.05e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 70.48  E-value: 1.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  231 SRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSE---ILNKLYDTAM 307
Cdd:PRK03918   227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiKLSEFYEEYL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  308 DKLEVVKK---DYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEmltqqrdtaiqlqhqcalslrRFETIHHELS 384
Cdd:PRK03918   307 DELREIEKrlsRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE---------------------ELEERHELYE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  385 KAtaqnKDLQWEMELLQSELTELR-SKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESK---- 459
Cdd:PRK03918   366 EA----KAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvc 441

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  460 ------------LKSSTSEKKAASEEM----EALRQIKDTVTMDAGRANKEVEILR-KQCKALCQELKEALQEADVAKCR 522
Cdd:PRK03918   442 grelteehrkelLEEYTAELKRIEKELkeieEKERKLRKELRELEKVLKKESELIKlKELAEQLKELEEKLKKYNLEELE 521

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  523 RDWAFQE--RDKIVAERDSIRTLCDNLRRERDrAVSELAEALRSLDDTRKQKNDVSRELKELNscvhreqMECQLEKEAR 600
Cdd:PRK03918   522 KKAEEYEklKEKLIKLKGEIKSLKKELEKLEE-LKKKLAELEKKLDELEEELAELLKELEELG-------FESVEELEER 593

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1039746878  601 FRQLM-AHSSHDSAIDTDSmEWETEVVEFERETEDID 636
Cdd:PRK03918   594 LKELEpFYNEYLELKDAEK-ELEREEKELKKLEEELD 629
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 307-604 1.47e-11

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 70.10  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  307 MDKLEVVKKD---YDALRKR-----YSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDtaiQLQHQCALSLRRFET 378
Cdd:TIGR02169  200 LERLRREREKaerYQALLKEkreyeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEE 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  379 IHHELSKATAQnkdlqwEMELLQSELTELRSKQVKT-AKESEKYKEERDAVYSEYKLImSERDQVISELDKLQTEVELAE 457
Cdd:TIGR02169  277 LNKKIKDLGEE------EQLRVKEKIGELEAEIASLeRSIAEKERELEDAEERLAKLE-AEIDKLLAEIEELEREIEEER 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  458 SKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAER 537
Cdd:TIGR02169  350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  538 DSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRE---LKELNSCVHREQMECQLE---KEARFRQL 604
Cdd:TIGR02169  430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEEYDRVEKELSKLQRElaeAEAQARAS 502
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 197-541 2.75e-11

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 68.99  E-value: 2.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  197 RAMSDLQ-SLQNQHTNALKRCEEVAKetdfyhtLHSRL---LSDQTQLKDDVDMLRR---ENGKLRRER-------NLLQ 262
Cdd:pfam15921  496 RTVSDLTaSLQEKERAIEATNAEITK-------LRSRVdlkLQELQHLKNEGDHLRNvqtECEALKLQMaekdkviEILR 568

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  263 QSWEDMKRLREEDQKEIGDLRAQQQQVLKhngssEILNKLYDtaMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLG 342
Cdd:pfam15921  569 QQIENMTQLVGQHGRTAGAMQVEKAQLEK-----EINDRRLE--LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG 641

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  343 EENQRLQKQtemLTQQRDTAIQLQHQCALSLRRFeTIHHELSKATAQNKdlQWEMELLQSELT-ELRSKQVKTAKESEKY 421
Cdd:pfam15921  642 SERLRAVKD---IKQERDQLLNEVKTSRNELNSL-SEDYEVLKRNFRNK--SEEMETTTNKLKmQLKSAQSELEQTRNTL 715

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  422 KEERDAVYSEYKLIMSERDQVIS---ELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEIL 498
Cdd:pfam15921  716 KSMEGSDGHAMKVAMGMQKQITAkrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL 795

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1039746878  499 RKQCKalcqELKEALQEADVAKCRRDWAFQERDKIV--AERDSIR 541
Cdd:pfam15921  796 RSQER----RLKEKVANMEVALDKASLQFAECQDIIqrQEQESVR 836
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
231-510 3.05e-11

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 66.47  E-value: 3.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  231 SRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDM-------KRLREEDQKEIGDLRAQQQQVLkhngssEILNKLY 303
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELreeaqelREKRDELNEKVKELKEERDELN------EKLNELR 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  304 DTA------MDKLEVVKKDYDALRKRYsekvamhnsdlsrlEQLgEENQrlqkQTEMLTQQRDTAIQLQhqcalsLRRFE 377
Cdd:COG1340     92 EELdelrkeLAELNKAGGSIDKLRKEI--------------ERL-EWRQ----QTEVLSPEEEKELVEK------IKELE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  378 TIHHELSKATAQNKDLQW---EMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVE 454
Cdd:COG1340    147 KELEKAKKALEKNEKLKElraELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  455 LAESKLKSSTSEKKAASEEMEALRQIKdtvtmDAGRANKEVEILRKQCKALCQELK 510
Cdd:COG1340    227 ELHEEIIELQKELRELRKELKKLRKKQ-----RALKREKEKEELEEKAEEIFEKLK 277
PDZ2_ZO1-like_ds cd06728
PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form ...
 733-804 3.33e-11

PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form domain-swapping dimers; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 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 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: 467210 [Multi-domain]  Cd Length: 79  Bit Score: 60.70  E-value: 3.33e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  733 KGSRPQDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 804
Cdd:cd06728      7 KSRKNDEYGLRLGSRIFVKEITPDSLAAKDGNLQEGDIILKINGTPVENLSLSEAKKLIEKSKDKLQLVVLR 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 248-516 5.31e-11

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 5.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  248 RRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQvlkhngsseiLNKLYDTAMDKLEVVKKDYDALRKRYSEk 327
Cdd:COG1196    224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE----------LEAELEELRLELEELELELEEAQAEEYE- 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  328 vamHNSDLSRLEqlgeenQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTEL 407
Cdd:COG1196    293 ---LLAELARLE------QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  408 RSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMD 487
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                          250       260
                   ....*....|....*....|....*....
gi 1039746878  488 AGRANKEVEILRKQCKALCQELKEALQEA 516
Cdd:COG1196    444 LEEAAEEEAELEEEEEALLELLAELLEEA 472
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 231-515 1.09e-10

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 66.97  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  231 SRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQ---QVLKHNgssEILNKLYDTam 307
Cdd:TIGR04523  338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdleSKIQNQ---EKLNQQKDE-- 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  308 dKLEVVKKDYDALRKRY---SEKVAMHNSDLSRLEqlgEENQRLQKQTEMLTQQRDtaiQLQHQCALSLRRFETIHH--- 381
Cdd:TIGR04523  413 -QIKKLQQEKELLEKEIerlKETIIKNNSEIKDLT---NQDSVKELIIKNLDNTRE---SLETQLKVLSRSINKIKQnle 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  382 -----------ELSKATAQNKDLQWEMELLQSELTELRSKQVK------------TAKESEKYKEERDAVYSEYKLIMSE 438
Cdd:TIGR04523  486 qkqkelkskekELKKLNEEKKELEEKVKDLTKKISSLKEKIEKlesekkekeskiSDLEDELNKDDFELKKENLEKEIDE 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  439 RDQVISEL----DKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALcQELKEALQ 514
Cdd:TIGR04523  566 KNKEIEELkqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI-KSKKNKLK 644


                   .
gi 1039746878  515 E 515
Cdd:TIGR04523  645 Q 645
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 633-702 1.18e-10

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: 59.61  E-value: 1.18e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  633 EDIDLK----ALGFDMAEGVNEPCFPGDCGIFVTKV-DKGSIA-DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd06709      1 EEITLKrgpsGLGFNIVGGTDQPYIPNDSGIYVAKIkEDGAAAiDGRLQEGDKILEINGQSLENLTHQDAVELFRN 76
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1366-1436 1.31e-10

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 59.22  E-value: 1.31e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1366 GSEPLGISIVSGEKG---GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1436
Cdd:pfam00595    8 GRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1357-1437 1.55e-10

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: 59.12  E-value: 1.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1357 EPRHVKVQKGSEpLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIG--QQCDTITIL 1434
Cdd:cd06729      1 DTRLVSFRKGGS-VGLRLAGGNDVGIFVAGVQEGSPAEKQGLQEGDQILKVNGVDFRNLTREEAVLFLLdlPKGEEVTIL 79


                   ...
gi 1039746878 1435 AQY 1437
Cdd:cd06729     80 AQS 82
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 747-802 1.78e-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: 59.15  E-value: 1.78e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  747 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 802
Cdd:cd06792     30 GIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVL 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
214-604 2.28e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.86  E-value: 2.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  214 KRCEEVAKETDFYHTLhSRLLSDQTQLKDDVDmlrRENGKLRRERNLLQQSWEDmkrlREEDQKEIGDLRAQQQQVLKHN 293
Cdd:PRK03918   283 KELKELKEKAEEYIKL-SEFYEEYLDELREIE---KRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRL 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  294 GSSEILNKLYDTAMDKLEVVKKdydaLRKRYSEKvamhnsdlsRLEQLGEENQRLQKQTEMLTQQRDTAIQlqhqcalSL 373
Cdd:PRK03918   355 EELEERHELYEEAKAKKEELER----LKKRLTGL---------TPEKLEKELEELEKAKEEIEEEISKITA-------RI 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  374 RRFETIHHELSKATAQNKDLQWEMELLQSELTE-----LRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDK 448
Cdd:PRK03918   415 GELKKEIKELKKAIEELKKAKGKCPVCGRELTEehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  449 LQTEVELA------ESKLKSSTSEK-KAASEEMEALRQIKDTVTMDAGRANKEVE---ILRKQCKALCQELKEALQE-AD 517
Cdd:PRK03918   495 LIKLKELAeqlkelEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEElAE 574

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  518 VAKCRRDWAF----------QERDKIVAERDSIRTLCDNLRR---ERDRAVSELAEALRSLDDTRKQKNDVSRELKELNS 584
Cdd:PRK03918   575 LLKELEELGFesveeleerlKELEPFYNEYLELKDAEKELEReekELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654

                          410       420
                   ....*....|....*....|
gi 1039746878  585 CVHREQMEcqlEKEARFRQL 604
Cdd:PRK03918   655 KYSEEEYE---ELREEYLEL 671
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 640-713 2.78e-10

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: 58.49  E-value: 2.78e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  640 LGFDMAEGVN---EPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 713
Cdd:cd06749     11 LGFSISGGIGsqgNPFRPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVNIEHGQAVSLLKSFQNTVDLVVER 87
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 735-800 2.95e-10

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: 58.56  E-value: 2.95e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  735 SRPQDSGI-----------SLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06694      8 KKDPQKGLgftivggensgSLDLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 306-638 3.60e-10

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 65.47  E-value: 3.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  306 AMDKLEVVKKDYDALRKRYSEKvamhnsdLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQhqcalsLRRFETIHHELSK 385
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEK-------RQQLERLRREREKAERYQALLKEKREYEGYEL------LKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  386 ATAQNKDLQWEMELLQSELTELrskqvktAKESEKYKEERDAVYSEYKLIMSERD-QVISELDKLQTEVELAESKLKsst 464
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIA--- 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  465 sekkaaseemEALRQIKDtvtMDAGRANKEVEILRKQCKAlcQELKEALQEADVakcrrdwafqERDKIVAERDSIRTLC 544
Cdd:TIGR02169  312 ----------EKERELED---AEERLAKLEAEIDKLLAEI--EELEREIEEERK----------RRDKLTEEYAELKEEL 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  545 DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELNSCVHREQMECQlEKEARFRQLMAhsshdsaidtDSMEWETE 624
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ-RLSEELADLNA----------AIAGIEAK 435

                          330
                   ....*....|....
gi 1039746878  625 VVEFERETEDIDLK 638
Cdd:TIGR02169  436 INELEEEKEDKALE 449
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 745-800 4.58e-10

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: 58.07  E-value: 4.58e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  745 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06690     29 SPGIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMDLIRTSGDKLRF 84
SH3_ZO-1 cd12026
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ...
 1607-1667 4.73e-10

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-1 plays an essential role in embryonic development. It regulates the assembly and dynamics of the cortical cytoskeleton at cell-cell junctions. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-1 is the largest of the three ZO proteins and contains an actin-binding region and domains of unknown function designated alpha and ZU5. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212959  Cd Length: 65  Bit Score: 57.01  E-value: 4.73e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1607 DSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSK 1667
Cdd:cd12026      1 DSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNK 61
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
239-646 5.58e-10

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.40  E-value: 5.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  239 QLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLreedQKEIGDLRAQQQQVLKHNGSSEILNKLyDTAMDKLEVVKKDYD 318
Cdd:COG4717     75 ELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELEELREELEKLEKLLQLLPLYQEL-EALEAELAELPERLE 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  319 ALRKRYSEKVAMHNsdlsRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCAlsLRRFETIHHELSKATAQNKDLQWEME 398
Cdd:COG4717    150 ELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELE 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  399 LLQSELTELRSKQVKTAKESEKYKEERDAV----------------------------------------YSEYKLIMSE 438
Cdd:COG4717    224 ELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKE 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  439 RDQV-----ISELDKLQTEVELAESKLKSSTSekkaASEEMEALRQIKDTVTMDAGRANKEVEIlrkQCKALCQELKEAL 513
Cdd:COG4717    304 AEELqalpaLEELEEEELEELLAALGLPPDLS----PEELLELLDRIEELQELLREAEELEEEL---QLEELEQEIAALL 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  514 QEADVAKcrrDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDT--RKQKNDVSRELKELnscvhREQM 591
Cdd:COG4717    377 AEAGVED---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEEL-----EEEL 448

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  592 ECQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAE 646
Cdd:COG4717    449 EELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 149-607 6.42e-10

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 63.76  E-value: 6.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  149 LSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQslqnqhtnalkrcEEVAketdfyht 228
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK-------------EELR-------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  229 lhsRLLSDQTQLKDDVDMLRRENGKLRRERN-LLQQSWEDMKRLREEDQkeigDLRAQQQQVLkhngsseilnkLYDTAM 307
Cdd:pfam07888   91 ---QSREKHEELEEKYKELSASSEELSEEKDaLLAQRAAHEARIRELEE----DIKTLTQRVL-----------ERETEL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  308 DKL-EVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCAlslrrfeTIHHELskA 386
Cdd:pfam07888  153 ERMkERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTIT-------TLTQKL--T 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  387 TAQNKDLqwEMELLQSELTELRSKQVKTAKESEKYKEERDAVyseykliMSERDQVISELDKL-----QTEVELAESKLK 461
Cdd:pfam07888  224 TAHRKEA--ENEALLEELRSLQERLNASERKVEGLGEELSSM-------AAQRDRTQAELHQArlqaaQLTLQLADASLA 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  462 ssTSEKKAA-SEEMEALRQikdtvtmdagRANKEVEILRKQCKALcQELKEALQEAdvakcrrdwafqerdkivaerdsi 540
Cdd:pfam07888  295 --LREGRARwAQERETLQQ----------SAEADKDRIEKLSAEL-QRLEERLQEE------------------------ 337

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  541 rtlcdnlRRERDRAVSELAealRSLDDTRKQKNDVSRELKELNSCV---HREQMECQLEKearfRQLMAH 607
Cdd:pfam07888  338 -------RMEREKLEVELG---REKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAEK----QELLEY 393
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 1359-1437 7.34e-10

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: 57.38  E-value: 7.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1359 RHVKVQKG-SEPLGISIVSGEKGGV--YVSKVTLGSIAHQ-AGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:cd06800      1 RKVLLSKEpHEGLGISITGGKEHGVpiLISEIHEGQPADRcGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITLE 80


                   ...
gi 1039746878 1435 AQY 1437
Cdd:cd06800     81 VVY 83
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 636-713 8.02e-10

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: 57.27  E-value: 8.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  636 DLKALGFDMAEGVNEPCF-PGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 712
Cdd:cd06703     10 DGKGLGFSIAGGKGSTPFrDGDEGIFISRITEGGAAdrDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITLVVE 89


                   .
gi 1039746878  713 R 713
Cdd:cd06703     90 R 90
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 239-646 9.71e-10

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 64.04  E-value: 9.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  239 QLKDDVDMLRRENGKLRRERNLLQQSWEDMK-RLREEDQKeigdlrAQQQQVLKHNGSSEILNklYDTAMDKLEVVKKDY 317
Cdd:pfam01576  135 KLEEDILLLEDQNSKLSKERKLLEERISEFTsNLAEEEEK------AKSLSKLKNKHEAMISD--LEERLKKEEKGRQEL 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  318 DALRKRYSEKVAMHNSDLSRLE-QLGEENQRLQKQTEML----------TQQRDTAI----QLQHQCALSLRRFETIHHE 382
Cdd:pfam01576  207 EKAKRKLEGESTDLQEQIAELQaQIAELRAQLAKKEEELqaalarleeeTAQKNNALkkirELEAQISELQEDLESERAA 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  383 LSKATAQNKDLQWEMELLQSEL----------TELRSKQVKTAKESEKYKEERDAVYSEYKLIMSER-DQVISELDKlqt 451
Cdd:pfam01576  287 RNKAEKQRRDLGEELEALKTELedtldttaaqQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKhTQALEELTE--- 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  452 evELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRAnkEVEILRKQCKALCQELKEALQEADVAKCRRdwafQER- 530
Cdd:pfam01576  364 --QLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ--DSEHKRKKLEGQLQELQARLSESERQRAEL----AEKl 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  531 DKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTR-------KQKNDVSRELKEL----NSCvhREQMECQLEKEA 599
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLSTRLRQLederNSL--QEQLEEEEEAKR 513

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039746878  600 RF-RQLMAHSSH--DSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAE 646
Cdd:pfam01576  514 NVeRQLSTLQAQlsDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 1359-1424 9.80e-10

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: 56.89  E-value: 9.80e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1359 RHVKVQKGS--EPLGISIVSG-EKG-GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06755      1 RTVTLTRPSreSPLHFSLLGGsEKGfGIFVSKVEKGSKAAEAGLKRGDQILEVNGQNFENITLKKALEIL 70
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 1361-1433 1.05e-09

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: 56.91  E-value: 1.05e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1361 VKVQKGSEPLGISIVSG-----EKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1433
Cdd:cd06789      6 VTLKKVGNGMGLSIVAAkgagqDKLGIYIKSVVKGGAADLDGrLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTL 84
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1514-1592 1.13e-09

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: 56.40  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1514 RIVFIKKSQLDLGVHLCGGNLH--GVFVAEVEDDSPAKgPDG-LVPGDLILEYGSLDMRSRTVEDVyVEMLK-PKDSLRL 1589
Cdd:cd00136      1 TVTLEKDPGGGLGFSIRGGKDGggGIFVSRVEPGGPAA-RDGrLRVGDRILEVNGVSLEGLTHEEA-VELLKsAGGEVTL 78


                   ...
gi 1039746878 1590 KVQ 1592
Cdd:cd00136     79 TVR 81
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 656-714 1.68e-09

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: 56.91  E-value: 1.68e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  656 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKAL-------LNGEGAINMVVRRR 714
Cdd:cd23059     36 DLGIFIKSIIHGGAAskDGRLRVNDQLIAVNGESLLGLTNSEAMETLrramsteGNIRGMIQLVVARR 103
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 1361-1434 2.14e-09

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: 56.07  E-value: 2.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1361 VKVQKGSEPLGISIVSG-----EKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:cd06792      5 VELSKKDGSLGISVTGGintsvRHGGIYVKSLVPGGAAEQDGrIQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLV 84
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 741-792 2.91e-09

PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467174 [Multi-domain]  Cd Length: 99  Bit Score: 56.20  E-value: 2.91e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  741 GISLENGVYAAAVV----------PGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLR 792
Cdd:cd06686     21 GIQLQGGVFATETLsspplisfiePDSPAERCGVLQVGDRVLSINGIPTEDRTLEEANQLLR 82
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 187-634 2.91e-09

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 62.50  E-value: 2.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  187 DYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAketdfyHTLHSRLLSDQTQLKDDVDMLRRENgklRRERNL---LQQ 263
Cdd:pfam01576  423 ESERQRAELAEKLSKLQSELESVSSLLNEAEGKN------IKLSKDVSSLESQLQDTQELLQEET---RQKLNLstrLRQ 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  264 SWEDMKRLREEDQKEIGDLRAQQQQVLKHNGS-SEILNKLYDTA--MDKLEVVKK----DYDALRKRYSEKVAMHnsdls 336
Cdd:pfam01576  494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQlSDMKKKLEEDAgtLEALEEGKKrlqrELEALTQQLEEKAAAY----- 568

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  337 rlEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDlqwEMELLQSELTELRSKQVKTAK 416
Cdd:pfam01576  569 --DKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAE---ERDRAEAEAREKETRALSLAR 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  417 ESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEV-ELAESK--LKSSTSEKKAASEEME-ALRQIKDT-----VTMD 487
Cdd:pfam01576  644 ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVhELERSKraLEQQVEEMKTQLEELEdELQATEDAklrleVNMQ 723

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  488 AGRANKEVEI-------------LRKQC---------------------KALCQELKEALQEADVAKCRRDWAFQERDKI 533
Cdd:pfam01576  724 ALKAQFERDLqardeqgeekrrqLVKQVreleaelederkqraqavaakKKLELDLKELEAQIDAANKGREEAVKQLKKL 803

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  534 VAE-RDSIRTLcDNLRRERDRAVSElaealrSLDDTRKQKNDVSR--ELKELNSCVHREQMECQLEKEARFRQLMAHSSH 610
Cdd:pfam01576  804 QAQmKDLQREL-EEARASRDEILAQ------SKESEKKLKNLEAEllQLQEDLAASERARRQAQQERDELADEIASGASG 876

                          490       500
                   ....*....|....*....|....
gi 1039746878  611 DSAIDTDSMEWETEVVEFERETED 634
Cdd:pfam01576  877 KSALQDEKRRLEARIAQLEEELEE 900
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 753-800 3.08e-09

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: 55.31  E-value: 3.08e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039746878  753 VVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06734     33 IIPGSPADRCGQLKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTL 80
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 215-604 3.22e-09

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 62.11  E-value: 3.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  215 RCEEVAKETDFYHTLHSRLLSDQTQLKDDVDmlrRENGKLRRERNLLQQSWEDMKRLREEDQKEigdLRAQQQQVLKHNG 294
Cdd:pfam01576  626 RAEAEAREKETRALSLARALEEALEAKEELE---RTNKQLRAEMEDLVSSKDDVGKNVHELERS---KRALEQQVEEMKT 699

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  295 SSEILNKLYDTAMD---KLEVvkkDYDALRkrysekvAMHNSDLSRLEQLGEENQR-LQKQT-EMLTQ------QRDTAI 363
Cdd:pfam01576  700 QLEELEDELQATEDaklRLEV---NMQALK-------AQFERDLQARDEQGEEKRRqLVKQVrELEAElederkQRAQAV 769

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  364 QLQHQCALSLRRFETIHHELSK----ATAQNKDLQWEMELLQSELTELRSKQ---VKTAKESEKYKE--ERDAVYSEYKL 434
Cdd:pfam01576  770 AAKKKLELDLKELEAQIDAANKgreeAVKQLKKLQAQMKDLQRELEEARASRdeiLAQSKESEKKLKnlEAELLQLQEDL 849

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  435 IMSER--DQVISELDKLQTEvelaeskLKSSTSEKKAASEEMealRQIKDTVTMdagrankeveilrkqckaLCQELKEA 512
Cdd:pfam01576  850 AASERarRQAQQERDELADE-------IASGASGKSALQDEK---RRLEARIAQ------------------LEEELEEE 901

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  513 LQEADVAKCRRDWAFQERDKIVAERDSIRTLC---DNLRRERDRAVSELAEALRSLDDTRKQKNDVSreLKELNSCVhrE 589
Cdd:pfam01576  902 QSNTELLNDRLRKSTLQVEQLTTELAAERSTSqksESARQQLERQNKELKAKLQEMEGTVKSKFKSS--IAALEAKI--A 977

                          410
                   ....*....|....*
gi 1039746878  590 QMECQLEKEARFRQL 604
Cdd:pfam01576  978 QLEEQLEQESRERQA 992
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 622-715 3.27e-09

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: 55.46  E-value: 3.27e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878   622 ETEVVEFERETEDidlkaLGFDMAEGVNEpcfpgDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 700
Cdd:smart00228    1 EPRLVELEKGGGG-----LGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                            90
                    ....*....|....*
gi 1039746878   701 LNGEGAINMVVRRRK 715
Cdd:smart00228   71 KKAGGKVTLTVLRGG 85
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1361-1424 3.59e-09

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: 55.35  E-value: 3.59e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878 1361 VKVQKGSePLGISIVSG-EKG-GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06741      6 LVVEDGQ-SLGLMIRGGaEYGlGIYVTGVDPGSVAENAGLKVGDQILEVNGRSFLDITHDEAVKIL 70
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1361-1420 4.32e-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: 55.13  E-value: 4.32e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878 1361 VKVQKGS-EPLGISIVSG-EKG-GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd10833      4 VTVEKSPdGSLGFSVRGGsEHGlGIFVSKVEEGSAAERAGLCVGDKITEVNGVSLENITMSSA 66
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1512-1593 5.47e-09

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: 54.50  E-value: 5.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1512 DPRIV-FIKKSqlDLGVHLCGGNLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDMRSRTVEDV--YVEMLKPKDSLR 1588
Cdd:cd06729      1 DTRLVsFRKGG--SVGLRLAGGNDVGIFVAGVQEGSPAEK-QGLQEGDQILKVNGVDFRNLTREEAvlFLLDLPKGEEVT 77


                   ....*
gi 1039746878 1589 LKVQY 1593
Cdd:cd06729     78 ILAQS 82
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1607-1669 5.65e-09

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 53.70  E-value: 5.65e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  1607 DSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGvfgsWMAWQLDENaqkiQRGQIPSKYV 1669
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG----WWKGRLGRG----KEGLFPSNYV 55
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1358-1439 6.39e-09

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: 54.75  E-value: 6.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1358 PRHVKVQKGSEPLGISIVSG--EKGGVYVSKVTLGSIA-HQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:cd06796      2 PRVVELPKTEEGLGFNVMGGkeQNSPIYISRIIPGGVAdRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLV 81


                   ....*
gi 1039746878 1435 AQYNP 1439
Cdd:cd06796     82 VRYTP 86
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
400-600 6.60e-09

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 59.54  E-value: 6.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  400 LQSELTELRSK------QVKTAKES-EKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKS---STSEKKA 469
Cdd:COG1340     34 LNEELKELAEKrdelnaQVKELREEaQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAElnkAGGSIDK 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  470 ASEEMEALRQIKDTVTMD-----------------AGRANKEVEI-------------LRKQCKALCQELKEALQEADVA 519
Cdd:COG1340    114 LRKEIERLEWRQQTEVLSpeeekelvekikelekeLEKAKKALEKneklkelraelkeLRKEAEEIHKKIKELAEEAQEL 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  520 KCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQkndvSRELKELNSCVHREQMECQLEKEA 599
Cdd:COG1340    194 HEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE----LKKLRKKQRALKREKEKEELEEKA 269


                   .
gi 1039746878  600 R 600
Cdd:COG1340    270 E 270
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 725-804 9.90e-09

PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family domain PDZ5 is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467170 [Multi-domain]  Cd Length: 85  Bit Score: 53.89  E-value: 9.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  725 LHINLSGQKGSRPQDSGIslengvyAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 804
Cdd:cd06682     13 LGITISAPKNRKPGDPLI-------ISDVKKGSVAHRTGTLEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIRK 85
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 1357-1436 1.04e-08

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: 54.25  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1357 EPRHVKVQK-GSEPLGISIVSG-----------EKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLI 1423
Cdd:cd06671      1 PPRRVELWRePGKSLGISIVGGrvmgsrlsngeEIRGIFIKHVLEDSPAGRNGtLKTGDRILEVNGVDLRNATHEEAVEA 80

                           90
                   ....*....|...
gi 1039746878 1424 IGQQCDTITILAQ 1436
Cdd:cd06671     81 IRNAGNPVVFLVQ 93
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 198-597 1.06e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 60.52  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  198 AMSDLQSLQNQhtnaLKRCEEVAKETDfyhTLHSRLLSDqtqLKDDVDMLRRENGKLRR---------ERNLLQQSWEDM 268
Cdd:pfam15921  290 ARSQANSIQSQ----LEIIQEQARNQN---SMYMRQLSD---LESTVSQLRSELREAKRmyedkieelEKQLVLANSELT 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  269 KRLREEDQ--KEIGDLRAQQQQVLK--HNGSSEIL------NKLYDTAMDKLEVVkkdyDALRKRYSEKvamhNSDLSRL 338
Cdd:pfam15921  360 EARTERDQfsQESGNLDDQLQKLLAdlHKREKELSlekeqnKRLWDRDTGNSITI----DHLRRELDDR----NMEVQRL 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  339 EQLgeeNQRLQKQTEMLTQQRDTAIQLQHQcalSLRRfetihheLSKATAQnkdLQWEMELLQSELTELRSKQVkTAKES 418
Cdd:pfam15921  432 EAL---LKAMKSECQGQMERQMAAIQGKNE---SLEK-------VSSLTAQ---LESTKEMLRKVVEELTAKKM-TLESS 494

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  419 EK---------YKEER--DAVYSEYKLIMSERDQVISELDKLQTEvelaESKLKSSTSEKKAASEEM-------EALRQI 480
Cdd:pfam15921  495 ERtvsdltaslQEKERaiEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQTECEALKLQMaekdkviEILRQQ 570

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  481 KDTVTM---DAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSE 557
Cdd:pfam15921  571 IENMTQlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD 650

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1039746878  558 LAEA----LRSLDDTRKQKNDVSRELKEL--NSCVHREQMECQLEK 597
Cdd:pfam15921  651 IKQErdqlLNEVKTSRNELNSLSEDYEVLkrNFRNKSEEMETTTNK 696
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1512-1593 1.44e-08

PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 53.48  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1512 DPRIVFIKKSQLDLGVHLCGGNLHGVFVAEVEDDSPAKgPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLKV 1591
Cdd:cd06767      2 EPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAH-QAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                   ..
gi 1039746878 1592 QY 1593
Cdd:cd06767     81 QY 82
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 655-714 1.45e-08

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: 53.51  E-value: 1.45e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  655 GDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 714
Cdd:cd06758     27 GDIGIFVAGVEEGGSAdrDGRLKKGDELLMINGQSLIGLSHQEAVAILRSSASPVQLVIASK 88
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
198-604 1.55e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.05  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  198 AMSDLQSLQNQHTNALKRCE---EVAKET----DFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKR 270
Cdd:PRK02224   207 RLNGLESELAELDEEIERYEeqrEQARETrdeaDEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  271 LREEDQKEIGDLRAQQQQvlkhnGSSEIlnklyDTAMDKLEVVKKDYDALRKRYSEK---VAMHNSDLSRL----EQLGE 343
Cdd:PRK02224   287 RLEELEEERDDLLAEAGL-----DDADA-----EAVEARREELEDRDEELRDRLEECrvaAQAHNEEAESLredaDDLEE 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  344 ENQRLQKQTEML-----------TQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKqV 412
Cdd:PRK02224   357 RAEELREEAAELeseleeareavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT-L 435

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  413 KTAKES-EKYKEERDAVY----------SEYKLIMSERDQVISELD----KLQTEVELAESKLKSSTSEKKAASEeMEAL 477
Cdd:PRK02224   436 RTARERvEEAEALLEAGKcpecgqpvegSPHVETIEEDRERVEELEaeleDLEEEVEEVEERLERAEDLVEAEDR-IERL 514

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  478 RQIKDTVT--MDAGRANKE-----VEILRKQCKALCQELKEALQEADVAKCRRDWAFQErdkiVAERDSIRTLCDNlRRE 550
Cdd:PRK02224   515 EERREDLEelIAERRETIEekrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE----VAELNSKLAELKE-RIE 589

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  551 RDRAVSELAEALRSLDDTRKQKNDVSRELKELNScVHREQMEcqlEKEARFRQL 604
Cdd:PRK02224   590 SLERIRTLLAAIADAEDEIERLREKREALAELND-ERRERLA---EKRERKREL 639
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 146-581 1.66e-08

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 60.13  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  146 VENLSIQLRLMTR---ERNELRKRLAFATHGATFDkrpyhrLNPDYERLKIQcVRAMSDLQSLQNQHTNALK-RCEEVAK 221
Cdd:pfam15921   80 LEEYSHQVKDLQRrlnESNELHEKQKFYLRQSVID------LQTKLQEMQME-RDAMADIRRRESQSQEDLRnQLQNTVH 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  222 ETDFYHTLHSRLLSD-QTQLKDDVDMLRRENGKLRRERNLLQQSWE-DMKRLREEDQKEIGDLRAQQQQVlkhngsSEIL 299
Cdd:pfam15921  153 ELEAAKCLKEDMLEDsNTQIEQLRKMMLSHEGVLQEIRSILVDFEEaSGKKIYEHDSMSTMHFRSLGSAI------SKIL 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  300 NKLyDTAMDKLE----VVKKDYDALRKRYSEKVAM---HNSDlsRLEQLGEENQ-RLQKQTEMLTQQRDTAIQLQHQCAL 371
Cdd:pfam15921  227 REL-DTEISYLKgrifPVEDQLEALKSESQNKIELllqQHQD--RIEQLISEHEvEITGLTEKASSARSQANSIQSQLEI 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  372 SLrrfETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKY-----------KEERDAVYSEYKLIMSERD 440
Cdd:pfam15921  304 IQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanselteaRTERDQFSQESGNLDDQLQ 380

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  441 QVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRankeVEILRKQCKALCQELKEalqeadvak 520
Cdd:pfam15921  381 KLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQR----LEALLKAMKSECQGQME--------- 447

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878  521 cRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKE 581
Cdd:pfam15921  448 -RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 630-713 1.89e-08

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: 53.79  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  630 RETEDIDL-----KALGFDMAeGVNEPCfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDL-INKDKKQAIKALL 701
Cdd:cd06689     13 RQVEYIELekpesGGLGFSVV-GLKSEN-RGELGIFVQEIQPGSVAarDGRLKENDQILAINGQPLdQSISHQQAIAILQ 90

                           90
                   ....*....|..
gi 1039746878  702 NGEGAINMVVRR 713
Cdd:cd06689     91 QAKGSVELVVAR 102
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1357-1434 2.68e-08

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: 53.02  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1357 EPRHVKVQKGS--EPLGISIVSGEK---GGVYVSKVTL-GSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1430
Cdd:cd06677      2 EITTIEIHRSDpyEELGISIVGGNDtplINIVIQEVYRdGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLRQPCPV 81


                   ....*.
gi 1039746878 1431 --ITIL 1434
Cdd:cd06677     82 lrLTVL 87
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
 1607-1667 3.08e-08

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-3 is critical for epidermal barrier function. It regulates cyclin D1-dependent cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-3 is the smallest of the three ZO proteins. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212961  Cd Length: 65  Bit Score: 52.18  E-value: 3.08e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1607 DSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSK 1667
Cdd:cd12028      1 DSFYIRTHFDYEPDPPSGLSFTRGEVFHVLDTMHRGKLGSWLAVRMGRDLREMEKGIIPNQ 61
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1361-1420 3.10e-08

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: 52.62  E-value: 3.10e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1361 VKVQKGSEPLGISIV-------SGEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06791      5 VELVKDEQGLGITIAgyvgekaSGELSGIFVKSIIPGSAADQDGrIQVNDQIIAVDGVNLQGFTNQEA 72
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1357-1434 3.39e-08

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: 52.94  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1357 EPRHVKVQKGSEP-------LGISIVSGEKG-----GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLI 1423
Cdd:cd06714      3 LIGRIILQRDPKDgsvsgngLGLKVVGGKMTesgrlGAYVTKVKPGSVADTVGhLREGDEVLEWNGISLQGKTFEEVQDI 82

                           90
                   ....*....|.
gi 1039746878 1424 IGQQCDTITIL 1434
Cdd:cd06714     83 ISQSKGEVELV 93
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 625-713 3.67e-08

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: 52.67  E-value: 3.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  625 VVEFERETedidlKALGFDMAEGVNEPCFPG-DCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd06704      2 TITIERQT-----GGLGISIAGGKGSTPYKGdDEGIFISRVTEGGPAAkAGVRVGDKLLEVNGVDLVDADHHEAVEALKN 76

                           90
                   ....*....|.
gi 1039746878  703 GEGAINMVVRR 713
Cdd:cd06704     77 SGNTVTMVVLR 87
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
386-612 3.95e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 3.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  386 ATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDA-----VYSEYKLIMSERDQVISELDKLQTEVELAESKL 460
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaEYSWDEIDVASAEREIAELEAELERLDASSDDL 687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  461 KSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEveilRKQCKALCQELKEALQEA-DVAKCRRDWAFQERDKIVAERDS 539
Cdd:COG4913    688 AALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAV 763

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  540 IRTLCDNLRRERDRAVSELAEALRSLDDTRKQ--------KNDVSRELKELNS--CVHREQMECQL-EKEARFRQLMAHS 608
Cdd:COG4913    764 ERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLPEylALLDRLEEDGLpEYEERFKELLNEN 843


                   ....
gi 1039746878  609 SHDS 612
Cdd:COG4913    844 SIEF 847
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 235-584 4.44e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 58.49  E-value: 4.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  235 SDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREED---QKEIGDLRAQQQQV-----LKHNGSSEILNKLyDTA 306
Cdd:TIGR04523  173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNkslESQISELKKQNNQLkdnieKKQQEINEKTTEI-SNT 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  307 MDKLEVVKKDYDALRKRYSEK---VAMHNSDLSRLE----QLGEENQRLQKQTEM---------LTQQRDTAIQLQHQCA 370
Cdd:TIGR04523  252 QTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKELEkqlnQLKSEISDLNNQKEQdwnkelkseLKNQEKKLEEIQNQIS 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  371 LSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERdavyseYKLIMSERDqVISELDKLQ 450
Cdd:TIGR04523  332 QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI------KNLESQIND-LESKIQNQE 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  451 TEVELAESKLKSSTSEKKAASEEMEALR--------QIKDTVTMDAGRaNKEVEILRKQCKALCQELKEALQEADVAKCR 522
Cdd:TIGR04523  405 KLNQQKDEQIKKLQQEKELLEKEIERLKetiiknnsEIKDLTNQDSVK-ELIIKNLDNTRESLETQLKVLSRSINKIKQN 483

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  523 RDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELNS 584
Cdd:TIGR04523  484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1359-1433 5.22e-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: 5.22e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1359 RHVKVQK-GSEPLGISIVSG-EKG-GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQcDTITI 1433
Cdd:cd06737      3 RLVRLDRrGPESLGFSVRGGlEHGcGLFVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINLIKTK-KTVSL 79
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 1366-1424 6.21e-08

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: 51.58  E-value: 6.21e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1366 GSEPLGISIVSGEKG-GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd23060      8 ANGGLGFSLVGGEGGsGIFVKSISPGGVADRDGrLQVGDRLLQVNGESVIGLSHSKAVNIL 68
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 136-639 6.42e-08

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 57.81  E-value: 6.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  136 LLTEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKR 215
Cdd:pfam05483  246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  216 C-------EEVAKETDFYHTLHSRLLsdqTQLKDDVDMLRRengKLRRERNLLQQSWEDMKRLREEDQKEIGDLraqqqq 288
Cdd:pfam05483  326 IcqlteekEAQMEELNKAKAAHSFVV---TEFEATTCSLEE---LLRTEQQRLEKNEDQLKIITMELQKKSSEL------ 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  289 vlkhngssEILNKLYDTAMDKLEVVKKDYDALRKRYSEKvamhnsdlSRLEQLGEENQRLQKQTEMLTQQRDTAIQ-LQH 367
Cdd:pfam05483  394 --------EEMTKFKNNKEVELEELKKILAEDEKLLDEK--------KQFEKIAEELKGKEQELIFLLQAREKEIHdLEI 457

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  368 QCALS-------LRRFETIHHELSKATAQNKDLQWEMELLQSELTELRS---------------------------KQVK 413
Cdd:pfam05483  458 QLTAIktseehyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlelkkhqediinckkqeermlKQIE 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  414 TAKESE-KYKEERDAVYSEYKlimSERDQVISELDKlqtevelaesklksstSEKKAASEEMEALRQIKDTVTMDAGRAN 492
Cdd:pfam05483  538 NLEEKEmNLRDELESVREEFI---QKGDEVKCKLDK----------------SEENARSIEYEVLKKEKQMKILENKCNN 598

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  493 --KEVEILRKQCKALCQELKeALQEADVAKCRRDWAFQER-DKIVAERDSIRT----LCDNLRRE-RDRAVSElaEALrs 564
Cdd:pfam05483  599 lkKQIENKNKNIEELHQENK-ALKKKGSAENKQLNAYEIKvNKLELELASAKQkfeeIIDNYQKEiEDKKISE--EKL-- 673

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  565 LDDTRKQKNDVSRELKelnscVHRE-QMECQlEKEARFRQLMahSSHDSAIDTDSMEWETEVVEFE-RETEDIDLKA 639
Cdd:pfam05483  674 LEEVEKAKAIADEAVK-----LQKEiDKRCQ-HKIAEMVALM--EKHKHQYDKIIEERDSELGLYKnKEQEQSSAKA 742
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-485 6.60e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 6.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  147 ENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETdfy 226
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL--- 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  227 htlhSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQvlkhngsseiLNKLYDTA 306
Cdd:TIGR02168  757 ----TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------LNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  307 MDKLEVVKKDYDALRKRY----------SEKVAMHNSDLSRLEQLGEEnqrLQKQTEMLTQQRDtaiQLQHQCALSLRRF 376
Cdd:TIGR02168  823 RERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEE---LESELEALLNERA---SLEEALALLRSEL 896

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  377 ETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYS-EYKLIMSERDQVISELDKLQTEVEL 455
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKR 976

                          330       340       350
                   ....*....|....*....|....*....|
gi 1039746878  456 AESKLKSSTSEKKAASEEMEALRQIKDTVT 485
Cdd:TIGR02168  977 LENKIKELGPVNLAAIEEYEELKERYDFLT 1006
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 138-636 6.72e-08

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 58.13  E-value: 6.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  138 TEQQANDTVENLSIQLRLMTRERNELRKRLA--------FATHGATFDKRpYHRLNPDYERLKIQCVRAMSDLQSLQNQ- 208
Cdd:TIGR00606  299 TDEQLNDLYHNHQRTVREKERELVDCQRELEklnkerrlLNQEKTELLVE-QGRLQLQADRHQEHIRARDSLIQSLATRl 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  209 HTNALKRCEEVAKETDFYHTLHSRLLSDQ--------TQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIG 280
Cdd:TIGR00606  378 ELDGFERGPFSERQIKNFHTLVIERQEDEaktaaqlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK 457

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  281 DLRAQQQQVlkHNGSSEILNKLYDTAMDKLEVVKKDYDAL---RKRYSEKVAMHNSDLSR-LEQLGEENQRL------QK 350
Cdd:TIGR00606  458 FVIKELQQL--EGSSDRILELDQELRKAERELSKAEKNSLtetLKKEVKSLQNEKADLDRkLRKLDQEMEQLnhhtttRT 535

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  351 QTEMLTQQRDTA------IQLQHQCALS--------LRRFETIHHELSKATAQNKDlqwEMELLQSELTELRSKQVKTAK 416
Cdd:TIGR00606  536 QMEMLTKDKMDKdeqirkIKSRHSDELTsllgyfpnKKQLEDWLHSKSKEINQTRD---RLAKLNKELASLEQNKNHINN 612

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  417 EsEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQ-------IKDTVTMDAG 489
Cdd:TIGR00606  613 E-LESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpVCQRVFQTEA 691

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  490 RANKEVEILRKQCKALCQELKEAlqEADVAKCRRdwafqERDKIVAERDSIRTLCDNLRRErdraVSELAEALRSLD-DT 568
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKST--ESELKKKEK-----RRDEMLGLAPGRQSIIDLKEKE----IPELRNKLQKVNrDI 760

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  569 RKQKNDVSRELKELNS----------------CVHREQMECQlEKEARFRQLMAHSshdsaidtDSMEWETEVVEFERET 632
Cdd:TIGR00606  761 QRLKNDIEEQETLLGTimpeeesakvcltdvtIMERFQMELK-DVERKIAQQAAKL--------QGSDLDRTVQQVNQEK 831


                   ....
gi 1039746878  633 EDID 636
Cdd:TIGR00606  832 QEKQ 835
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 656-713 7.80e-08

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: 51.51  E-value: 7.80e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  656 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDkkQAIKALLNGEGAINMVVRR 713
Cdd:cd06716     30 DTGIYVSEVDPNSIAakDGRIREGDQILQINGVDVQNRE--EAIALLSEEEKSITLLVAR 87
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 724-804 7.93e-08

PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 51.54  E-value: 7.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  724 PLHINLSGQKgsRPQDSgislengVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd06683     14 PLGITISGTE--EPFDP-------IVISGLTEGGLAERTGAIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTLKIS 84


                   .
gi 1039746878  804 K 804
Cdd:cd06683     85 R 85
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1360-1424 7.99e-08

PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467166 [Multi-domain]  Cd Length: 82  Bit Score: 51.48  E-value: 7.99e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1360 HVKVQK-GSEPLGISIVS-GEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06678      2 HVTLNKrDGEQLGIKLVRkKDEPGVFILDLLEGGLAARDGrLKSDDRVLAINGQDLRHGTPEQAAQII 69
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 296-484 8.35e-08

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 56.11  E-value: 8.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  296 SEILNKLyDTAMDKLEvvkkdydALRKRYSEKVAMHnsdlSRLEQlgeENQRLQKQTEMLTQQRDTAIQLQHQCALSLRR 375
Cdd:pfam09728    7 MQLLNKL-DSPEEKLA-------ALCKKYAELLEEM----KRLQK---DLKKLKKKQDQLQKEKDQLQSELSKAILAKSK 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  376 FETIHHELSKataQNKDLQWEMELLQSELTELR----------------------SKQVKTAKESEKYKEERDAVYSEYK 433
Cdd:pfam09728   72 LEKLCRELQK---QNKKLKEESKKLAKEEEEKRkelsekfqstlkdiqdkmeeksEKNNKLREENEELREKLKSLIEQYE 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  434 LimseRDQVISELDK-LQTEVELAESKLKSSTS--EKKAASEEMEALRQIKDTV 484
Cdd:pfam09728  149 L----RELHFEKLLKtKELEVQLAEAKLQQATEeeEKKAQEKEVAKARELKAQV 198
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 725-793 9.07e-08

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: 51.58  E-value: 9.07e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  725 LHINLSGQKGSRPQDSGIslengvYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd06758     14 LGIQITGGKGSKRGDIGI------FVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAILRS 76
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
387-631 1.02e-07

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.69  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  387 TAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSE 466
Cdd:COG1340      7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  467 KKAASEEMEALRQIKDTvtmdAGRANKEVEILRKQCKAL--------------------CQELKEALQEADVAKCRRDWA 526
Cdd:COG1340     87 LNELREELDELRKELAE----LNKAGGSIDKLRKEIERLewrqqtevlspeeekelvekIKELEKELEKAKKALEKNEKL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  527 FQERDKIVAERDSIRTLCD---NLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELNSCV---HREQMECQLEKEAR 600
Cdd:COG1340    163 KELRAELKELRKEAEEIHKkikELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAdelHEEIIELQKELREL 242

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1039746878  601 FRQLMAHSSHDSAIdtdSMEWETEVVEFERE 631
Cdd:COG1340    243 RKELKKLRKKQRAL---KREKEKEELEEKAE 270
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 633-713 1.05e-07

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: 51.10  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  633 EDIDLK----ALGFDMAEGVNEPCFP---GDCGIFVTKVDKGSIAdGR--LRVNDWLLRINDVDLINKDKKQAIKALLNG 703
Cdd:cd06702      1 EEIHLVkaggPLGLSIVGGSDHSSHPfgvDEPGIFISKVIPDGAA-AKsgLRIGDRILSVNGKDLRHATHQEAVSALLSP 79

                           90
                   ....*....|
gi 1039746878  704 EGAINMVVRR 713
Cdd:cd06702     80 GQEIKLLVRH 89
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 752-792 1.07e-07

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


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 51.33  E-value: 1.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1039746878  752 AVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 792
Cdd:cd06782     20 SPIPGGPAEKAG-IKPGDVIVAVDGESVRGMSLDEVVKLLR 59
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 299-634 1.15e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 57.29  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  299 LNKLYDTAMDKLEV------VKKDYDALRKRysEKVAMHNSDLSRLEQLGEENQRLQKQtemltqqrdtaiqLQHqcals 372
Cdd:pfam02463  175 LKKLIEETENLAELiidleeLKLQELKLKEQ--AKKALEYYQLKEKLELEEEYLLYLDY-------------LKL----- 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  373 LRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIM-SERDQVISELDKLQT 451
Cdd:pfam02463  235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELkSELLKLERRKVDDEE 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  452 EVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQckalcQELKEALQEADVAKCRRDWAFQErd 531
Cdd:pfam02463  315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL-----QEKLEQLEEELLAKKKLESERLS-- 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  532 kivaERDSIRTLCDNLRRERDRAVSELAEALRSL-DDTRKQKNDVSRELKELNSCVHREQMECQLEKEARFRQLMAHSSH 610
Cdd:pfam02463  388 ----SAAKLKEEELELKSEEEKEAQLLLELARQLeDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463

                          330       340
                   ....*....|....*....|....
gi 1039746878  611 DSAIDTDSMEWETEVVEFERETED 634
Cdd:pfam02463  464 ELELKKSEDLLKETQLVKLQEQLE 487
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1512-1600 1.24e-07

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: 51.20  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1512 DPRIVFIKKSQLDLGVHLCGG-NLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLK 1590
Cdd:cd06795      1 EPRKIVLHKGSTGLGFNIVGGeDGEGIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTII 80

                           90
                   ....*....|
gi 1039746878 1591 VQYRHEEFTR 1600
Cdd:cd06795     81 AQYKPEEYSR 90
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 718-804 1.26e-07

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 50.61  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  718 GGKVV-TPLHInlsgqkgSRpqdsgislengvyaaaVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQD 796
Cdd:cd06753     16 GGKDFnQPLTI-------SR----------------VTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKIKAATG 71


                   ....*...
gi 1039746878  797 SLTLSLLK 804
Cdd:cd06753     72 SLSLTLER 79
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1365-1439 1.33e-07

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: 50.78  E-value: 1.33e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1365 KGSEPLGISIVSGEKG--GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITILAQYNP 1439
Cdd:cd06752      8 PPGEQLGFNIRGGKASglGIFISKVIPDSDAHRLGLKEGDQILSVNGVDFEDIEHSEAVKVL-KTAREIQMRVRYFP 83
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
282-636 1.50e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  282 LRAQQQQVLKHNGSSEILNKlydTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRD- 360
Cdd:COG4717     51 LEKEADELFKPQGRKPELNL---KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  361 -TAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSK--------QVKTAKESEKYKEERDAVYSE 431
Cdd:COG4717    128 lPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQR 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  432 YKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKK-------------------AASEEMEALRQIKDTVTMDAGRAN 492
Cdd:COG4717    208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLA 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  493 KEVEILRKQCKALCQElkeaLQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQ- 571
Cdd:COG4717    288 LLFLLLAREKASLGKE----AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEl 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  572 -KNDVSRELKEL---NSCVHREQMECQLEKEARFRQLMAH-------------SSHDSAIDTDSMEWETEVVEFERETED 634
Cdd:COG4717    364 qLEELEQEIAALlaeAGVEDEEELRAALEQAEEYQELKEEleeleeqleellgELEELLEALDEEELEEELEELEEELEE 443


                   ..
gi 1039746878  635 ID 636
Cdd:COG4717    444 LE 445
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 742-803 1.81e-07

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: 49.94  E-value: 1.81e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  742 ISLENGVYAAAVVPGSPAakEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd06769     16 AGSERPVVVRSVTPGGPS--EGKLLPGDQILKINNEPVEDLPRERVIDLIRECKDSIVLTVL 75
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 1383-1433 2.02e-07

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: 50.67  E-value: 2.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1383 YVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1433
Cdd:cd06746     45 YLESVDPGGVADKAGLKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVL 95
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 1359-1433 2.23e-07

PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467208 [Multi-domain]  Cd Length: 80  Bit Score: 49.96  E-value: 2.23e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1359 RHVKVQKG-SEPLGISIvSGEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1433
Cdd:cd06726      1 RLVEFEKArDEPLGATI-KMEEDSVIVARILHGGMAHRSGlLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTF 76
PDZ4_PDZD2-PDZ2_hPro-IL-16-like cd06760
PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 ...
 747-795 2.34e-07

PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 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 4 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 second PDZ domain (PDZ2) 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 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: 467241 [Multi-domain]  Cd Length: 90  Bit Score: 50.35  E-value: 2.34e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1039746878  747 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQ 795
Cdd:cd06760     32 GIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLNEAYAILSQCK 80
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1370-1420 2.35e-07

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: 50.35  E-value: 2.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1370 LGISIVSGeKG---------GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06704     12 LGISIAGG-KGstpykgddeGIFISRVTEGGPAAKAGVRVGDKLLEVNGVDLVDADHHEA 70
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1359-1424 2.50e-07

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: 50.05  E-value: 2.50e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1359 RHV--KVQKGSEPLGISIVSG-EKG-GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06740      2 RQVtlKRSKSHEGLGFSIRGGaEHGvGIYVSLVEPGSLAEKEGLRVGDQILRVNDVSFEKVTHAEAVKIL 71
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 737-803 2.62e-07

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: 50.06  E-value: 2.62e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  737 PQDS-GISLENG---------VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd06675      9 PQDSlGISIAGGvgsplgdvpVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKNASGTIILQVV 85
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
384-573 2.85e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.91  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  384 SKATAQNKDLQWEMELLQSELTELRSkqvktakESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSS 463
Cdd:COG4372     27 AALSEQLRKALFELDKLQEELEQLRE-------ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  464 TSEKKAASEEMEALRQikdtvtmDAGRANKEVEILRKQCKALCQELKE-----ALQEADVAKCRRDWAFQERDKIVAERD 538
Cdd:COG4372    100 QEELESLQEEAEELQE-------ELEELQKERQDLEQQRKQLEAQIAElqseiAEREEELKELEEQLESLQEELAALEQE 172

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1039746878  539 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKN 573
Cdd:COG4372    173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 734-803 3.17e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 49.59  E-value: 3.17e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  734 GSRPQDSGISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:pfam00595   13 GFSLKGGSDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 183-485 3.44e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.41  E-value: 3.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  183 RLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENG-------KLR 255
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQqkdeqikKLQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  256 RERNLLQQSWEDMKRLREEDQKEIGDLRAQ----QQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMH 331
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  332 NSDLSRLEQLGEENQRL-QKQTEMLTQQRD--------------------------TAIQLQHQCALSLRRFETIHHELS 384
Cdd:TIGR04523  499 KKLNEEKKELEEKVKDLtKKISSLKEKIEKlesekkekeskisdledelnkddfelKKENLEKEIDEKNKEIEELKQTQK 578

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  385 KATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKsST 464
Cdd:TIGR04523  579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK-EI 657

                          330       340
                   ....*....|....*....|.
gi 1039746878  465 SEKKAaseemEALRQIKDTVT 485
Cdd:TIGR04523  658 RNKWP-----EIIKKIKESKT 673
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
334-562 4.42e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 4.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  334 DLSRLEQLGEenqRLQKQTEMLTQQRDTAIQLQHQcALSLRRFETIHHELSKATAQNKDLQWEMEL--LQSELTELRSKQ 411
Cdd:COG4913    236 DLERAHEALE---DAREQIELLEPIRELAERYAAA-RERLAELEYLRAALRLWFAQRRLELLEAELeeLRAELARLEAEL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  412 VKTAKESEKYKEERDAVYSEYklimseRDQVISELDKLQTEVELAESKLKsstsEKKAASEE-MEALRQIKDTVTMDAgr 490
Cdd:COG4913    312 ERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELE----ERERRRARlEALLAALGLPLPASA-- 379

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  491 anKEVEILRKQCKALCQELKEALQEADV----AKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEAL 562
Cdd:COG4913    380 --EEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 741-792 4.59e-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: 54.11  E-value: 4.59e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  741 GISL---ENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 792
Cdd:COG0793     63 GAELgeeDGKVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLLR 116
PDZ5_PTPN13-like cd06697
PDZ domain 5 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 724-800 4.91e-07

PDZ domain 5 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 5 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 PDZ5 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: 467183 [Multi-domain]  Cd Length: 87  Bit Score: 49.26  E-value: 4.91e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  724 PLHINLSGQKGSRPQdsgislenGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06697     14 QLGLKLTGGSDSKYQ--------VIYVLEIVPGSAAAEEGSLQPLDIIHYINGVSTQGMTLEDAVRALEASLPTVVL 82
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1360-1434 5.08e-07

PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family domain PDZ5 is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467170 [Multi-domain]  Cd Length: 85  Bit Score: 49.27  E-value: 5.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1360 HVKVQKGSEP-LGISIVSGEK----GGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITI 1433
Cdd:cd06682      2 HVKLPKRSGVgLGITISAPKNrkpgDPLIISDVKKGSVAHRTGtLEPGDKLLAIDNIRLDNCSMEDAAQIL-QQAEDIVK 80


                   .
gi 1039746878 1434 L 1434
Cdd:cd06682     81 L 81
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
 744-800 5.08e-07

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: 49.42  E-value: 5.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  744 LENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd23071     28 LDLGIFIASIIPGGPAEKDGRIKPGGRLISLNNISLEGVTFNTAVKILQNSPDEVEL 84
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 138-650 5.12e-07

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 55.23  E-value: 5.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  138 TEQQANDTVEN-LSIQLRLMTRERNELRKRLA---FATHGATFDKRpyHRLNPDYERLKIQCVRAMSDLQSLQNQHTNAL 213
Cdd:pfam12128  276 SRQEERQETSAeLNQLLRTLDDQWKEKRDELNgelSAADAAVAKDR--SELEALEDQHGAFLDADIETAAADQEQLPSWQ 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  214 KRCEEVAKETDFYHTLH--------SRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDM-----KRLREEDQKEIG 280
Cdd:pfam12128  354 SELENLEERLKALTGKHqdvtakynRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlqaleSELREQLEAGKL 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  281 DLRAQQQQVLKHNG------------SSEILNK-----LYDTAMDKLEVVKKDYDALRkrySEKVAMHNSDLSRLEQLGE 343
Cdd:pfam12128  434 EFNEEEYRLKSRLGelklrlnqatatPELLLQLenfdeRIERAREEQEAANAEVERLQ---SELRQARKRRDQASEALRQ 510

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  344 ENQRLQKQtemltQQRDTAIQLQ-HQCALSLRRF---------ETIHHELSKATAQNKDLQWEM--ELLQSELT----EL 407
Cdd:pfam12128  511 ASRRLEER-----QSALDELELQlFPQAGTLLHFlrkeapdweQSIGKVISPELLHRTDLDPEVwdGSVGGELNlygvKL 585

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  408 RSKQVKT---AKESEKYKEERDAVYSEY-------KLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEAL 477
Cdd:pfam12128  586 DLKRIDVpewAASEEELRERLDKAEEALqsarekqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSE 665

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  478 -RQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIV-----AERDSIRTLCDNLRRER 551
Cdd:pfam12128  666 kDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVegaldAQLALLKAAIAARRSGA 745

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  552 DRAVSELAE----ALRSLDDTRKQKNDVSRELKELNSCVhrEQMECQLEKEARFRQLMAH--SSHDSAIDTDSMEWETEV 625
Cdd:pfam12128  746 KAELKALETwykrDLASLGVDPDVIAKLKREIRTLERKI--ERIAVRRQEVLRYFDWYQEtwLQRRPRLATQLSNIERAI 823

                          570       580
                   ....*....|....*....|....*....
gi 1039746878  626 VEFE----RETEDIDLKALGFDMAEGVNE 650
Cdd:pfam12128  824 SELQqqlaRLIADTKLRRAKLEMERKASE 852
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 745-803 5.23e-07

PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467208 [Multi-domain]  Cd Length: 80  Bit Score: 48.80  E-value: 5.23e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  745 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd06726     21 EDSVIVARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLI 79
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 725-792 5.39e-07

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: 49.59  E-value: 5.39e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  725 LHINLSGQKGSrpQDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLR 792
Cdd:cd23059     18 LGVSVKGKTSK--EDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETLR 83
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 1370-1420 5.76e-07

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: 49.20  E-value: 5.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039746878 1370 LGISIVSGEKG-GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06674     16 LGLSIVGKRNDtGVFVSDIVKGGAADADGrLMQGDQILSVNGEDVRNASQEAA 68
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 1367-1420 6.60e-07

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: 49.14  E-value: 6.60e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1367 SEPLGISIV------SGEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06692      7 SKGLGIKIIggyrenTGEEFGIFIKRILPGGLAATDGrLKEGDLILEVNGESLQGVTNERA 67
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 627-713 6.80e-07

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: 48.75  E-value: 6.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  627 EFERETEDIDlKALGFDMAEGVNEPCFPGdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGE 704
Cdd:cd06792      2 VFEVELSKKD-GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAeqDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAG 78


                   ....*....
gi 1039746878  705 GAINMVVRR 713
Cdd:cd06792     79 QVVTLVLER 87
PDZ_PICK1-like cd06722
PDZ domain of PICK1 (protein interacting with C-kinase 1) and similar domains; PDZ (PSD-95 ...
 741-804 6.82e-07

PDZ domain of PICK1 (protein interacting with C-kinase 1) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PICK1, and related domains. PICK1 (also known as PRKCA-binding protein and protein kinase C-alpha-binding protein) plays a key role in regulating trafficking of binding partners by altering either their subcellular targeting and/or surface expression. PICK1 plays a role in synaptic plasticity by regulating the trafficking and internalization of amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptors; the PICK1-PDZ domain binds the AMPA receptor subunits. The PICK1 PDZ domain also binds glutamate transporters, Eph receptors, metabotropic glutamate receptors, and ASICs (acid-sensing ion channels), among others. Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes. 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 PICK-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: 467205 [Multi-domain]  Cd Length: 84  Bit Score: 48.95  E-value: 6.82e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  741 GISLENG------VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 804
Cdd:cd06722     14 GISIGGGapycpcLYIVQVFDNTPAAKDGTLAAGDEIVGVNGKSVKGKTKVEVAKMIQAVKGEVTIHYNK 83
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 728-800 7.44e-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: 48.59  E-value: 7.44e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  728 NLSGQKGsrpqdsgislENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06768     15 NLHAEKG----------RPGHFIREVDPGSPAERAG-LKDGDRLVEVNGENVEGESHEQVVEKIKASGNQVTL 76
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 146-489 7.90e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 7.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  146 VENLSIQLRLMTR---ERNELR-KRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAK 221
Cdd:TIGR02168  202 LKSLERQAEKAERykeLKAELReLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  222 ETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKhngSSEILNK 301
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE---ELESLEA 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  302 LYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQlqhqcalslrrfETIHH 381
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ------------EIEEL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  382 ELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLK 461
Cdd:TIGR02168  427 LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506

                          330       340
                   ....*....|....*....|....*...
gi 1039746878  462 SSTSEKKAASEEMEALRQIKDTVTMDAG 489
Cdd:TIGR02168  507 GVKALLKNQSGLSGILGVLSELISVDEG 534
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 728-800 8.13e-07

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: 48.48  E-value: 8.13e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  728 NLSGQKGSRPQdsGISLE----NGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06767      5 HVSIEKGSEPL--GISIVsgenGGIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQCGDTITM 78
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1360-1434 8.23e-07

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: 48.42  E-value: 8.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1360 HVKVQKGSEPLGISIVSGeKG--------GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1430
Cdd:cd06724      1 EIKLVKGPKGLGFSIAGG-VGnqhipgdnGIYVTKIIEGGAAQKDGrLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDV 79


                   ....
gi 1039746878 1431 ITIL 1434
Cdd:cd06724     80 VYLK 83
PDZ1_APBA1_3-like cd06720
PDZ domain 1 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ...
 748-794 9.19e-07

PDZ domain 1 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as (X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2), which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins such as APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,2,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467203 [Multi-domain]  Cd Length: 86  Bit Score: 48.41  E-value: 9.19e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1039746878  748 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 794
Cdd:cd06720     29 VVVANMMPGGPAARSGKLNIGDQIMSINGTSLVGLPLSTCQAIIKNL 75
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 639-713 9.72e-07

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: 48.42  E-value: 9.72e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  639 ALGFDMA--EGVNEPCFP-GDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 713
Cdd:cd06727     10 GFGFGIAvsGGRDNPHFQsGDTSIVISDVLKGGPAEGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANITVKR 87
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
158-428 9.95e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 9.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  158 RERNELRKRLAfaTHGATF--DKRPYH-RLnpdYERLKIQCVRAMSDL---QSLQN---------QH----TNALKRCEE 218
Cdd:COG4913    155 FDIRALKARLK--KQGVEFfdSFSAYLaRL---RRRLGIGSEKALRLLhktQSFKPigdlddfvrEYmleePDTFEAADA 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  219 VAKETDFYHTLHSRLLSDQTQlkddVDMLRRengkLRRERNLLQQSWEDMKRLRE--------EDQKEIGDLRAQQQQvl 290
Cdd:COG4913    230 LVEHFDDLERAHEALEDAREQ----IELLEP----IRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAELEE-- 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  291 khngsseiLNKLYDTAMDKLEVVKKDYDALRKRYSE-KVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRD----TAIQL 365
Cdd:COG4913    300 --------LRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRArleaLLAAL 371

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  366 QHQCALSLRRFETIHHELSKATAQNKDLQwemELLQSELTELRSKQVKTAKESEKYKEERDAV 428
Cdd:COG4913    372 GLPLPASAEEFAALRAEAAALLEALEEEL---EALEEALAEAEAALRDLRRELRELEAEIASL 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 400-582 1.00e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  400 LQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALR- 478
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKe 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  479 ----QIKDTVTM-------------DAGRANKEVEILR---KQCKALCQELKEALQEADvakcrrdwafQERDKIVAERD 538
Cdd:COG4942    105 elaeLLRALYRLgrqpplalllspeDFLDAVRRLQYLKylaPARREQAEELRADLAELA----------ALRAELEAERA 174

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039746878  539 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKEL 582
Cdd:COG4942    175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 140-641 1.12e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  140 QQANDTVENLSIQLRLMTRERNELRKRLAfathgatfdkrpyhRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEV 219
Cdd:COG1196    270 EELRLELEELELELEEAQAEEYELLAELA--------------RLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  220 AKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEI- 298
Cdd:COG1196    336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLEr 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  299 ---LNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRR 375
Cdd:COG1196    416 lerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  376 FETIH--HELSKATAQNKDLQWEMELLQSELTELRSkqvkTAKESEKYKEERDAVYSEYKLIMSERD--QVISELDKLQ- 450
Cdd:COG1196    496 LLEAEadYEGFLEGVKAALLLAGLRGLAGAVAVLIG----VEAAYEAALEAALAAALQNIVVEDDEVaaAAIEYLKAAKa 571

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  451 ---TEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEIL-------------RKQCKALCQELKEALQ 514
Cdd:COG1196    572 graTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgrtlvaarleaaLRRAVTLAGRLREVTL 651

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  515 EADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELNSCVHREQMECQ 594
Cdd:COG1196    652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  595 LEKEARFRQLMAHSSHDSAIDTDSM-------EWETEVVEFEREtedidLKALG 641
Cdd:COG1196    732 AEREELLEELLEEEELLEEEALEELpeppdleELERELERLERE-----IEALG 780
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1359-1420 1.16e-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: 47.95  E-value: 1.16e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878 1359 RHVKVQKgsEP---LGISIvsgeKGG------VYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06801      1 RTVRVVK--QDvggLGISI----KGGaehkmpILISKIFKGQAADQTGqLFVGDAILSVNGENLEDATHDEA 66
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
147-559 1.16e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  147 ENLSIQLRLMTRERNELRKRLAfathgatfDKRPYHRLnpdYERLK--------IQCVRAMSDLQSLQNQHTNALKRCEE 218
Cdd:PRK03918   334 EEKEERLEELKKKLKELEKRLE--------ELEERHEL---YEEAKakkeelerLKKRLTGLTPEKLEKELEELEKAKEE 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  219 VAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQswEDMKRLREEDQKEIGDLRAQQQqvlkhngssEI 298
Cdd:PRK03918   403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEKELK---------EI 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  299 LNKLydtamDKLEVVKKDYDALRKRYSEKVAMHnSDLSRLEQLGEE-----NQRLQKQTEMLTQQRDTAIQLQHQCALSL 373
Cdd:PRK03918   472 EEKE-----RKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  374 RRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEY---KLIMSERDQVISELDKLQ 450
Cdd:PRK03918   546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYlelKDAEKELEREEKELKKLE 625

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  451 TEVELAESKLKSSTSEKKAASEEMEALRQIKD------------TVTMDAGRANKEVEIL---RKQCKALCQELKEALQE 515
Cdd:PRK03918   626 EELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeelreeylELSRELAGLRAELEELekrREEIKKTLEKLKEELEE 705

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1039746878  516 ADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELA 559
Cdd:PRK03918   706 REKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIA 749
SH3_ZO-2 cd12027
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a ...
 1606-1667 1.23e-06

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-2 plays an essential role in embryonic development. It is critical for the blood-testis barrier integrity and male fertility. It also regulates the expression of cyclin D1 and cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-2 contains an actin-binding region and a domain of unknown function designated beta. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212960  Cd Length: 63  Bit Score: 47.61  E-value: 1.23e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878 1606 GDSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLdenAQKIQRGQIPSK 1667
Cdd:cd12027      1 GDSFFIRTHFEYEKELPQSLAFTRGEIFRVVDTLYDGKLGNWLAVRI---GNELEKGLIPNK 59
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
218-604 1.24e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  218 EVAKETdFYHTLHSRLLSdqtQLKDDVDMLRRENGKlRRERNL--LQQSWEDMKRLRE------EDQKEIGDLRAQQQQV 289
Cdd:COG4717     33 EAGKST-LLAFIRAMLLE---RLEKEADELFKPQGR-KPELNLkeLKELEEELKEAEEkeeeyaELQEELEELEEELEEL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  290 lkhngssEILNKLYDTAMDKLEVVKKDYDALRKRysEKVAMHNSDL-SRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQ 368
Cdd:COG4717    108 -------EAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELpERLEELEERLEELRELEEELEELEAELAELQEE 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  369 CALSLRRF-ETIHHELSKATAQNKDLQWEMELLQSELTELRSK-------------QVKTAKESEKYKEER--------- 425
Cdd:COG4717    179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEEleeleeeleqlenELEAAALEERLKEARlllliaaal 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  426 -------DAVYSEYKLIM---------------------SERDQVISELDKLQTEVELAESKLKS-----STSEKKAASE 472
Cdd:COG4717    259 lallglgGSLLSLILTIAgvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEE 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  473 EMEALRQIKDTVTMDAGRANKEVEIlrkQCKALCQELKEALQEADV-------AKCRRdwaFQERDKIVAERDSIRTLC- 544
Cdd:COG4717    339 LLELLDRIEELQELLREAEELEEEL---QLEELEQEIAALLAEAGVedeeelrAALEQ---AEEYQELKEELEELEEQLe 412

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  545 ---------------DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKEL-NSCVHREQMECQLEKEARFRQL 604
Cdd:COG4717    413 ellgeleellealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLeEDGELAELLQELEELKAELREL 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-448 1.31e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  138 TEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNaLKRce 217
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNE-- 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  218 evaketdFYHTLHSRLLSDQTQLKD---DVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEI---GDLRAQQQQVLk 291
Cdd:TIGR02168  818 -------EAANLRERLESLERRIAAterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELealLNERASLEEAL- 889

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  292 hngssEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLgeeNQRLQKQTEMLT-QQRDTaiqlqhqca 370
Cdd:TIGR02168  890 -----ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSeEYSLT--------- 952

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  371 lslrrFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSER---DQVISELD 447
Cdd:TIGR02168  953 -----LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKetlEEAIEEID 1027


                   .
gi 1039746878  448 K 448
Cdd:TIGR02168 1028 R 1028
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 745-802 1.44e-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: 47.73  E-value: 1.44e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  745 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 802
Cdd:cd10817     21 ENGIVIKSLTEGGPAAKDGRLKVGDQILAVDDESVVGCPYEKAISLLKTAKGTVKLTV 78
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 739-803 1.51e-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: 48.02  E-value: 1.51e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  739 DSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd23058     25 DNPTGGSGPIYIKNILPKGAAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKLGGTVSLV 89
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1360-1433 1.56e-06

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: 47.77  E-value: 1.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1360 HVKVQKGSEPLGISIVSG-EKG-GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQA-RLIIGQQCDTITI 1433
Cdd:cd10834      5 HLYTTSDDYCLGFNIRGGsEYGlGIYVSKVDPGGLAEQNGIKVGDQILAVNGVSFEDITHSKAvEVLKSQTHLMLTI 81
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 1361-1420 1.63e-06

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: 47.67  E-value: 1.63e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1361 VKVQKGSEPLGISIVSGEK---GGVYVSKV-TLGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06673      6 IEINKGKKGLGLSIVGGSDtllGAIIIHEVyEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEA 69
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 1359-1410 1.70e-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: 1.70e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1359 RHVKVQK-GSEPLGISIVSG---EKG-GVYVSKVTLGSIAHQAGLEY-GDQLLEFNGI 1410
Cdd:cd06718      1 RRVELIKpPGKPLGFYIRDGngvERVpGIFISRLVLGSLADSTGLLAvGDEILEVNGV 58
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 746-802 1.78e-06

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: 47.35  E-value: 1.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  746 NGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 802
Cdd:cd23060     23 SGIFVKSISPGGVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
336-583 1.87e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  336 SRLEQLGEENQRLQKQTEMLTQQRDTAiqlqhqcalsLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTA 415
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREELEQA----------REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  416 -------KESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDtvTMDA 488
Cdd:COG4372    101 eeleslqEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSE 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  489 GRANKEVEILRKQckALCQELKEALQEADVakcrrdWAFQERDKIVAERDSIRTlcDNLRRERDRAVSELAEALRSLDDT 568
Cdd:COG4372    179 AEAEQALDELLKE--ANRNAEKEEELAEAE------KLIESLPRELAEELLEAK--DSLEAKLGLALSALLDALELEEDK 248

                          250
                   ....*....|....*
gi 1039746878  569 RKQKNDVSRELKELN 583
Cdd:COG4372    249 EELLEEVILKEIEEL 263
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 205-602 2.07e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 53.05  E-value: 2.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  205 LQNQHTNALKRCEEVAKETDFYHTLHSrLLSDQTQLKDDVDMLRRENGKLRRERN-----LLQQSWEDMKRLREEDQKEI 279
Cdd:TIGR00618  357 IRDAHEVATSIREISCQQHTLTQHIHT-LQQQKTTLTQKLQSLCKELDILQREQAtidtrTSAFRDLQGQLAHAKKQQEL 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  280 GDLRAQQQQVLKHNGSSEI------LNKLYdTAMDKLEVVKKDYDALRKRYSEKVAMHnsdLSRLEQLGEENQRLQKQTE 353
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEklekihLQESA-QSLKEREQQLQTKEQIHLQETRKKAVV---LARLLELQEEPCPLCGSCI 511

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  354 MLTQQRDTAIQLQHQCALSLR----------RFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKE 423
Cdd:TIGR00618  512 HPNPARQDIDNPGPLTRRMQRgeqtyaqletSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN 591

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  424 ERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQCK 503
Cdd:TIGR00618  592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP 671

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  504 ALCQELKEALQEADVAKCRRDWAFQErdkIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELkeLN 583
Cdd:TIGR00618  672 KELLASRQLALQKMQSEKEQLTYWKE---MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQS--LK 746

                          410
                   ....*....|....*....
gi 1039746878  584 SCVHREQMECQLEKEARFR 602
Cdd:TIGR00618  747 ELMHQARTVLKARTEAHFN 765
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 631-702 2.37e-06

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: 47.23  E-value: 2.37e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  631 ETEDIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd06791      1 ETFEVELvkdeQGLGITIAGYVGEKASGELSGIFVKSIIPGSAAdqDGRIQVNDQIIAVDGVNLQGFTNQEAVEVLRN 78
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 329-575 2.76e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.69  E-value: 2.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  329 AMHnSDLSRLEQLgeenQRLQKQTEMLTQQRDTaiqLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELR 408
Cdd:COG1579      1 AMP-EDLRALLDL----QELDSELDRLEHRLKE---LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  409 SKQvktakesEKYKEERDAVyseykliMSERdqvisELDKLQTEVELAESKLKSSTSEKKAASEEMEALRqikdtvtmda 488
Cdd:COG1579     73 ARI-------KKYEEQLGNV-------RNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELE---------- 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  489 granKEVEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIVAERDSirtlcdnLRRERDRAVSELAEALRSL-DD 567
Cdd:COG1579    124 ----EELAELEAELAELEAELEEKKAELD----------EELAELEAELEE-------LEAEREELAAKIPPELLALyER 182


                   ....*...
gi 1039746878  568 TRKQKNDV 575
Cdd:COG1579    183 IRKRKNGL 190
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 1360-1434 2.79e-06

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: 47.33  E-value: 2.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1360 HVKVQKGSEPLGISIVSG------------EKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQ 1427
Cdd:cd10822      5 HKLRQGENLILGFSIGGGidqdpsknpfsyTDKGIYVTRVSEGGPAEKAGLQVGDKILQVNGWDMTMVTHKQAVKRLTKK 84


                   ....*..
gi 1039746878 1428 CDTITIL 1434
Cdd:cd10822     85 KPVLRML 91
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 1364-1435 2.81e-06

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: 47.39  E-value: 2.81e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1364 QKGsepLGISIVSGEKG-----GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1435
Cdd:cd06694     12 QKG---LGFTIVGGENSgsldlGIFVKSIIPGGPADKDGrIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVELII 86
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 725-804 2.81e-06

PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 47.27  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
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gi 1039746878  725 LHINLSGQKGSRP---QDSGIslengvYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLS 801
Cdd:cd06704     12 LGISIAGGKGSTPykgDDEGI------FISRVTEGGPAAKAG-VRVGDKLLEVNGVDLVDADHHEAVEALKNSGNTVTMV 84


                   ...
gi 1039746878  802 LLK 804
Cdd:cd06704     85 VLR 87
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 1361-1432 2.91e-06

PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 46.85  E-value: 2.91e-06
                           10        20        30        40        50        60        70
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gi 1039746878 1361 VKVQKGSEPLGISIVSGEKGG-VYVSKVTLGSIAHQAGLEY-GDQLLEFNGINLRSATEQQARLIIGQQCDTIT 1432
Cdd:cd06799      3 VRLVKNNEPLGATIKRDEKTGaIVVARIMRGGAADRSGLIHvGDELREVNGISVEGKDPEEVIQILANSQGPIT 76
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 745-800 3.08e-06

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: 46.88  E-value: 3.08e-06
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gi 1039746878  745 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06724     27 DNGIYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYL 82
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 748-803 3.19e-06

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: 46.95  E-value: 3.19e-06
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gi 1039746878  748 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd06676     28 IYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTLTVL 83
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 743-805 3.21e-06

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: 46.92  E-value: 3.21e-06
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gi 1039746878  743 SLENGVYAAAVVPgSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 805
Cdd:cd06696     24 KDDNGCYIHDIVQ-DPAKSDGRLRPGDRLIMVNGVDVTNMSHTEAVSLLRAAPKEVTLVLGRA 85
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 1366-1436 3.33e-06

PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Zasp52-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 46.75  E-value: 3.33e-06
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gi 1039746878 1366 GSEPLGISIVSGEKGG--VYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1436
Cdd:cd23068      9 SNTPWGFRLQGGADFGqpLSIQKVNPGSPADKAGLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQ 81
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1357-1436 3.40e-06

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: 47.26  E-value: 3.40e-06
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gi 1039746878 1357 EPRHVKVQKGSEPLGISIVSGeKG---------GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1426
Cdd:cd06703      1 ETITTTLIRDGKGLGFSIAGG-KGstpfrdgdeGIFISRITEGGAADRDGkLQVGDRVLSINGVDVTEARHDQAVALLTS 79

                           90
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gi 1039746878 1427 QCDTITILAQ 1436
Cdd:cd06703     80 SSPTITLVVE 89
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 748-814 3.43e-06

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: 46.96  E-value: 3.43e-06
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gi 1039746878  748 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLkvfpqssSWSG 814
Cdd:cd06680     30 FFVKSIVPGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTVV-------SWPG 89
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 734-800 4.21e-06

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: 46.50  E-value: 4.21e-06
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gi 1039746878  734 GSRPQDSGISLENGVYAAAVVPGSPAakEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06727     19 GGRDNPHFQSGDTSIVISDVLKGGPA--EGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANI 83
PRK01156 PRK01156
chromosome segregation protein; Provisional
 183-587 4.30e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.83  E-value: 4.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  183 RLNPDYERLK--IQCVRA-MSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERN 259
Cdd:PRK01156   163 SLERNYDKLKdvIDMLRAeISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  260 LLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKR---YSEKVAMHNSDLS 336
Cdd:PRK01156   243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDienKKQILSNIDAEIN 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  337 RLEQlgeenqrLQKQTEMLTQQRDTAIQLQhqcalslRRFETIHHELSkataqnkDLQWEMELLQSELTELRSKQVKTAK 416
Cdd:PRK01156   323 KYHA-------IIKKLSVLQKDYNDYIKKK-------SRYDDLNNQIL-------ELEGYEMDYNSYLKSIESLKKKIEE 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  417 ESEKYKEERDAVYSEYKL-------IMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEAL------------ 477
Cdd:PRK01156   382 YSKNIERMSAFISEILKIqeidpdaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgtt 461

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  478 ------RQIKDTVTMDAGRANKEVEILRKQCKALCQE------LKEALQEADVAKCRRDWAFQE--RDKIVAERDSIRTL 543
Cdd:PRK01156   462 lgeeksNHIINHYNEKKSRLEEKIREIEIEVKDIDEKivdlkkRKEYLESEEINKSINEYNKIEsaRADLEDIKIKINEL 541

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  544 CD------------------NLRRERDRAVSELAE-ALRSLDDTRKQKNDVSRELKELNSCVH 587
Cdd:PRK01156   542 KDkhdkyeeiknrykslkleDLDSKRTSWLNALAViSLIDIETNRSRSNEIKKQLNDLESRLQ 604
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 747-800 5.02e-06

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: 46.83  E-value: 5.02e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  747 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06701     39 GIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTL 92
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 741-786 5.45e-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: 46.41  E-value: 5.45e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039746878  741 GISLEN--GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE 786
Cdd:cd06718     20 GNGVERvpGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDD 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
406-712 5.62e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 5.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  406 ELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVT 485
Cdd:COG4372     14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  486 MDAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSL 565
Cdd:COG4372     94 AELAQAQEELESLQEEAEELQEELEELQ--------------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  566 DDTRKQKNDVSRELKELNSCVHREQMEcQLEKEARfRQLMAHSSHDSAIDTdSMEWETEVVEFERETEDIDLKALGFDMA 645
Cdd:COG4372    160 ESLQEELAALEQELQALSEAEAEQALD-ELLKEAN-RNAEKEEELAEAEKL-IESLPRELAEELLEAKDSLEAKLGLALS 236

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  646 EGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 712
Cdd:COG4372    237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLN 303
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 198-596 6.24e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 51.33  E-value: 6.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  198 AMSDLQSLQNQHTNALKRCEEvaKETDFYHTLHSRLLSDQTQLkddVDMLRRENGKLRRERnllqQSWEDMKRLREEDQK 277
Cdd:pfam01576  317 AQQELRSKREQEVTELKKALE--EETRSHEAQLQEMRQKHTQA---LEELTEQLEQAKRNK----ANLEKAKQALESENA 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  278 EI-GDLRAQQQQvlkhNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDL----SRLEQLGEENQRLQKQT 352
Cdd:pfam01576  388 ELqAELRTLQQA----KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELesvsSLLNEAEGKNIKLSKDV 463

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  353 EMLTQQ-RDTAIQLQHQC----ALS--LRRFE----TIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKY 421
Cdd:pfam01576  464 SSLESQlQDTQELLQEETrqklNLStrLRQLEdernSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEAL 543

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  422 KEERDavyseyklimserdqviseldKLQTEVELAESKLKsstsEKKAASEEMEA----LRQIKDTVTMDAGRANKEVEI 497
Cdd:pfam01576  544 EEGKK---------------------RLQRELEALTQQLE----EKAAAYDKLEKtknrLQQELDDLLVDLDHQRQLVSN 598

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  498 LRKQCKALCQELKEalQEADVAKcrrdwAFQERDKivAERDSirtlcdnlrRERD-------RAVSELAEALRSLDDTRK 570
Cdd:pfam01576  599 LEKKQKKFDQMLAE--EKAISAR-----YAEERDR--AEAEA---------REKEtralslaRALEEALEAKEELERTNK 660

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1039746878  571 Q-----------KNDVSRELKELNSCvhREQMECQLE 596
Cdd:pfam01576  661 QlraemedlvssKDDVGKNVHELERS--KRALEQQVE 695
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 640-714 6.98e-06

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: 46.19  E-value: 6.98e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  640 LGFDMAEGVNEPcfpgdcGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 714
Cdd:cd06795     14 LGFNIVGGEDGE------GIFISFILAGGPADlsGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIAQYK 84
PTZ00121 PTZ00121
MAEBL; Provisional
 266-636 7.19e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 7.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  266 EDMKRLRE----EDQKEIGDLRAQQQQVLKHNGSSEILNKlydtamdkleVVKKDYDALRKRYSEKVAMHNSDLSRLEQL 341
Cdd:PTZ00121  1549 DELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKK----------AEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  342 GEENQRLQKQTEmltqQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQ--VKTAKESE 419
Cdd:PTZ00121  1619 KIKAEELKKAEE----EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEedEKKAAEAL 1694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  420 KYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILR 499
Cdd:PTZ00121  1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  500 KQCKALcqeLKEALQEADvAKCRRDWAFQERD-----KIVAERDSIRTLCDNLRRERDraVSELAEALRSLDDTRKQKND 574
Cdd:PTZ00121  1775 KEKEAV---IEEELDEED-EKRRMEVDKKIKDifdnfANIIEGGKEGNLVINDSKEME--DSAIKEVADSKNMQLEEADA 1848

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  575 VSRELKELNSCVHREqmecqlekearfrqlmAHSSHDSAIDTDSMEWETEVVEFERETEDID 636
Cdd:PTZ00121  1849 FEKHKFNKNNENGED----------------GNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 292-629 7.48e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 51.26  E-value: 7.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  292 HNGSSEILNKLYDTAMDKLEVVKKDYDALrkrYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCal 371
Cdd:pfam05483   55 NSGDCHYQEGLKDSDFENSEGLSRLYSKL---YKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFEN-- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  372 slrrfETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQT 451
Cdd:pfam05483  130 -----EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRV 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  452 EVElaESKLKSSTSEKkaasEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKE---ALQEAdvakcrRDWAFQ 528
Cdd:pfam05483  205 QAE--NARLEMHFKLK----EDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDltfLLEES------RDKANQ 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  529 ERDKIVAERDSIRTLCDnlrrERDRAVSELAEALRSLDDTRKQKNDVSRELKELNSCVhreqmeCQL--EKEARFRQL-M 605
Cdd:pfam05483  273 LEEKTKLQDENLKELIE----KKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTI------CQLteEKEAQMEELnK 342

                          330       340
                   ....*....|....*....|....
gi 1039746878  606 AHSSHDSAIdtdsMEWETEVVEFE 629
Cdd:pfam05483  343 AKAAHSFVV----TEFEATTCSLE 362
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 1359-1434 7.85e-06

PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP5, Drosophila Stardust, and related domains. MPP5 (also known as MAGUK p55 subfamily member 1, protein associated with Lin-7 1 or PALS1) and Drosophila Stardust are membrane-associated guanylate kinase (MAGUK)-like proteins that serve as signaling and scaffolding proteins, linking different proteins critical to the formation and maintenance of tight junctions (TJ) and apical-basal polarity. Apical-basal polarity determinants cluster in complexes; in particular, the Crumbs complex (Crb, MPP5, and PATJ) and the PAR/aPKC-complex (PAR-3, PAR-6, aPKC) determine the apical plasma membrane domain. Within the Crumbs complex, Crb is stabilized in the plasma membrane by MPP5, which in turn recruits PATJ and Lin-7 to the complex. MPP5 also links the Crumbs complex with the PAR/aPKC-complex. The Drosophila homolog of the Crumbs complex is the (CRB)-Stardust (Sdt)-Discs Lost (Dlt) complex. MPP5 also acts as an interaction partner for SARS-CoV envelope protein E, which results in delayed formation of TJs and dysregulation of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP5-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467259 [Multi-domain]  Cd Length: 79  Bit Score: 45.80  E-value: 7.85e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1359 RHVKVQKGSEPLGiSIVSGEKGGVYVSKVTLGSIAHQAGLEY-GDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:cd06798      1 KIVRIEKTREPLG-ATVRNEGDSVIISRIVKGGAAEKSGLLHeGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFL 76
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 439-631 7.89e-06

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 50.80  E-value: 7.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  439 RDQVISELDKLQTEVelAESKLKSSTSE--KKAASEEMEALRQIKDTVTMDAGRANKEvEILRKQCKALCQ-ELKE---- 511
Cdd:pfam05701   37 RKLVELELEKVQEEI--PEYKKQSEAAEaaKAQVLEELESTKRLIEELKLNLERAQTE-EAQAKQDSELAKlRVEEmeqg 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  512 --------ALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSREL---K 580
Cdd:pfam05701  114 iadeasvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELiatK 193

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039746878  581 ELNSCVHREQMECQlekEARFRQLMAHsshdsaiDTDSMEWETEVVEFERE 631
Cdd:pfam05701  194 ESLESAHAAHLEAE---EHRIGAALAR-------EQDKLNWEKELKQAEEE 234
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1610-1668 7.92e-06

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 44.76  E-value: 7.92e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1610 YIRALYDRLAEVEPELSFKKDDILYVDDTLPQGvfgsWMAWQLDENaqkiQRGQIPSKY 1668
Cdd:cd00174      1 YARALYDYEAQDDDELSFKKGDIITVLEKDDDG----WWEGELNGG----REGLFPANY 51
PDZ_2 pfam13180
PDZ domain;
742-803 8.22e-06

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 45.34  E-value: 8.22e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  742 ISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALdnKSLNECESLLRSC--QDSLTLSLL 803
Cdd:pfam13180    2 VDLEGGVVVVSVKSSGPAAKAG-LKAGDVILSIDGRKI--NDLTDLESALYGHkpGDTVTLQVY 62
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 729-800 8.67e-06

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: 46.10  E-value: 8.67e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  729 LSGQKGSRPQDSGislENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06703     18 IAGGKGSTPFRDG---DEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITL 86
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 217-519 8.78e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.89  E-value: 8.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  217 EEVAKETDFYHTLHSRLLSDQTQLkDDVDMLRRENGKLRRERNllqqswEDMKRLREEDQKEIGDlRAQQQQVLKHNGSS 296
Cdd:pfam17380  306 EEKAREVERRRKLEEAEKARQAEM-DRQAAIYAEQERMAMERE------RELERIRQEERKRELE-RIRQEEIAMEISRM 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  297 EILNKLYDTAMDKLEVVKKDYDALRKrysekvamhnsdlsrLEQLGEENQRLQKQT----EMLTQQRDTAIQLQhqcals 372
Cdd:pfam17380  378 RELERLQMERQQKNERVRQELEAARK---------------VKILEEERQRKIQQQkvemEQIRAEQEEARQRE------ 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  373 LRRFETIH-HELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKE---------ERDAVYSEYKLIMSERDQV 442
Cdd:pfam17380  437 VRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkilEKELEERKQAMIEEERKRK 516

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  443 ISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVtMDAGRANKEVEILRKQCKALCQ--ELKEALQEADVA 519
Cdd:pfam17380  517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRLEAMEREREMMRQivESEKARAEYEAT 594
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 717-794 8.96e-06

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: 46.01  E-value: 8.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  717 LGGKVVtplhinlsgqkGSRPQDSGislENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE-CESLLRSC 794
Cdd:cd06714     23 LGLKVV-----------GGKMTESG---RLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEvQDIISQSK 87
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 625-711 9.94e-06

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: 45.43  E-value: 9.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  625 VVEFERETEDidlkALGFDMAEGVNEPCfpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd06675      2 TVEIKRGPQD----SLGISIAGGVGSPL--GDVPVFIAMIQPNGVAaqTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKN 75


                   ....*....
gi 1039746878  703 GEGAINMVV 711
Cdd:cd06675     76 ASGTIILQV 84
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1514-1592 1.02e-05

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 45.35  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1514 RIVFIKKSQLDLGVHLCGGN---LHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLK 1590
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79


                   ..
gi 1039746878 1591 VQ 1592
Cdd:pfam00595   80 IL 81
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 745-803 1.09e-05

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: 45.67  E-value: 1.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  745 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd06692     25 EFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSILRSASASNHMSLL 83
PDZ1_L-delphilin-like cd06743
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1368-1431 1.24e-05

PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467225 [Multi-domain]  Cd Length: 76  Bit Score: 44.96  E-value: 1.24e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878 1368 EPLGISIvsGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRS-ATEQQARLiiGQQCDTI 1431
Cdd:cd06743      9 EAFGFSI--GGSGPCYILSVEEGSSAHAAGLQPGDQILELDGQDVSSlSCEAIIAL--ARRCPSV 69
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 710-796 1.33e-05

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: 45.39  E-value: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  710 VVRR-RKSLGgkvvtplhINLSGQKGSRPQDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECE 788
Cdd:cd06671      7 LWREpGKSLG--------ISIVGGRVMGSRLSNGEEIRGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEAV 78


                   ....*...
gi 1039746878  789 SLLRSCQD 796
Cdd:cd06671     79 EAIRNAGN 86
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 707-781 1.35e-05

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: 48.99  E-value: 1.35e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  707 INMVVRRRKSL--GGKVVTPLhINLSGQKGSRP--QDSGISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDN 781
Cdd:COG0265    159 INLAKRVVEQLieTGRVRRGW-LGVTIQPVTPElaEALGLPEPEGVLVARVEPGSPAAKAG-LRPGDVILAVDGKPVTS 235
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 734-783 1.48e-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: 45.20  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039746878  734 GSRPQDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKS 783
Cdd:cd23063     18 RGEVKVSPNTKTTGIFIKGIIPDSPAHKCGRLKVGDRILSVNGNDVRNST 67
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
 1371-1426 1.65e-05

PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CARD11, CARD14, and related domains. CARD11 (also known as CARD-containing MAGUK protein 1, CARMA1, Bimp3) and CARD14 (also known as CARD-containing MAGUK protein 2, CARMA2, Bimp2) belong to the CARD-containing membrane-associated guanylate kinase (MAGUK) protein family. They play several crucial biological functions, including regulation of immune response and inflammation. The CARD11-Bcl10-MALT1 (CBM) complex bridges T cell receptor signaling to the canonical IkappaB kinase (IKK)/NF-kappaB pathway. CARD14 can form an analogous biochemical complex to activate NF-kappaB during specialized immunity. The CBM complex of CARD14/CARMA2 may bind with TRAF6 and get involved in IL-17 pathways in keratinocytes. The preponderance of protein interactions occurs through the N-terminal half of CARD11 that includes the CARD, LATCH, and coiled-coil domains; the C-terminal PDZ-SH3-MAGUK region binds the adhesion and degranulation-promoting adapter protein (ADAP) and aryl hydrocarbon receptor interacting protein (AIP). 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 CARD11 and CARD14-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: 467218 [Multi-domain]  Cd Length: 75  Bit Score: 44.56  E-value: 1.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1371 GISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNG--------INLRSATEQQARLIIGQ 1426
Cdd:cd06736     12 QITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGcirgerqsVSLEDCTKEEAHWTLQR 75
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1359-1420 1.70e-05

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: 44.94  E-value: 1.70e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1359 RHVKVQKG-SEPLGISIVSGEKGG-----VYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06679      1 KTVTIKKEpSESLGISVAGGRGSRrgdlpIYVTNVQPDGCLGRDGrIKKGDVLLSINGISLTNLSHSEA 69
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
228-501 1.77e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  228 TLHSRLLSDQTQLKDDVDMLRRENGKLRRErnlLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAM 307
Cdd:COG4372     24 ILIAALSEQLRKALFELDKLQEELEQLREE---LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  308 DKLEVVKKDYDALRKRYSEkvamHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAI-QLQHQCALSLRRFETIHHELSKA 386
Cdd:COG4372    101 EELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELkELEEQLESLQEELAALEQELQAL 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  387 TAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSE 466
Cdd:COG4372    177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1039746878  467 KKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQ 501
Cdd:COG4372    257 LKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 640-711 1.78e-05

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: 45.29  E-value: 1.78e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  640 LGFDMAEGVNE----PCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 711
Cdd:cd06701     17 LGISIRGGAKGhagnPLDPTDEGIFISKINPDGAAarDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTLLV 94
PDZ_neurabin-like cd06790
PDZ domain of neurabin-1 and neurabin-2, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1361-1420 2.02e-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: 2.02e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1361 VKVQKGSEPLGISIV-------SG-EKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06790      5 VELEKGSEGLGISIIgmgvgadAGlEKLGIFVKTVTEGGAAQRDGrIQVNDQIVEVDGISLVGVTQAFA 73
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 144-573 2.24e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 49.44  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  144 DTVENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ------HTNALK--- 214
Cdd:pfam10174  254 DEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQnsdckqHIEVLKesl 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  215 -------------------RCEE----VAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLrrerNLLQQSWEDM-KR 270
Cdd:pfam10174  334 takeqraailqtevdalrlRLEEkesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKI----NVLQKKIENLqEQ 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  271 LREEDqKEIGDLRaQQQQVLKHNGSSEilnklyDTAMDKLEVVKKDYDALRKRYSEKVAMHNSD-LSRLEQLGEENQRLQ 349
Cdd:pfam10174  410 LRDKD-KQLAGLK-ERVKSLQTDSSNT------DTALTTLEEALSEKERIIERLKEQREREDRErLEELESLKKENKDLK 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  350 KQTEML----TQQRDTAIQLQHQcALSLRRfetihhELSKATAQNKDLQWEMELLQSELTELRSkQVKTAKESEKYKEER 425
Cdd:pfam10174  482 EKVSALqpelTEKESSLIDLKEH-ASSLAS------SGLKKDSKLKSLEIAVEQKKEECSKLEN-QLKKAHNAEEAVRTN 553

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  426 DAVYSEYKLIMSERDQVISELDKLQTEVE-----LAESKLKSSTSEKKAASEEMEALRQIKDTVT-----------MDAG 489
Cdd:pfam10174  554 PEINDRIRLLEQEVARYKEESGKAQAEVErllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKkvanikhgqqeMKKK 633

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  490 RANKEVEILR-----------KQCKALCQELKEALQEADVAKCRrdwaFQERDKIVAERDSIRTlcdNLRRERDRAVSEL 558
Cdd:pfam10174  634 GAQLLEEARRrednladnsqqLQLEELMGALEKTRQELDATKAR----LSSTQQSLAEKDGHLT---NLRAERRKQLEEI 706

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1039746878  559 AE-----------------ALRSLDDTRKQKN 573
Cdd:pfam10174  707 LEmkqeallaaisekdaniALLELSSSKKKKT 738
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
151-562 2.36e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  151 IQLRLMTRERNELRKRLAfathgaTFDKRpYHRLNPDYERLKiqcvRAMSDLQSLQNQHTNALKRCEEVAKETDFyhtlh 230
Cdd:COG4717    125 LQLLPLYQELEALEAELA------ELPER-LEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSL----- 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  231 sRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRlrEEDQKEIGDLRAQQQQVLKHN-------GSSEILNKLY 303
Cdd:COG4717    189 -ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--ELEQLENELEAAALEERLKEArlllliaAALLALLGLG 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  304 DTAMDKLEVVKK----------DYDALRKRYSEKvamHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSL 373
Cdd:COG4717    266 GSLLSLILTIAGvlflvlgllaLLFLLLAREKAS---LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  374 -RRFETIHHELSKATAQNKDLQWEM------ELLQ----SELTELRSKqVKTAKESEKYKEERDAVYSEYKLIMSERDQV 442
Cdd:COG4717    343 lDRIEELQELLREAEELEEELQLEEleqeiaALLAeagvEDEEELRAA-LEQAEEYQELKEELEELEEQLEELLGELEEL 421

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  443 ISELDKLQTEVELAESKlksstSEKKAASEEMEALRQikdtvtmDAGRANKEVEILRKQckalcQELKEALQEADVAKCR 522
Cdd:COG4717    422 LEALDEEELEEELEELE-----EELEELEEELEELRE-------ELAELEAELEQLEED-----GELAELLQELEELKAE 484

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1039746878  523 RDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEAL 562
Cdd:COG4717    485 LRELAEEWAALKLALELLEEAREEYREERLPPVLERASEY 524
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 1362-1592 2.46e-05

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


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 49.14  E-value: 2.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1362 KVQKGSepLGISI--VSGEK---------GGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQ---ARLIIGqq 1427
Cdd:TIGR02037  230 KVKRGW--LGVTIqeVTSDLakslglekqRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRraiGTLKPG-- 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1428 cDTITILAQYNPHIHQLNshsrssshldpaatphSTLQGSSAGTPEhpsvidplmEQDEGPGTPPAKQSAsstrsvgDTT 1507
Cdd:TIGR02037  306 -KKVTLGILRKGKEKTIT----------------VTLGASPEEQAS---------SSNPFLGLTVANLSP-------EIR 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1508 KKTPDPrivfikksqldlgvhlcgGNLHGVFVAEVEDDSPAKGPdGLVPGDLILEYGSLDMRSrtVEDVY--VEMLKPKD 1585
Cdd:TIGR02037  353 KELRLK------------------GDVKGVVVTKVVSGSPAARA-GLQPGDVILSVNQQPVSS--VAELRkvLARAKKGG 411


                   ....*..
gi 1039746878 1586 SLRLKVQ 1592
Cdd:TIGR02037  412 RVALLIL 418
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 1361-1425 2.47e-05

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: 44.65  E-value: 2.47e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878 1361 VKVQKGSEPLGISIvSGEKG------GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIG 1425
Cdd:cd06758      5 MHLLKEKGGLGIQI-TGGKGskrgdiGIFVAGVEEGGSADRDGrLKKGDELLMINGQSLIGLSHQEAVAILR 75
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 751-800 2.68e-05

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 43.29  E-value: 2.68e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039746878  751 AAVVPGSPAAKEGsLAVGDRIVAINGIALdnKSLNECESLLRSCQDSLTL 800
Cdd:pfam17820    3 TAVVPGSPAERAG-LRVGDVILAVNGKPV--RSLEDVARLLQGSAGESVT 49
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1359-1424 2.73e-05

PDZ domain 6 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 6 of multi-PDZ-domain protein 1 (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 PDZ6 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 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: 467158 [Multi-domain]  Cd Length: 87  Bit Score: 44.17  E-value: 2.73e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1359 RHVKVQKGSEPLGISIVSGEKG-GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06670      5 RTITIVKGNSSLGITVSADKDGnGCIVKSIIHGGAVSRDGrISVGDFIVSINNESLRNVTNAQARAIL 72
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 741-793 2.85e-05

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


Pssm-ID: 467172 [Multi-domain]  Cd Length: 87  Bit Score: 44.16  E-value: 2.85e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  741 GISL-------ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd06684     16 GITLststhrnKQVIVIDSIKPASIADRCGALHVGDHILSIDGTSVEHCSLAEATQLLAS 75
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 222-557 3.19e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  222 ETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQvlkhngSSEILNK 301
Cdd:TIGR00618  174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ------SHAYLTQ 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  302 LYDTAMDKlevvkkdyDALRKRYSEKVAmhnsdlsRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRF--ETI 379
Cdd:TIGR00618  248 KREAQEEQ--------LKKQQLLKQLRA-------RIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQqaQRI 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  380 HHEL-SKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAvySEYKLIMSERDQVISE---LDKLQTEVEL 455
Cdd:TIGR00618  313 HTELqSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH--EVATSIREISCQQHTLtqhIHTLQQQKTT 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  456 AESKLKSSTSEKKAASEE---MEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDK 532
Cdd:TIGR00618  391 LTQKLQSLCKELDILQREqatIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470

                          330       340
                   ....*....|....*....|....*
gi 1039746878  533 IVAERDSIRTLCdnLRRERDRAVSE 557
Cdd:TIGR00618  471 REQQLQTKEQIH--LQETRKKAVVL 493
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
371-600 3.27e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  371 LSLRRFETIHHELSKATaqnKDLQWEMELLQSELTelRSKQVKTA-KESEKYKEErdaVYSEYKLIMSERDQVISELDKL 449
Cdd:PRK03918   155 LGLDDYENAYKNLGEVI---KEIKRRIERLEKFIK--RTENIEELiKEKEKELEE---VLREINEISSELPELREELEKL 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  450 QTEV--------ELAESKLKSSTSEKKAASEEmEALRQIKDTVTmdagRANKEVEILRKQCKALcQELKEALQEADVAKc 521
Cdd:PRK03918   227 EKEVkeleelkeEIEELEKELESLEGSKRKLE-EKIRELEERIE----ELKKEIEELEEKVKEL-KELKEKAEEYIKLS- 299

                          170       180       190       200       210       220       230       240
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gi 1039746878  522 rrdwafQERDKIVAERDSIRTLCDNLRRER---DRAVSELAEALRSLDDTRKQKNDVSRELKELNSCVHREQMECQLEKE 598
Cdd:PRK03918   300 ------EFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373


                   ..
gi 1039746878  599 AR 600
Cdd:PRK03918   374 LE 375
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 1359-1423 3.27e-05

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467194 [Multi-domain]  Cd Length: 76  Bit Score: 43.78  E-value: 3.27e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878 1359 RHVKVQKGSEPLGISIvSGEKGGVyVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSAT-EQQARLI 1423
Cdd:cd06710      1 RTVEIARGRAGYGFTI-SGQAPCV-LSCVVRGSPADVAGLKAGDQILAVNGINVSKAShEDVVKLI 64
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 640-711 3.38e-05

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


Pssm-ID: 467273 [Multi-domain]  Cd Length: 80  Bit Score: 43.88  E-value: 3.38e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  640 LGFDMAEGvnepcfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 711
Cdd:cd23060     12 LGFSLVGG------EGGSGIFVKSISPGGVAdrDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 1361-1423 3.49e-05

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: 43.92  E-value: 3.49e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1361 VKVQKGSEPLGISIVSGEKggVYVSKVTLGSIAHQAGLEYGDQLLEFNGINL-RSATEQQARLI 1423
Cdd:cd06711      3 ITIQRGKDGFGFTICDDSP--VRVQAVDPGGPAEQAGLQQGDTVLQINGQPVeRSKCVELAHAI 64
PDZ5_INAD-like cd23066
PDZ domain 5 of inactivation no after potential D (INAD), and related domains; PDZ (PSD-95 ...
 747-804 3.56e-05

PDZ domain 5 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 5 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 PDZ45 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 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: 467279 [Multi-domain]  Cd Length: 80  Bit Score: 43.65  E-value: 3.56e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  747 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 804
Cdd:cd23066     23 GCTIADLLPGGYAEIDGKLQKGDIITKFNGDALSGLPFQVCYALFKGANGKISLEVTR 80
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 745-800 3.97e-05

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: 43.80  E-value: 3.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  745 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIalDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06716     30 DTGIYVSEVDPNSIAAKDGRIREGDQILQINGV--DVQNREEAIALLSEEEKSITL 83
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 744-800 4.04e-05

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: 44.02  E-value: 4.04e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  744 LENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd23072     28 LDLGIFISSITPGGPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTL 84
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 625-716 4.16e-05

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467180 [Multi-domain]  Cd Length: 92  Bit Score: 43.92  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  625 VVEFERETEdidlKALGFDMAEGVNEPCFpgDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd06694      4 IVTLKKDPQ----KGLGFTIVGGENSGSL--DLGIFVKSIIPGGPAdkDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQN 77

                           90
                   ....*....|....
gi 1039746878  703 GEGAINMVVRRRKS 716
Cdd:cd06694     78 APDKVELIISQPKS 91
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 640-712 4.18e-05

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 43.81  E-value: 4.18e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  640 LGFDMAEGVNEpcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 712
Cdd:pfam00595   12 LGFSLKGGSDQ----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1361-1433 4.43e-05

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: 43.48  E-value: 4.43e-05
                           10        20        30        40        50        60        70
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gi 1039746878 1361 VKVQKGSEPLGISIVSGEKGG-----VYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1433
Cdd:cd06676      2 ITLERGSDGLGFSIVGGFGSPhgdlpIYVKTVFEKGAAAEDGrLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTL 80
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 711-802 4.51e-05

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: 43.79  E-value: 4.51e-05
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gi 1039746878  711 VRRRKSLGGkvvtpLHINLSGQKGSRPQDSGISLengVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESL 790
Cdd:cd06695      4 VKLTKGSSG-----LGFSFLGGENNSPEDPFSGL---VRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSL 75

                           90
                   ....*....|..
gi 1039746878  791 LRSCQDSLTLSL 802
Cdd:cd06695     76 LRGAPPEVTLLL 87
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1516-1592 4.54e-05

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: 43.78  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1516 VFIKKSQLDLGVHLCGGNLH----------GVFVAEVEDDSPAkGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKD 1585
Cdd:cd06702      3 IHLVKAGGPLGLSIVGGSDHsshpfgvdepGIFISKVIPDGAA-AKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPGQ 81


                   ....*..
gi 1039746878 1586 SLRLKVQ 1592
Cdd:cd06702     82 EIKLLVR 88
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 749-803 4.75e-05

PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 43.94  E-value: 4.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  749 YAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd23070     39 HVSAVLEGGAADKAG-VRKGDRILEVNGVNVEGATHKQVVDLIKSGGDELTLTVI 92
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 745-800 4.89e-05

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: 44.16  E-value: 4.89e-05
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gi 1039746878  745 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALD-NKSLNECESLLRSCQDSLTL 800
Cdd:cd06689     42 ELGIFVQEIQPGSVAARDGRLKENDQILAINGQPLDqSISHQQAIAILQQAKGSVEL 98
PDZ4_PDZD2-PDZ2_hPro-IL-16-like cd06760
PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 ...
 1360-1426 4.94e-05

PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 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 4 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 second PDZ domain (PDZ2) 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 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: 467241 [Multi-domain]  Cd Length: 90  Bit Score: 43.80  E-value: 4.94e-05
                           10        20        30        40        50        60        70
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gi 1039746878 1360 HVKVQKgsEP---LGISIVS----GEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1426
Cdd:cd06760      6 EVTLNK--EPgvgLGIGLCClpleNDIPGIFIHHLSPGSVAHMDGrLRRGDQILEINGTSLRNVTLNEAYAILSQ 78
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1383-1434 5.23e-05

PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 43.94  E-value: 5.23e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1383 YVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII--GQQCDTITIL 1434
Cdd:cd23070     39 HVSAVLEGGAADKAGVRKGDRILEVNGVNVEGATHKQVVDLIksGGDELTLTVI 92
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 417-589 5.25e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 46.58  E-value: 5.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  417 ESEKYKEERDAVySEYKLIMSERDQVISELDKLQTEV-----ELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRA 491
Cdd:cd07596      2 EDQEFEEAKDYI-LKLEEQLKKLSKQAQRLVKRRRELgsalgEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  492 NKEVeilRKQCKALCQELKEALQEADVAKCrrdwAFQERDKIVAERDSIRTLCDNLRRERDRAVS-------ELAEALRS 564
Cdd:cd07596     81 EAQA---NQELVKLLEPLKEYLRYCQAVKE----TLDDRADALLTLQSLKKDLASKKAQLEKLKAapgikpaKVEELEEE 153

                          170       180
                   ....*....|....*....|....*
gi 1039746878  565 LDDTRKQKNDVSRELKELNSCVHRE 589
Cdd:cd07596    154 LEEAESALEEARKRYEEISERLKEE 178
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1359-1434 5.36e-05

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: 43.75  E-value: 5.36e-05
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gi 1039746878 1359 RHVKVQKG-SEPLGISIVSGEKG-----------GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIG 1425
Cdd:cd06701      5 QELTIVKEpGEKLGISIRGGAKGhagnpldptdeGIFISKINPDGAAARDGrLKVGQRILEVNGQSLLGATHQEAVRILR 84


                   ....*....
gi 1039746878 1426 QQCDTITIL 1434
Cdd:cd06701     85 SVGDTLTLL 93
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1360-1433 5.66e-05

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: 43.77  E-value: 5.66e-05
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gi 1039746878 1360 HVKVQKG-SEPLGISIV---SGEKG--GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSA-TEQQARLIIGQQCDTI 1431
Cdd:cd06689     17 YIELEKPeSGGLGFSVVglkSENRGelGIFVQEIQPGSVAARDGrLKENDQILAINGQPLDQSiSHQQAIAILQQAKGSV 96


                   ..
gi 1039746878 1432 TI 1433
Cdd:cd06689     97 EL 98
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 625-712 6.06e-05

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: 43.20  E-value: 6.06e-05
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gi 1039746878  625 VVEFERETEdidlkALGFDMAEGVNEpcfpgDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd06796      4 VVELPKTEE-----GLGFNVMGGKEQ-----NSPIYISRIIPGGVADrhGGLKRGDQLLSVNGVSVEGEHHEKAVELLKA 73

                           90
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gi 1039746878  703 GEGAINMVVR 712
Cdd:cd06796     74 AQGSVKLVVR 83
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 658-713 6.12e-05

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: 43.19  E-value: 6.12e-05
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gi 1039746878  658 GIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKaLLNGEGAINMVVRR 713
Cdd:cd10833     27 GIFVSKVEEGSAAErAGLCVGDKITEVNGVSLENITMSSAVK-VLTGSNRLRMVVRR 82
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 735-803 6.30e-05

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: 43.44  E-value: 6.30e-05
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gi 1039746878  735 SRPQDSGISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKslNECESLLRSCQ--DSLTLSLL 803
Cdd:cd06779     14 LLAKELGLPVNRGVLVAEVIPGSPAAKAG-LKEGDVILSVNGKPVTSF--NDLRAALDTKKpgDSLNLTIL 81
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 339-581 6.54e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 6.54e-05
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gi 1039746878  339 EQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKES 418
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  419 EKYKEE-RDAVYSEYKLIMSERDQVISEldklQTEVELAESKLKSSTSEKKAASEEMEALRQIKdtvtmdagranKEVEI 497
Cdd:COG4942    100 EAQKEElAELLRALYRLGRQPPLALLLS----PEDFLDAVRRLQYLKYLAPARREQAEELRADL-----------AELAA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  498 LRKQCKALCQELKEALQEADvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSR 577
Cdd:COG4942    165 LRAELEAERAELEALLAELE----------EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234


                   ....
gi 1039746878  578 ELKE 581
Cdd:COG4942    235 EAAA 238
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 640-713 6.71e-05

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: 43.48  E-value: 6.71e-05
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gi 1039746878  640 LGFDMAEGVNE-----PCFPGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 713
Cdd:cd10822     15 LGFSIGGGIDQdpsknPFSYTDKGIYVTRVSEGGPAEkAGLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKPVLRMLVTR 94
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1361-1433 7.07e-05

PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 43.06  E-value: 7.07e-05
                           10        20        30        40        50        60        70
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gi 1039746878 1361 VKVQKGSEPLGISIVSGEKGG--VYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1433
Cdd:cd06683      6 VELKRYGGPLGITISGTEEPFdpIVISGLTEGGLAERTGaIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTL 81
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 1380-1417 7.32e-05

circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of HtrA family serine proteases including human HtrA1, HtrA2 (mitochondrial), HtrA3, and HtrA4, and related domains. These proteases are key enzymes associated with pregnancy. Their diverse biological functions include cell growth proliferation, migration and apoptosis. They are also implicated in disorders including Alzheimer's, Parkinson's, arthritis and cancer. HtrA1 (also known as high-temperature requirement A serine peptidase 1, L56, and serine protease 11) substrates include extracellular matrix proteins, proteoglycans, and insulin-like growth factor (IGF)-binding proteins. HtrA1 also inhibits signaling by members of the transforming growth factor beta (TGF-beta) family. 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 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 HtrA-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: 467624 [Multi-domain]  Cd Length: 98  Bit Score: 43.26  E-value: 7.32e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1039746878 1380 GGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATE 1417
Cdd:cd06785     31 SGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSD 68
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 1359-1420 7.49e-05

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: 43.40  E-value: 7.49e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1359 RHVKVQKGSEPLGISIVS-----GEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd23058      6 LHIQLKKGPEGLGFSITSrdnptGGSGPIYIKNILPKGAAIQDGrLKAGDRLLEVNGVDVTGKTQEEV 73
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 659-713 7.62e-05

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: 42.90  E-value: 7.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  659 IFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 713
Cdd:cd23068     27 LSIQKVNPGSPADKAgLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 733-779 7.69e-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: 43.04  E-value: 7.69e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1039746878  733 KGSRPQDSGIslengvYAAAVVPGSPAAKEGSLAVGDRIVAINGIAL 779
Cdd:cd06789     23 KGAGQDKLGI------YIKSVVKGGAADLDGRLQAGDQLLSVDGHSL 63
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 753-804 7.77e-05

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: 42.90  E-value: 7.77e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  753 VVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 804
Cdd:cd23068     32 VNPGSPADKAG-LRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 1359-1434 7.85e-05

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: 42.81  E-value: 7.85e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1359 RHVKVQKGSEPLGISiVSGEKG--GVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:cd06768      1 RLCHLVKGPEGYGFN-LHAEKGrpGHFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQVVEKIKASGNQVTLL 77
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 748-807 8.02e-05

PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 43.00  E-value: 8.02e-05
                           10        20        30        40        50        60
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gi 1039746878  748 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 807
Cdd:cd06799     25 IVVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQGPIT---FKLIP 81
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 655-700 8.76e-05

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: 42.74  E-value: 8.76e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039746878  655 GDCGIFVTKVDKGSI--ADGRLRVNDWLLRINDVDLINKDKKQAIKAL 700
Cdd:cd06717     24 GDGGIYVGSIMKGGAvaADGRIEPGDMILQVNDISFENMSNDDAVRVL 71
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 1361-1424 9.00e-05

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: 43.05  E-value: 9.00e-05
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gi 1039746878 1361 VKVQKGSEPLGISIVSGEK-----GGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06690      6 VELERGPKGLGLGLIDGLHtplrsPGIYIRTLVPDSPAARDGrLRLGDRILAVNGTSLVGADYQSAMDLI 75
PDZ7_GRIP1-2-like cd06685
PDZ domain 7 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1360-1436 9.26e-05

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: 42.63  E-value: 9.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1360 HVKVQK--GSEPLGISIVSG--EKGgVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1435
Cdd:cd06685      5 KVTLYKdsDTEDFGFSVSDGlyEKG-VYVNAIRPGGPADLSGLQPYDRILQVNHVRTRDFDCCLVVPLIAESGDKLELVV 83


                   .
gi 1039746878 1436 Q 1436
Cdd:cd06685     84 S 84
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 314-630 9.69e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.42  E-value: 9.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  314 KKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIH------------H 381
Cdd:pfam15921   73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSqedlrnqlqntvH 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  382 ELSKATAQNKDL---------QWEMELLQSE--LTELRSKQVKTAKESEKYKEERDAVYS-EYKLIMSERDQVISELDK- 448
Cdd:pfam15921  153 ELEAAKCLKEDMledsntqieQLRKMMLSHEgvLQEIRSILVDFEEASGKKIYEHDSMSTmHFRSLGSAISKILRELDTe 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  449 ---LQTEVELAESKLKSSTSEKKAASE-------------------EMEALRQIKDTVTMDAGRANKEVEILRKQCKA-- 504
Cdd:pfam15921  233 isyLKGRIFPVEDQLEALKSESQNKIElllqqhqdrieqlisehevEITGLTEKASSARSQANSIQSQLEIIQEQARNqn 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  505 ---LCQeLKEAlqEADVAKCRRDWAFQER---DKIvaerdsirtlcDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRE 578
Cdd:pfam15921  313 smyMRQ-LSDL--ESTVSQLRSELREAKRmyeDKI-----------EELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  579 LKELNSCVHREQMECQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFER 630
Cdd:pfam15921  379 LQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQR 430
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 748-800 9.75e-05

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: 42.26  E-value: 9.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  748 VYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06744     21 VYIESVDPGSAAERAG-LKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMPTL 72
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 727-803 1.01e-04

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: 42.69  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  727 INLSGQKG-------SRPQDSGIslengvYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQdSLT 799
Cdd:cd06738      7 ISLVGTRGlgcsissGPTQKPGI------FISNVKPGSLAEEVG-LEVGDQIVEVNGTSFTNVDHKEAVMALKSSR-HLT 78


                   ....
gi 1039746878  800 LSLL 803
Cdd:cd06738     79 ITVR 82
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 654-713 1.04e-04

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: 43.01  E-value: 1.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  654 PGDCGIFVTKV-DKG-SIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGE--GAINMVVRR 713
Cdd:cd23058     29 GGSGPIYIKNIlPKGaAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKlgGTVSLVVSR 92
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 1359-1433 1.07e-04

PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1, and related domains. MPP1 (also known as MAGUK p55 subfamily member 1, erythrocyte membrane protein p55, EMP55) is a membrane-associated guanylate kinase (MAGUK)-like protein which forms a complex with protein 4.1 and glycophorin C (GPC) at the cytoplasmic face of the plasma membrane; this complex is essential for cytoskeleton-membrane linkage in erythrocytes and many non-erythroid cells, and participates in the determination of membrane stability and cell shape. MPP1, by interacting with various scaffold proteins and cytoskeletal proteins in the postsynaptic density, also plays an important role in organizing synaptic and non-synaptic structures. MPP1 is also a component of the Crumbs protein complex in the mammalian retina and may link the Usher protein network and the Crumbs protein complex. The MPP1 PDZ domain binding partners include GPC, ABCC4, and CADM1/Necl-2/SynCAM1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467266 [Multi-domain]  Cd Length: 81  Bit Score: 42.54  E-value: 1.07e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1359 RHVKVQKGS-EPLGISIVSGEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1433
Cdd:cd10830      1 RLVQFEKNTeEPMGITLKLNEKQSCIVARILHGGMIHRQGsLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVSL 77
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-479 1.10e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  253 KLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQvlkhngsseiLNKLYDTAMDKLEVVKKDYDALRKRysekvamhn 332
Cdd:COG4942     24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----------LERRIAALARRIRALEQELAALEAE--------- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  333 sdLSRLE-QLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSL----RRFETIHHELSKATAQNKDLQWEMELLQSELTEL 407
Cdd:COG4942     85 --LAELEkEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  408 RSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQ 479
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1361-1416 1.12e-04

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: 42.26  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878 1361 VKVQKGSEPLGISIVSgeKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSAT 1416
Cdd:cd06744      2 VRVYRGNGSFGFTLRG--HAPVYIESVDPGSAAERAGLKPGDRILFLNGLDVRNCS 55
PTZ00121 PTZ00121
MAEBL; Provisional
 179-600 1.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  179 RPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDfyhtlhsrllSDQTQLKDDVDMLRRENGKLRREr 258
Cdd:PTZ00121  1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE----------AKKAEEKKKADEAKKKAEEAKKA- 1317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  259 nllqqswEDMKRLREEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDALRKRYSE---------KVA 329
Cdd:PTZ00121  1318 -------DEAKKKAEEAKKKADAAKKKAEEAKK---AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEakkkadaakKKA 1387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  330 MHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQcALSLRRFEtihhELSKATAQNKdlqwemellQSELTELRS 409
Cdd:PTZ00121  1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK-AEEKKKAD----EAKKKAEEAK---------KADEAKKKA 1453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  410 KQVKTAKESEKYKEERDAVYSEYKliMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASE--------EMEALRQIK 481
Cdd:PTZ00121  1454 EEAKKAEEAKKKAEEAKKADEAKK--KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaeeakKADEAKKAE 1531

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  482 DTVTMDAGRANKEVEILRKQCKAlcQELKEALQEADVAKCRRDwafQERDKIVAERDSIRTLCDNLRRERDRAVSEL--- 558
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKA--EELKKAEEKKKAEEAKKA---EEDKNMALRKAEEAKKAEEARIEEVMKLYEEekk 1606

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1039746878  559 --AEALRSLDDTRKQKNDVSRELKELNSCvhrEQMECQLEKEAR 600
Cdd:PTZ00121  1607 mkAEEAKKAEEAKIKAEELKKAEEEKKKV---EQLKKKEAEEKK 1647
SH3_CAS cd11844
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins ...
 1612-1648 1.27e-04

Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes including migration, chemotaxis, apoptosis, differentiation, and progenitor cell function. They mediate the signaling of integrins at focal adhesions where they localize, and thus, regulate cell invasion and survival. Over-expression of these proteins is implicated in poor prognosis, increased metastasis, and resistance to chemotherapeutics in many cancers such as breast, lung, melanoma, and glioblastoma. CAS proteins have also been linked to the pathogenesis of inflammatory disorders, Alzheimer's, Parkinson's, and developmental defects. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Vertebrates contain four CAS proteins: BCAR1 (or p130Cas), NEDD9 (or HEF1), EFS (or SIN), and CASS4 (or HEPL). The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212778  Cd Length: 56  Bit Score: 41.56  E-value: 1.27e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1039746878 1612 RALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWM 1648
Cdd:cd11844      3 RALYDNVAESPDELAFRRGDILTVLEQNTAGLEGWWL 39
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 1361-1420 1.40e-04

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: 42.38  E-value: 1.40e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1361 VKVQKGSEPLGISIVSG------EKG----GVYVSKVT-LGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06715      5 VVLHRENGSLGFNIIGGrpcennQEGssseGIYVSKIVeNGPAADEGGLQVHDRIIEVNGKDLSKATHEEA 75
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 622-711 1.41e-04

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: 42.31  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  622 ETEVVEFERETEdidlkALGFDMAEGvnepcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKAL 700
Cdd:cd06767      2 EPRHVSIEKGSE-----PLGISIVSG-------ENGGIFVSSVTEGSLAHqAGLEYGDQLLEVNGINLRNATEQQAALIL 69

                           90
                   ....*....|.
gi 1039746878  701 LNGEGAINMVV 711
Cdd:cd06767     70 RQCGDTITMLV 80
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 747-803 1.51e-04

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: 42.17  E-value: 1.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  747 GVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd06729     24 GIFVAGVQEGSPAEKQG-LQEGDQILKVNGVDFRNLTREEAVLFLLDLPKGEEVTIL 79
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 239-515 1.53e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 46.61  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  239 QLKDDVDMLRRENGKLRRERnllqqswEDMKRLREEDQKEIGDLRAQQQQvlkhngsseiLNKLYDTAmdklEVVKKDYD 318
Cdd:pfam05622   63 LLQKQLEQLQEENFRLETAR-------DDYRIKCEELEKEVLELQHRNEE----------LTSLAEEA----QALKDEMD 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  319 ALRKRySEKVAMHNSDLS----RLEQLGEenqrLQKQTEMLtqQRDTAIQLQHQCALslrrfetiHHELSKATA---QNK 391
Cdd:pfam05622  122 ILRES-SDKVKKLEATVEtykkKLEDLGD----LRRQVKLL--EERNAEYMQRTLQL--------EEELKKANAlrgQLE 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  392 DLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKL------QTEVELAESKLKSSTS 465
Cdd:pfam05622  187 TYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEELrcaqlqQAELSQADALLSPSSD 266

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039746878  466 EKKAASEEMEALrQIKDTVTmdagRANKEVEILRKQCKALCQELKEALQE 515
Cdd:pfam05622  267 PGDNLAAEIMPA-EIREKLI----RLQHENKMLRLGQEGSYRERLTELQQ 311
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
276-592 1.55e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  276 QKEIGDLRAQQQQVlkhNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEML 355
Cdd:COG4372     44 QEELEQLREELEQA---REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  356 TQQRDTAIQlqhqcalslrrfetihhELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEER-----DAVYS 430
Cdd:COG4372    121 QKERQDLEQ-----------------QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELqalseAEAEQ 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  431 EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGR--ANKEVEILRKQCKALCQE 508
Cdd:COG4372    184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEleEDKEELLEEVILKEIEEL 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  509 LKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELNSCVHR 588
Cdd:COG4372    264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343


                   ....
gi 1039746878  589 EQME 592
Cdd:COG4372    344 QLLL 347
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 410-646 1.66e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.89  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  410 KQVKTAKESEKYKEERDAVYSEYKLIMSER----DQVISELDKLQTEVELAESKLKSstsEKKAASEEMEALRQIKDTVT 485
Cdd:pfam02463  145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEAlkklIEETENLAELIIDLEELKLQELK---LKEQAKKALEYYQLKEKLEL 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  486 MDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRdwaFQERDKIVAERDSIRTLC----DNLRRERDRAVSELAEA 561
Cdd:pfam02463  222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE---IEKEEEKLAQVLKENKEEekekKLQEEELKLLAKEEEEL 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  562 LRSLDDTRKQKNDVSRELKELNSCVHREQMECQLEKEARFRQLMAHSSHDSAIdtdsmEWETEVVEFERETEDIDLKALG 641
Cdd:pfam02463  299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKR-----EAEEEEEEELEKLQEKLEQLEE 373


                   ....*
gi 1039746878  642 FDMAE 646
Cdd:pfam02463  374 ELLAK 378
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 1513-1582 1.68e-04

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: 42.31  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1513 PRIVFIKK-SQLDLGVHLCGGN-----------LHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVyVEM 1580
Cdd:cd06671      2 PRRVELWRePGKSLGISIVGGRvmgsrlsngeeIRGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEA-VEA 80


                   ..
gi 1039746878 1581 LK 1582
Cdd:cd06671     81 IR 82
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
751-786 1.76e-04

Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 46.35  E-value: 1.76e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1039746878  751 AAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNE 786
Cdd:COG3975    499 TSVLWGSPAYKAG-LSAGDELLAIDGLRVTADNLDD 533
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 748-800 1.91e-04

PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467215 [Multi-domain]  Cd Length: 85  Bit Score: 41.83  E-value: 1.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  748 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL----RSCQDSLTL 800
Cdd:cd06733     27 VSIGAIVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKVVDLMgnaaRNGQVNLTV 83
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 751-781 1.97e-04

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 45.85  E-value: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1039746878  751 AAVVPGSPAAKEGsLAVGDRIVAINGIALDN 781
Cdd:COG0750    133 GEVVPGSPAAKAG-LQPGDRIVAINGQPVTS 162
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 658-712 2.04e-04

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: 41.54  E-value: 2.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  658 GIFVTKVDKGSIAD--GrLRVNDWLLRINDVDLINKDKKQAIKALLnGEGAINMVVR 712
Cdd:cd06738     28 GIFISNVKPGSLAEevG-LEVGDQIVEVNGTSFTNVDHKEAVMALK-SSRHLTITVR 82
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 746-803 2.07e-04

PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP5, Drosophila Stardust, and related domains. MPP5 (also known as MAGUK p55 subfamily member 1, protein associated with Lin-7 1 or PALS1) and Drosophila Stardust are membrane-associated guanylate kinase (MAGUK)-like proteins that serve as signaling and scaffolding proteins, linking different proteins critical to the formation and maintenance of tight junctions (TJ) and apical-basal polarity. Apical-basal polarity determinants cluster in complexes; in particular, the Crumbs complex (Crb, MPP5, and PATJ) and the PAR/aPKC-complex (PAR-3, PAR-6, aPKC) determine the apical plasma membrane domain. Within the Crumbs complex, Crb is stabilized in the plasma membrane by MPP5, which in turn recruits PATJ and Lin-7 to the complex. MPP5 also links the Crumbs complex with the PAR/aPKC-complex. The Drosophila homolog of the Crumbs complex is the (CRB)-Stardust (Sdt)-Discs Lost (Dlt) complex. MPP5 also acts as an interaction partner for SARS-CoV envelope protein E, which results in delayed formation of TJs and dysregulation of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP5-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467259 [Multi-domain]  Cd Length: 79  Bit Score: 41.56  E-value: 2.07e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  746 NGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 803
Cdd:cd06798     21 DSVIISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFLLI 78
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 ...
 1361-1424 2.14e-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: 2.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1361 VKVQKGSEPLGISIvSGEKGG----VYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06672      4 IELEKGSSGLGLSL-AGNKDRsrmsVFVVGIDPDGAAGKDGrIQVGDELLEINGQVLYGRSHLNASAII 71
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 747-802 2.18e-04

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: 41.58  E-value: 2.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  747 GVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQdSLTLSL 802
Cdd:cd06740     28 GIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKILRVSK-KLVLSV 81
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 152-569 2.39e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.48  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  152 QLRLMTRERNELRKRLAfathGATFDKRPYHRL----------------NPDYERLKIQCVRAMSDLQSLQNQHTNALKR 215
Cdd:COG3096    786 RLEELRAERDELAEQYA----KASFDVQKLQRLhqafsqfvgghlavafAPDPEAELAALRQRRSELERELAQHRAQEQQ 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  216 CEEVAketdfyhtlhsrllsdqTQLKDDVDMLRRengkLRRERNLLQQswEDMKRLREEDQKEIGDLRAQQQQVLKHNGS 295
Cdd:COG3096    862 LRQQL-----------------DQLKEQLQLLNK----LLPQANLLAD--ETLADRLEELREELDAAQEAQAFIQQHGKA 918

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  296 SEILNKLYDTamdkLEVVKKDYDALRKRYsekvamhnsdlsrlEQLGEENQRLQKQTEMLTQ--QRDTAIQLQHQCALsl 373
Cdd:COG3096    919 LAQLEPLVAV----LQSDPEQFEQLQADY--------------LQAKEQQRRLKQQIFALSEvvQRRPHFSYEDAVGL-- 978

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  374 rrfetihheLSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYklimSERDQVISELdklqtEV 453
Cdd:COG3096    979 ---------LGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR----DAKQQTLQEL-----EQ 1040

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  454 ELAESKLKSSTSEKKAASEEMealRQIKDTVTMDAGRANkEVEILRKQCKALCQELKEALQEADvakcrRDWaFQERDKI 533
Cdd:COG3096   1041 ELEELGVQADAEAEERARIRR---DELHEELSQNRSRRS-QLEKQLTRCEAEMDSLQKRLRKAE-----RDY-KQEREQV 1110

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1039746878  534 VAERDSirtLCDNLRRERDRAV------SEL----AEALRSLDDTR 569
Cdd:COG3096   1111 VQAKAG---WCAVLRLARDNDVerrlhrRELaylsADELRSMSDKA 1153
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 755-800 2.40e-04

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: 41.41  E-value: 2.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1039746878  755 PGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06801     34 KGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTL 79
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 749-805 2.42e-04

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: 42.20  E-value: 2.42e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  749 YAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 805
Cdd:cd06746     45 YLESVDPGGVADKAG-LKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVLKVVTV 100
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1370-1428 2.47e-04

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 41.50  E-value: 2.47e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1370 LGISIVSGEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIgQQC 1428
Cdd:cd06667     12 LGFGIVGGKSTGVVVKTILPGGVADRDGrLRSGDHILQIGDTNLRGMGSEQVAQVL-RQC 70
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 1383-1434 2.47e-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: 40.59  E-value: 2.47e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039746878 1383 YVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSaTEQQARLIIGQQCDTITIL 1434
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRS-LEDVARLLQGSAGESVTLT 51
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 1379-1433 2.51e-04

circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. 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 BsHtrA-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: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 41.85  E-value: 2.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878 1379 KGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1433
Cdd:cd06781     29 NKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDTVKV 83
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 722-793 2.54e-04

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: 41.48  E-value: 2.54e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  722 VTPLHINLSGqkGSRPQDsgislenGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd06755     11 ESPLHFSLLG--GSEKGF-------GIFVSKVEKGSKAAEAG-LKRGDQILEVNGQNFENITLKKALEILRN 72
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 1366-1420 2.55e-04

PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This INAD-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467276 [Multi-domain]  Cd Length: 87  Bit Score: 41.73  E-value: 2.55e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1366 GSEPLGISIVSGE--------KGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd23063      8 EKKSFGICIVRGEvkvspntkTTGIFIKGIIPDSPAHKCGrLKVGDRILSVNGNDVRNSTEQAA 71
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 658-713 2.66e-04

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: 41.48  E-value: 2.66e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  658 GIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKaLLNGEGAINMVVRR 713
Cdd:cd06741     27 GIYVTGVDPGSVAENAgLKVGDQILEVNGRSFLDITHDEAVK-ILKSSKHLIMTVKD 82
PTZ00121 PTZ00121
MAEBL; Provisional
 212-650 2.74e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  212 ALKRCEEVAKETDfyhtlhsrLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWE-----DMKRLREEDQK-EIGDLRAQ 285
Cdd:PTZ00121  1396 AKKKAEEDKKKAD--------ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkadEAKKKAEEAKKaEEAKKKAE 1467

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  286 QQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKvamHNSDLSRLEQLGEENQRLQKQTEmlTQQRDTAIQL 365
Cdd:PTZ00121  1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK---KKADEAKKAEEAKKADEAKKAEE--AKKADEAKKA 1542

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  366 QH-QCALSLRRFEtihhELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKEseKYKEERDAVYSEYKLIMSERDQVIS 444
Cdd:PTZ00121  1543 EEkKKADELKKAE----ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAE 1616

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  445 ELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKdtvtmdagRANKEVEILRKQCKALCQELKEALQEADVAKCRRD 524
Cdd:PTZ00121  1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK--------KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  525 WAFQERDKIVAERDSIRTL----------CDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELNSCVHREQMECQ 594
Cdd:PTZ00121  1689 KAAEALKKEAEEAKKAEELkkkeaeekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  595 LEKEARfrqlmahsSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAEGVNE 650
Cdd:PTZ00121  1769 KAEEIR--------KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 745-800 3.09e-04

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: 41.50  E-value: 3.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  745 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06674     26 DTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGKVRL 81
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 224-566 3.59e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.81  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  224 DFYHTLHSRLLSDQTQLKDdvdmLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQV------LKHNGSSE 297
Cdd:TIGR00606  695 EFISDLQSKLRLAPDKLKS----TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVnrdiqrLKNDIEEQ 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  298 ilNKLYDTAMDKLEvvkkdydalrkrySEKVAMhnSDLSRLEQLGEENQRLQKQTEMLTQQRD------TAIQLQHQCAL 371
Cdd:TIGR00606  771 --ETLLGTIMPEEE-------------SAKVCL--TDVTIMERFQMELKDVERKIAQQAAKLQgsdldrTVQQVNQEKQE 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  372 SLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKE-------SEKYKEERDAVYSEYKLIMSERDQVIS 444
Cdd:TIGR00606  834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNlqrrqqfEEQLVELSTEVQSLIREIKDAKEQDSP 913

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  445 ELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTM-------------DAGRANKEVEILRKQCK-ALCQELK 510
Cdd:TIGR00606  914 LETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGymkdienkiqdgkDDYLKQKETELNTVNAQlEECEKHQ 993

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  511 EALQEaDVAKCRRDWAFQERDKivaerdsiRTLCDNL-RRERDRAVSELAEALRSLD 566
Cdd:TIGR00606  994 EKINE-DMRLMRQDIDTQKIQE--------RWLQDNLtLRKRENELKEVEEELKQHL 1041
PDZ4_PDZD2-PDZ2_hPro-IL-16-like cd06760
PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 ...
 651-713 3.70e-04

PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 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 4 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 second PDZ domain (PDZ2) 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 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: 467241 [Multi-domain]  Cd Length: 90  Bit Score: 41.10  E-value: 3.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  651 PCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN-GEGAINMVVRR 713
Cdd:cd06760     25 PLENDIPGIFIHHLSPGSVAhmDGRLRRGDQILEINGTSLRNVTLNEAYAILSQcKPGPVTLIISR 90
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 724-796 3.75e-04

PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467166 [Multi-domain]  Cd Length: 82  Bit Score: 41.08  E-value: 3.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  724 PLHINLSGQKGsrpqdsgislENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQD 796
Cdd:cd06678     12 QLGIKLVRKKD----------EPGVFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQASGE 74
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
 1359-1422 3.86e-04

PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP6, MPP2, and related domains. MPP6 (also known as MAGUK p55 subfamily member, Protein associated with Lin-7, 2 (PALS2), Veli-associated MAGUK 1, and VAM-1) is a membrane-associated guanylate kinase (MAGUK)-like protein. MPP6 is a regulator of Lin-7 expression and localization. MPP6 is also known to bind cell-adhesion protein, nectin-like molecule-2 (Necl-2), and localize to the basolateral plasma membrane in mammalian epithelial cells. MPP2 (also known as MAGUK p55 subfamily member 2) is a postsynaptic protein that links SynCAM1 cell adhesion molecules to core components of the postsynaptic density. Other members of this family include the Drosophila Vari protein, an essential basolateral septate junction protein which interacts with the cell-adhesion protein neurexin IV. 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 MPP6-MPP2-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: 467268 [Multi-domain]  Cd Length: 78  Bit Score: 40.67  E-value: 3.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878 1359 RHVKVQK-GSEPLGIsIVSGEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARL 1422
Cdd:cd10832      1 RMVGIRKnPGEPLGV-TVRLEEGELVIARILHGGMIDRQGlLHVGDIIKEVNGVPVGSPEQLQEML 65
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 197-634 3.97e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.81  E-value: 3.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  197 RAMSDLQSLQNQHTNALKRCEEVAKE-TDFYHTLH---SRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLr 272
Cdd:TIGR00606  518 RKLDQEMEQLNHHTTTRTQMEMLTKDkMDKDEQIRkikSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKL- 596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  273 eedQKEIGDLRAQQQQVLKHNGS-SEILNKLYDTAMD---------KLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLG 342
Cdd:TIGR00606  597 ---NKELASLEQNKNHINNELESkEEQLSSYEDKLFDvcgsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLT 673

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  343 EENQRLqkqtemltqqrdtaiqlqhqCALSLRRFETihhelskataqNKDLQWEMELLQSELTELRSKQVKTAKESEKYK 422
Cdd:TIGR00606  674 DENQSC--------------------CPVCQRVFQT-----------EAELQEFISDLQSKLRLAPDKLKSTESELKKKE 722

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  423 EERDAVY-------SEYKLIMSERDQVISELDKLQTEVElaesKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEV 495
Cdd:TIGR00606  723 KRRDEMLglapgrqSIIDLKEKEIPELRNKLQKVNRDIQ----RLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQ 798

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  496 EILRKQCKALCQELKEaLQEADVakcrrDWAFQERDKIVAERDsirtlcdnlrRERDRAVSELAEALRSLDDTRKQKNDV 575
Cdd:TIGR00606  799 MELKDVERKIAQQAAK-LQGSDL-----DRTVQQVNQEKQEKQ----------HELDTVVSKIELNRKLIQDQQEQIQHL 862

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  576 SRELKELNScvHREQMECQLEKEARFRQlmahsshdsaidtDSMEWETEVVEFERETED 634
Cdd:TIGR00606  863 KSKTNELKS--EKLQIGTNLQRRQQFEE-------------QLVELSTEVQSLIREIKD 906
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1370-1422 4.00e-04

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


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 44.37  E-value: 4.00e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1370 LGISIVS-----------GEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1422
Cdd:COG0265    180 LGVTIQPvtpelaealglPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSARDLQRLL 243
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 336-520 4.02e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  336 SRLEQLGEENQRLQKQTEMLTQQRDTAIQlqhqcalslrrfetihhELSKATAQNKDLQWEMELLQSELTELRSKQVKTA 415
Cdd:COG3883     23 KELSELQAELEAAQAELDALQAELEELNE-----------------EYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  416 KESEK-----YKEERDAVYSE-----------------YKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEE 473
Cdd:COG3883     86 EELGEraralYRSGGSVSYLDvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1039746878  474 MEALRQikdtvTMDAGRANKEVEI--LRKQCKALCQELKEALQEADVAK 520
Cdd:COG3883    166 LEAAKA-----ELEAQQAEQEALLaqLSAEEAAAEAQLAELEAELAAAE 209
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 748-802 4.05e-04

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 40.65  E-value: 4.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  748 VYAAAVVPGSPAAKEGsLAVGDRIVAINGiaLDNK--SLNECESLLRSC-QDSLTLSL 802
Cdd:cd06712     23 VQVASVDPGSCAAEAG-LKEGDYIVSVGG--VDCKwsKHSEVVKLLKSAgEEGLELQV 77
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 1612-1670 4.18e-04

Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212706 [Multi-domain]  Cd Length: 53  Bit Score: 39.98  E-value: 4.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1612 RALYDRLAEVEPELSFKKDDILYVDDTLPQGvfgsWmaWQLDENAQKiqrGQIPSKYVM 1670
Cdd:cd11772      3 RALYDYEAQHPDELSFEEGDLLYISDKSDPN----W--WKATCGGKT---GLIPSNYVE 52
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
1370-1473 4.19e-04

Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 45.20  E-value: 4.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1370 LGISiVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSAT--EQQARLIIGqqcDTITILAQYNPHIHQLnsh 1447
Cdd:COG3975    485 LGLR-VSADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTADNldDALAAYKPG---DPIELLVFRRDELRTV--- 557

                           90       100
                   ....*....|....*....|....*...
gi 1039746878 1448 srsssHLDPAATPHST--LQGSSAGTPE 1473
Cdd:COG3975    558 -----TVTLAAAPADTykLERVEGATPA 580
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 638-713 4.21e-04

PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467166 [Multi-domain]  Cd Length: 82  Bit Score: 40.69  E-value: 4.21e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  638 KALGFDMAEGVNEPcfpgdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 713
Cdd:cd06678     11 EQLGIKLVRKKDEP------GVFILDLLEGGLAarDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQASGERVHFVVSR 82
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
336-604 4.35e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  336 SRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFEtihhelskataqnkDLQWEMELLQSELTELRSKQVKTA 415
Cdd:PRK02224   206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE--------------ERREELETLEAEIEDLRETIAETE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  416 KESEKYKEErdavyseykliMSERDQVISELDKLQTEVeLAESKLKSSTSEKKAA-----SEEMEALRQIKDTVTMDAGR 490
Cdd:PRK02224   272 REREELAEE-----------VRDLRERLEELEEERDDL-LAEAGLDDADAEAVEArreelEDRDEELRDRLEECRVAAQA 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  491 ANKEVEILRKQCKALCQELKEALQEADV-----------------------------------AKCRRDWAFQERDKIVA 535
Cdd:PRK02224   340 HNEEAESLREDADDLEERAEELREEAAEleseleeareavedrreeieeleeeieelrerfgdAPVDLGNAEDFLEELRE 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  536 ERDSIR----TLCDNLRRERDRAvsELAEALR-------------------SLDDTRKQKNDVSRELKELNSCVHR---- 588
Cdd:PRK02224   420 ERDELRereaELEATLRTARERV--EEAEALLeagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEveer 497

                          330
                   ....*....|....*..
gi 1039746878  589 -EQMECQLEKEARFRQL 604
Cdd:PRK02224   498 lERAEDLVEAEDRIERL 514
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 1369-1420 4.44e-04

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: 40.81  E-value: 4.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1369 PLGISIVS----GEKGGVYVSKVT-LGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06717     11 FLGISIVGqsneRGDGGIYVGSIMkGGAVAADGRIEPGDMILQVNDISFENMSNDDA 67
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 738-808 4.61e-04

PDZ domain 1 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 1 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP) and related domains; Drosophila bazooka PDZ1 belongs to a different PDZ family. 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: Par-3 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 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: 467178 [Multi-domain]  Cd Length: 98  Bit Score: 41.06  E-value: 4.61e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878  738 QDSGISLenGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLsLLKVFPQ 808
Cdd:cd06691     27 SLSGRTL--GLLIRGIEEGSRAERDGRFQENDCIVEINGVDLIDKSFEQAQDIFRQAMRSPEV-KLHVVPA 94
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 725-804 4.64e-04

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: 40.84  E-value: 4.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  725 LHINLSGQKGSRPQDSGISLEnGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 804
Cdd:cd06715     14 LGFNIIGGRPCENNQEGSSSE-GIYVSKIVENGPAADEGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKEPIVVQVLR 92
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 747-800 4.69e-04

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: 40.70  E-value: 4.69e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  747 GVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRScQDSLTL 800
Cdd:cd06737     28 GLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLIKT-KKTVSL 79
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1516-1592 4.69e-04

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: 40.88  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1516 VFIKKSQLD-LGVHLCGGNLHG--VFVAEVEDDSPAKgPDGLVPGDLILEYGSLDMRSRTVEDVyVEMLKPKDSLRLKVQ 1592
Cdd:cd10833      4 VTVEKSPDGsLGFSVRGGSEHGlgIFVSKVEEGSAAE-RAGLCVGDKITEVNGVSLENITMSSA-VKVLTGSNRLRMVVR 81
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 633-713 4.85e-04

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 40.73  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  633 EDIDL----KALGFDMAEGVNEpcfpgdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGA 706
Cdd:cd06667      1 EVIELvndgSGLGFGIVGGKST-------GVVVKTILPGGVAdrDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSH 73


                   ....*..
gi 1039746878  707 INMVVRR 713
Cdd:cd06667     74 VRLVVAR 80
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 437-606 5.10e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  437 SERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEAL--------RQIKDT------VTMDAGRANKEVEILRKQC 502
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriaalaRRIRALeqelaaLEAELAELEKEIAELRAEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  503 KALCQELKEALQEADVAKCRRDWAF-------------------------QERDKIVAERDSIRTLCDNLRRERDR---A 554
Cdd:COG4942    100 EAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaparrEQAEELRADLAELAALRAELEAERAEleaL 179

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039746878  555 VSELAEALRSLDDTRKQKNDVSREL-KELNScvHREQMECQLEKEARFRQLMA 606
Cdd:COG4942    180 LAELEEERAALEALKAERQKLLARLeKELAE--LAAELAELQQEAEELEALIA 230
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
 1612-1669 5.62e-04

Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212792 [Multi-domain]  Cd Length: 55  Bit Score: 39.68  E-value: 5.62e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1612 RALYDRLAEVEPELSFKKDDILYVDDTLPQgvfGSWMAWQLDENAQkiqrGQIPSKYV 1669
Cdd:cd11858      3 KALYDFAGSVANELSLKKDDIVYIVQKEDN---GWWLAKKLDESKE----GWVPAAYL 53
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 1536-1591 5.67e-04

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: 40.54  E-value: 5.67e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878 1536 GVFVAEVEDDSPAKgPDGLVPGDLILEY------GSLDMRSRtvedvyVEMLKPKDSLRLKV 1591
Cdd:cd10839     26 GALVAQVLPDSPAA-KAGLKAGDVILSLngkpitSSADLRNR------VATTKPGTKVELKI 80
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 657-712 6.04e-04

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: 40.37  E-value: 6.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  657 CGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLNGEgAINMVVR 712
Cdd:cd06752     25 LGIFISKVIPDSDAHRLgLKEGDQILSVNGVDFEDIEHSEAVKVLKTAR-EIQMRVR 80
46 PHA02562
endonuclease subunit; Provisional
 306-582 6.24e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.62  E-value: 6.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  306 AMDKLEVVK--------KDYDALRKRYSEKVAMHNSDLSRLEQLGeeNQRLQKQTEMLTQQRDTAiqlqhqcalslrrfE 377
Cdd:PHA02562   167 EMDKLNKDKirelnqqiQTLDMKIDHIQQQIKTYNKNIEEQRKKN--GENIARKQNKYDELVEEA--------------K 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  378 TIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEErdavyseykLIMSERDQV-------ISELDKLQ 450
Cdd:PHA02562   231 TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV---------IKMYEKGGVcptctqqISEGPDRI 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  451 TEVelaESKLKSSTSEKKAASEEMEALRQIKDtvtmdagrankevEILRKQCKAlcQELKealqeADVAKCRRDWAfqer 530
Cdd:PHA02562   302 TKI---KDKLKELQHSLEKLDTAIDELEEIMD-------------EFNEQSKKL--LELK-----NKISTNKQSLI---- 354

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  531 dKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKEL 582
Cdd:PHA02562   355 -TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 1357-1420 6.36e-04

PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), 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 5 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 PDZ5 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: 467157 [Multi-domain]  Cd Length: 98  Bit Score: 40.67  E-value: 6.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1357 EPRHVKVQKGSEPLGISI------VSGEKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06669      7 EVTVIELEKGDRGLGFSIldyqdpLDPSETVIVIRSLVPGGVAEQDGrLLPGDRLVFVNDVSLENASLDEA 77
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 722-794 6.57e-04

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: 40.43  E-value: 6.57e-04
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gi 1039746878  722 VTPLHINLSGQkgsrpqdSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 794
Cdd:cd06717      9 VNFLGISIVGQ-------SNERGDGGIYVGSIMKGGAVAADGRIEPGDMILQVNDISFENMSNDDAVRVLREA 74
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 337-460 6.64e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.44  E-value: 6.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  337 RLEQLGEENQRLQKQtemLTQQRDTAIQLQHQcalsLRRFETIHHELSKAtaqnkdlqwEMELLQsELTELRSKQVKTAK 416
Cdd:pfam20492   14 RLKQYEEETKKAQEE---LEESEETAEELEEE----RRQAEEEAERLEQK---------RQEAEE-EKERLEESAEMEAE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039746878  417 ESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKL 460
Cdd:pfam20492   77 EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 745-800 6.68e-04

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: 40.32  E-value: 6.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  745 ENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06702     31 EPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVSALLSPGQEIKL 85
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 1535-1599 6.70e-04

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


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 40.35  E-value: 6.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1535 HGVFVAEVEDDSPAKGPdGLVPGDLILEYGSLDMRSrtVEDVY--VEMLKPKDSLRLKVQYRHEEFT 1599
Cdd:cd06779     25 RGVLVAEVIPGSPAAKA-GLKEGDVILSVNGKPVTS--FNDLRaaLDTKKPGDSLNLTILRDGKTLT 88
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 724-802 6.80e-04

PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467167 [Multi-domain]  Cd Length: 88  Bit Score: 40.31  E-value: 6.80e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  724 PLHINLSGQKGSRPQDSGIslengvYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 802
Cdd:cd06679     12 SLGISVAGGRGSRRGDLPI------YVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSIVL 84
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 204-389 6.89e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.97  E-value: 6.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  204 SLQNQHTNALKRCEEvaketdFYHTLHSRLLSDQTQLKDDVDMLRRengKLRRERNLLQQSWEDMKRLRE---EDQKEIG 280
Cdd:pfam13851    1 ELMKNHEKAFNEIKN------YYNDITRNNLELIKSLKEEIAELKK---KEERNEKLMSEIQQENKRLTEplqKAQEEVE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  281 DLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEkvamhnsdlsrLEQlgEENQRLQKQTEML--TQQ 358
Cdd:pfam13851   72 ELRKQLENYEKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEK-----------VER--ERDELYDKFEAAIqdVQQ 138

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039746878  359 RdtaIQLQHQcaLSLRRFETIHHELSKATAQ 389
Cdd:pfam13851  139 K---TGLKNL--LLEKKLQALGETLEKKEAQ 164
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
422-600 7.21e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 7.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  422 KEERDAVYSEYKLIMSERDQV---ISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIK-------DTVTMDAGRA 491
Cdd:COG4913    592 KDDRRRIRSRYVLGFDNRAKLaalEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeiDVASAEREIA 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  492 NKEVEI--LRK---QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 566
Cdd:COG4913    672 ELEAELerLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1039746878  567 DTRKQKNDVSRELKELnscvhREQMECQLEKEAR 600
Cdd:COG4913    752 EERFAAALGDAVEREL-----RENLEERIDALRA 780
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 1361-1420 7.29e-04

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: 40.35  E-value: 7.29e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1361 VKVQKGSEPLGISIVSG-------EKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06709      3 ITLKRGPSGLGFNIVGGtdqpyipNDSGIYVAKIKEDGAAAIDGrLQEGDKILEINGQSLENLTHQDA 70
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 398-613 7.30e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.50  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  398 ELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISEL----DKLQTEVELAESKLKSSTSEKKAASEE 473
Cdd:pfam07888   30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELesrvAELKEELRQSREKHEELEEKYKELSAS 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  474 MEALRQIKDTVTmdAGRANKEVEI--LRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRER 551
Cdd:pfam07888  110 SEELSEEKDALL--AQRAAHEARIreLEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  552 DRAVSELAEALRSLDDTRKQ----KNDVSRELKELNSCVHREQMECQLEKEARFRQLMAHSSHDSA 613
Cdd:pfam07888  188 RSLSKEFQELRNSLAQRDTQvlqlQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 658-696 7.50e-04

PDZ domain 1 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 1 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP) and related domains; Drosophila bazooka PDZ1 belongs to a different PDZ family. 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: Par-3 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 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: 467178 [Multi-domain]  Cd Length: 98  Bit Score: 40.68  E-value: 7.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1039746878  658 GIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQA 696
Cdd:cd06691     34 GLLIRGIEEGSRAerDGRFQENDCIVEINGVDLIDKSFEQA 74
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 235-472 7.83e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 7.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  235 SDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQvlkhngsseilnklydtAMDKLEVVK 314
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-----------------LQAEIAEAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  315 KDYDALRKRYSEKVA---MHNSDLSRLEQL------GEENQRLQKQTEMLTQQRDTAIQLQhqcalslrrfetihhelsK 385
Cdd:COG3883     79 AEIEERREELGERARalyRSGGSVSYLDVLlgsesfSDFLDRLSALSKIADADADLLEELK------------------A 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  386 ATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKlimSERDQVISELDKLQTEVELAESKLKSSTS 465
Cdd:COG3883    141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS---AEEAAAEAQLAELEAELAAAEAAAAAAAA 217


                   ....*..
gi 1039746878  466 EKKAASE 472
Cdd:COG3883    218 AAAAAAA 224
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 ...
 741-793 7.98e-04

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: 40.32  E-value: 7.98e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  741 GISLEN-GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd06762     21 GSDLENkSITVHRVFPSGLAAQEGTIQKGDRILSINGKSLKGVTHGDALSVLKQ 74
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 1384-1436 7.99e-04

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 39.98  E-value: 7.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039746878 1384 VSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1436
Cdd:cd10820     26 VAKIRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 741-800 8.10e-04

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: 40.05  E-value: 8.10e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  741 GISL----ENGV--YAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06800     14 GISItggkEHGVpiLISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITL 79
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 632-803 8.12e-04

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


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 44.13  E-value: 8.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  632 TEDIdLKALGFDMAEGVnepcfpgdcgiFVTKVDKGSIAD-GRLRVNDWLLRINDVD----------------------- 687
Cdd:TIGR02037  244 TSDL-AKSLGLEKQRGA-----------LVAQVLPGSPAEkAGLKAGDVITSVNGKPissfadlrraigtlkpgkkvtlg 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  688 LINKDKKQAIKALLNGEGAINMVvrRRKSLGGKVVTPLhinlsgQKGSRPQDSGISLENGVYAAAVVPGSPAAKEGsLAV 767
Cdd:TIGR02037  312 ILRKGKEKTITVTLGASPEEQAS--SSNPFLGLTVANL------SPEIRKELRLKGDVKGVVVTKVVSGSPAARAG-LQP 382

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1039746878  768 GDRIVAINGIALdnKSLNECESLLRSCQDSLTLSLL 803
Cdd:TIGR02037  383 GDVILSVNQQPV--SSVAELRKVLARAKKGGRVALL 416
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1612-1668 8.29e-04

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 39.10  E-value: 8.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1612 RALYDRLAEVEPELSFKKDDILYVDDTlPQGvfgswmAWQLDENAQKIQRGQIPSKY 1668
Cdd:cd11845      3 VALYDYEARTDDDLSFKKGDRLQILDD-SDG------DWWLARHLSTGKEGYIPSNY 52
fliJ PRK07720
flagellar biosynthesis chaperone FliJ;
310-449 8.48e-04

flagellar biosynthesis chaperone FliJ;


Pssm-ID: 181091 [Multi-domain]  Cd Length: 146  Bit Score: 41.60  E-value: 8.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  310 LEVVKKDYDALRKRYSEKVamhnsdlSRLEQLGEENQRLQKQTEMLTQQRDTAIQ-------LQHQCALSLRRFETIHHe 382
Cdd:PRK07720    11 LELKENEKEKALGEYEEAV-------SRFEQVAEKLYELLKQKEDLEQAKEEKLQsglsiqeIRHYQQFVTNLERTIDH- 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  383 LSKATAQNKDlqwEMELLQSELTELrSKQVKtakeseKYKEERDAVYSEYKLIMSERDQviSELDKL 449
Cdd:PRK07720    83 YQLLVMQARE---QMNRKQQDLTEK-NIEVK------KYEKMKEKKQEMFALEEKAAEM--KEMDEI 137
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 386-584 8.76e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 8.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  386 ATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLK---S 462
Cdd:COG3883     14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  463 STSEKKAASEEMEALRQIKDTVTMdAGRANKeVEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIVAERDSIRT 542
Cdd:COG3883     94 ALYRSGGSVSYLDVLLGSESFSDF-LDRLSA-LSKIADADADLLEELKADKAELE----------AKKAELEAKLAELEA 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039746878  543 LCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELNS 584
Cdd:COG3883    162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 638-692 8.83e-04

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: 39.86  E-value: 8.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  638 KALGFDMAEGVNEPCFPGdcgIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKD 692
Cdd:cd06718     11 KPLGFYIRDGNGVERVPG---IFISRLVLGSLADstGLLAVGDEILEVNGVEVTGKS 64
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 1610-1668 9.04e-04

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 39.19  E-value: 9.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1610 YIRALYDRLAEVEPELSFKKDDILYVDDTLPQGvfgsWmaWQ--LDENAQKIQRGQIPSKY 1668
Cdd:cd11883      1 VVVALYDFTPKSKNQLSFKAGDIIYVLNKDPSG----W--WDgvIISSSGKVKRGWFPSNY 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
221-606 9.14e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 9.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  221 KETDFYHTLHSRLLSDQTQLK-DDVDMLRRE-----------NGKLRRE---RNLLQQSW---EDMKRLREEDQKEIGDL 282
Cdd:COG4913    543 KPHPFRAWLEAELGRRFDYVCvDSPEELRRHpraitragqvkGNGTRHEkddRRRIRSRYvlgFDNRAKLAALEAELAEL 622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  283 RAQQQQVlkhngsseilnklyDTAMDKLEVVKKDYDALRKRYsEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTA 362
Cdd:COG4913    623 EEELAEA--------------EERLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  363 IQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEER-DAVYSEYKLIMSE--- 438
Cdd:COG4913    688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDAVErel 767

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  439 RDQVISELDKLQTEVELAESKLksstsekkaaseeMEALRQIK-----DTVTMDAG-RANKEVEILRKQCKAlcQELKEA 512
Cdd:COG4913    768 RENLEERIDALRARLNRAEEEL-------------ERAMRAFNrewpaETADLDADlESLPEYLALLDRLEE--DGLPEY 832

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  513 LQEadvakcrrdwaFQERdKIVAERDSIRTLCDNLRRERDRAVSELAE---ALRSLD---------DTRKQKNDVSREL- 579
Cdd:COG4913    833 EER-----------FKEL-LNENSIEFVADLLSKLRRAIREIKERIDPlndSLKRIPfgpgrylrlEARPRPDPEVREFr 900

                          410       420
                   ....*....|....*....|....*..
gi 1039746878  580 KELNSCVHREQMECQLEKEARFRQLMA 606
Cdd:COG4913    901 QELRAVTSGASLFDEELSEARFAALKR 927
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
398-583 9.50e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 9.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  398 ELLQSELTELRSKQVKTAKESEKYKEERDAVYSEyklimSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEAL 477
Cdd:COG3206    178 EFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS-----EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  478 RQIKDTVTmdagrANKEVEILRKQCKALCQELKEALQEadvakcrrdwaFQERD-KIVAERDSIRTLCDNLRRERDRA-- 554
Cdd:COG3206    253 PDALPELL-----QSPVIQQLRAQLAELEAELAELSAR-----------YTPNHpDVIALRAQIAALRAQLQQEAQRIla 316

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039746878  555 ------------VSELAEALRSLDDTRKQKNDVSRELKELN 583
Cdd:COG3206    317 sleaelealqarEASLQAQLAQLEARLAELPELEAELRRLE 357
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 734-800 9.65e-04

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: 40.11  E-value: 9.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  734 GSRPQDSGIslengvYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06796     20 GGKEQNSPI------YISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKL 80
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 753-777 1.03e-03

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: 39.89  E-value: 1.03e-03
                           10        20
                   ....*....|....*....|....*
gi 1039746878  753 VVPGSPAAKEGSLAVGDRIVAINGI 777
Cdd:cd06731     32 VVPDGPAALDGKLRTGDVLVSVNDT 56
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 645-714 1.06e-03

PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of afadin (AFDN, also known as ALL1-fused gene from chromosome 6 protein (AF6) and MLLT4), and related domains. AFDN belongs to the adhesion system, probably together with the E-cadherin-catenin system, that plays a role in the organization of homotypic, interneuronal, and heterotypic cell-cell adherens junctions. The AFDN PDZ domain interaction partners include poliovirus receptor-related protein PRR2/nectin, the junctional adhesion molecule (JAM), the breakpoint-cluster-region protein (BCR), connexin36 (Cx36), and a subset of Eph-related receptor tyrosine kinases; it can also bind low molecular weight ligands, in competition with a natural peptide ligand. Other AFDN-binding proteins have been identified. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This AFDN family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467251 [Multi-domain]  Cd Length: 89  Bit Score: 39.96  E-value: 1.06e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  645 AEGVNEPcfpgDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 714
Cdd:cd06789     22 AKGAGQD----KLGIYIKSVVKGGAAdlDGRLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTLEVAKQ 89
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 1367-1422 1.07e-03

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: 39.97  E-value: 1.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878 1367 SEPLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1422
Cdd:cd06779     12 SPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAAL 67
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1515-1582 1.16e-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: 39.18  E-value: 1.16e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1515 IVFIKKSQLDLGVHLCGgnlHG-VFVAEVEDDSPAKGPdGLVPGDLILEYGSLDMRSRTVEDVyVEMLK 1582
Cdd:cd06744      1 TVRVYRGNGSFGFTLRG---HApVYIESVDPGSAAERA-GLKPGDRILFLNGLDVRNCSHDKV-VSLLQ 64
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 1378-1421 1.19e-03

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


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 40.38  E-value: 1.19e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039746878 1378 EKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQAR 1421
Cdd:cd10838     31 EVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRI 74
SH3_NEDD9 cd12002
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, ...
 1612-1648 1.24e-03

Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, Neural precursor cell Expressed, Developmentally Down-regulated 9; NEDD9 is also called human enhancer of filamentation 1 (HEF1) or CAS-L (Crk-associated substrate in lymphocyte). It was first described as a gene predominantly expressed in early embryonic brain, and was also isolated from a screen of human proteins that regulate filamentous budding in yeast, and as a tyrosine phosphorylated protein in lymphocytes. It promotes metastasis in different solid tumors. NEDD9 localizes in focal adhesions and associates with FAK and Abl kinase. It also interacts with SMAD3 and the proteasomal machinery which allows its rapid turnover; these interactions are not shared by other CAS proteins. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212935  Cd Length: 57  Bit Score: 38.81  E-value: 1.24e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1039746878 1612 RALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWM 1648
Cdd:cd12002      3 RALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWL 39
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 747-800 1.28e-03

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: 39.65  E-value: 1.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  747 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06795     26 GIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTI 79
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 742-800 1.29e-03

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: 39.58  E-value: 1.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  742 ISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06709     25 IPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDAVELFRNAGEDVKL 83
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 747-793 1.30e-03

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: 39.55  E-value: 1.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1039746878  747 GVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd06741     27 GIYVTGVDPGSVAENAG-LKVGDQILEVNGRSFLDITHDEAVKILKS 72
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 ...
 623-712 1.36e-03

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: 39.52  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  623 TEVVEFERetediDLKALGFDMAEGVNEPCfpGDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQA---I 697
Cdd:cd06763      1 AVTVELEK-----GSAGLGFSLEGGKGSPL--GDRPLTIKRIFKGGAAEqsGVLQVGDEILQINGTSLQGLTRFEAwniI 73

                           90
                   ....*....|....*
gi 1039746878  698 KALlnGEGAINMVVR 712
Cdd:cd06763     74 KSL--PEGPVTLLIR 86
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 310-548 1.37e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.52  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  310 LEVVKKDYDALRKRysekvaMHNSDLsRLEQLGEENQRLQKQTEMLTQQRDTA--------------IQLQHQcalslrr 375
Cdd:pfam05622    2 LSEAQEEKDELAQR------CHELDQ-QVSLLQEEKNSLQQENKKLQERLDQLesgddsgtpggkkyLLLQKQ------- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  376 FETIHHELSKATAQNKDLQWEMELLQSELTELRSKQ---VKTAKESEKYKEERDAV-YSEYKLIMSERdQVISELDKLQt 451
Cdd:pfam05622   68 LEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNeelTSLAEEAQALKDEMDILrESSDKVKKLEA-TVETYKKKLE- 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  452 evELAESKLKSSTSEKKAAsEEMEALRQIKDtvtmDAGRAN---KEVEILRKQCKALCQELKEALQEADVAKC------- 521
Cdd:pfam05622  146 --DLGDLRRQVKLLEERNA-EYMQRTLQLEE----ELKKANalrGQLETYKRQVQELHGKLSEESKKADKLEFeykklee 218

                          250       260
                   ....*....|....*....|....*..
gi 1039746878  522 RRDWAFQERDKIVAERDSIRTLCDNLR 548
Cdd:pfam05622  219 KLEALQKEKERLIIERDTLRETNEELR 245
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
137-388 1.37e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  137 LTEQQANDTVENLSIQLRLMTRERNELRKRLAFAThgatfdKRPYHRLNPDYERLKiQCVRAMSDLQSLQNQHtnALKRC 216
Cdd:COG4717    298 ASLGKEAEELQALPALEELEEEELEELLAALGLPP------DLSPEELLELLDRIE-ELQELLREAEELEEEL--QLEEL 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  217 EE----------VAKETDFYHTL--HSRLLSDQTQLKDDVDMLRRENG------------KLRRERNLLQQSWEDMKRLR 272
Cdd:COG4717    369 EQeiaallaeagVEDEEELRAALeqAEEYQELKEELEELEEQLEELLGeleellealdeeELEEELEELEEELEELEEEL 448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  273 EEDQKEIGDLRAQQQQvLKHNGSSEILNKLYDTAMDKLEVVKKDYDALrkRYSEKVAMHNSDLSRLEQLGEENQRLQKQT 352
Cdd:COG4717    449 EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAAL--KLALELLEEAREEYREERLPPVLERASEYF 525

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1039746878  353 EMLTQQRDTAIQLQHQCALSLRRFETIH---HELSKATA 388
Cdd:COG4717    526 SRLTDGRYRLIRIDEDLSLKVDTEDGRTrpvEELSRGTR 564
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 245-431 1.38e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  245 DMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQqvlKHNGSSEILNKLYDTAMDKLEVVK--KDYDALRK 322
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRnnKEYEALQK 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  323 rysekvamhnsdlsRLEQLGEENQRLQKQTEMLTQQRDTAIQlqhqcalslrrfetihhELSKATAQNKDLQwemELLQS 402
Cdd:COG1579     97 --------------EIESLKRRISDLEDEILELMERIEELEE-----------------ELAELEAELAELE---AELEE 142

                          170       180
                   ....*....|....*....|....*....
gi 1039746878  403 ELTELRSKQVKTAKESEKYKEERDAVYSE 431
Cdd:COG1579    143 KKAELDEELAELEAELEELEAEREELAAK 171
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 732-795 1.42e-03

PDZ domain 6 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 6 of multi-PDZ-domain protein 1 (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 PDZ6 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 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: 467158 [Multi-domain]  Cd Length: 87  Bit Score: 39.54  E-value: 1.42e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  732 QKGSrpQDSGISLE-----NGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQ 795
Cdd:cd06670     10 VKGN--SSLGITVSadkdgNGCIVKSIIHGGAVSRDGRISVGDFIVSINNESLRNVTNAQARAILRRAS 76
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 373-605 1.44e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.98  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  373 LRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVY-SEYKLIMSERDQVISELDKLQT 451
Cdd:pfam13868   33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRqEEYEEKLQEREQMDEIVERIQE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  452 EvELAESKLKSStsEKKAASEEM-EALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQE- 529
Cdd:pfam13868  113 E-DQAEAEEKLE--KQRQLREEIdEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARl 189

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  530 RDKIVAERDSIRTLcDNLRRERDRAVSELAEALRSLDDTRK---QKNDVSRELKELNSCvHREQMECQLEKEARFRQLM 605
Cdd:pfam13868  190 RAQQEKAQDEKAER-DELRAKLYQEEQERKERQKEREEAEKkarQRQELQQAREEQIEL-KERRLAEEAEREEEEFERM 266
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 1359-1416 1.47e-03

PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. 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 MPP6-MPP2-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: 467267 [Multi-domain]  Cd Length: 81  Bit Score: 39.39  E-value: 1.47e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1359 RHVKVQKGS-EPLGISIVSGEKGGVYVSKVTLGSIAH-QAGLEYGDQLLEFNGINLRSAT 1416
Cdd:cd10831      1 RLVQFQKNTdEPMGITLKMNEDGRCIVARIMHGGMIHrQGTLHVGDEIREINGISVANQT 60
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
 755-802 1.51e-03

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). 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 shroom2,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 39.24  E-value: 1.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039746878  755 PGSPAAKEGSLAVGDRIVAINGIALdNKSLNECESLLRSCQDSLTLSL 802
Cdd:cd06750     34 EGGKAASVGKLQVGDEVVNINGVPL-SGSRQEAIQLVKGSHKTLKLVV 80
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1535-1602 1.53e-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: 42.44  E-value: 1.53e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1535 HGVFVAEVEDDSPA-KGpdGLVPGDLILEYGSLDMRSrtVEDV--YVEMLKPKDSLRLKVqYRHEEFTRVK 1602
Cdd:COG0265    201 EGVLVARVEPGSPAaKA--GLRPGDVILAVDGKPVTS--ARDLqrLLASLKPGDTVTLTV-LRGGKELTVT 266
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 238-410 1.63e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 41.81  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  238 TQLKDDVDMLRRENGKLRRERNLLQQSW-EDMKRLR--EEDQKEIgdlraqQQQVLKHNGSSEILNKLYDTAMDKLEVVK 314
Cdd:pfam15619   14 KELQNELAELQSKLEELRKENRLLKRLQkRQEKALGkyEGTESEL------PQLIARHNEEVRVLRERLRRLQEKERDLE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  315 KdydALRKRYSEkvaMH--NSDLSRLEQLGE-----ENQRLQKQTEMLT---QQRDTAIQ-LQHQCALSLRRFetiHHEL 383
Cdd:pfam15619   88 R---KLKEKEAE---LLrlRDQLKRLEKLSEdknlaEREELQKKLEQLEaklEDKDEKIQdLERKLELENKSF---RRQL 158

                          170       180
                   ....*....|....*....|....*..
gi 1039746878  384 SKATAQNKDLQWEMELLQSELTELRSK 410
Cdd:pfam15619  159 AAEKKKHKEAQEEVKILQEEIERLQQK 185
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 247-650 1.81e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.27  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  247 LRRENGKLRRERNLLQQSWEDMKrLREEDQKEIgdLRAQQQQVLKhngsseILNKLYDTAMDKleVVKKDYDALRKRYSE 326
Cdd:pfam10174  121 LQSEHERQAKELFLLRKTLEEME-LRIETQKQT--LGARDESIKK------LLEMLQSKGLPK--KSGEEDWERTRRIAE 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  327 KVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRD---------TAIQLQHQCALSLRRfetihhelskataQNKDLQWEM 397
Cdd:pfam10174  190 AEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPdpaktkalqTVIEMKDTKISSLER-------------NIRDLEDEV 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  398 ELLQSEL---TELRSKQVKtakESEKYKeerdavySEYKLIMSERDQVISELDKLQTEVELAESKLKSSTS--------- 465
Cdd:pfam10174  257 QMLKTNGllhTEDREEEIK---QMEVYK-------SHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNqnsdckqhi 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  466 ----------EKKAAS------------EEMEA----------------------LRQIKDTVTMDAGRAN---KEVEIL 498
Cdd:pfam10174  327 evlkesltakEQRAAIlqtevdalrlrlEEKESflnkktkqlqdlteekstlageIRDLKDMLDVKERKINvlqKKIENL 406

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  499 RKQCK---ALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIrtlCDNLRRERDRAVSELAEALRSLddtrKQKNdv 575
Cdd:pfam10174  407 QEQLRdkdKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERI---IERLKEQREREDRERLEELESL----KKEN-- 477

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  576 sRELKELNSCVHREqmecQLEKEARFRQLMAHSS--------HDSAIDTDSMEWETEVVEFEReTEDIDLKALGFDMAEG 647
Cdd:pfam10174  478 -KDLKEKVSALQPE----LTEKESSLIDLKEHASslassglkKDSKLKSLEIAVEQKKEECSK-LENQLKKAHNAEEAVR 551


                   ...
gi 1039746878  648 VNE 650
Cdd:pfam10174  552 TNP 554
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 240-475 1.87e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 42.03  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  240 LKDDVDMLRRENGKLRrernllQQSWEDMKRLREEDQKEigDLRAQQQQVLKHngSSEILNKLYDTAMDKLEVVKKDYDA 319
Cdd:pfam17078    8 LHDQIDALTKTNLQLT------VQSQNLLSKLEIAQQKE--SKFLENLASLKH--ENDNLSSMLNRKERRLKDLEDQLSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  320 LRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHqcalslRRFETIHHELSKATAQNKDLQWEMEl 399
Cdd:pfam17078   78 LKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQN------EYKDHYQQEINTLQESLEDLKLENE- 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878  400 lqSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQ-VISELDKLQTEVELAESKLKSSTSEKKA--ASEEME 475
Cdd:pfam17078  151 --KQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKIleYAEKME 227
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 621-700 1.95e-03

PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), 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 5 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 PDZ5 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: 467157 [Multi-domain]  Cd Length: 98  Bit Score: 39.52  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  621 WETEVVEFERETEDidlKALGFDMAEgVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIK 698
Cdd:cd06669      4 WSDEVTVIELEKGD---RGLGFSILD-YQDPLDPSETVIVIRSLVPGGVAeqDGRLLPGDRLVFVNDVSLENASLDEAVQ 79


                   ..
gi 1039746878  699 AL 700
Cdd:cd06669     80 AL 81
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 1367-1434 2.04e-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: 2.04e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039746878 1367 SEPLGISIVSG----EKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSatEQQARLIIGQQCDTITIL 1434
Cdd:cd06716     14 QEKLGLTLCYRtddeEDTGIYVSEVDPNSIAAKDGrIREGDQILQINGVDVQN--REEAIALLSEEEKSITLL 84
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 640-711 2.05e-03

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


Pssm-ID: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 39.25  E-value: 2.05e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  640 LGFDMAEGVNEpcFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 711
Cdd:cd06680     13 LGFSIVGGYEE--SHGNQPFFVKSIVPGTPAynDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTV 84
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 200-427 2.07e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  200 SDLQSLQNQHTNALKRCEEVAKEtdfyhtlHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQsweDMKRLreedQKEI 279
Cdd:COG4942     27 AELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEA---ELAEL----EKEI 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  280 GDLRAQ---QQQVLkhngsSEILNKLYDTA-MDKLEVVKKDYDAL----RKRYSEKVAmhNSDLSRLEQLGEENQRLQKQ 351
Cdd:COG4942     93 AELRAEleaQKEEL-----AELLRALYRLGrQPPLALLLSPEDFLdavrRLQYLKYLA--PARREQAEELRADLAELAAL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  352 TEMLTQQRDTAIQLQHQCALSLRRFETIHHE----LSKATAQNKDLQWEMELLQSELTELRsKQVKTAKESEKYKEERDA 427
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELE-ALIARLEAEAAAAAERTP 244
PDZ_LIMK-like cd06754
PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 764-793 2.12e-03

PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the LIMK protein family, and related domains. The LIMK family is composed of LIMK1 and LIMK2, which are common downstream effectors of several signalization pathways and function as signaling nodes that control cytoskeleton dynamics through the phosphorylation of cofilin family proteins. They also control microtubule dynamics. The LIMK1 PDZ domain binds tubulin and nischarin. LIMK1 also binds a carboxy-terminal motif of membrane type 1-matrix metalloproteinase (MT1-MMP, also known as MMP14) having features of a PDZ domain-binding site; MT1-MMP is a major protease involved in dissemination of carcinoma cells during cancer progression. 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 LIMK-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: 467236 [Multi-domain]  Cd Length: 92  Bit Score: 39.18  E-value: 2.12e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039746878  764 SLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd06754     50 SLHVGDRILEVNGTPVRDLSLEEIDDLIQS 79
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1360-1420 2.39e-03

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: 38.73  E-value: 2.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1360 HVKVQKGSEPLGISIVSGEKGGVY--VSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06731      3 RTSLKKSARGFGFTIIGGDEPDEFlqIKSVVPDGPAALDGkLRTGDVLVSVNDTCVLGYTHADV 66
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
197-516 2.39e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  197 RAMSDLQSLQNQHTNALKRCEEVAKEtdfyhtlhsrLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQ 276
Cdd:COG4372     42 KLQEELEQLREELEQAREELEQLEEE----------LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  277 KeigdLRAQQQQvlkhngsseiLNKLYDTAMDKLEVVKKDYDALRKRYSEKVAmhnsdlsRLEQLGEENQRLQKQTEMLT 356
Cdd:COG4372    112 E----LQEELEE----------LQKERQDLEQQRKQLEAQIAELQSEIAEREE-------ELKELEEQLESLQEELAALE 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  357 QQRDTAIQLQHQCALSlrrfetihhELSKATAQNKDLQWEMELLQsELTELRSKQVKTAKESEKYKEERDAVYSEYKLIM 436
Cdd:COG4372    171 QELQALSEAEAEQALD---------ELLKEANRNAEKEEELAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  437 SERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEA 516
Cdd:COG4372    241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 741-807 2.40e-03

PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. 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 MPP6-MPP2-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: 467267 [Multi-domain]  Cd Length: 81  Bit Score: 38.62  E-value: 2.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878  741 GISL----ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 807
Cdd:cd10831     14 GITLkmneDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSIT---FKIVP 81
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 747-804 2.44e-03

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: 38.75  E-value: 2.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  747 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 804
Cdd:cd06791     32 GIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEAVEVLRNTGQVVHLTLAR 89
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 309-638 2.70e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  309 KLEVVKKDYDALRKRYSEKVamhnsdlsrlEQLGEENQRLQKQTEMLTQQRdTAIQlqhQCALSLRRFETIHHELskATA 388
Cdd:pfam12128  605 RLDKAEEALQSAREKQAAAE----------EQLVQANGELEKASREETFAR-TALK---NARLDLRRLFDEKQSE--KDK 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  389 QNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISE-----LDKLQTEVELAESKLKSs 463
Cdd:pfam12128  669 KNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGaldaqLALLKAAIAARRSGAKA- 747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  464 tsekkaaseEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWA----FQERDKIVAE--- 536
Cdd:pfam12128  748 ---------ELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYqetwLQRRPRLATQlsn 818

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  537 -RDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELnscvhreqmECQLEKEARFRqlmahsshdsaID 615
Cdd:pfam12128  819 iERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGL---------RCEMSKLATLK-----------ED 878

                          330       340
                   ....*....|....*....|...
gi 1039746878  616 TDSMEWETEVVEFERETEDIDLK 638
Cdd:pfam12128  879 ANSEQAQGSIGERLAQLEDLKLK 901
PDZ3_PDZD7-like cd06751
PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1361-1426 2.82e-03

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: 38.57  E-value: 2.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1361 VKVQKGSEPLGISIVSGEKGG----VYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1426
Cdd:cd06751      4 VELSKMKQSLGISISGGIESKvqpvVKIEKIFPGGAAALSGnLKAGYELVSVDGESLQQVTHQQAVDIIRR 74
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
 1359-1424 2.85e-03

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: 38.82  E-value: 2.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1359 RHVKVQKGSEpLGISIVSG----EKGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06698      3 QLITVAKSTG-LGLSIVGGinrpEGPMVFIQEVIPGGDCYKDGrLRPGDQLVSINKESLIGVTLEEAKSIL 72
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 714-781 2.95e-03

circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. 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 BsHtrA-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: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 38.77  E-value: 2.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  714 RKSLGGKVVTPLHINLSGQKGSRPQDSgisLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDN 781
Cdd:cd06781      1 RPSLGISMVDLSDVPEYEQQSLKLPSN---VNKGVYVAQVQSNSPAEKAG-LKKGDVITKLDGKKVES 64
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1360-1436 3.01e-03

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: 38.33  E-value: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1360 HVKVQKGSEPLGISIVSGE---KGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1435
Cdd:cd06735      3 SVELERGPKGFGFSIRGGReynNMPLYVLRLAEDGPAQRDGrLRVGDQILEINGESTQGMTHAQAIELIRSGGSVVRLLL 82


                   .
gi 1039746878 1436 Q 1436
Cdd:cd06735     83 R 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 ...
 1361-1420 3.03e-03

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: 38.36  E-value: 3.03e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878 1361 VKVQKGSEPLGISIvSGEKGG------VYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06763      4 VELEKGSAGLGFSL-EGGKGSplgdrpLTIKRIFKGGAAEQSGvLQVGDEILQINGTSLQGLTRFEA 69
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 747-800 3.03e-03

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 38.42  E-value: 3.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  747 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06667     23 GVVVKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRL 76
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1366-1424 3.04e-03

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 38.28  E-value: 3.04e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878 1366 GSEPLGISIVsgekGGV------YVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1424
Cdd:cd06753      6 GPAPWGFRLQ----GGKdfnqplTISRVTPGGKAAQANLRPGDVILAINGESTEGMTHLEAQNKI 66
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 322-600 3.04e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  322 KRYSEKVAMHNSDLSRLE----QLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKD----L 393
Cdd:pfam01576   15 QKVKERQQKAESELKELEkkhqQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEErsqqL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  394 QWEMELLQSELTELrsKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISE--LDKLQTEVELAESKLKSSTSEKKAAS 471
Cdd:pfam01576   95 QNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEdqNSKLSKERKLLEERISEFTSNLAEEE 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  472 EEMEALRQIKDTVTMdagrANKEVEILRKQCKALCQELKEAlqeadvaKCRRDWAFQERDKIVAErdsIRTLCDNLRRER 551
Cdd:pfam01576  173 EKAKSLSKLKNKHEA----MISDLEERLKKEEKGRQELEKA-------KRKLEGESTDLQEQIAE---LQAQIAELRAQL 238

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039746878  552 DRAVSELAEALRSLDDTRKQKNDVSRELKELNSCVHREQMECQLEKEAR 600
Cdd:pfam01576  239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR 287
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 254-520 3.04e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 42.32  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  254 LRRERNLLQQSWEDMKRLREEDQK-----EIGDLRAQQ-QQVLKHNGSSEilnklydtAMDKLEVVKkdydalrkrysek 327
Cdd:pfam05701   72 LESTKRLIEELKLNLERAQTEEAQakqdsELAKLRVEEmEQGIADEASVA--------AKAQLEVAK------------- 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  328 vAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCAL---------------------SLRRFETIHHE---- 382
Cdd:pfam05701  131 -ARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSaskeiektveeltieliatkeSLESAHAAHLEaeeh 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  383 -LSKATAQNKD-LQWEMELLQS--ELTELRsKQVKTAKESE-----------KYKEERDAvYSEYKLIMSERDQVISE-- 445
Cdd:pfam05701  210 rIGAALAREQDkLNWEKELKQAeeELQRLN-QQLLSAKDLKskletasalllDLKAELAA-YMESKLKEEADGEGNEKkt 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  446 -------LDKLQTEVELAESKLKSSTSEKK-----AAS------EEMEALRQIKDTVTM----------DAGRANKEVEI 497
Cdd:pfam05701  288 stsiqaaLASAKKELEEVKANIEKAKDEVNclrvaAASlrseleKEKAELASLRQREGMasiavssleaELNRTKSEIAL 367

                          330       340       350
                   ....*....|....*....|....*....|
gi 1039746878  498 LRKQCKALCQE-------LKEALQEADVAK 520
Cdd:pfam05701  368 VQAKEKEAREKmvelpkqLQQAAQEAEEAK 397
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 ...
 723-783 3.12e-03

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: 38.43  E-value: 3.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746878  723 TPLHINLSGQKgSRPQDSgislengVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKS 783
Cdd:cd06672     11 SGLGLSLAGNK-DRSRMS-------VFVVGIDPDGAAGKDGRIQVGDELLEINGQVLYGRS 63
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 308-481 3.13e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.05  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
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gi 1039746878  308 DKLEVVKKDYDALRKRYSEkVAMHNSDLSR-LEQLGEENQRLQKQTEmlTQQRDTAiqlqhqcalSLRRFETIHHELSKa 386
Cdd:pfam13851   33 EEIAELKKKEERNEKLMSE-IQQENKRLTEpLQKAQEEVEELRKQLE--NYEKDKQ---------SLKNLKARLKVLEK- 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  387 taQNKDLQWEMELLqseltELRSKQVKTAKEsEKYKEERDAVY-----SEYKLIMSERdqvisELDKLQTEVELAESKLK 461
Cdd:pfam13851  100 --ELKDLKWEHEVL-----EQRFEKVERERD-ELYDKFEAAIQdvqqkTGLKNLLLEK-----KLQALGETLEKKEAQLN 166

                          170       180
                   ....*....|....*....|
gi 1039746878  462 SStseKKAASEEMEALRQIK 481
Cdd:pfam13851  167 EV---LAAANLDPDALQAVT 183
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 752-802 3.16e-03

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467194 [Multi-domain]  Cd Length: 76  Bit Score: 38.00  E-value: 3.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039746878  752 AVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 802
Cdd:cd06710     26 CVVRGSPADVAG-LKAGDQILAVNGINVSKASHEDVVKLIGKCTGVLRLVI 75
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 640-713 3.18e-03

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: 38.53  E-value: 3.18e-03
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gi 1039746878  640 LGFDMAEG---VNEPCFPGDCGIFVTKV-DKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 713
Cdd:cd06715     14 LGFNIIGGrpcENNQEGSSSEGIYVSKIvENGPAADeGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKEPIVVQVLR 92
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 1383-1434 3.39e-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: 38.37  E-value: 3.39e-03
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gi 1039746878 1383 YVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1434
Cdd:cd06713     38 YVCRVHEDSPAYLAGLTAGDVILSVNGVSVEGASHQEIVELIRSSGNTLRLE 89
Filament pfam00038
Intermediate filament protein;
388-596 3.54e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.83  E-value: 3.54e-03
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gi 1039746878  388 AQNKDLQWEMELLQseltelrskQVKTAKES---EKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSST 464
Cdd:pfam00038   25 QQNKLLETKISELR---------QKKGAEPSrlySLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDEL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  465 SEKKAASEEMEALRQIKDTVTM----------------DAGRANKEVEI--LRKQCK----------ALCQELKEALQ-- 514
Cdd:pfam00038   96 NLRTSAENDLVGLRKDLDEATLarvdleakieslkeelAFLKKNHEEEVreLQAQVSdtqvnvemdaARKLDLTSALAei 175

                          170       180       190       200       210       220       230       240
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gi 1039746878  515 ----EADVAKCRRD---WaFQER-----------------------------DKIVAERDSIRTLCDNLrrerDRAVSEL 558
Cdd:pfam00038  176 raqyEEIAAKNREEaeeW-YQSKleelqqaaarngdalrsakeeitelrrtiQSLEIELQSLKKQKASL----ERQLAET 250

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1039746878  559 AEAL-RSLDDTRKQKNDVSRELKELnscvhREQMECQLE 596
Cdd:pfam00038  251 EERYeLQLADYQELISELEAELQET-----RQEMARQLR 284
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 741-776 3.67e-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: 3.67e-03
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gi 1039746878  741 GISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAING 776
Cdd:cd10839     20 GLKEPKGALVAQVLPDSPAAKAG-LKAGDVILSLNG 54
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 747-776 4.01e-03

circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis YlbL and related domains. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. Deletion of both proteases leads to accumulation of the cell division inhibitor YneA. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This YlbL family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467637 [Multi-domain]  Cd Length: 83  Bit Score: 38.24  E-value: 4.01e-03
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gi 1039746878  747 GVYAAAVVPGSPAAkeGSLAVGDRIVAING 776
Cdd:cd23080      1 GVYVLSVVENMPAK--GILEAGDKITAIDG 28
SH3_BCAR1 cd12001
Src homology 3 domain of the CAS (Crk-Associated Substrate) scaffolding protein family member, ...
 1612-1648 4.04e-03

Src homology 3 domain of the CAS (Crk-Associated Substrate) scaffolding protein family member, Breast Cancer Anti-estrogen Resistance 1; BCAR1, also called p130cas or CASS1, is the founding member of the CAS family of scaffolding proteins and was originally identified through its ability to associate with Crk. The name BCAR1 was designated because the human gene was identified in a screen for genes that promote resistance to tamoxifen. It is widely expressed and its deletion is lethal in mice. It plays a role in regulating cell motility, survival, proliferation, transformation, cancer progression, and bacterial pathogenesis. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212934  Cd Length: 68  Bit Score: 37.71  E-value: 4.04e-03
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gi 1039746878 1612 RALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWM 1648
Cdd:cd12001      6 KALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWL 42
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 658-722 4.16e-03

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: 37.80  E-value: 4.16e-03
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gi 1039746878  658 GIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQaikallngegainmVVRRRKSLGGKVV 722
Cdd:cd06768     24 GHFIREVDPGSPAErAGLKDGDRLVEVNGENVEGESHEQ--------------VVEKIKASGNQVT 75
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 1535-1599 4.35e-03

circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of HtrA family serine proteases including human HtrA1, HtrA2 (mitochondrial), HtrA3, and HtrA4, and related domains. These proteases are key enzymes associated with pregnancy. Their diverse biological functions include cell growth proliferation, migration and apoptosis. They are also implicated in disorders including Alzheimer's, Parkinson's, arthritis and cancer. HtrA1 (also known as high-temperature requirement A serine peptidase 1, L56, and serine protease 11) substrates include extracellular matrix proteins, proteoglycans, and insulin-like growth factor (IGF)-binding proteins. HtrA1 also inhibits signaling by members of the transforming growth factor beta (TGF-beta) family. 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 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 HtrA-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: 467624 [Multi-domain]  Cd Length: 98  Bit Score: 38.25  E-value: 4.35e-03
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gi 1039746878 1535 HGVFVAEVEDDSPA-KGpdGLVPGDLILEYGslDMRSRTVEDVYvEMLKPKDSLRLKVQYRHEEFT 1599
Cdd:cd06785     31 SGVYVHKVIPGSPAqRA--GLKDGDVIISIN--GKPVKSSSDVY-EAVKSGSSLLVVVRRGNEDLL 91
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 751-807 4.36e-03

PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1, and related domains. MPP1 (also known as MAGUK p55 subfamily member 1, erythrocyte membrane protein p55, EMP55) is a membrane-associated guanylate kinase (MAGUK)-like protein which forms a complex with protein 4.1 and glycophorin C (GPC) at the cytoplasmic face of the plasma membrane; this complex is essential for cytoskeleton-membrane linkage in erythrocytes and many non-erythroid cells, and participates in the determination of membrane stability and cell shape. MPP1, by interacting with various scaffold proteins and cytoskeletal proteins in the postsynaptic density, also plays an important role in organizing synaptic and non-synaptic structures. MPP1 is also a component of the Crumbs protein complex in the mammalian retina and may link the Usher protein network and the Crumbs protein complex. The MPP1 PDZ domain binding partners include GPC, ABCC4, and CADM1/Necl-2/SynCAM1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467266 [Multi-domain]  Cd Length: 81  Bit Score: 37.92  E-value: 4.36e-03
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gi 1039746878  751 AAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 807
Cdd:cd10830     28 ARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVS---LKVIP 81
F-BAR_srGAP1 cd07683
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 230-453 4.46e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs. srGAP1, also called Rho GTPase-Activating Protein 13 (ARHGAP13), is a Cdc42- and RhoA-specific GAP and is expressed later in the development of CNS (central nervous system) tissues. It is an important downstream signaling molecule of Robo1. srGAP1 contains an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153367 [Multi-domain]  Cd Length: 253  Bit Score: 41.21  E-value: 4.46e-03
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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  230 HSRLLSDQTQLKddVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEIlNKLYdTAMDK 309
Cdd:cd07683      6 QQKCLEQQTEMR--VQLLQDLQDFFRKKAEIESEYSRNLEKLAERFMAKTRSTKDHQQYKKDQNLLSPV-NCWY-LLLNQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  310 LEVVKKDYDALRKRYSEKVAMhnsdlsRLEQLGEENQRL-QKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATA 388
Cdd:cd07683     82 VRRESKDHATLSDIYLNNVIM------RFMQISEDSTRMfKKSKEIAFQLHEDLMKVLNELYTVMKTYHMYHTESISAES 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  389 QNKDLQWEME--------LLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKL-IMSERDQVISELDKLQTEV 453
Cdd:cd07683    156 KLKEAEKQEEkqigrsgdPVFHIRLEDRHQRRSSVKKIEKMKEKRQAKYSENKLkSIKARNEYLLTLEATNASV 229
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 753-793 4.47e-03

PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), 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 5 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 PDZ5 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: 467157 [Multi-domain]  Cd Length: 98  Bit Score: 38.36  E-value: 4.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1039746878  753 VVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd06669     43 LVPGGVAEQDGRLLPGDRLVFVNDVSLENASLDEAVQALKS 83
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 658-712 4.67e-03

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: 37.88  E-value: 4.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039746878  658 GIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 712
Cdd:cd23063     31 GIFIKGIIPDSPAHkcGRLKVGDRILSVNGNDVRNSTEQAAIDLIKEADFKIVLEIQ 87
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 747-793 4.67e-03

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: 38.14  E-value: 4.67e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1039746878  747 GVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd10834     28 GIYVSKVDPGGLAEQNG-IKVGDQILAVNGVSFEDITHSKAVEVLKS 73
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 1357-1434 5.08e-03

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467285 [Multi-domain]  Cd Length: 92  Bit Score: 38.24  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1357 EPRHVKVQKGSEP-LGISIVSGEKG-----GVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCD 1429
Cdd:cd23072      1 EITLVNLKKDAKYgLGFQIVGGEKSgrldlGIFISSITPGGPADLDGrLKPGDRLISVNDVSLEGLSHDAAVEILQNAPE 80


                   ....*
gi 1039746878 1430 TITIL 1434
Cdd:cd23072     81 DVTLV 85
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1508-1592 5.24e-03

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: 37.92  E-value: 5.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878 1508 KKTPDPRIVfikkSQLDLGVHLCGG-----NLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLK 1582
Cdd:cd06714     10 QRDPKDGSV----SGNGLGLKVVGGkmtesGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEVQDIISQ 85

                           90
                   ....*....|
gi 1039746878 1583 PKDSLRLKVQ 1592
Cdd:cd06714     86 SKGEVELVVS 95
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 396-563 5.27e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  396 EMELLQSELTELRSK--QVKTAKESEKyKEERDAVYSEYKLIMSERDQVISELDKLQTEVElaesklksstsEKKAASEE 473
Cdd:COG0542    405 EIDSKPEELDELERRleQLEIEKEALK-KEQDEASFERLAELRDELAELEEELEALKARWE-----------AEKELIEE 472

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  474 MEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAkcrrdwafqerdKIVA-------------ERDSI 540
Cdd:COG0542    473 IQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIA------------EVVSrwtgipvgkllegEREKL 540

                          170       180
                   ....*....|....*....|....*..
gi 1039746878  541 RTLCDNLrRER----DRAVSELAEALR 563
Cdd:COG0542    541 LNLEEEL-HERvigqDEAVEAVADAIR 566
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 655-691 5.39e-03

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: 37.92  E-value: 5.39e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1039746878  655 GDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINK 691
Cdd:cd06714     36 GRLGAYVTKVKPGSVADtvGHLREGDEVLEWNGISLQGK 74
PDZ0_GgPro-IL-16-like cd23062
PDZ domain 0 of Gallus gallus interleukin-16, and related domains; N-terminal PDZ (PSD-95 ...
 730-793 5.42e-03

PDZ domain 0 of Gallus gallus interleukin-16, and related domains; N-terminal PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1) of Gallus gallus IL16, and related domains. This IL16-PDZ0 domain is not found in the human pro-interleukin-16 (isoform 1, 1332 AA, pro-IL-16) which has 4 PDZ domains (PDZ1-4). Gallus gallus IL-16 has 5 PDZ domains: this N-terminal PDZ0, followed by 4 PDZ domains (PDZ1-4) which are homologous to human pro-IL-16 PDZ1-4. 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, including Gallus gallus IL-16 in the development of ovarian tumor and tumor-associated neoangiogenesis (TAN) in laying hens, an animal model of spontaneous ovarian cancer. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This IL16-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: 467275 [Multi-domain]  Cd Length: 83  Bit Score: 37.95  E-value: 5.42e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  730 SGQKGSRPQDSGiSLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 793
Cdd:cd23062     11 SGIKLSRNPNCA-SLWKGFTGCHVPAGGTANRDGCLSPRDELLTLNGQSLKDLSSKEAESLIQS 73
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1360-1408 5.72e-03

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: 37.71  E-value: 5.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039746878 1360 HVKVQKGSEPLGISIVSGEK-GGVYVSKVTLGSIAHQAG-LEYGDQLLEFN 1408
Cdd:cd10817      1 HVELPKDQGGLGIAISEEDTeNGIVIKSLTEGGPAAKDGrLKVGDQILAVD 51
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 656-715 5.76e-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: 37.65  E-value: 5.76e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  656 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK 715
Cdd:cd06674     26 DTGVFVSDIVKGGAAdaDGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGKVRLEVGRLK 87
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 622-702 5.80e-03

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: 38.07  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  622 ETEVVEFERETEdidlKALGFDMAEGVNEPCFPGD----CGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQ 695
Cdd:cd06671      1 PPRRVELWREPG----KSLGISIVGGRVMGSRLSNgeeiRGIFIKHVLEDSPAGrnGTLKTGDRILEVNGVDLRNATHEE 76


                   ....*..
gi 1039746878  696 AIKALLN 702
Cdd:cd06671     77 AVEAIRN 83
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 ...
 747-779 6.13e-03

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: 37.64  E-value: 6.13e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039746878  747 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIAL 779
Cdd:cd06759     30 GIYVKTIFPGGAAAEDGRLKEGDEILEVNGESL 62
mukB PRK04863
chromosome partition protein MukB;
147-492 6.36e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 6.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  147 ENLSIQLRlmtRERNELRKRLAfathGATFDKRPYHRLNPDYERLKIQCVR---------AMSDLQSLQNQHTNALKRCE 217
Cdd:PRK04863   785 EKRIEQLR---AEREELAERYA----TLSFDVQKLQRLHQAFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHE 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  218 EVaketdfyhtlHSRLLSDQTQLKDDVDMLRrengKLRRERNLLqqswedmkrLREEDQKEIGDLRAQQQQ-------VL 290
Cdd:PRK04863   858 SQ----------EQQQRSQLEQAKEGLSALN----RLLPRLNLL---------ADETLADRVEEIREQLDEaeeakrfVQ 914

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  291 KHNGSSEILNKLYDTamdkLEVVKKDYDALRKRYSE------KVAMHNSDLSRLEQ-------------LGEE---NQRL 348
Cdd:PRK04863   915 QHGNALAQLEPIVSV----LQSDPEQFEQLKQDYQQaqqtqrDAKQQAFALTEVVQrrahfsyedaaemLAKNsdlNEKL 990

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  349 QKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHEL-SKATAQNKDLQwemELLQsELTELRSKQvkTAKESEKYKEERDA 427
Cdd:PRK04863   991 RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLkSSYDAKRQMLQ---ELKQ-ELQDLGVPA--DSGAEERARARRDE 1064

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  428 VYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVtMDAGRAN 492
Cdd:PRK04863  1065 LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDN 1128
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 660-713 6.43e-03

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 36.74  E-value: 6.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746878  660 FVTKVDKGSIAD-GRLRVNDWLLRINDVDLinKDKKQAIKALLNGEGA-INMVVRR 713
Cdd:pfam17820    1 VVTAVVPGSPAErAGLRVGDVILAVNGKPV--RSLEDVARLLQGSAGEsVTLTVRR 54
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 640-715 7.01e-03

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467285 [Multi-domain]  Cd Length: 92  Bit Score: 37.86  E-value: 7.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  640 LGFDMAEGvnEPCFPGDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK 715
Cdd:cd23072     15 LGFQIVGG--EKSGRLDLGIFISSITPGGPADldGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVSQPK 90
COG5022 COG5022
Myosin heavy chain [General function prediction only];
333-584 7.14e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  333 SDLSRLEQLGEENQRLQKQTEMLTQQRdTAIQLQHQCalSLRRFETIHHELSKATAQNKDLqwemELLQSELTELRSKQ- 411
Cdd:COG5022    804 SLLGSRKEYRSYLACIIKLQKTIKREK-KLRETEEVE--FSLKAEVLIQKFGRSLKAKKRF----SLLKKETIYLQSAQr 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  412 -VKTAKESEKYKEERDAVySEYKLIMSERDQVISELDKLQTEVELAESKLKS--STSEKKAASEemealRQIKDTVTMDA 488
Cdd:COG5022    877 vELAERQLQELKIDVKSI-SSLKLVNLELESEIIELKKSLSSDLIENLEFKTelIARLKKLLNN-----IDLEEGPSIEY 950

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  489 GRaNKEVEILRKQCKalcqELKEALQEadvakcrrdwafqerdkivaeRDSIRTLCDNLRRERDRAVSELAEALRSLDDT 568
Cdd:COG5022    951 VK-LPELNKLHEVES----KLKETSEE---------------------YEDLLKKSTILVREGNKANSELKNFKKELAEL 1004

                          250
                   ....*....|....*.
gi 1039746878  569 RKQKNDVSRELKELNS 584
Cdd:COG5022   1005 SKQYGALQESTKQLKE 1020
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1371-1436 7.18e-03

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: 37.33  E-value: 7.18e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1371 GISIvsgeKGGVYVSKVTLGS-IAHQAGLEYGDQLLEFNGINL--RSATEQQARLIIGQQCDTITILAQ 1436
Cdd:cd06765     11 GISL----ENGVFISRIVPGSpAAKEGSLTVGDRIIAINGIALdnKSLSECEALLRSCRDSLSLSLMKV 75
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 640-713 7.52e-03

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: 37.29  E-value: 7.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039746878  640 LGFDMAEGVNepcfpgDCGIFVTK-VDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 713
Cdd:cd06696     16 LGFTVTKGKD------DNGCYIHDiVQDPAKSDGRLRPGDRLIMVNGVDVTNMSHTEAVSLLRAAPKEVTLVLGR 84
PDZ1_GRIP1-2-like cd06687
PDZ domain 1 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 723-800 7.73e-03

PDZ domain 1 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467175 [Multi-domain]  Cd Length: 83  Bit Score: 37.39  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  723 TPLHINLSG--QKGSRPQDSGISlengvyaaavvPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 800
Cdd:cd06687     11 STLGLTVSGgiDKDGKPRVSNLR-----------PGGIAARSDQLNVGDYIKSVNGIRTTKLRHDEIISLLKNVGERVVL 79
PDZ3_harmonin cd06739
PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic ...
 724-797 7.78e-03

PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of harmonin isoforms a and b, 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 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: 467221 [Multi-domain]  Cd Length: 94  Bit Score: 37.67  E-value: 7.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  724 PLHINLSGQKGSrpqdsgiSLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDS 797
Cdd:cd06739     13 PLDLALEGGIDS-------PLGGKIVVSAVYEGGAADKHGGIVKGDQIMMVNGKSLTDVTLAEAEAALQRAMNS 79
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 1370-1413 7.83e-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: 37.46  E-value: 7.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039746878 1370 LGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLR 1413
Cdd:cd06782      4 IGIEIGKDDDGYLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVR 47
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 753-781 8.07e-03

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


Pssm-ID: 467638 [Multi-domain]  Cd Length: 83  Bit Score: 37.17  E-value: 8.07e-03
                           10        20
                   ....*....|....*....|....*....
gi 1039746878  753 VVPGSPAAKEGsLAVGDRIVAINGIALDN 781
Cdd:cd23081      6 VVANSPAAEAG-LKPGDRILKIDGQKVRT 33
PDZ_ARHGAP21_23-like cd06756
PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1382-1435 8.11e-03

PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGAP21, ARHGAP23, and related domains. This subfamily includes the GAPs (GTPase activating proteins): ARHGAP21 (Rho GTPase-activating protein 21; also known as Rho GTPase-activating protein 10, Rho-type GTPase-activating protein 21) and ARHGAP23 (Rho GTPase-activating protein 23; also known as Rho-type GTPase-activating protein 23). GAPs deactivate Rho GTPases by accelerating GTP hydrolysis. ARHGAP21/23 interact with a planar cell polarity (PCP) protein Pk1 to regulate a lateral signaling pathway in migrating cells. The ARHGAP21 PDZ domain binds claudin-2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGAP21-23-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467238 [Multi-domain]  Cd Length: 109  Bit Score: 37.82  E-value: 8.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039746878 1382 VYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITILA 1435
Cdd:cd06756     55 IFVKQVKEGGPAHQAGLCTGDRIVKVNGESVIGKTYSQVIALI-QNSDSTLELS 107
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 658-700 8.26e-03

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: 37.34  E-value: 8.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039746878  658 GIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 700
Cdd:cd06740     28 GIYVSLVEPGSLAEKEgLRVGDQILRVNDVSFEKVTHAEAVKIL 71
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1362-1433 8.45e-03

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


Pssm-ID: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 37.33  E-value: 8.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878 1362 KVQKGSepLGISIVSGEKGG-----VYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1433
Cdd:cd06680      7 RSSSGS--LGFSIVGGYEEShgnqpFFVKSIVPGTPAYNDGrLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTL 82
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 258-480 8.64e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.99  E-value: 8.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  258 RNLLQQSWEDMKRLrEEDQKEIGDLRAQQQQVLKhngssEILNKLYDTaMDKLEvvKKDY----DALRKRYSEKVAMHNS 333
Cdd:pfam06160  178 REVLEKLEEETDAL-EELMEDIPPLYEELKTELP-----DQLEELKEG-YREME--EEGYalehLNVDKEIQQLEEQLEE 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  334 DLSRLEQL-----GEENQRLQKQTEMLTQQRDTAIQLQHQCalsLRRFETIHHELSKATAQNKDLQWEMELLQ------- 401
Cdd:pfam06160  249 NLALLENLeldeaEEALEEIEERIDQLYDLLEKEVDAKKYV---EKNLPEIEDYLEHAEEQNKELKEELERVQqsytlne 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  402 SELTELRS--KQVKTAK----ESEKYKEERDAVYSEyklIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEME 475
Cdd:pfam06160  326 NELERVRGleKQLEELEkrydEIVERLEEKEVAYSE---LQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLD 402


                   ....*
gi 1039746878  476 ALRQI 480
Cdd:pfam06160  403 EFKLE 407
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 639-700 8.81e-03

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: 37.23  E-value: 8.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746878  639 ALGFDMAEGVNEPcfPGDCGIFVTKVD-KGSIA-DGRLRVNDWLLRINDVDLINKDKKQAIKAL 700
Cdd:cd06679     12 SLGISVAGGRGSR--RGDLPIYVTNVQpDGCLGrDGRIKKGDVLLSINGISLTNLSHSEAVAVL 73
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 ...
 638-712 8.90e-03

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: 37.25  E-value: 8.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746878  638 KALGFDMAEGVNEPcfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN-GEGAINMVVR 712
Cdd:cd06759     12 KGLGFSIVGGRDSP--RGPMGIYVKTIFPGGAAaeDGRLKEGDEILEVNGESLQGLTHQEAIQKFKQiKKGLVVLTVR 87
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 747-776 8.94e-03

circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of HtrA family serine proteases including human HtrA1, HtrA2 (mitochondrial), HtrA3, and HtrA4, and related domains. These proteases are key enzymes associated with pregnancy. Their diverse biological functions include cell growth proliferation, migration and apoptosis. They are also implicated in disorders including Alzheimer's, Parkinson's, arthritis and cancer. HtrA1 (also known as high-temperature requirement A serine peptidase 1, L56, and serine protease 11) substrates include extracellular matrix proteins, proteoglycans, and insulin-like growth factor (IGF)-binding proteins. HtrA1 also inhibits signaling by members of the transforming growth factor beta (TGF-beta) family. 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 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 HtrA-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: 467624 [Multi-domain]  Cd Length: 98  Bit Score: 37.48  E-value: 8.94e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039746878  747 GVYAAAVVPGSPAAKEGsLAVGDRIVAING 776
Cdd:cd06785     32 GVYVHKVIPGSPAQRAG-LKDGDVIISING 60
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
445-640 9.31e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 9.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  445 ELDKLQTEVELAESKLKS------STSEKKAASEEMEALRQIKDTVtmDAGRANKEVEILRKQCKALCQELKEALQEADV 518
Cdd:COG4913    236 DLERAHEALEDAREQIELlepireLAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELER 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746878  519 AKcrrdwafqerdkivAERDSIRTLCDNLRRERDRA-VSELAEALRSLDDTRKQKNDVSRELKELNSCVHREQMECQLEK 597
Cdd:COG4913    314 LE--------------ARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039746878  598 E---ARFRQLMAH----SSHDSAIDTDSMEWETEVVEFERETEDI--DLKAL 640
Cdd:COG4913    380 EefaALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELeaEIASL 431
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 656-702 9.65e-03

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: 36.78  E-value: 9.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039746878  656 DCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLN 702
Cdd:cd06729     22 DVGIFVAGVQEGSPAEKQgLQEGDQILKVNGVDFRNLTREEAVLFLLD 69
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 1361-1420 9.84e-03

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: 37.24  E-value: 9.84e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746878 1361 VKVQKGSEPLGISIVSGE--------KGGVYVSKVTLGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1420
Cdd:cd06695      4 VKLTKGSSGLGFSFLGGEnnspedpfSGLVRIKKLFPGQPAAESGlIQEGDVILAVNGEPLKGLSYQEV 72
 
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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