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Conserved domains on  [gi|741978460|ref|XP_010818904|]
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disks large homolog 5 isoform X4 [Bos taurus]

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 ...
 615-709 6.18e-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: 197.62  E-value: 6.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  615 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCLPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 694
Cdd:cd06764     1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                          90
                  ....*....|....*
gi 741978460  695 LLNGEGAINMVVRRR 709
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 ...
 1315-1396 1.95e-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: 167.12  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1315 EEPRHVKLQKGSEPLGISIVSGEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1394
Cdd:cd06767     1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                  ..
gi 741978460 1395 QY 1396
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 ...
 1470-1550 1.99e-48

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: 167.18  E-value: 1.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1470 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKV 1549
Cdd:cd06766     1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                  .
gi 741978460 1550 Q 1550
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 ...
 721-797 1.38e-43

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: 152.89  E-value: 1.38e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  721 HINLSGHKDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 797
Cdd:cd06765     1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1703-1879 3.01e-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: 147.44  E-value: 3.01e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1703 QKVDCTSLRPVLILG---PFLDVVKEMLVNEAPSKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1779
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1780 ITEKNRHCLLDVAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylKDKVTQRHSKEQFETAQKIEQEYsRYFTGVV 1859
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 741978460   1860 QGGALSSICTQILAVVNQEQ 1879
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1568-1630 8.41e-34

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: 124.76  E-value: 8.41e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460 1568 YIRALYERLAEVEPELSFKKDDILYVDDTLPQGSFGSWMAWQLDENAQKMQRGQIPSKYVMDQ 1630
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 ...
 1396-1470 2.80e-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: 118.08  E-value: 2.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1396 YNPHMHQLSSHSRSSSHLDPVGIHSTLQGSGATTPEHPSVIDPLMEQDEGPGTPPAKQSIPSS------RMVGDATKKTP 1469
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTTPATsphnsfRMPGDANKRVP 80


                   .
gi 741978460  1470 E 1470
Cdd:pfam16610   81 E 81
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 129-213 5.06e-30

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: 114.66  E-value: 5.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   129 KAPSPPPVLSDRQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTTFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQSQ 208
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 741978460   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 ...
 338-636 1.94e-17

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: 89.35  E-value: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   338 LEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTTQAK 413
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   414 TAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANK 493
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   494 EAEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKN 573
Cdd:TIGR02168  860 EIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460   574 DVSRELKELKEQMESQLEK--EARFRHLMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 636
Cdd:TIGR02168  926 QLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 860-1287 5.50e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  860 PPGGSSSFLHKPFPGGPFSVSPQACP--SASERSLSSFRSDASGERGYGPAD--MRSRRPLLPfeTEVGPCGA-AEAPLD 934
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPrdDPAPGRVSRPRRARRLGRAAQASSppQRPRRRAAR--PTVGSLTSlADPPPP 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  935 KAEPDSAhsggtwPKAVLSSVAGPEKLSVYRKPKqrksifdPNTFKRPQTPPKIDYLLPGSGPAHSPLPSKRVGPLTPPK 1014
Cdd:PHA03247 2705 PPTPEPA------PHALVSATPLPPGPAAARQAS-------PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1015 PPRRGdsikfqhkleTSSESEATLVGSSPSTSPPSALPPDVDPGDPMHASPPRKARVRIASSYCPEGDRDSSYLPAKKSc 1094
Cdd:PHA03247 2772 PAAPA----------AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP- 2840

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1095 dedLTSQKEQKCTPASGELSP--DLQEWAPYSPGHSSrhsnpPFYPSRASVGTVPRSLAPSTVSSVLRNPIYTVRSHRVG 1172
Cdd:PHA03247 2841 ---PPPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAK-----PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1173 PCSSP-PIPREAGPHGLHPSVQHQGRLSLDLSPRACsdcsdmrashgsnslPSSARLATGSSSNLQFKAeriKIPSTPRY 1251
Cdd:PHA03247 2913 APPPPqPQPQPPPPPQPQPPPPPPPRPQPPLAPTTD---------------PAGAGEPSGAVPQPWLGA---LVPGRVAV 2974

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 741978460 1252 PRSVVGSDRGSLSHSECSTPPQSPLSVEGLSSCSQS 1287
Cdd:PHA03247 2975 PRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASS 3010
PRK04778 super family cl32064
septation ring formation regulator EzrA; Provisional
 189-407 2.47e-05

septation ring formation regulator EzrA; Provisional


The actual alignment was detected with superfamily member PRK04778:

Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.06  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  189 ERLKIQCVRAMSDLQSLQSQHTNALKrcEEVAKETD-FYHTL------HSRLLSDQTQLKDDVDMLRRENGQLLRERNLL 261
Cdd:PRK04778  259 QDLKEQIDENLALLEELDLDEAEEKN--EEIQERIDqLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  262 QQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------ALRK 322
Cdd:PRK04778  337 KQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGLRK 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  323 rySEKVAIHNsdLSRLEQMEEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATAQN 390
Cdd:PRK04778  412 --DELEAREK--LERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATEDV 485

                         250
                  ....*....|....*....
gi 741978460  391 KDLQWEMELL--QSELTEL 407
Cdd:PRK04778  486 ETLEEETEELveNATLTEQ 504
 
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 ...
 615-709 6.18e-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: 197.62  E-value: 6.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  615 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCLPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 694
Cdd:cd06764     1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                          90
                  ....*....|....*
gi 741978460  695 LLNGEGAINMVVRRR 709
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 ...
 1315-1396 1.95e-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: 167.12  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1315 EEPRHVKLQKGSEPLGISIVSGEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1394
Cdd:cd06767     1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                  ..
gi 741978460 1395 QY 1396
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 ...
 1470-1550 1.99e-48

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: 167.18  E-value: 1.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1470 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKV 1549
Cdd:cd06766     1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                  .
gi 741978460 1550 Q 1550
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 ...
 721-797 1.38e-43

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: 152.89  E-value: 1.38e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  721 HINLSGHKDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 797
Cdd:cd06765     1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1703-1879 3.01e-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: 147.44  E-value: 3.01e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1703 QKVDCTSLRPVLILG---PFLDVVKEMLVNEAPSKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1779
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1780 ITEKNRHCLLDVAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylKDKVTQRHSKEQFETAQKIEQEYsRYFTGVV 1859
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 741978460   1860 QGGALSSICTQILAVVNQEQ 1879
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1568-1630 8.41e-34

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: 124.76  E-value: 8.41e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460 1568 YIRALYERLAEVEPELSFKKDDILYVDDTLPQGSFGSWMAWQLDENAQKMQRGQIPSKYVMDQ 1630
Cdd:cd11860     1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
dbPDZ_assoc pfam16610
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1396-1470 2.80e-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: 118.08  E-value: 2.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1396 YNPHMHQLSSHSRSSSHLDPVGIHSTLQGSGATTPEHPSVIDPLMEQDEGPGTPPAKQSIPSS------RMVGDATKKTP 1469
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTTPATsphnsfRMPGDANKRVP 80


                   .
gi 741978460  1470 E 1470
Cdd:pfam16610   81 E 81
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 129-213 5.06e-30

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: 114.66  E-value: 5.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   129 KAPSPPPVLSDRQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTTFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQSQ 208
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 741978460   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 ...
 1316-1398 7.41e-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: 7.41e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1316 EPRHVKLQKGSEPLGISIVSG--EKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....*
gi 741978460   1394 AQYNP 1398
Cdd:smart00228   81 VLRGG 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 338-636 1.94e-17

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: 89.35  E-value: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   338 LEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTTQAK 413
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   414 TAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANK 493
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   494 EAEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKN 573
Cdd:TIGR02168  860 EIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460   574 DVSRELKELKEQMESQLEK--EARFRHLMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 636
Cdd:TIGR02168  926 QLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1470-1553 4.44e-15

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 72.03  E-value: 4.44e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1470 EPRVVFIKKSQLELGVHLCGG--NLHGVFVAEVEDDSPARGpDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRL 1547
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79


                    ....*.
gi 741978460   1548 KVQYRP 1553
Cdd:smart00228   80 TVLRGG 85
Guanylate_kin pfam00625
Guanylate kinase;
1709-1878 7.88e-15

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 74.72  E-value: 7.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1709 SLRPVLILGPFL---DVVKEMLVNEAPSKFCRC---------PLEV-----MKASQQAIERGVKDCLFVDYKRRSGHFDV 1771
Cdd:pfam00625    1 SRRPVVLSGPSGvgkSHIKKALLSEYPDKFGYSvphttrpprKGEVdgkdyYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1772 TTVASIKEITEKNRHCLLDVAPHAIERLHHMHIYPIVIFIHYKSAKHIKEqrdpiyLKDKVTQRHSKEQFETAQKIEQEY 1851
Cdd:pfam00625   81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQR------RLKGRGKEQEEKINKRMAAAEQEF 154

                          170       180
                   ....*....|....*....|....*...
gi 741978460  1852 SRY-FTGVVQGGALSSICTQILAVVNQE 1878
Cdd:pfam00625  155 QHYeFDVIIVNDDLEEAYKKLKEALEAE 182
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 715-793 5.11e-13

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: 66.25  E-value: 5.11e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460    715 KVVTPLHINLSGHKDSGisleNGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:smart00228    9 KGGGGLGFSLVGGKDEG----GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
218-641 1.04e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 73.26  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  218 EVAKETdFYHTLHSRLLSdqtQLKDDVDMLRRENGQL----LRERNLLQQSWEDMKRLHEE---DQKEIGDLRAQQQQVl 290
Cdd:COG4717    33 EAGKST-LLAFIRAMLLE---RLEKEADELFKPQGRKpelnLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEEL- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  291 khngssEILNKLYDTAMDKLEVVKKDYDaLRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCA 370
Cdd:COG4717   108 ------EAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  371 LSLRRF-EAIHHELNKATAQNKDLQWEMELLQSELTELR-------------TTQAKTAKESEKYKEER----------- 425
Cdd:COG4717   181 ELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQeeleeleeeleqlENELEAAALEERLKEARlllliaaalla 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  426 -----DAVYSEYKLIM---------------------SERDQVISELDKLQTEVELAESKLKS-----STSEKKAASEEM 474
Cdd:COG4717   261 llglgGSLLSLILTIAgvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEELL 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  475 EALRQIKDTVTMDAGRANKEAEIlrkQCKALCQELKEALQEADVAKcrrDWAFQERDKIVAERDSIRTLCDNLRRERDRA 554
Cdd:COG4717   341 ELLDRIEELQELLREAEELEEEL---QLEELEQEIAALLAEAGVED---EEELRAALEQAEEYQELKEELEELEEQLEEL 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  555 VSELAEALRSLDDT--RKQKNDVSRELKELKEQMESQLEKEARFRHLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDL 632
Cdd:COG4717   415 LGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494


                  ....*....
gi 741978460  633 KALGFDMAE 641
Cdd:COG4717   495 LKLALELLE 503
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 217-619 1.24e-12

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: 72.62  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   217 EEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQ----QQVLKH 292
Cdd:pfam07888   55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRaaheARIREL 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   293 NGSSEILNK---LYDTAMDKL-EVVKKDYDALRKRYSEKVAIHnsdlSRLEQMEEENQRLLKQTEMLTQ---QRDT-AIQ 364
Cdd:pfam07888  135 EEDIKTLTQrvlERETELERMkERAKKAGAQRKEEEAERKQLQ----AKLQQTEEELRSLSKEFQELRNslaQRDTqVLQ 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   365 LQHQCAlslrrfeAIHHELNkaTAQNKDLqwEMELLQSELTELRTTQAKTAKESEKYKEERDAVyseykliMSERDQVIS 444
Cdd:pfam07888  211 LQDTIT-------TLTQKLT--TAHRKEA--ENEALLEELRSLQERLNASERKVEGLGEELSSM-------AAQRDRTQA 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   445 ELDKL-----QTEVELAESKLKssTSEKKAA-SEEMEALRQikdTVTMDAGRANK-EAEILRKQckalcqelkEALQEAD 517
Cdd:pfam07888  273 ELHQArlqaaQLTLQLADASLA--LREGRARwAQERETLQQ---SAEADKDRIEKlSAELQRLE---------ERLQEER 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   518 VakcrrdwafqERDKIVAE----RDSIRTLCDNLRRErdraVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKE 593
Cdd:pfam07888  339 M----------EREKLEVElgreKDCNRVQLSESRRE----LQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404

                          410       420
                   ....*....|....*....|....*.
gi 741978460   594 ARFRHLMAHSSHDSAIDTDSMEWETE 619
Cdd:pfam07888  405 ADAKWSEAALTSTERPDSPLSDSEDE 430
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
336-633 5.72e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 67.76  E-value: 5.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  336 SRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEaihhelnkataqnkDLQWEMELLQSELTELRTTQAKTA 415
Cdd:PRK02224  206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE--------------ERREELETLEAEIEDLRETIAETE 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  416 KESEKYKEErdavyseykliMSERDQVISELDKLQTEVeLAESKLKSSTSEKKAA-----SEEMEALRQIKDTVTMDAGR 490
Cdd:PRK02224  272 REREELAEE-----------VRDLRERLEELEEERDDL-LAEAGLDDADAEAVEArreelEDRDEELRDRLEECRVAAQA 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  491 ANKEAEILRKQCKALCQELKEALQEA-----DVAKCRRDWAfQERDKIVAERDSIRTL---CDNLRRERDRAVSELAEAL 562
Cdd:PRK02224  340 HNEEAESLREDADDLEERAEELREEAaelesELEEAREAVE-DRREEIEELEEEIEELrerFGDAPVDLGNAEDFLEELR 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  563 RSLDDTRKQKNDVSRELKELKEQMEsqlekEARfRHLMA-----------HSSHDSAIDtdsmEWETEVVEFERETEDID 631
Cdd:PRK02224  419 EERDELREREAELEATLRTARERVE-----EAE-ALLEAgkcpecgqpveGSPHVETIE----EDRERVEELEAELEDLE 488


                  ..
gi 741978460  632 LK 633
Cdd:PRK02224  489 EE 490
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1320-1395 1.83e-10

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 58.83  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1320 VKLQK-GSEPLGISIVSGEKG---GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1395
Cdd:pfam00595    2 VTLEKdGRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-485 2.30e-09

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: 62.77  E-value: 2.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   140 RQVNEKVENLSIQLRLMTRERNELRKRLAfathgttfdkrpyhRLNPDYERLKIQCVRAMSDLQSLQSQHTNALKRCEEV 219
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   220 AKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngsseiL 299
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------L 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   300 NKLYDTAMDKLEVVKKDYDALRKRY----------SEKVAIHNSDLSRLEQMEEEnqrLLKQTEMLTQQRDtaiQLQHQC 369
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEE---LESELEALLNERA---SLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   370 ALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYS-EYKLIMSERDQVISELDK 448
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEE 969

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 741978460   449 LQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVT 485
Cdd:TIGR02168  970 ARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 617-710 2.93e-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: 2.93e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460    617 ETEVVEFERETEDidlkaLGFDMAEGVNEpclpgDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 695
Cdd:smart00228    1 EPRLVELEKGGGG-----LGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                            90
                    ....*....|....*
gi 741978460    696 LNGEGAINMVVRRRK 710
Cdd:smart00228   71 KKAGGKVTLTVLRGG 85
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1565-1627 5.80e-08

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: 51.00  E-value: 5.80e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460   1565 DSFYIRALYERLAEVEPELSFKKDDILYVDDTLPQGsfgsWMAWQLDenaqKMQRGQIPSKYV 1627
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG----WWKGRLG----RGKEGLFPSNYV 55
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 417-592 1.02e-07

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: 54.67  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  417 ESEKYKEERDAVySEYKLIMSERDQVISELDKLQTEV-----ELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRA 491
Cdd:cd07596     2 EDQEFEEAKDYI-LKLEEQLKKLSKQAQRLVKRRRELgsalgEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  492 NKEAeilRKQCKALCQELKEALQEADVAKCrrdwAFQERDKIVAERDSIRTLCDNLRRERDRAVS-------ELAEALRS 564
Cdd:cd07596    81 EAQA---NQELVKLLEPLKEYLRYCQAVKE----TLDDRADALLTLQSLKKDLASKKAQLEKLKAapgikpaKVEELEEE 153

                         170       180
                  ....*....|....*....|....*...
gi 741978460  565 LDDTRKQKNDVSRELKELKEQMESQLEK 592
Cdd:cd07596   154 LEEAESALEEARKRYEEISERLKEELKR 181
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-496 1.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  144 EKVENLSIQLRLMTRERNELRKRLAfathgttfDKRPYHRLnpdYERLKiqcvRAMSDLQSLQSQHT------------N 211
Cdd:PRK03918  331 KELEEKEERLEELKKKLKELEKRLE--------ELEERHEL---YEEAK----AKKEELERLKKRLTgltpeklekeleE 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  212 ALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRREN------GQLLRE---RNLLQQSWEDMKRLhEEDQKEIG-- 280
Cdd:PRK03918  396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEehrKELLEEYTAELKRI-EKELKEIEek 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  281 --DLRAQQQQVLKHNGSSEILNKLYDTA--------------MDKLEVVKKDYDALRKRYSE---KVAIHNSDLSRLEQM 341
Cdd:PRK03918  475 erKLRKELRELEKVLKKESELIKLKELAeqlkeleeklkkynLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEEL 554

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  342 EEENQRLLKQ--------TEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAK 413
Cdd:PRK03918  555 KKKLAELEKKldeleeelAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  414 TAKES-------------------EKYKEERD----------AVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSST 464
Cdd:PRK03918  635 LAETEkrleelrkeleelekkyseEEYEELREeylelsrelaGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714

                         410       420       430
                  ....*....|....*....|....*....|...
gi 741978460  465 SEKKAAsEEMEALRQ-IKDTVTMDAGRANKEAE 496
Cdd:PRK03918  715 KLEKAL-ERVEELREkVKKYKALLKERALSKVG 746
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 719-793 1.52e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 50.36  E-value: 1.52e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460   719 PLHINLSGHKDSGIsleNGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:pfam00595   11 GLGFSLKGGSDQGD---PGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 731-782 4.48e-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: 4.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 741978460  731 GISL---ENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 782
Cdd:COG0793    63 GAELgeeDGKVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLLR 116
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1472-1550 6.64e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 48.82  E-value: 6.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1472 RVVFIKKSQLELGVHLCGGN---LHGVFVAEVEDDSPARGpDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLK 1548
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79


                   ..
gi 741978460  1549 VQ 1550
Cdd:pfam00595   80 IL 81
PHA03247 PHA03247
large tegument protein UL36; Provisional
 860-1287 5.50e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  860 PPGGSSSFLHKPFPGGPFSVSPQACP--SASERSLSSFRSDASGERGYGPAD--MRSRRPLLPfeTEVGPCGA-AEAPLD 934
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPrdDPAPGRVSRPRRARRLGRAAQASSppQRPRRRAAR--PTVGSLTSlADPPPP 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  935 KAEPDSAhsggtwPKAVLSSVAGPEKLSVYRKPKqrksifdPNTFKRPQTPPKIDYLLPGSGPAHSPLPSKRVGPLTPPK 1014
Cdd:PHA03247 2705 PPTPEPA------PHALVSATPLPPGPAAARQAS-------PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1015 PPRRGdsikfqhkleTSSESEATLVGSSPSTSPPSALPPDVDPGDPMHASPPRKARVRIASSYCPEGDRDSSYLPAKKSc 1094
Cdd:PHA03247 2772 PAAPA----------AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP- 2840

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1095 dedLTSQKEQKCTPASGELSP--DLQEWAPYSPGHSSrhsnpPFYPSRASVGTVPRSLAPSTVSSVLRNPIYTVRSHRVG 1172
Cdd:PHA03247 2841 ---PPPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAK-----PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1173 PCSSP-PIPREAGPHGLHPSVQHQGRLSLDLSPRACsdcsdmrashgsnslPSSARLATGSSSNLQFKAeriKIPSTPRY 1251
Cdd:PHA03247 2913 APPPPqPQPQPPPPPQPQPPPPPPPRPQPPLAPTTD---------------PAGAGEPSGAVPQPWLGA---LVPGRVAV 2974

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 741978460 1252 PRSVVGSDRGSLSHSECSTPPQSPLSVEGLSSCSQS 1287
Cdd:PHA03247 2975 PRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASS 3010
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1493-1549 7.07e-06

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: 49.76  E-value: 7.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460 1493 HGVFVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKV 1549
Cdd:COG0265   201 EGVLVARVEPGSPAaKA--GLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTV 256
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 189-407 2.47e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.06  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  189 ERLKIQCVRAMSDLQSLQSQHTNALKrcEEVAKETD-FYHTL------HSRLLSDQTQLKDDVDMLRRENGQLLRERNLL 261
Cdd:PRK04778  259 QDLKEQIDENLALLEELDLDEAEEKN--EEIQERIDqLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  262 QQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------ALRK 322
Cdd:PRK04778  337 KQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGLRK 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  323 rySEKVAIHNsdLSRLEQMEEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATAQN 390
Cdd:PRK04778  412 --DELEAREK--LERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATEDV 485

                         250
                  ....*....|....*....
gi 741978460  391 KDLQWEMELL--QSELTEL 407
Cdd:PRK04778  486 ETLEEETEELveNATLTEQ 504
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 183-485 2.57e-05

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: 49.25  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   183 RLNPDYERLKIQCVRAMSDLQSLQSQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQL-------L 255
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeqikklQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   256 RERNLLQQSWEDMKRLHEEDQKEIGDLRAQ----QQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIH 331
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   332 NSDLSRLEQMEEENQRLLKQTEMLTQ----------QRDTAI-----------------QLQHQCALSLRRFEAIHHELN 384
Cdd:TIGR04523  499 KKLNEEKKELEEKVKDLTKKISSLKEkieklesekkEKESKIsdledelnkddfelkkeNLEKEIDEKNKEIEELKQTQK 578

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   385 KATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKsST 464
Cdd:TIGR04523  579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK-EI 657

                          330       340
                   ....*....|....*....|.
gi 741978460   465 SEKKAaseemEALRQIKDTVT 485
Cdd:TIGR04523  658 RNKWP-----EIIKKIKESKT 673
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 635-707 4.05e-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: 4.05e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460   635 LGFDMAEGVNEpclpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 707
Cdd:pfam00595   12 LGFSLKGGSDQ----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 1493-1549 2.09e-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: 46.06  E-value: 2.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  1493 HGVFVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKV 1549
Cdd:TIGR02037  257 RGALVAQVLPGSPAeKA--GLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGI 312
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1329-1381 2.09e-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: 45.14  E-value: 2.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1329 LGISIVS-----------GEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1381
Cdd:COG0265   180 LGVTIQPvtpelaealglPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSARDLQRLL 243
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 152-476 4.17e-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: 45.71  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  152 QLRLMTRERNELRKRLAFAThgttFDKRPYHRL----------------NPDYERLKIQCVRAMSDLQSLQSQHTNALKR 215
Cdd:COG3096   786 RLEELRAERDELAEQYAKAS----FDVQKLQRLhqafsqfvgghlavafAPDPEAELAALRQRRSELERELAQHRAQEQQ 861

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  216 CEEVAKETDFYHTLHSRLLSDQTQLKDD-----VDMLRRENGQLLRERNLLQQSWEDMKRLheEDQKEIgdLRAQQQQVl 290
Cdd:COG3096   862 LRQQLDQLKEQLQLLNKLLPQANLLADEtladrLEELREELDAAQEAQAFIQQHGKALAQL--EPLVAV--LQSDPEQF- 936

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  291 khngssEILNKLYDTAMDKLEVVKKDYDAL---RKR-----YSEKVAI--HNSDLS-----RLEQMEEEnqrllkqtemL 355
Cdd:COG3096   937 ------EQLQADYLQAKEQQRRLKQQIFALsevVQRrphfsYEDAVGLlgENSDLNeklraRLEQAEEA----------R 1000

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  356 TQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQseltelrtTQAKTAKEsEKYKEERDAVYSEYKLI 435
Cdd:COG3096  1001 REAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG--------VQADAEAE-ERARIRRDELHEELSQN 1071

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 741978460  436 MSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEA 476
Cdd:COG3096  1072 RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 238-423 2.32e-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: 41.04  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   238 TQLKDDVDMLRRENGQLLRERNLLQQswedMKRLHEEDQKEIGDLRAQQQQVL-KHNGSSEILNKLYDTAMDKLEVVKKd 316
Cdd:pfam15619   14 KELQNELAELQSKLEELRKENRLLKR----LQKRQEKALGKYEGTESELPQLIaRHNEEVRVLRERLRRLQEKERDLER- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   317 ydALRKRYSEkvaIH--NSDLSRLEQM--------EEENQRLLKQTEMLTQQRDTAIQ-LQHQCALSLRRFeaiHHELNK 385
Cdd:pfam15619   89 --KLKEKEAE---LLrlRDQLKRLEKLsedknlaeREELQKKLEQLEAKLEDKDEKIQdLERKLELENKSF---RRQLAA 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 741978460   386 ATAQNKDLQWEMELLQSELTELRTtqaktaKESEKYKE 423
Cdd:pfam15619  161 EKKKHKEAQEEVKILQEEIERLQQ------KLKEKERE 192
 
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 ...
 615-709 6.18e-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: 197.62  E-value: 6.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  615 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCLPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 694
Cdd:cd06764     1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                          90
                  ....*....|....*
gi 741978460  695 LLNGEGAINMVVRRR 709
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 ...
 1315-1396 1.95e-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: 167.12  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1315 EEPRHVKLQKGSEPLGISIVSGEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1394
Cdd:cd06767     1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                  ..
gi 741978460 1395 QY 1396
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 ...
 1470-1550 1.99e-48

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: 167.18  E-value: 1.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1470 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKV 1549
Cdd:cd06766     1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                  .
gi 741978460 1550 Q 1550
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 ...
 721-797 1.38e-43

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: 152.89  E-value: 1.38e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  721 HINLSGHKDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 797
Cdd:cd06765     1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1703-1879 3.01e-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: 147.44  E-value: 3.01e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1703 QKVDCTSLRPVLILG---PFLDVVKEMLVNEAPSKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1779
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1780 ITEKNRHCLLDVAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylKDKVTQRHSKEQFETAQKIEQEYsRYFTGVV 1859
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 741978460   1860 QGGALSSICTQILAVVNQEQ 1879
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1568-1630 8.41e-34

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: 124.76  E-value: 8.41e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460 1568 YIRALYERLAEVEPELSFKKDDILYVDDTLPQGSFGSWMAWQLDENAQKMQRGQIPSKYVMDQ 1630
Cdd:cd11860     1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
dbPDZ_assoc pfam16610
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1396-1470 2.80e-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: 118.08  E-value: 2.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1396 YNPHMHQLSSHSRSSSHLDPVGIHSTLQGSGATTPEHPSVIDPLMEQDEGPGTPPAKQSIPSS------RMVGDATKKTP 1469
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTTPATsphnsfRMPGDANKRVP 80


                   .
gi 741978460  1470 E 1470
Cdd:pfam16610   81 E 81
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 129-213 5.06e-30

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: 114.66  E-value: 5.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   129 KAPSPPPVLSDRQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTTFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQSQ 208
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 741978460   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 ...
 1316-1398 7.41e-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: 7.41e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1316 EPRHVKLQKGSEPLGISIVSG--EKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....*
gi 741978460   1394 AQYNP 1398
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) ...
 1316-1398 1.09e-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: 82.40  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1316 EPRHVKLQKGSEPLGISIVSGEKG-GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:cd06795     1 EPRKIVLHKGSTGLGFNIVGGEDGeGIFISFILAGGPADLSGeLRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTII 80


                  ....*
gi 741978460 1394 AQYNP 1398
Cdd:cd06795    81 AQYKP 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 338-636 1.94e-17

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: 89.35  E-value: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   338 LEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTTQAK 413
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   414 TAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANK 493
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   494 EAEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKN 573
Cdd:TIGR02168  860 EIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460   574 DVSRELKELKEQMESQLEK--EARFRHLMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 636
Cdd:TIGR02168  926 QLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1319-1393 2.48e-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: 75.27  E-value: 2.48e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1319 HVKLQKGS-EPLGISIVSGE--KGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:cd00136     1 TVTLEKDPgGGLGFSIRGGKdgGGGIFVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLT 79
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1316-1395 6.11e-16

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: 74.35  E-value: 6.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1316 EPRHVKLQKGSEPLGISIVSGEKGGVYVSKVTGGSIAHQA-GLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1394
Cdd:cd06766     1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPdGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                  .
gi 741978460 1395 Q 1395
Cdd:cd06766    81 Q 81
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 702-790 6.45e-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: 74.12  E-value: 6.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  702 INMVVRRRKSLGgkvvtplhINLSGhkdsGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL 781
Cdd:cd00136     2 VTLEKDPGGGLG--------FSIRG----GKDGGGGIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELL 69


                  ....*....
gi 741978460  782 RSCQDSLTL 790
Cdd:cd00136    70 KSAGGEVTL 78
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 628-709 1.47e-15

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: 73.50  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  628 EDIDL----KALGFDMAEGVNEPCLPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGA 701
Cdd:cd06723     2 EEITLergnSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAaaDGRLRVNDIILRVNDVDVRNVTHSVAVEALKEAGSI 81


                  ....*...
gi 741978460  702 INMVVRRR 709
Cdd:cd06723    82 VRLYVKRR 89
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1470-1553 4.44e-15

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 72.03  E-value: 4.44e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   1470 EPRVVFIKKSQLELGVHLCGG--NLHGVFVAEVEDDSPARGpDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRL 1547
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79


                    ....*.
gi 741978460   1548 KVQYRP 1553
Cdd:smart00228   80 TVLRGG 85
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 620-707 7.09e-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: 7.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  620 VVEFERETEdidlKALGFDMAEGVNepclpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd00136     1 TVTLEKDPG----GGLGFSIRGGKD-----GGGGIFVSRVEPGGPAarDGRLRVGDRILEVNGVSLEGLTHEEAVELLKS 71

                          90
                  ....*....|
gi 741978460  698 GEGAINMVVR 707
Cdd:cd00136    72 AGGEVTLTVR 81
Guanylate_kin pfam00625
Guanylate kinase;
1709-1878 7.88e-15

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 74.72  E-value: 7.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1709 SLRPVLILGPFL---DVVKEMLVNEAPSKFCRC---------PLEV-----MKASQQAIERGVKDCLFVDYKRRSGHFDV 1771
Cdd:pfam00625    1 SRRPVVLSGPSGvgkSHIKKALLSEYPDKFGYSvphttrpprKGEVdgkdyYFVSKEEMERDISANEFLEYAQFSGNMYG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1772 TTVASIKEITEKNRHCLLDVAPHAIERLHHMHIYPIVIFIHYKSAKHIKEqrdpiyLKDKVTQRHSKEQFETAQKIEQEY 1851
Cdd:pfam00625   81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQR------RLKGRGKEQEEKINKRMAAAEQEF 154

                          170       180
                   ....*....|....*....|....*...
gi 741978460  1852 SRY-FTGVVQGGALSSICTQILAVVNQE 1878
Cdd:pfam00625  155 QHYeFDVIIVNDDLEEAYKKLKEALEAE 182
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 297-597 1.87e-14

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: 79.33  E-value: 1.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   297 EILNKLYDTA--MDKLEVV----KKDYDALRK------RYSE-KVAIHNSDLS----RLEQMEEENQRLLKQTEMLTQQR 359
Cdd:TIGR02168  176 ETERKLERTRenLDRLEDIlnelERQLKSLERqaekaeRYKElKAELRELELAllvlRLEELREELEELQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   360 DTAIQLQHQCALSLRRFEAIHHELNKataqnkdlqwEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSER 439
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEE----------EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   440 DQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKdtvtmdagranKEAEILRKQCKALCQELKEALQEADva 519
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL-----------EELESRLEELEEQLETLRSKVAQLE-- 392

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460   520 kcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDdtRKQKNDVSRELKELKEQMESQLEKEARFR 597
Cdd:TIGR02168  393 --------LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLE 460
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 183-550 5.09e-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: 5.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   183 RLNPDYERLKIQCVRAMSDLQSLQsQHTNALKRCEEVAKETdfyhtlHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQ 262
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIE-NRLDELSQELSDASRK------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   263 QSWEDMKRLHEEDQKEIGDLRAQQQQVlkhngsSEILNKLYDT-AMDKLEVVKKDYDALRKRYSEKVAihnsdlsRLEQM 341
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKL------EEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEA-------RLREI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   342 EEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNkatAQNKDLQWEMELLQSELTELRTTQAKTAKESEKY 421
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   422 KEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDtvtmdagrankeaeiLRKQ 501
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED---------------VQAE 959

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460   502 CKALCQELKE-------ALQEADVAKCRRDWAFQERDKIVAERDSIRTL---CDNLRRE 550
Cdd:TIGR02169  960 LQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERieeYEKKKRE 1018
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 248-597 5.96e-14

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: 77.79  E-value: 5.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   248 RRENGQLLRERNL--LQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDALRK--- 322
Cdd:TIGR02168  667 KTNSSILERRREIeeLEEKIEELEEKIAELEKALAELRKELEELEE---ELEQLRKELEELSRQISALRKDLARLEAeve 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   323 RYSEKVAIHNSDLSRL-EQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKataqnkdlqwemelLQ 401
Cdd:TIGR02168  744 QLEERIAQLSKELTELeAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE--------------LR 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   402 SELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQ-------VISELDKLQTEVELAESKLKSSTSEKKAASEEM 474
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEElsediesLAAEIEELEELIEELESELEALLNERASLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   475 EALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEALQEADVAKCRRDwAFQER----------------DKIVAERD 538
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-NLQERlseeysltleeaealeNKIEDDEE 968

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460   539 SIRTLCDNLRRERDR-------AVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEARFR 597
Cdd:TIGR02168  969 EARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE-EIDREARER 1033
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1325-1392 7.31e-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: 68.50  E-value: 7.31e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1325 GSEPLGISIVSG--EKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITI 1392
Cdd:cd06738    11 GTRGLGCSISSGptQKPGIFISNVKPGSLAEEVGLEVGDQIVEVNGTSFTNVDHKEAVMAL-KSSRHLTI 79
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 231-595 8.53e-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: 77.42  E-value: 8.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   231 SRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMK-RLHE------EDQKEIGDLRAQQQQVLK-HNGSSEILNKL 302
Cdd:TIGR02169  663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEnRLDElsqelsDASRKIGEIEKEIEQLEQeEEKLKERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   303 yDTAMDKLEVVKKDYDALRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRD-TAIQLQHqcalslRRFEAIHH 381
Cdd:TIGR02169  743 -EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEEEV------SRIEARLR 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   382 ELNKATaqnKDLQWEMELLQSELTELRTTQAKTakesekyKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLK 461
Cdd:TIGR02169  816 EIEQKL---NRLTLEKEYLEKEIQELQEQRIDL-------KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   462 SSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEAlqeadvakcrrDWAFQERDKIVAERDSIR 541
Cdd:TIGR02169  886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI-----------EDPKGEDEEIPEEELSLE 954

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460   542 TLCDNLRR-ERD---------RAVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEAR 595
Cdd:TIGR02169  955 DVQAELQRvEEEiralepvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE-EYEKKKR 1017
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 715-793 5.11e-13

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: 66.25  E-value: 5.11e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460    715 KVVTPLHINLSGHKDSGisleNGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:smart00228    9 KGGGGLGFSLVGGKDEG----GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
 1568-1625 8.15e-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: 65.00  E-value: 8.15e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460 1568 YIRALYERLAEVEPELSFKKDDILYVDDTLPQGSFGSWMAWQLDENAQKMQRGQIPSK 1625
Cdd:cd11859     1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGTVGSWQAVRVGRNHQELERGVIPNK 58
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 629-697 9.08e-13

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: 65.37  E-value: 9.08e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460  629 DIDL----KALGFDMAEGVNEPCLPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd06724     1 EIKLvkgpKGLGFSIAGGVGNQHIPGDNGIYVTKIIEGGAAqkDGRLQVGDKLLAVNDVSLEEVTHEEAVAALKN 75
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
218-641 1.04e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 73.26  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  218 EVAKETdFYHTLHSRLLSdqtQLKDDVDMLRRENGQL----LRERNLLQQSWEDMKRLHEE---DQKEIGDLRAQQQQVl 290
Cdd:COG4717    33 EAGKST-LLAFIRAMLLE---RLEKEADELFKPQGRKpelnLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEEL- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  291 khngssEILNKLYDTAMDKLEVVKKDYDaLRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCA 370
Cdd:COG4717   108 ------EAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  371 LSLRRF-EAIHHELNKATAQNKDLQWEMELLQSELTELR-------------TTQAKTAKESEKYKEER----------- 425
Cdd:COG4717   181 ELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQeeleeleeeleqlENELEAAALEERLKEARlllliaaalla 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  426 -----DAVYSEYKLIM---------------------SERDQVISELDKLQTEVELAESKLKS-----STSEKKAASEEM 474
Cdd:COG4717   261 llglgGSLLSLILTIAgvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEELL 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  475 EALRQIKDTVTMDAGRANKEAEIlrkQCKALCQELKEALQEADVAKcrrDWAFQERDKIVAERDSIRTLCDNLRRERDRA 554
Cdd:COG4717   341 ELLDRIEELQELLREAEELEEEL---QLEELEQEIAALLAEAGVED---EEELRAALEQAEEYQELKEELEELEEQLEEL 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  555 VSELAEALRSLDDT--RKQKNDVSRELKELKEQMESQLEKEARFRHLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDL 632
Cdd:COG4717   415 LGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494


                  ....*....
gi 741978460  633 KALGFDMAE 641
Cdd:COG4717   495 LKLALELLE 503
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 217-619 1.24e-12

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: 72.62  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   217 EEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQ----QQVLKH 292
Cdd:pfam07888   55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRaaheARIREL 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   293 NGSSEILNK---LYDTAMDKL-EVVKKDYDALRKRYSEKVAIHnsdlSRLEQMEEENQRLLKQTEMLTQ---QRDT-AIQ 364
Cdd:pfam07888  135 EEDIKTLTQrvlERETELERMkERAKKAGAQRKEEEAERKQLQ----AKLQQTEEELRSLSKEFQELRNslaQRDTqVLQ 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   365 LQHQCAlslrrfeAIHHELNkaTAQNKDLqwEMELLQSELTELRTTQAKTAKESEKYKEERDAVyseykliMSERDQVIS 444
Cdd:pfam07888  211 LQDTIT-------TLTQKLT--TAHRKEA--ENEALLEELRSLQERLNASERKVEGLGEELSSM-------AAQRDRTQA 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   445 ELDKL-----QTEVELAESKLKssTSEKKAA-SEEMEALRQikdTVTMDAGRANK-EAEILRKQckalcqelkEALQEAD 517
Cdd:pfam07888  273 ELHQArlqaaQLTLQLADASLA--LREGRARwAQERETLQQ---SAEADKDRIEKlSAELQRLE---------ERLQEER 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   518 VakcrrdwafqERDKIVAE----RDSIRTLCDNLRRErdraVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKE 593
Cdd:pfam07888  339 M----------EREKLEVElgreKDCNRVQLSESRRE----LQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404

                          410       420
                   ....*....|....*....|....*.
gi 741978460   594 ARFRHLMAHSSHDSAIDTDSMEWETE 619
Cdd:pfam07888  405 ADAKWSEAALTSTERPDSPLSDSEDE 430
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1472-1550 1.75e-12

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: 64.49  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1472 RVVFIKKSQLELGVHLCGGNLH--GVFVAEVEDDSPArGPDG-LVPGDLILEYGGLDVRSKTVEEVyVEMLK-PKDSVRL 1547
Cdd:cd00136     1 TVTLEKDPGGGLGFSIRGGKDGggGIFVSRVEPGGPA-ARDGrLRVGDRILEVNGVSLEGLTHEEA-VELLKsAGGEVTL 78


                  ...
gi 741978460 1548 KVQ 1550
Cdd:cd00136    79 TVR 81
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 743-790 3.81e-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: 63.79  E-value: 3.81e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 741978460  743 VVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06681    37 VRPGGPADREGTIKPGDRLLSVDGISLHGATHAEAMSILKQCGQEATL 84
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1320-1395 4.01e-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: 63.81  E-value: 4.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1320 VKLQKGSEPLGISIVSG----------EKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1389
Cdd:cd06702     3 IHLVKAGGPLGLSIVGGsdhsshpfgvDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPGQE 82


                  ....*.
gi 741978460 1390 ITILAQ 1395
Cdd:cd06702    83 IKLLVR 88
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 337-634 6.68e-12

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: 71.25  E-value: 6.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   337 RLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLR----RFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQA 412
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   413 KTAKESEKYKEE----RDAVYS-EYKLIMSERDQVISELDKLQTEV-------ELAESKLKSSTSEKKAASEEMEALRQI 480
Cdd:TIGR02169  762 ELEARIEELEEDlhklEEALNDlEARLSHSRIPEIQAELSKLEEEVsriearlREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   481 KDTVTMDAGRANKEAEILRKQCKALCQELKEalqeadvakcrrdwafqerdKIVAERDSIRTLCDnLRRERDRAVSELAE 560
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEE--------------------LEAALRDLESRLGD-LKKERDELEAQLRE 900

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460   561 ALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRHLMAHSSHDSAIDTDSMEWETEVVEFERET---EDIDLKA 634
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIralEPVNMLA 977
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 239-587 8.75e-12

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: 70.87  E-value: 8.75e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   239 QLKDDVDMLRRENGQLLRERNLLqqswedmKRLHEEDQ----KEIGDLRAQQQQVLKhngssEIlnklyDTAMDKLEVVK 314
Cdd:TIGR02169  195 EKRQQLERLRREREKAERYQALL-------KEKREYEGyellKEKEALERQKEAIER-----QL-----ASLEEELEKLT 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   315 KDYDALRKRYSEKVaihnsdlsrlEQMEEENQRLLKQT--EMLTQQRDTAiQLQHQCALSLRRFEAIHHELNKATAQNKD 392
Cdd:TIGR02169  258 EEISELEKRLEEIE----------QLLEELNKKIKDLGeeEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   393 LQWEMELLQSELTELRttqaktaKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASE 472
Cdd:TIGR02169  327 LEAEIDKLLAEIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   473 EMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERD 552
Cdd:TIGR02169  400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 741978460   553 RAVSELAEALRSLDDTRKQKNDVSRELKELKEQME 587
Cdd:TIGR02169  480 RVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 720-792 9.23e-12

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: 62.61  E-value: 9.23e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460  720 LHINLSGHKDSGISLeNGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 792
Cdd:cd06792    14 LGISVTGGINTSVRH-GGIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVL 85
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 179-630 9.79e-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: 70.14  E-value: 9.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   179 RPYHRLNPDYERLKIQCVRAMSDLQSLQSQHTNALKRCE---EVAKETDFYHTLHSRLLSDQTQLKDDvdmLRRENGQLL 255
Cdd:pfam05483   78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEaqrKAIQELQFENEKVSLKLEEEIQENKD---LIKENNATR 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   256 RERNLLQQ----SWEDMKRLHEEdqkeigdlRAQQQQV---LKHNGSSEIlnklydTAMDKLEV------------VKKD 316
Cdd:pfam05483  155 HLCNLLKEtcarSAEKTKKYEYE--------REETRQVymdLNNNIEKMI------LAFEELRVqaenarlemhfkLKED 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   317 YDA---LRKRYSEKVAIHNSDLSRLE-QMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKD 392
Cdd:pfam05483  221 HEKiqhLEEEYKKEINDKEKQVSLLLiQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   393 LQWEME-------LLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKL----QTEVELAESKLK 461
Cdd:pfam05483  301 IKMSLQrsmstqkALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELlrteQQRLEKNEDQLK 380

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   462 SSTSEKKAASEEMEALRQIKDtvtmdagraNKEAEIlrkqckalcQELKEALQEADVAKCRRdwafQERDKIVAERDSIR 541
Cdd:pfam05483  381 IITMELQKKSSELEEMTKFKN---------NKEVEL---------EELKKILAEDEKLLDEK----KQFEKIAEELKGKE 438

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   542 TLCDNLRRERDRAVSELAEALRSlddTRKQKNDVSRELKELKEQMESQLEKEArfrHLMAHSSHDSaIDTDSMEWETE-- 619
Cdd:pfam05483  439 QELIFLLQAREKEIHDLEIQLTA---IKTSEEHYLKEVEDLKTELEKEKLKNI---ELTAHCDKLL-LENKELTQEASdm 511

                          490
                   ....*....|.
gi 741978460   620 VVEFERETEDI 630
Cdd:pfam05483  512 TLELKKHQEDI 522
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 215-597 1.01e-11

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: 70.59  E-value: 1.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   215 RCEEVAKETDFYHTLHSRLLSDQTQLKDDVDmlrRENGQLLRERNLLQQSWEDM-KRLHE-EDQKeigdlRAQQQQVLKH 292
Cdd:pfam01576  626 RAEAEAREKETRALSLARALEEALEAKEELE---RTNKQLRAEMEDLVSSKDDVgKNVHElERSK-----RALEQQVEEM 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   293 NGSSEILNKLYDTAMD---KLEVvkkDYDALRkrysekvAIHNSDLS-RLEQMEEENQRLLKQT-EMLTQ------QRDT 361
Cdd:pfam01576  698 KTQLEELEDELQATEDaklRLEV---NMQALK-------AQFERDLQaRDEQGEEKRRQLVKQVrELEAElederkQRAQ 767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   362 AIQLQHQCALSLRRFEAIHHELNK----ATAQNKDLQWEMELLQSELTELRTTQAK---TAKESEKYKE--ERDAVYSEY 432
Cdd:pfam01576  768 AVAAKKKLELDLKELEAQIDAANKgreeAVKQLKKLQAQMKDLQRELEEARASRDEilaQSKESEKKLKnlEAELLQLQE 847

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   433 KLIMSER--DQVISELDKLQTEvelaeskLKSSTSEKKAASEEMEALrqikdtvtmdagrankEAEILRkqckaLCQELK 510
Cdd:pfam01576  848 DLAASERarRQAQQERDELADE-------IASGASGKSALQDEKRRL----------------EARIAQ-----LEEELE 899

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   511 EALQEADVAKCRRDWAFQERDKIVAERDSIRTLC---DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK-EQM 586
Cdd:pfam01576  900 EEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSqksESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKiAQL 979

                          410
                   ....*....|.
gi 741978460   587 ESQLEKEARFR 597
Cdd:pfam01576  980 EEQLEQESRER 990
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 200-595 1.62e-11

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: 69.66  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   200 SDLQSLQSQhTNALKrcEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQK-- 277
Cdd:TIGR04523  218 SQISELKKQ-NNQLK--DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlk 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   278 -EIGDLRAQQQQVLKHNGSSEILNKlydtaMDKLEVVKKDYDALRKRYSE--------KVAIHNSDL------------- 335
Cdd:TIGR04523  295 sEISDLNNQKEQDWNKELKSELKNQ-----EKKLEEIQNQISQNNKIISQlneqisqlKKELTNSESensekqreleekq 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   336 SRLEQMEEENQRLLKQTEMLTQQ-RDTAIQLQHQcalslrrfeaihHELNKATAQN-KDLQWEMELLQSELTELRTT--- 410
Cdd:TIGR04523  370 NEIEKLKKENQSYKQEIKNLESQiNDLESKIQNQ------------EKLNQQKDEQiKKLQQEKELLEKEIERLKETiik 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   411 QAKTAKESEKYKEERDAVYSEYKLIMSERDQVIS-----------ELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQ 479
Cdd:TIGR04523  438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   480 ikdtvtmdagranKEAEILRKQcKALCQELKEalqeadvakcrrdwafqERDKIVAERDSIRTLCDNLRR--------ER 551
Cdd:TIGR04523  518 -------------KISSLKEKI-EKLESEKKE-----------------KESKISDLEDELNKDDFELKKenlekeidEK 566

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 741978460   552 DRAVSELAEALRSLDDTRKQKNDV----SRELKELKEQME------SQLEKEAR 595
Cdd:TIGR04523  567 NKEIEELKQTQKSLKKKQEEKQELidqkEKEKKDLIKEIEekekkiSSLEKELE 620
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 137-541 2.38e-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: 69.38  E-value: 2.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   137 LSDRqvNEKVENLSIQLRLMTRE-RNELRKRLAfATHGTTFDKRPYHRLNPDYERLKIQCVRAMSDL----QSLQSQH-- 209
Cdd:pfam15921  421 LDDR--NMEVQRLEALLKAMKSEcQGQMERQMA-AIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkMTLESSErt 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   210 ----TNALKRCEEVAKETDFYHT-LHSRL---LSDQTQLKDDVDMLRRENGQL------LRERN----LLQQSWEDMKRL 271
Cdd:pfam15921  498 vsdlTASLQEKERAIEATNAEITkLRSRVdlkLQELQHLKNEGDHLRNVQTECealklqMAEKDkvieILRQQIENMTQL 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   272 HEEDQKEIGDLRAQQQQVLKhngssEILNKLYDtaMDKLEVVKKDYDA----LRKRYS----EKVAIHNSDLSRL---EQ 340
Cdd:pfam15921  578 VGQHGRTAGAMQVEKAQLEK-----EINDRRLE--LQEFKILKDKKDAkireLEARVSdlelEKVKLVNAGSERLravKD 650

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   341 MEEENQRLLKQTEmltQQRDTAIQLQHQCALSLRRFEAIHHELNKATaqNKdLQWEMELLQSELTELRTTqAKTAKESEK 420
Cdd:pfam15921  651 IKQERDQLLNEVK---TSRNELNSLSEDYEVLKRNFRNKSEEMETTT--NK-LKMQLKSAQSELEQTRNT-LKSMEGSDG 723

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   421 YKEErdAVYSEYKLIMSERDQViselDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRK 500
Cdd:pfam15921  724 HAMK--VAMGMQKQITAKRGQI----DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 741978460   501 QCKalcqELKEALQEADVAKCRRDWAFQERDKIV--AERDSIR 541
Cdd:pfam15921  798 QER----RLKEKVANMEVALDKASLQFAECQDIIqrQEQESVR 836
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 248-585 4.08e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.42  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  248 RRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVlkhNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEK 327
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL---EAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  328 VAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQlqhqcalslrrfeaihhELNKATAQNKDLQWEMELLQSELTEL 407
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEE-----------------ELEELEEELEEAEEELEEAEAELAEA 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  408 RTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMD 487
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  488 AGRANKEAEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIvaerdsirtlcDNLRRERDRAVSELaEALRSLDD 567
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAA----------LLEAAL-----------AELLEELAEAAARL-LLLLEAEA 501

                         330
                  ....*....|....*...
gi 741978460  568 TRKQKNDVSRELKELKEQ 585
Cdd:COG1196   502 DYEGFLEGVKAALLLAGL 519
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 239-593 5.58e-11

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: 67.89  E-value: 5.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   239 QLKDDVDMLRRENGQLLRERNLLQQSWEDMK-RLHEEDQ--KEIGDLRAQQQQVLkhngsSEILNKLYDTAMDKLEVVKk 315
Cdd:pfam01576  135 KLEEDILLLEDQNSKLSKERKLLEERISEFTsNLAEEEEkaKSLSKLKNKHEAMI-----SDLEERLKKEEKGRQELEK- 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   316 dydALRKRYSEKVAIHN--SDLS--------RLEQMEEENQRLLKQTEMLTQQRDTAI----QLQHQCALSLRRFEAIHH 381
Cdd:pfam01576  209 ---AKRKLEGESTDLQEqiAELQaqiaelraQLAKKEEELQAALARLEEETAQKNNALkkirELEAQISELQEDLESERA 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   382 ELNKATAQNKDLQWEMELLQselTELRTTQAKTAKESEkYKEERDAVYSEYKLIMSER----DQVISELDKLQTEV---- 453
Cdd:pfam01576  286 ARNKAEKQRRDLGEELEALK---TELEDTLDTTAAQQE-LRSKREQEVTELKKALEEEtrshEAQLQEMRQKHTQAleel 361

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   454 --ELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRAnkEAEILRKQCKALCQELKEALQEADVAKCRRdwafQER- 530
Cdd:pfam01576  362 teQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ--DSEHKRKKLEGQLQELQARLSESERQRAEL----AEKl 435

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460   531 DKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTR-------KQKNDVSRELKELKEQ---MESQLEKE 593
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLSTRLRQLEDErnsLQEQLEEE 508
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
336-633 5.72e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 67.76  E-value: 5.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  336 SRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEaihhelnkataqnkDLQWEMELLQSELTELRTTQAKTA 415
Cdd:PRK02224  206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE--------------ERREELETLEAEIEDLRETIAETE 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  416 KESEKYKEErdavyseykliMSERDQVISELDKLQTEVeLAESKLKSSTSEKKAA-----SEEMEALRQIKDTVTMDAGR 490
Cdd:PRK02224  272 REREELAEE-----------VRDLRERLEELEEERDDL-LAEAGLDDADAEAVEArreelEDRDEELRDRLEECRVAAQA 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  491 ANKEAEILRKQCKALCQELKEALQEA-----DVAKCRRDWAfQERDKIVAERDSIRTL---CDNLRRERDRAVSELAEAL 562
Cdd:PRK02224  340 HNEEAESLREDADDLEERAEELREEAaelesELEEAREAVE-DRREEIEELEEEIEELrerFGDAPVDLGNAEDFLEELR 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  563 RSLDDTRKQKNDVSRELKELKEQMEsqlekEARfRHLMA-----------HSSHDSAIDtdsmEWETEVVEFERETEDID 631
Cdd:PRK02224  419 EERDELREREAELEATLRTARERVE-----EAE-ALLEAgkcpecgqpveGSPHVETIE----EDRERVEELEAELEDLE 488


                  ..
gi 741978460  632 LK 633
Cdd:PRK02224  489 EE 490
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1316-1396 6.23e-11

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: 60.27  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1316 EPRHVKLQKGSEpLGISIVSGEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIG--QQCDTITIL 1393
Cdd:cd06729     1 DTRLVSFRKGGS-VGLRLAGGNDVGIFVAGVQEGSPAEKQGLQEGDQILKVNGVDFRNLTREEAVLFLLdlPKGEEVTIL 79


                  ...
gi 741978460 1394 AQY 1396
Cdd:cd06729    80 AQS 82
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 1318-1383 8.36e-11

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: 59.97  E-value: 8.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1318 RHVKLQKGS--EPLGISIVSG-EKG-GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd06755     1 RTVTLTRPSreSPLHFSLLGGsEKGfGIFVSKVEKGSKAAEAGLKRGDQILEVNGQNFENITLKKALEIL 70
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1470-1558 8.70e-11

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: 60.06  E-value: 8.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1470 EPRVVFIKKSQLELGVHLCGG-NLHGVFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLK 1548
Cdd:cd06795     1 EPRKIVLHKGSTGLGFNIVGGeDGEGIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTII 80

                          90
                  ....*....|
gi 741978460 1549 VQYRPEEFSK 1558
Cdd:cd06795    81 AQYKPEEYSR 90
PDZ2_ZO1-like_ds cd06728
PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form ...
 725-794 1.10e-10

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: 59.16  E-value: 1.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460  725 SGHKDS-GISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 794
Cdd:cd06728     8 SRKNDEyGLRLGSRIFVKEITPDSLAAKDGNLQEGDIILKINGTPVENLSLSEAKKLIEKSKDKLQLVVLR 78
SH3_ZO-1 cd12026
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ...
 1565-1625 1.25e-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: 58.94  E-value: 1.25e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460 1565 DSFYIRALYERLAEVEPELSFKKDDILYVDDTLPQGSFGSWMAWQLDENAQKMQRGQIPSK 1625
Cdd:cd12026     1 DSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNK 61
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 1320-1392 1.52e-10

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: 59.22  E-value: 1.52e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1320 VKLQKGSEPLGISIVSG-----EKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1392
Cdd:cd06789     6 VTLKKVGNGMGLSIVAAkgagqDKLGIYIKSVVKGGAADLDGrLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTL 84
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 306-633 1.71e-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: 66.63  E-value: 1.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   306 AMDKLEVVKKDYDALRKRYSEKvaihnsdLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQhqcalsLRRFEAIHHELNK 385
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEK-------RQQLERLRREREKAERYQALLKEKREYEGYEL------LKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   386 ATAQNKDLQWEMELLQSELTELrttqaktAKESEKYKEERDAVYSEYKLIMSERD-QVISELDKLQTEVELAESKLKsst 464
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIA--- 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   465 sekkaaseemEALRQIKDtvtMDAGRANKEAEILRKQCKAlcQELKEALQEADVakcrrdwafqERDKIVAERDSIRTLC 544
Cdd:TIGR02169  312 ----------EKERELED---AEERLAKLEAEIDKLLAEI--EELEREIEEERK----------RRDKLTEEYAELKEEL 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   545 DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQmESQLEKEARFRHlMAHSSHDSAIDtdsmEWETEVVEFE 624
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE-LDRLQEELQRLS-EELADLNAAIA----GIEAKINELE 440


                   ....*....
gi 741978460   625 RETEDIDLK 633
Cdd:TIGR02169  441 EEKEDKALE 449
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 628-697 1.71e-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: 59.23  E-value: 1.71e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  628 EDIDLK----ALGFDMAEGVNEPCLPGDCGIFVTKV-DKGSIA-DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd06709     1 EEITLKrgpsGLGFNIVGGTDQPYIPNDSGIYVAKIkEDGAAAiDGRLQEGDKILEINGQSLENLTHQDAVELFRN 76
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1320-1395 1.83e-10

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 58.83  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1320 VKLQK-GSEPLGISIVSGEKG---GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1395
Cdd:pfam00595    2 VTLEKdGRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 1320-1393 2.05e-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: 58.76  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1320 VKLQKGSEPLGISIVSG-----EKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:cd06792     5 VELSKKDGSLGISVTGGintsvRHGGIYVKSLVPGGAAEQDGrIQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLV 84
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 198-635 2.09e-10

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: 66.30  E-value: 2.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   198 AMSDLQSLQSQhtnaLKRCEEVAKETDfyhTLHSRLLSDqtqLKDDVDMLRRENGQLLR---------ERNLLQQSWEDM 268
Cdd:pfam15921  290 ARSQANSIQSQ----LEIIQEQARNQN---SMYMRQLSD---LESTVSQLRSELREAKRmyedkieelEKQLVLANSELT 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   269 KRLHEEDQ--KEIGDLRAQQQQVLK--HNGSSEIL------NKLYDTAMDKLEVVkkdyDALRKRYSEKvaihNSDLSRL 338
Cdd:pfam15921  360 EARTERDQfsQESGNLDDQLQKLLAdlHKREKELSlekeqnKRLWDRDTGNSITI----DHLRRELDDR----NMEVQRL 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   339 EQmeeenqrLLKqtemlTQQRDTAIQLQHQCAlslrRFEAIHHELNKATAQNKDLQWEMELLQSELTELrTTQAKTAKES 418
Cdd:pfam15921  432 EA-------LLK-----AMKSECQGQMERQMA----AIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-TAKKMTLESS 494

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   419 EK---------YKEER--DAVYSEYKLIMSERDQVISELDKLQTEvelaESKLKSSTSEKKAASEEM-------EALRQI 480
Cdd:pfam15921  495 ERtvsdltaslQEKERaiEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQTECEALKLQMaekdkviEILRQQ 570

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   481 KDTVTMDAGRANKEAEILRKQCKALCQELKE---ALQEADVAKCRRDWAFQERDKIVAErdsirtlcdnLRRERDRAVSE 557
Cdd:pfam15921  571 IENMTQLVGQHGRTAGAMQVEKAQLEKEINDrrlELQEFKILKDKKDAKIRELEARVSD----------LELEKVKLVNA 640

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460   558 LAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRHLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKAL 635
Cdd:pfam15921  641 GSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 635-708 2.35e-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: 58.88  E-value: 2.35e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  635 LGFDMAEGVN---EPCLPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 708
Cdd:cd06749    11 LGFSISGGIGsqgNPFRPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVNIEHGQAVSLLKSFQNTVDLVVER 87
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 1318-1396 2.50e-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: 58.54  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1318 RHVKLQKG-SEPLGISIVSGEKGGV--YVSKVTGGSIAHQ-AGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:cd06800     1 RKVLLSKEpHEGLGISITGGKEHGVpiLISEIHEGQPADRcGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITLE 80


                  ...
gi 741978460 1394 AQY 1396
Cdd:cd06800    81 VVY 83
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
337-592 2.56e-10

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 63.78  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  337 RLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEmelLQSELTELRttqaktaK 416
Cdd:COG1340    23 EIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE---LNEKLNELR-------E 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  417 ESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEV-------ELAEsKLKSSTSEKKAASEEMEALRQIKDTVTmdag 489
Cdd:COG1340    93 ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekELVE-KIKELEKELEKAKKALEKNEKLKELRA---- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  490 rankEAEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDS-------IRTLCDNLRRERDRAVSELAEAL 562
Cdd:COG1340   168 ----ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADElhkeiveAQEKADELHEEIIELQKELRELR 243

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 741978460  563 RSLDDTRKQKNDVSR-----ELKELKEQMESQLEK 592
Cdd:COG1340   244 KELKKLRKKQRALKRekekeELEEKAEEIFEKLKK 278
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1470-1551 3.24e-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: 57.96  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1470 EPRVV-FIKKSQLelGVHLCGGNLHGVFVAEVEDDSPARGpDGLVPGDLILEYGGLDVRSKTVEEV--YVEMLKPKDSVR 1546
Cdd:cd06729     1 DTRLVsFRKGGSV--GLRLAGGNDVGIFVAGVQEGSPAEK-QGLQEGDQILKVNGVDFRNLTREEAvlFLLDLPKGEEVT 77


                  ....*
gi 741978460 1547 LKVQY 1551
Cdd:cd06729    78 ILAQS 82
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 142-593 3.38e-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: 65.04  E-value: 3.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   142 VNEKVENLSIQLRLMTRERNELRKR-LAFATHGTTFDKrpyhrlnpdyERLKIQcvramSDLQSLQSQHTNALKRCEEVA 220
Cdd:TIGR04523  143 FLTEIKKKEKELEKLNNKYNDLKKQkEELENELNLLEK----------EKLNIQ-----KNIDKIKNKLLKLELLLSNLK 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   221 KETDFYHTLHSRLL---SDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEigdLRAQQQQVLKHNGSSE 297
Cdd:TIGR04523  208 KKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ---LSEKQKELEQNNKKIK 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   298 ILNKLYDTAMDKLEVVKKdydalrkrysEKVAIHNSDL-SRLEQMEEENQRLLKQtemLTQQRDTAIQLQHQCAlSLRRf 376
Cdd:TIGR04523  285 ELEKQLNQLKSEISDLNN----------QKEQDWNKELkSELKNQEKKLEEIQNQ---ISQNNKIISQLNEQIS-QLKK- 349

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   377 eaihhELNKATAQNKDLQWEMELLQSELTELRttqaktaKESEKYKEERdavyseYKLIMSERDqVISELDKLQTEVELA 456
Cdd:TIGR04523  350 -----ELTNSESENSEKQRELEEKQNEIEKLK-------KENQSYKQEI------KNLESQIND-LESKIQNQEKLNQQK 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   457 ESKLKSSTSEKKAASEEMEALRQikdTVTmdagRANKEAEILRKQCKALCQELKEalqeadvAKCRRDWAFQERDKIVAE 536
Cdd:TIGR04523  411 DEQIKKLQQEKELLEKEIERLKE---TII----KNNSEIKDLTNQDSVKELIIKN-------LDNTRESLETQLKVLSRS 476

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460   537 RDSIRTLCDNLRRERDRAVSElaealrsLDDTRKQKNDVSRELKELKEQMESQLEKE 593
Cdd:TIGR04523  477 INKIKQNLEQKQKELKSKEKE-------LKKLNEEKKELEEKVKDLTKKISSLKEKI 526
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 238-589 4.01e-10

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: 65.13  E-value: 4.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   238 TQLKDDVDMLRRENGQLLRERNllqqsweDMKRLHEEDQKEIGDLRAQQQQVLKHngsseiLNKLYDTAM---DKLEVVK 314
Cdd:pfam05483  488 IELTAHCDKLLLENKELTQEAS-------DMTLELKKHQEDIINCKKQEERMLKQ------IENLEEKEMnlrDELESVR 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   315 KDYdaLRKRYSEKVAIHNSDlsrlEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHElNKA-----TAQ 389
Cdd:pfam05483  555 EEF--IQKGDEVKCKLDKSE----ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKAlkkkgSAE 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   390 NKDLQ-WEMELLQSELtELRTTQAKTAKESEKYKEERDavyseyklimserDQVISElDKLQTEVELAEsklksstsekk 468
Cdd:pfam05483  628 NKQLNaYEIKVNKLEL-ELASAKQKFEEIIDNYQKEIE-------------DKKISE-EKLLEEVEKAK----------- 681

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   469 aaseemealrqikdtVTMDagrankEAEILRKQCKALCQElKEALQEADVAKCRRDWafqerDKIVAERDSIRTLCDNLR 548
Cdd:pfam05483  682 ---------------AIAD------EAVKLQKEIDKRCQH-KIAEMVALMEKHKHQY-----DKIIEERDSELGLYKNKE 734

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 741978460   549 RERDRAVSELAEALRSLDD---TRKQKNDVSRELKElKEQMESQ 589
Cdd:pfam05483  735 QEQSSAKAALEIELSNIKAellSLKKQLEIEKEEKE-KLKMEAK 777
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 735-790 4.48e-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: 4.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  735 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06690    29 SPGIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMDLIRTSGDKLRF 84
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 351-641 4.50e-10

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: 65.08  E-value: 4.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   351 QTEMLTQQRDTAI-QLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVy 429
Cdd:TIGR02168  667 KTNSSILERRREIeELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL- 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   430 seykliMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQikdtvtmDAGRANKEAEILRKQCKALCQEL 509
Cdd:TIGR02168  746 ------EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-------QIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   510 KEalqeadvakcrrdwafqerdkivaerdsirtlcdnLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESq 589
Cdd:TIGR02168  813 TL-----------------------------------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES- 856

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 741978460   590 lekearfrhlMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAE 641
Cdd:TIGR02168  857 ----------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 733-790 4.65e-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: 58.18  E-value: 4.65e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  733 SLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06694    27 SLDLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 385-597 7.20e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 7.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  385 KATAQN----KDLQWEMEllqSELTELRTtQAKTAKESEKYKEE---RDAVyseykLIMSERDQVISELDKLQTEVELAE 457
Cdd:COG1196   182 EATEENlerlEDILGELE---RQLEPLER-QAEKAERYRELKEElkeLEAE-----LLLLKLRELEAELEELEAELEELE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  458 SKLKSSTSEKKAASEEMEALRQikdtvtmDAGRANKEAEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAER 537
Cdd:COG1196   253 AELEELEAELAELEAELEELRL-------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  538 DSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFR 597
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 702-790 1.09e-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: 56.85  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  702 INMVVRRRKSLG-GKVVTPLHINLSGHKdsgislengvyAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESL 780
Cdd:cd06734     2 YDVTLTRRENEGfGFVIISSVNKKSGSK-----------IGRIIPGSPADRCGQLKVGDRILAVNGISILNLSHGDIVNL 70

                          90
                  ....*....|
gi 741978460  781 LRSCQDSLTL 790
Cdd:cd06734    71 IKDSGLSVTL 80
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1317-1398 1.18e-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: 56.68  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1317 PRHVKLQKGSEPLGISIVSG--EKGGVYVSKVTGGSIA-HQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:cd06796     2 PRVVELPKTEEGLGFNVMGGkeQNSPIYISRIIPGGVAdRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLV 81


                  ....*
gi 741978460 1394 AQYNP 1398
Cdd:cd06796    82 VRYTP 86
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 651-709 1.38e-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: 1.38e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  651 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKAL-------LNGEGAINMVVRRR 709
Cdd:cd23059    36 DLGIFIKSIIHGGAAskDGRLRVNDQLIAVNGESLLGLTNSEAMETLrramsteGNIRGMIQLVVARR 103
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 728-782 1.43e-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: 56.97  E-value: 1.43e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460  728 KDSGISLENGVYAAAVV----------PGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLR 782
Cdd:cd06686    18 KGFGIQLQGGVFATETLsspplisfiePDSPAERCGVLQVGDRVLSINGIPTEDRTLEEANQLLR 82
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1318-1392 1.81e-09

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: 56.11  E-value: 1.81e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460 1318 RHVKLQK-GSEPLGISIVSG-EKG-GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQcDTITI 1392
Cdd:cd06737     3 RLVRLDRrGPESLGFSVRGGlEHGcGLFVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINLIKTK-KTVSL 79
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 299-596 2.09e-09

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: 63.07  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   299 LNKLYDTAMDKLEV------VKKDYDALRKRysEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQhqcaLS 372
Cdd:pfam02463  175 LKKLIEETENLAELiidleeLKLQELKLKEQ--AKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL----RD 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   373 LRRFEAIhhelnkataQNKDLQWEMELLQSELTELRttqaKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTE 452
Cdd:pfam02463  249 EQEEIES---------SKQEIEKEEEKLAQVLKENK----EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   453 VELAESKLKSSTSEKKAASEEMEALRQIKDTVtmdagRANKEAEILRKQCKALCQELKEALQEADVAKCRRDWAFQErdk 532
Cdd:pfam02463  316 LKESEKEKKKAEKELKKEKEEIEELEKELKEL-----EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS--- 387

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460   533 ivaERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDvsRELKELKEQMESQLEKEARF 596
Cdd:pfam02463  388 ---SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK--EELEILEEEEESIELKQGKL 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-485 2.30e-09

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: 62.77  E-value: 2.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   140 RQVNEKVENLSIQLRLMTRERNELRKRLAfathgttfdkrpyhRLNPDYERLKIQCVRAMSDLQSLQSQHTNALKRCEEV 219
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   220 AKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngsseiL 299
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------L 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   300 NKLYDTAMDKLEVVKKDYDALRKRY----------SEKVAIHNSDLSRLEQMEEEnqrLLKQTEMLTQQRDtaiQLQHQC 369
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEE---LESELEALLNERA---SLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   370 ALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYS-EYKLIMSERDQVISELDK 448
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEE 969

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 741978460   449 LQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVT 485
Cdd:TIGR02168  970 ARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 231-515 2.39e-09

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: 62.35  E-value: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   231 SRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQ---QVLKHNgssEILNKLYDTam 307
Cdd:TIGR04523  338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdleSKIQNQ---EKLNQQKDE-- 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   308 dKLEVVKKDYDALRKRY---SEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQ--------LQHQCALSLRRF 376
Cdd:TIGR04523  413 -QIKKLQQEKELLEKEIerlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkIKQNLEQKQKEL 491

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   377 EAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAK------------TAKESEKYKEERDAVYSEYKLIMSERDQVIS 444
Cdd:TIGR04523  492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKlesekkekeskiSDLEDELNKDDFELKKENLEKEIDEKNKEIE 571

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460   445 EL----DKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALcQELKEALQE 515
Cdd:TIGR04523  572 ELkqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI-KSKKNKLKQ 645
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1320-1379 2.60e-09

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: 55.70  E-value: 2.60e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460 1320 VKLQKGSEPLGISIV-------SGEKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06791     5 VELVKDEQGLGITIAgyvgekaSGELSGIFVKSIIPGSAADQDGrIQVNDQIIAVDGVNLQGFTNQEA 72
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 617-710 2.93e-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: 2.93e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460    617 ETEVVEFERETEDidlkaLGFDMAEGVNEpclpgDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 695
Cdd:smart00228    1 EPRLVELEKGGGG-----LGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                            90
                    ....*....|....*
gi 741978460    696 LNGEGAINMVVRRRK 710
Cdd:smart00228   71 KKAGGKVTLTVLRGG 85
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 631-708 3.07e-09

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: 55.73  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  631 DLKALGFDMAEGV-NEPCLPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 707
Cdd:cd06703    10 DGKGLGFSIAGGKgSTPFRDGDEGIFISRITEGGAAdrDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITLVVE 89


                  .
gi 741978460  708 R 708
Cdd:cd06703    90 R 90
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1316-1393 3.80e-09

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: 55.64  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1316 EPRHVKLQKGSEP-------LGISIVSGEKG-----GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLI 1382
Cdd:cd06714     3 LIGRIILQRDPKDgsvsgngLGLKVVGGKMTesgrlGAYVTKVKPGSVADTVGhLREGDEVLEWNGISLQGKTFEEVQDI 82

                          90
                  ....*....|.
gi 741978460 1383 IGQQCDTITIL 1393
Cdd:cd06714    83 ISQSKGEVELV 93
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
382-594 3.92e-09

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 59.92  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  382 ELNKATAQNKDLQWEmelLQSELTELRTT----QAKTAKESEK---YKEERDAVYSEYKLIMSERDQVISELDKLQTEVE 454
Cdd:COG1340    19 ELREEIEELKEKRDE---LNEELKELAEKrdelNAQVKELREEaqeLREKRDELNEKVKELKEERDELNEKLNELREELD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  455 LAESKLKS---STSEKKAASEEMEALRQIKDTVTMDAG----------RANKEAEILRKQCKALcQELKEALQEADVAKC 521
Cdd:COG1340    96 ELRKELAElnkAGGSIDKLRKEIERLEWRQQTEVLSPEeekelvekikELEKELEKAKKALEKN-EKLKELRAELKELRK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  522 RRDWAFQ-------ERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEA 594
Cdd:COG1340   175 EAEEIHKkikelaeEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQR 254
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1318-1383 4.39e-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: 54.96  E-value: 4.39e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1318 RHVKLQKGS-EPLGISIVSG-EKG-GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd06741     2 RKVNLVVEDgQSLGLMIRGGaEYGlGIYVTGVDPGSVAENAGLKVGDQILEVNGRSFLDITHDEAVKIL 70
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 1316-1395 4.44e-09

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: 55.40  E-value: 4.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1316 EPRHVKLQK-GSEPLGISIVSG-----------EKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLI 1382
Cdd:cd06671     1 PPRRVELWRePGKSLGISIVGGrvmgsrlsngeEIRGIFIKHVLEDSPAGRNGtLKTGDRILEVNGVDLRNATHEEAVEA 80

                          90
                  ....*....|...
gi 741978460 1383 IGQQCDTITILAQ 1395
Cdd:cd06671    81 IRNAGNPVVFLVQ 93
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1327-1379 4.79e-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: 54.75  E-value: 4.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 741978460 1327 EPLGISIVSG-EKG-GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd10833    12 GSLGFSVRGGsEHGlGIFVSKVEEGSAAERAGLCVGDKITEVNGVSLENITMSSA 66
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
 1565-1625 5.34e-09

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: 54.11  E-value: 5.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460 1565 DSFYIRALYERLAEVEPELSFKKDDILYVDDTLPQGSFGSWMAWQLDENAQKMQRGQIPSK 1625
Cdd:cd12028     1 DSFYIRTHFDYEPDPPSGLSFTRGEVFHVLDTMHRGKLGSWLAVRMGRDLREMEKGIIPNQ 61
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 187-629 5.78e-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: 61.34  E-value: 5.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   187 DYERLKIQCVRAMSDLQSLQSQHTNALKRCEEVAketdfyHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWE 266
Cdd:pfam01576  423 ESERQRAELAEKLSKLQSELESVSSLLNEAEGKN------IKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLED 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   267 DMKRLHEEDQKEIGDLRAQQQQVLKHNGS-SEILNKLYDTA--MDKLEVVKK----DYDALRKRYSEKVAIHnsdlsrlE 339
Cdd:pfam01576  497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQlSDMKKKLEEDAgtLEALEEGKKrlqrELEALTQQLEEKAAAY-------D 569

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   340 QMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDlqwEMELLQSELTELRTTQAKTAKESE 419
Cdd:pfam01576  570 KLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAE---ERDRAEAEAREKETRALSLARALE 646

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   420 KYKEERDAVYSEYKLIMSERDQVISELDKLQTEV-ELAESK--LKSSTSEKKAASEEME-ALRQIKDT-----VTMDAGR 490
Cdd:pfam01576  647 EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVhELERSKraLEQQVEEMKTQLEELEdELQATEDAklrleVNMQALK 726

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   491 ANKEAEI-------------LRKQC---------------------KALCQELKEALQEADVAKCRRDWAFQERDKIVAE 536
Cdd:pfam01576  727 AQFERDLqardeqgeekrrqLVKQVreleaelederkqraqavaakKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   537 -RDSIRTLcDNLRRERDRAVSElaealrSLDDTRKQKNdVSRELKELKEQMES--------QLEKEARFRHLMAHSSHDS 607
Cdd:pfam01576  807 mKDLQREL-EEARASRDEILAQ------SKESEKKLKN-LEAELLQLQEDLAAserarrqaQQERDELADEIASGASGKS 878

                          490       500
                   ....*....|....*....|..
gi 741978460   608 AIDTDSMEWETEVVEFERETED 629
Cdd:pfam01576  879 ALQDEKRRLEARIAQLEEELEE 900
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1470-1551 6.18e-09

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: 54.64  E-value: 6.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1470 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLK 1548
Cdd:cd06767     2 EPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAhQA--GLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITML 79


                  ...
gi 741978460 1549 VQY 1551
Cdd:cd06767    80 VQY 82
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1316-1393 6.38e-09

PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467165 [Multi-domain]  Cd Length: 89  Bit Score: 54.56  E-value: 6.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1316 EPRHVKLQKGS--EPLGISIVSGEK---GGVYVSKV-TGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1389
Cdd:cd06677     2 EITTIEIHRSDpyEELGISIVGGNDtplINIVIQEVyRDGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLRQPCPV 81


                  ....*.
gi 741978460 1390 --ITIL 1393
Cdd:cd06677    82 lrLTVL 87
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 141-479 8.55e-09

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: 60.85  E-value: 8.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   141 QVNEKVENLSI-------QLRLMTRERN------ELRKRLAfathgttfDKRPYHRLNpDYERLKIQCVRAMSDLQSLQS 207
Cdd:TIGR02169  181 EVEENIERLDLiidekrqQLERLRREREkaeryqALLKEKR--------EYEGYELLK-EKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   208 QHTNALKRCEEVAKEtdfYHTLHSRLLSDQTQLKDdvdMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQ 287
Cdd:TIGR02169  252 ELEKLTEEISELEKR---LEEIEQLLEELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   288 QvlkhnGSSEILNKLYD-TAMDK-LEVVKKDYDALRKRYSEKVAIHNSDLSRLEQMEEENQRLL-------KQTEMLTQQ 358
Cdd:TIGR02169  326 K-----LEAEIDKLLAEiEELEReIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelkdyrEKLEKLKRE 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   359 RDTAIQLQHQCALSLRRFEA----IHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKL 434
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 741978460   435 IMSERDQVISELDKLQTEVELAESKLKSStsekKAASEEMEALRQ 479
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERVRGG----RAVEEVLKASIQ 521
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1319-1383 8.85e-09

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: 54.17  E-value: 8.85e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460 1319 HVKLQK-GSEPLGISIVS-GEKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd06678     2 HVTLNKrDGEQLGIKLVRkKDEPGVFILDLLEGGLAARDGrLKSDDRVLAINGQDLRHGTPEQAAQII 69
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 625-708 9.18e-09

PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467176 [Multi-domain]  Cd Length: 102  Bit Score: 54.56  E-value: 9.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  625 RETEDIDL-----KALGFDMAeGVNEPCLpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDL-INKDKKQAIKALL 696
Cdd:cd06689    13 RQVEYIELekpesGGLGFSVV-GLKSENR-GELGIFVQEIQPGSVAarDGRLKENDQILAINGQPLdQSISHQQAIAILQ 90

                          90
                  ....*....|..
gi 741978460  697 NGEGAINMVVRR 708
Cdd:cd06689    91 QAKGSVELVVAR 102
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 650-709 1.42e-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: 1.42e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460  650 GDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 709
Cdd:cd06758    27 GDIGIFVAGVEEGGSAdrDGRLKKGDELLMINGQSLIGLSHQEAVAILRSSASPVQLVIASK 88
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 1320-1383 1.69e-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: 53.12  E-value: 1.69e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460 1320 VKLQK-GSEPLGISIVSGEKG-GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd23060     2 IELEKpANGGLGFSLVGGEGGsGIFVKSISPGGVADRDGrLQVGDRLLQVNGESVIGLSHSKAVNIL 68
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
231-510 2.05e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 58.00  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  231 SRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDM-------KRLHEEDQKEIGDLRAQQQQVLkhngssEILNKLY 303
Cdd:COG1340    18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELreeaqelREKRDELNEKVKELKEERDELN------EKLNELR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  304 DTA------MDKLEVVKKDYDALRKRYsekvaihnsdlsrlEQMEEEnqrllKQTEMLTQQRDTAIQLQhqcalsLRRFE 377
Cdd:COG1340    92 EELdelrkeLAELNKAGGSIDKLRKEI--------------ERLEWR-----QQTEVLSPEEEKELVEK------IKELE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  378 AIHHELNKATAQNKDLQW---EMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVE 454
Cdd:COG1340   147 KELEKAKKALEKNEKLKElraELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  455 LAESKLKSSTSEKKAASEEMEALRQIKdtvtmDAGRANKEAEILRKQCKALCQELK 510
Cdd:COG1340   227 ELHEEIIELQKELRELRKELKKLRKKQ-----RALKREKEKEELEEKAEEIFEKLK 277
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 145-634 2.59e-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: 58.96  E-value: 2.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   145 KVENLSIQLRLMTRERNELRKRLAFATHGTTFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQSQHTNALKRCEEVAKE-- 222
Cdd:pfam05483  255 KMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEke 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   223 -----------------TDFYHT---LHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLqqswEDMKRLHEEDQKEIGDL 282
Cdd:pfam05483  335 aqmeelnkakaahsfvvTEFEATtcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL----EEMTKFKNNKEVELEEL 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   283 R---AQQQQVLKHNGSSE-ILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNSDLSRLEQMEE-----ENQRLlKQTE 353
Cdd:pfam05483  411 KkilAEDEKLLDEKKQFEkIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelEKEKL-KNIE 489

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   354 MLTqqrdtaiqlqHQCALSLrrfeaihhELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEE----RDAVY 429
Cdd:pfam05483  490 LTA----------HCDKLLL--------ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKemnlRDELE 551

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   430 SEYKLIMSERDQVISELDKlqtevelaesklksstSEKKAASEEMEALRQIKDTVTMDAGRAN--KEAEILRKQCKALCQ 507
Cdd:pfam05483  552 SVREEFIQKGDEVKCKLDK----------------SEENARSIEYEVLKKEKQMKILENKCNNlkKQIENKNKNIEELHQ 615

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   508 ELKeALQEADVAKCRRDWAFQER-DKIVAERDSIRT----LCDNLRRE-RDRAVSElaEALrsLDDTRKQKNDVSRELKE 581
Cdd:pfam05483  616 ENK-ALKKKGSAENKQLNAYEIKvNKLELELASAKQkfeeIIDNYQKEiEDKKISE--EKL--LEEVEKAKAIADEAVKL 690

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460   582 LKEQMESQLEKEARFRHLMAHSSH--DSAIDtdsmEWETEVVEFE-RETEDIDLKA 634
Cdd:pfam05483  691 QKEIDKRCQHKIAEMVALMEKHKHqyDKIIE----ERDSELGLYKnKEQEQSSAKA 742
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 719-794 2.62e-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: 52.69  E-value: 2.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  719 PLHINLSGHKDsgisLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 794
Cdd:cd06683    14 PLGITISGTEE----PFDPIVISGLTEGGLAERTGAIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTLKISR 85
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1318-1398 2.69e-08

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: 52.70  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1318 RHVKLQK-GSEPLGISIVSGEKG--GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITILA 1394
Cdd:cd06752     1 RTVVLKRpPGEQLGFNIRGGKASglGIFISKVIPDSDAHRLGLKEGDQILSVNGVDFEDIEHSEAVKVL-KTAREIQMRV 79


                  ....
gi 741978460 1395 QYNP 1398
Cdd:cd06752    80 RYFP 83
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 400-595 3.48e-08

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: 57.85  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  400 LQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALR- 478
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKe 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  479 ----QIKDTVTM-------------DAGRANKEAEILR---KQCKALCQELKEALQEADvakcrrdwafQERDKIVAERD 538
Cdd:COG4942   105 elaeLLRALYRLgrqpplalllspeDFLDAVRRLQYLKylaPARREQAEELRADLAELA----------ALRAELEAERA 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  539 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQmESQLEKEAR 595
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIA 230
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 724-794 3.57e-08

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: 52.15  E-value: 3.57e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460  724 LSGHKDSGISLengvYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 794
Cdd:cd06753    14 LQGGKDFNQPL----TISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLER 79
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
303-595 3.87e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  303 YDTAMDKLEVVKKDYDALRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQ-TEMLTQQRDTAIQLQHQCALsLRRFEAIHH 381
Cdd:PRK03918  160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREiNEISSELPELREELEKLEKE-VKELEELKE 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  382 ELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYS------EYKLIMSERDQVISELDKLQTEVEL 455
Cdd:PRK03918  239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSR 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  456 AESKLK------SSTSEKKAASEEMEA-LRQIKDTVTM---------DAGRANKEAEILRKQCKalCQELKEALQEADVA 519
Cdd:PRK03918  319 LEEEINgieeriKELEEKEERLEELKKkLKELEKRLEEleerhelyeEAKAKKEELERLKKRLT--GLTPEKLEKELEEL 396

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  520 KCRRDWAFQERDKIVAERDSIRtlcdNLRRERDRAVSELAEAL-------RSLDDTRKQK---------NDVSRELKELK 583
Cdd:PRK03918  397 EKAKEEIEEEISKITARIGELK----KEIKELKKAIEELKKAKgkcpvcgRELTEEHRKElleeytaelKRIEKELKEIE 472

                         330
                  ....*....|..
gi 741978460  584 EQmESQLEKEAR 595
Cdd:PRK03918  473 EK-ERKLRKELR 483
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 628-708 4.16e-08

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: 52.26  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  628 EDIDLK----ALGFDMAEGVNEPCLP---GDCGIFVTKVDKGSIAdGR--LRVNDWLLRINDVDLINKDKKQAIKALLNG 698
Cdd:cd06702     1 EEIHLVkaggPLGLSIVGGSDHSSHPfgvDEPGIFISKVIPDGAA-AKsgLRIGDRILSVNGKDLRHATHQEAVSALLSP 79

                          90
                  ....*....|
gi 741978460  699 EGAINMVVRR 708
Cdd:cd06702    80 GQEIKLLVRH 89
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
231-599 4.18e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  231 SRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSE---ILNKLYDTAM 307
Cdd:PRK03918  227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiKLSEFYEEYL 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  308 DKLEVVKK---DYDALRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEML---TQQRDTAIQL-----QHQCALSLRRF 376
Cdd:PRK03918  307 DELREIEKrlsRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerHELYEEAKAKkeeleRLKKRLTGLTP 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  377 EAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYK---------------EERDAVYSEYKLIMS---- 437
Cdd:PRK03918  387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteEHRKELLEEYTAELKriek 466

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  438 ---ERDQVISELDKLQTEVELA--------------------ESKLKSSTSEK-KAASEEMEALRQIKDTVTMDAGRANK 493
Cdd:PRK03918  467 elkEIEEKERKLRKELRELEKVlkkeseliklkelaeqlkelEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKK 546

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  494 EAE---ILRKQCKALCQELKEALQE-ADVAKCRRDWAF----------QERDKIVAERDSIRTLCDNLRR---ERDRAVS 556
Cdd:PRK03918  547 ELEkleELKKKLAELEKKLDELEEElAELLKELEELGFesveeleerlKELEPFYNEYLELKDAEKELEReekELKKLEE 626

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 741978460  557 ELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRHL 599
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
333-583 4.92e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 4.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  333 SDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQcALSLRRFEAIhhelnKATAQNKDLQWEMELLQSELTELRTTQA 412
Cdd:COG4913   232 EHFDDLERAHEALEDAREQIELLEPIRELAERYAAA-RERLAELEYL-----RAALRLWFAQRRLELLEAELEELRAELA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  413 KTAKEsekykeerdavyseyklimseRDQVISELDKLQTEV-ELAESKLKSSTSEKKAASEEMEALRQIKDtvtmdagRA 491
Cdd:COG4913   306 RLEAE---------------------LERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELE-------ER 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  492 NKEAEILRKQCKALcqELKEALQEADVAkcrrdwafqerdkivAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQ 571
Cdd:COG4913   358 ERRRARLEALLAAL--GLPLPASAEEFA---------------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420

                         250
                  ....*....|..
gi 741978460  572 KNDVSRELKELK 583
Cdd:COG4913   421 LRELEAEIASLE 432
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 651-708 5.21e-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: 51.89  E-value: 5.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  651 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDkkQAIKALLNGEGAINMVVRR 708
Cdd:cd06716    30 DTGIYVSEVDPNSIAakDGRIREGDQILQINGVDVQNRE--EAIALLSEEEKSITLLVAR 87
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1319-1393 5.57e-08

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: 51.96  E-value: 5.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1319 HVKLQKGSEP-LGISIVSGEK----GGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITI 1392
Cdd:cd06682     2 HVKLPKRSGVgLGITISAPKNrkpgDPLIISDVKKGSVAHRTGtLEPGDKLLAIDNIRLDNCSMEDAAQIL-QQAEDIVK 80


                  .
gi 741978460 1393 L 1393
Cdd:cd06682    81 L 81
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1565-1627 5.80e-08

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: 51.00  E-value: 5.80e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460   1565 DSFYIRALYERLAEVEPELSFKKDDILYVDDTLPQGsfgsWMAWQLDenaqKMQRGQIPSKYV 1627
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG----WWKGRLG----RGKEGLFPSNYV 55
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1318-1383 6.22e-08

PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 51.60  E-value: 6.22e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1318 RHVKLQKGS--EPLGISIVSG-EKG-GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd06740     2 RQVTLKRSKshEGLGFSIRGGaEHGvGIYVSLVEPGSLAEKEGLRVGDQILRVNDVSFEKVTHAEAVKIL 71
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-489 6.34e-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: 6.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   140 RQVNEKVENLSIQLRLMTR------ERNELRKRLAfATHGTTFDKRpYHRLNPDYERLKIQCVRAMSDLQSLQSQHTNAL 213
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERykelkaELRELELALL-VLRLEELREE-LEELQEELKEAEEELEELTAELQELEEKLEELR 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   214 KRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhn 293
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE-- 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   294 gSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQcalsl 373
Cdd:TIGR02168  352 -ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE----- 425

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   374 rrfeaihHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEV 453
Cdd:TIGR02168  426 -------LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 741978460   454 ELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAG 489
Cdd:TIGR02168  499 ENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
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 ...
 727-785 7.03e-08

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: 51.89  E-value: 7.03e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460  727 HKDSGISL------------ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQ 785
Cdd:cd06760    10 NKEPGVGLgiglcclplendIPGIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLNEAYAILSQCK 80
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
187-593 7.06e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.77  E-value: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  187 DYERLKIQCVRAMSDLQSLQSQHTNALKRCEEVAKETDFYHTLHsRLLSDQTQLKDDVDMLRRENGQLLRERnlLQQSWE 266
Cdd:PRK03918  318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEK--LEKELE 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  267 DMKRLHEEDQKEIGDLRAQQQQVlkhNGSSEILNKlydtAMDKLEVVK------------KDYDALRKRYSEKVAIHNSD 334
Cdd:PRK03918  395 ELEKAKEEIEEEISKITARIGEL---KKEIKELKK----AIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKE 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  335 LSRLEQMEEENQRLLKQTEM-------LTQQRDTAIQLqhqcalslrrfEAIHHELNKATAQNKDLQW-EMELLQSELTE 406
Cdd:PRK03918  468 LKEIEEKERKLRKELRELEKvlkkeseLIKLKELAEQL-----------KELEEKLKKYNLEELEKKAeEYEKLKEKLIK 536

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  407 LRTTQ---AKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTE-VELAESKLKsstsEKKAASEEMEALRQIKd 482
Cdd:PRK03918  537 LKGEIkslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLK----ELEPFYNEYLELKDAE- 611

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  483 tvtmdagranKEAEILRKQCKALCQELKEALQEADVAKCRrdwaFQERDKIVAERDSIRTLCD--NLRRERDRAVSELAE 560
Cdd:PRK03918  612 ----------KELEREEKELKKLEEELDKAFEELAETEKR----LEELRKELEELEKKYSEEEyeELREEYLELSRELAG 677

                         410       420       430
                  ....*....|....*....|....*....|...
gi 741978460  561 ALRSLDDTRKQKNDVSRELKELKEQMESQLEKE 593
Cdd:PRK03918  678 LRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 1319-1379 8.47e-08

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: 51.51  E-value: 8.47e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1319 HVKLQKGS-EPLGISIVSGEKG-GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06674     5 TVELQKKPgRGLGLSIVGKRNDtGVFVSDIVKGGAADADGrLMQGDQILSVNGEDVRNASQEAA 68
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1319-1393 9.86e-08

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: 51.11  E-value: 9.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1319 HVKLQKGSEPLGISIVSGeKG--------GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1389
Cdd:cd06724     1 EIKLVKGPKGLGFSIAGG-VGnqhipgdnGIYVTKIIEGGAAQKDGrLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDV 79


                  ....
gi 741978460 1390 ITIL 1393
Cdd:cd06724    80 VYLK 83
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 417-592 1.02e-07

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: 54.67  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  417 ESEKYKEERDAVySEYKLIMSERDQVISELDKLQTEV-----ELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRA 491
Cdd:cd07596     2 EDQEFEEAKDYI-LKLEEQLKKLSKQAQRLVKRRRELgsalgEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  492 NKEAeilRKQCKALCQELKEALQEADVAKCrrdwAFQERDKIVAERDSIRTLCDNLRRERDRAVS-------ELAEALRS 564
Cdd:cd07596    81 EAQA---NQELVKLLEPLKEYLRYCQAVKE----TLDDRADALLTLQSLKKDLASKKAQLEKLKAapgikpaKVEELEEE 153

                         170       180
                  ....*....|....*....|....*...
gi 741978460  565 LDDTRKQKNDVSRELKELKEQMESQLEK 592
Cdd:cd07596   154 LEEAESALEEARKRYEEISERLKEELKR 181
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 742-782 1.05e-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: 1.05e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 741978460  742 AVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 782
Cdd:cd06782    20 SPIPGGPAEKAG-IKPGDVIVAVDGESVRGMSLDEVVKLLR 59
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 136-636 1.16e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  136 VLSDRQVNEKVENLSIQLRLMTRERNELRKRLAfathgttfdkrpyhRLNPDYERLKIQCVRAMSDLQSLQSQHTNALKR 215
Cdd:COG1196   231 LLKLRELEAELEELEAELEELEAELEELEAELA--------------ELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  216 CEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhnGS 295
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--EL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  296 SEILNKLYDTAMDKLEVVKKDYdALRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRR 375
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  376 FEAihhELNKATAQNKDLQWEMELLQSELTELRTTQAKtAKESEKYKEERDAVYSEY---------KLIMSERDQVISEL 446
Cdd:COG1196   454 LEE---EEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFlegvkaallLAGLRGLAGAVAVL 529

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  447 DKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRAN--------------------------KEAEILRK 500
Cdd:COG1196   530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpldkiraraalaaalargaigaavDLVASDLR 609

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  501 QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAE------------------RDSIRTLCDNLRRERDRAVSELAEAL 562
Cdd:COG1196   610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrevtlegeggsaggsltGGSRRELLAALLEAEAELEELAERLA 689

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  563 RSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRHLMAHSSHDSAI----------------------DTDSMEWETEV 620
Cdd:COG1196   690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREElleelleeeelleeealeelpePPDLEELEREL 769

                         570
                  ....*....|....*.
gi 741978460  621 VEFEREtedidLKALG 636
Cdd:COG1196   770 ERLERE-----IEALG 780
SH3_ZO-2 cd12027
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a ...
 1564-1625 1.26e-07

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: 50.30  E-value: 1.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460 1564 GDSFYIRALYERLAEVEPELSFKKDDILYVDDTLPQGSFGSWMAWQLdenAQKMQRGQIPSK 1625
Cdd:cd12027     1 GDSFFIRTHFEYEKELPQSLAFTRGEIFRVVDTLYDGKLGNWLAVRI---GNELEKGLIPNK 59
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 1318-1392 1.44e-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: 50.73  E-value: 1.44e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460 1318 RHVKLQKG-SEPLGISIvSGEKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1392
Cdd:cd06726     1 RLVEFEKArDEPLGATI-KMEEDSVIVARILHGGMAHRSGlLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTF 76
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-496 1.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  144 EKVENLSIQLRLMTRERNELRKRLAfathgttfDKRPYHRLnpdYERLKiqcvRAMSDLQSLQSQHT------------N 211
Cdd:PRK03918  331 KELEEKEERLEELKKKLKELEKRLE--------ELEERHEL---YEEAK----AKKEELERLKKRLTgltpeklekeleE 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  212 ALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRREN------GQLLRE---RNLLQQSWEDMKRLhEEDQKEIG-- 280
Cdd:PRK03918  396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEehrKELLEEYTAELKRI-EKELKEIEek 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  281 --DLRAQQQQVLKHNGSSEILNKLYDTA--------------MDKLEVVKKDYDALRKRYSE---KVAIHNSDLSRLEQM 341
Cdd:PRK03918  475 erKLRKELRELEKVLKKESELIKLKELAeqlkeleeklkkynLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEEL 554

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  342 EEENQRLLKQ--------TEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAK 413
Cdd:PRK03918  555 KKKLAELEKKldeleeelAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  414 TAKES-------------------EKYKEERD----------AVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSST 464
Cdd:PRK03918  635 LAETEkrleelrkeleelekkyseEEYEELREeylelsrelaGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714

                         410       420       430
                  ....*....|....*....|....*....|...
gi 741978460  465 SEKKAAsEEMEALRQ-IKDTVTMDAGRANKEAE 496
Cdd:PRK03918  715 KLEKAL-ERVEELREkVKKYKALLKERALSKVG 746
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 719-793 1.52e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 50.36  E-value: 1.52e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460   719 PLHINLSGHKDSGIsleNGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:pfam00595   11 GLGFSLKGGSDQGD---PGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 732-793 1.64e-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: 50.32  E-value: 1.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460  732 ISLENGVYAAAVVPGSPAakEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:cd06769    16 AGSERPVVVRSVTPGGPS--EGKLLPGDQILKINNEPVEDLPRERVIDLIRECKDSIVLTVL 75
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1329-1379 1.80e-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: 1.80e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1329 LGISIVSGeKG---------GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06704    12 LGISIAGG-KGstpykgddeGIFISRVTEGGPAAKAGVRVGDKLLEVNGVDLVDADHHEA 70
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 720-794 1.93e-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: 50.42  E-value: 1.93e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  720 LHINLSG--HKDSGISLengvYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 794
Cdd:cd06682    13 LGITISApkNRKPGDPL----IISDVKKGSVAHRTGTLEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIRK 85
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 1342-1392 2.15e-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: 2.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 741978460 1342 YVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1392
Cdd:cd06746    45 YLESVDPGGVADKAGLKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVL 95
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
373-636 2.42e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  373 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVyseykliMSERDQVISELDKLQTE 452
Cdd:COG4372    37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA-------QAELAQAQEELESLQEE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  453 VELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEAlqEADVAKCRRDWAFQERDK 532
Cdd:COG4372   110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  533 IVAER----DSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRHLMAHSSHDSA 608
Cdd:COG4372   188 LLKEAnrnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267

                         250       260
                  ....*....|....*....|....*...
gi 741978460  609 IDTDSMEWETEVVEFERETEDIDLKALG 636
Cdd:COG4372   268 LVEKDTEEEELEIAALELEALEEAALEL 295
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 439-626 2.50e-07

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: 55.80  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   439 RDQVISELDKLQTEVelAESKLKSSTSE--KKAASEEMEALRQIKDTVTMDAGRANKEAEILRKQ---CKALCQELKE-- 511
Cdd:pfam05701   37 RKLVELELEKVQEEI--PEYKKQSEAAEaaKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDselAKLRVEEMEQgi 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   512 -------ALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKE 584
Cdd:pfam05701  115 adeasvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKE 194

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 741978460   585 QMESqlekearfrhlmAHSSHDSA----------IDTDSMEWETEVVEFERE 626
Cdd:pfam05701  195 SLES------------AHAAHLEAeehrigaalaREQDKLNWEKELKQAEEE 234
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 141-594 2.55e-07

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: 56.13  E-value: 2.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   141 QVNEKVENLSIQLRLMTRERNELRKrlafathgttfdkrpyHRLNPDYERLKIQCVRAMsdLQSLQSQHtNALKRCEEVA 220
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRAKLLM----------------KRAAHVKQQSSIEEQRRL--LQTLHSQE-IHIRDAHEVA 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   221 K----ETDFYHTLHSRLLSDQTQ----------LKDDVDMLRRENGQ---LLRERNLLQQSWEDMKRLHEEDQKEIGDLR 283
Cdd:TIGR00618  365 TsireISCQQHTLTQHIHTLQQQkttltqklqsLCKELDILQREQATidtRTSAFRDLQGQLAHAKKQQELQQRYAELCA 444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   284 AQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHnsdLSRLEQMEEENQRLLKQTEMLTQQRDTAI 363
Cdd:TIGR00618  445 AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVV---LARLLELQEEPCPLCGSCIHPNPARQDID 521

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   364 QLQHQCALSLR----------RFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYK 433
Cdd:TIGR00618  522 NPGPLTRRMQRgeqtyaqletSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE 601

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   434 LIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEAL 513
Cdd:TIGR00618  602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   514 QEADVAKCRRDWAFQErdkIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRE-LKELKEQMESQLEK 592
Cdd:TIGR00618  682 LQKMQSEKEQLTYWKE---MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQsLKELMHQARTVLKA 758


                   ..
gi 741978460   593 EA 594
Cdd:TIGR00618  759 RT 760
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 723-790 2.63e-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: 49.74  E-value: 2.63e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  723 NLSGHKDsgislENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06768    15 NLHAEKG-----RPGHFIREVDPGSPAERAG-LKDGDRLVEVNGENVEGESHEQVVEKIKASGNQVTL 76
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 620-708 2.66e-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: 49.97  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  620 VVEFERETedidlKALGFDMAEGVNE-PCLPGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd06704     2 TITIERQT-----GGLGISIAGGKGStPYKGDDEGIFISRVTEGGPAAkAGVRVGDKLLEVNGVDLVDADHHEAVEALKN 76

                          90
                  ....*....|.
gi 741978460  698 GEGAINMVVRR 708
Cdd:cd06704    77 SGNTVTMVVLR 87
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
397-592 2.77e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 54.53  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  397 MELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQtevelaeSKLKSSTSEKKAASEEMEA 476
Cdd:COG1340     3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELR-------EEAQELREKRDELNEKVKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  477 LRQIKDTVtmdagraNKEAEILRKQCKALCQELKEA-LQEADVAKCRRD-----WAFQ-------ERDKIVAERDSIRTL 543
Cdd:COG1340    76 LKEERDEL-------NEKLNELREELDELRKELAELnKAGGSIDKLRKEierleWRQQtevlspeEEKELVEKIKELEKE 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 741978460  544 CDNLRRERDRAvSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEK 592
Cdd:COG1340   149 LEKAKKALEKN-EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1316-1395 2.90e-07

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: 49.95  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1316 EPRHVKLQKGSEPLGISIVSGeKG---------GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1385
Cdd:cd06703     1 ETITTTLIRDGKGLGFSIAGG-KGstpfrdgdeGIFISRITEGGAADRDGkLQVGDRVLSINGVDVTEARHDQAVALLTS 79

                          90
                  ....*....|
gi 741978460 1386 QCDTITILAQ 1395
Cdd:cd06703    80 SSPTITLVVE 89
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
229-629 3.11e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  229 LHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRlHEEDQKEIGDLRAQqqqvlkhngsseilnkLYDTAMD 308
Cdd:PRK02224  204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELETLEAE----------------IEDLRET 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  309 KLEVvKKDYDALRKRYSEKVAihnsdlsRLEQMEEENQRLLKQTEMLTQQRDtaiqlqhqcALSLRRfeaihhelnkata 388
Cdd:PRK02224  267 IAET-EREREELAEEVRDLRE-------RLEELEEERDDLLAEAGLDDADAE---------AVEARR------------- 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  389 qnKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQviseldkLQTEVELAESKLKSSTSEKK 468
Cdd:PRK02224  317 --EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE-------LESELEEAREAVEDRREEIE 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  469 AASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKE---ALQEAD--VAKCRRdwaFQERDKI------VAER 537
Cdd:PRK02224  388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARerVEEAEA---LLEAGKCpecgqpVEGS 464

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  538 DSIRTLCDnlRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRHLMAhsSHDSAIDTDSMEWE 617
Cdd:PRK02224  465 PHVETIEE--DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIA--ERRETIEEKRERAE 540

                         410
                  ....*....|....*
gi 741978460  618 T---EVVEFERETED 629
Cdd:PRK02224  541 ElreRAAELEAEAEE 555
PDZ5_PTPN13-like cd06697
PDZ domain 5 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 719-790 3.58e-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: 49.65  E-value: 3.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460  719 PLHINLSGHKDSgisLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06697    14 QLGLKLTGGSDS---KYQVIYVLEIVPGSAAAEEGSLQPLDIIHYINGVSTQGMTLEDAVRALEASLPTVVL 82
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 1470-1550 3.75e-07

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: 50.01  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1470 EPRVVFIKK-SQLELGVHLCGGN-----------LHGVFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVyVE 1537
Cdd:cd06671     1 PPRRVELWRePGKSLGISIVGGRvmgsrlsngeeIRGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEA-VE 79

                          90
                  ....*....|....
gi 741978460 1538 MLK-PKDSVRLKVQ 1550
Cdd:cd06671    80 AIRnAGNPVVFLVQ 93
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 731-782 4.48e-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: 4.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 741978460  731 GISL---ENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 782
Cdd:COG0793    63 GAELgeeDGKVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLLR 116
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 728-793 4.49e-07

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: 49.56  E-value: 4.49e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  728 KDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:cd23058    24 RDNPTGGSGPIYIKNILPKGAAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKLGGTVSLV 89
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 735-793 4.69e-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: 49.19  E-value: 4.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460  735 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:cd06726    21 EDSVIVARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLI 79
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 720-782 4.74e-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: 49.97  E-value: 4.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  720 LHINLSGH---KDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLR 782
Cdd:cd23059    18 LGVSVKGKtskEDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETLR 83
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
 734-790 4.97e-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: 4.97e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  734 LENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd23071    28 LDLGIFIASIIPGGPAEKDGRIKPGGRLISLNNISLEGVTFNTAVKILQNSPDEVEL 84
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
336-586 5.06e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.14  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  336 SRLEQMEEENQRLLKQTEMLTQQRDTAiqlqhqcalsLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTA 415
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQA----------REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  416 KESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQikdtvTMDAGRANKEA 495
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE-----ELAALEQELQA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  496 EILRKQCKALCQELKEALQEADV--AKCRRDWAFQERDKIVAERDSIRTlcDNLRRERDRAVSELAEALRSLDDTRKQKN 573
Cdd:COG4372   176 LSEAEAEQALDELLKEANRNAEKeeELAEAEKLIESLPRELAEELLEAK--DSLEAKLGLALSALLDALELEEDKEELLE 253

                         250
                  ....*....|...
gi 741978460  574 DVSRELKELKEQM 586
Cdd:COG4372   254 EVILKEIEELELA 266
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 722-790 5.14e-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: 49.19  E-value: 5.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460  722 INLSGHKDS--GISLENGVYAAAVVPGSPAakEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06727    15 IAVSGGRDNphFQSGDTSIVISDVLKGGPA--EGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANI 83
PDZ_PICK1-like cd06722
PDZ domain of PICK1 (protein interacting with C-kinase 1) and similar domains; PDZ (PSD-95 ...
 728-794 5.71e-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: 5.71e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  728 KDS----GISLENG------VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 794
Cdd:cd06722     7 KDAqnliGISIGGGapycpcLYIVQVFDNTPAAKDGTLAAGDEIVGVNGKSVKGKTKVEVAKMIQAVKGEVTIHYNK 83
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 1320-1391 6.12e-07

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: 48.78  E-value: 6.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1320 VKLQKGSEPLGISIVSGEKGG-VYVSKVTGGSIAHQAGLEY-GDQLLEFNGINLRSATEQQARLIIGQQCDTIT 1391
Cdd:cd06799     3 VRLVKNNEPLGATIKRDEKTGaIVVARIMRGGAADRSGLIHvGDELREVNGISVEGKDPEEVIQILANSQGPIT 76
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 622-708 6.27e-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: 49.13  E-value: 6.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  622 EFERETEDIDlKALGFDMAEGVNEPCLPGdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGE 699
Cdd:cd06792     2 VFEVELSKKD-GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAeqDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAG 78


                  ....*....
gi 741978460  700 GAINMVVRR 708
Cdd:cd06792    79 QVVTLVLER 87
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1472-1550 6.64e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 48.82  E-value: 6.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1472 RVVFIKKSQLELGVHLCGGN---LHGVFVAEVEDDSPARGpDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLK 1548
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79


                   ..
gi 741978460  1549 VQ 1550
Cdd:pfam00595   80 IL 81
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 1320-1403 6.89e-07

PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ10 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467161 [Multi-domain]  Cd Length: 86  Bit Score: 48.83  E-value: 6.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1320 VKLQKGSEPLGISIVSGEK---GGVYVSKV-TGGSIAHQAGLEYGDQLLEFNGINLRSATEQQArliigqqcdtITILAQ 1395
Cdd:cd06673     6 IEINKGKKGLGLSIVGGSDtllGAIIIHEVyEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEA----------INVLRQ 75


                  ....*...
gi 741978460 1396 YNPHMHQL 1403
Cdd:cd06673    76 TPQKVRLL 83
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 721-792 7.31e-07

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: 48.50  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  721 HINLsgHKDSG-----IS---LENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 792
Cdd:cd10817     1 HVEL--PKDQGglgiaISeedTENGIVIKSLTEGGPAAKDGRLKVGDQILAVDDESVVGCPYEKAISLLKTAKGTVKLTV 78
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 295-603 7.33e-07

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: 54.34  E-value: 7.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   295 SSEILNKLYDTAMDKLEVVKKdydalrkrysEKVAIHnSDLSRLEQMEEENQRLLKQtemltqQRDTAIQLQHQCalslr 374
Cdd:pfam05483   72 NSEGLSRLYSKLYKEAEKIKK----------WKVSIE-AELKQKENKLQENRKIIEA------QRKAIQELQFEN----- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   375 rfEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVE 454
Cdd:pfam05483  130 --EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAE 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   455 laESKLKSSTSEKkaasEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKE---ALQEAdvakcrRDWAFQERD 531
Cdd:pfam05483  208 --NARLEMHFKLK----EDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDltfLLEES------RDKANQLEE 275

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460   532 KIVAERDSIRTLCDnlrrERDRAVSELAEALRSLDDTRKQKNDVSRELK-------ELKEQMESQLEKEARFRhlMAHS 603
Cdd:pfam05483  276 KTKLQDENLKELIE----KKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAK--AAHS 348
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 1320-1395 8.86e-07

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


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 48.29  E-value: 8.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1320 VKLQK--GSEPLGISIVSGEKGG--VYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1395
Cdd:cd23068     2 IRLRRddSNTPWGFRLQGGADFGqpLSIQKVNPGSPADKAGLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQ 81
PDZ1_APBA1_3-like cd06720
PDZ domain 1 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ...
 738-784 8.99e-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: 8.99e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 741978460  738 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 784
Cdd:cd06720    29 VVVANMMPGGPAARSGKLNIGDQIMSINGTSLVGLPLSTCQAIIKNL 75
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 140-595 1.02e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  140 RQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTTFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQSQHTNALKRCEEV 219
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  220 AKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEiL 299
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG-L 519

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  300 NKLYDTAMDKLEVVKKDYDALRKRYSEK-VAIHNSDLSRLEQMEEE--NQRLLKQTE--MLTQQRDTAIQLQHQCALSLR 374
Cdd:COG1196   520 RGLAGAVAVLIGVEAAYEAALEAALAAAlQNIVVEDDEVAAAAIEYlkAAKAGRATFlpLDKIRARAALAAALARGAIGA 599

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  375 RFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVE 454
Cdd:COG1196   600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  455 LAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIV 534
Cdd:COG1196   680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  535 AERDSIRTLCDNLRRERDR-------AVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEAR 595
Cdd:COG1196   760 PDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIE-EIDRETR 826
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
422-595 1.05e-06

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: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  422 KEERDAVYSEYKLIMSERDQV---ISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIK-------DTVTMDAGRA 491
Cdd:COG4913   592 KDDRRRIRSRYVLGFDNRAKLaalEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeiDVASAEREIA 671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  492 NKEAEI--LRK---QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 566
Cdd:COG4913   672 ELEAELerLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751

                         170       180
                  ....*....|....*....|....*....
gi 741978460  567 DTRKQKNDVSRELKELKEQMESQLEKEAR 595
Cdd:COG4913   752 EERFAAALGDAVERELRENLEERIDALRA 780
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 1326-1379 1.09e-06

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: 48.37  E-value: 1.09e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460 1326 SEPLGISIV------SGEKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06692     7 SKGLGIKIIggyrenTGEEFGIFIKRILPGGLAATDGrLKEGDLILEVNGESLQGVTNERA 67
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 1320-1394 1.13e-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: 48.55  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1320 VKLQKGSEP-LGISIVSGEKG-----GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1392
Cdd:cd06694     5 VTLKKDPQKgLGFTIVGGENSgsldlGIFVKSIIPGGPADKDGrIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84


                  ..
gi 741978460 1393 LA 1394
Cdd:cd06694    85 II 86
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 650-708 1.18e-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: 48.04  E-value: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460  650 GDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 708
Cdd:cd06727    29 GDTSIVISDVLKGGPAEGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANITVKR 87
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 237-588 1.27e-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: 53.64  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   237 QTQLKDDVDMLRRENGQLLRERNLLQQSW----------EDMK-------------------RLHEEDQkeigdlRAQQQ 287
Cdd:pfam01576   21 QQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaeaEEMRarlaarkqeleeilhelesRLEEEEE------RSQQL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   288 QVLKHNGSSEILN-----KLYDTAMDKLEVVKKDYDALRKRYSEKVAI---HNSDLSRLEQMEEEnqRLLKQTEMLTQQR 359
Cdd:pfam01576   95 QNEKKKMQQHIQDleeqlDEEEAARQKLQLEKVTTEAKIKKLEEDILLledQNSKLSKERKLLEE--RISEFTSNLAEEE 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   360 DTAIQLQ-----HQCALS-----LRRFEAIHHELNKAT----AQNKDLQWEMELLQSELTELRTTQAKtaKESE------ 419
Cdd:pfam01576  173 EKAKSLSklknkHEAMISdleerLKKEEKGRQELEKAKrkleGESTDLQEQIAELQAQIAELRAQLAK--KEEElqaala 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   420 KYKEERDAVYSEYKLImSERDQVISEldkLQTEVELAESKLKSSTSEKKAASEEMEALR-QIKDTVTMDAG----RANKE 494
Cdd:pfam01576  251 RLEEETAQKNNALKKI-RELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEALKtELEDTLDTTAAqqelRSKRE 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   495 AEI--------------------LRKQCKALCQELKEALQEADVAKCRRDWAFQ----ERDKIVAERDSIRTLCDNLRRE 550
Cdd:pfam01576  327 QEVtelkkaleeetrsheaqlqeMRQKHTQALEELTEQLEQAKRNKANLEKAKQalesENAELQAELRTLQQAKQDSEHK 406

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 741978460   551 RDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMES 588
Cdd:pfam01576  407 RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELES 444
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1318-1379 1.32e-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: 1.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460 1318 RHVKLQKgsEP---LGISIvsgeKGG------VYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06801     1 RTVRVVK--QDvggLGISI----KGGaehkmpILISKIFKGQAADQTGqLFVGDAILSVNGENLEDATHDEA 66
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 736-792 1.74e-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: 1.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  736 NGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 792
Cdd:cd23060    23 SGIFVKSISPGGVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
PTZ00121 PTZ00121
MAEBL; Provisional
 266-595 1.83e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  266 EDMKRLHEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDALRKRYSE---------KVAIHNSDLS 336
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKK---AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEakkkadaakKKAEEKKKAD 1394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  337 RLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQcALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAK 416
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  417 ESEKYKEERDAVySEYKLIMSERDQVISELDKLQTEVELAEsKLKSSTSEKKAasEEMEALRQIKDTVTMDAGRANKEAE 496
Cdd:PTZ00121 1474 EAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKAD 1549

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  497 ILRKqckalCQELKEALQEADVAKCRRDwafQERDKIVAERDSIRTLCDNLRRERDRAVSEL-----AEALRSLDDTRKQ 571
Cdd:PTZ00121 1550 ELKK-----AEELKKAEEKKKAEEAKKA---EEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmkAEEAKKAEEAKIK 1621

                         330       340
                  ....*....|....*....|....*.
gi 741978460  572 KNDVSRELKELK--EQMESQLEKEAR 595
Cdd:PTZ00121 1622 AEELKKAEEEKKkvEQLKKKEAEEKK 1647
PTZ00121 PTZ00121
MAEBL; Provisional
 266-661 1.86e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  266 EDMKRLHE----EDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTamdKLEVVKKDYDALRKRYSEKVaihnsdlsrleQM 341
Cdd:PTZ00121 1549 DELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA---RIEEVMKLYEEEKKMKAEEA-----------KK 1614

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  342 EEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH--HELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESE 419
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  420 KYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILR 499
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  500 KQCKALcqeLKEALQEADvAKCRRDWAFQERD-----KIVAERDSIRTLCDNLRRERDraVSELAEALrsldDTRKQKND 574
Cdd:PTZ00121 1775 KEKEAV---IEEELDEED-EKRRMEVDKKIKDifdnfANIIEGGKEGNLVINDSKEME--DSAIKEVA----DSKNMQLE 1844

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  575 VSRELKELKEQMESQLEKEarfrhlmAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKalgfDM-AEGVNEPCLPGDCG 653
Cdd:PTZ00121 1845 EADAFEKHKFNKNNENGED-------GNKEADFNKEKDLKEDDEEEIEEADEIEKIDKD----DIeREIPNNNMAGKNND 1913


                  ....*...
gi 741978460  654 IFVTKVDK 661
Cdd:PTZ00121 1914 IIDDKLDK 1921
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 222-631 1.87e-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: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   222 ETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngSSEILNK 301
Cdd:TIGR00618  174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ------SHAYLTQ 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   302 LYDTAMDKlevvkkdyDALRKRYSEKVAihnsdlsRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQcalslrrfEAIHH 381
Cdd:TIGR00618  248 KREAQEEQ--------LKKQQLLKQLRA-------RIEELRAQEAVLEETQERINRARKAAPLAAHI--------KAVTQ 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   382 ELNKATAQNKDLQWEMELLQSELTElRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELaESKLK 461
Cdd:TIGR00618  305 IEQQAQRIHTELQSKMRSRAKLLMK-RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIH 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   462 SSTSEKKAASEEMEALRQIKDTVTMDAGRAnkEAEILRK---QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERd 538
Cdd:TIGR00618  383 TLQQQKTTLTQKLQSLCKELDILQREQATI--DTRTSAFrdlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI- 459

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   539 sirtlcdnLRRERDRAVSELAEALRSLDDTRKQKNDVSR-ELKELKEQMESQLEKEARFRHLMAH--SSHDSAIDTDSME 615
Cdd:TIGR00618  460 --------HLQESAQSLKEREQQLQTKEQIHLQETRKKAvVLARLLELQEEPCPLCGSCIHPNPArqDIDNPGPLTRRMQ 531

                          410
                   ....*....|....*..
gi 741978460   616 -WETEVVEFERETEDID 631
Cdd:TIGR00618  532 rGEQTYAQLETSEEDVY 548
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1473-1550 1.89e-06

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 47.64  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1473 VVFIKKSQLELGVHLCGGNLH----------GVFVAEVEDDSPArGPDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPK 1542
Cdd:cd06702     2 EIHLVKAGGPLGLSIVGGSDHsshpfgvdepGIFISKVIPDGAA-AKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPG 80


                  ....*...
gi 741978460 1543 DSVRLKVQ 1550
Cdd:cd06702    81 QEIKLLVR 88
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1320-1392 2.03e-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: 47.34  E-value: 2.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1320 VKLQKGSEPLGISIVSGEKGG-----VYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1392
Cdd:cd06676     2 ITLERGSDGLGFSIVGGFGSPhgdlpIYVKTVFEKGAAAEDGrLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTL 80
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 1340-1393 2.06e-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: 47.72  E-value: 2.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1340 GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:cd10822    38 GIYVTRVSEGGPAEKAGLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKPVLRML 91
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 380-641 2.09e-06

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: 53.05  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   380 HHELNKATAQNKDLQwemELLQSELTEL----------RTTQAKTAKESEKYKEERDAVYSEYKLIMSER----DQVISE 445
Cdd:pfam02463  108 EYYINGKNVTKKEVA---ELLESQGISPeaynflvqggKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEAlkklIEETEN 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   446 LDKLQTEVELAESKLKSstsEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEALQEADVAKCRRdw 525
Cdd:pfam02463  185 LAELIIDLEELKLQELK---LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE-- 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   526 aFQERDKIVAERDSIRTLC----DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRHLMA 601
Cdd:pfam02463  260 -IEKEEEKLAQVLKENKEEekekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 741978460   602 HSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAE 641
Cdd:pfam02463  339 ELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 626-697 2.10e-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: 47.61  E-value: 2.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  626 ETEDIDL----KALGFDMAEGVNEPCLPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd06791     1 ETFEVELvkdeQGLGITIAGYVGEKASGELSGIFVKSIIPGSAAdqDGRIQVNDQIIAVDGVNLQGFTNQEAVEVLRN 78
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-448 2.41e-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: 52.75  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   140 RQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTTFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQSQHTNaLKrcEEV 219
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LN--EEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   220 AKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEdQKEIGDLRAQQQQVLkhngssEIL 299
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-LEALLNERASLEEAL------ALL 892

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   300 NKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNSDLSRLEQMEeenQRLLKQTEMLT-QQRDTaiqlqhqcalslrrFEA 378
Cdd:TIGR02168  893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE---VRIDNLQERLSeEYSLT--------------LEE 955

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460   379 IHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSER---DQVISELDK 448
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKetlEEAIEEIDR 1028
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1329-1392 2.52e-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: 47.38  E-value: 2.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460 1329 LGISIVSG-EKG-GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQA-RLIIGQQCDTITI 1392
Cdd:cd10834    15 LGFNIRGGsEYGlGIYVSKVDPGGLAEQNGIKVGDQILAVNGVSFEDITHSKAvEVLKSQTHLMLTI 81
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 726-793 2.87e-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: 46.97  E-value: 2.87e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  726 GHKDS-GISLENG---------VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:cd06675     8 GPQDSlGISIAGGvgsplgdvpVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKNASGTIILQVV 85
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 735-790 3.01e-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: 3.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  735 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
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 ...
 738-793 3.12e-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: 3.12e-06
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gi 741978460  738 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:cd06676    28 IYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTLTVL 83
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 733-795 3.14e-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: 3.14e-06
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gi 741978460  733 SLENGVYAAAVVPgSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 795
Cdd:cd06696    24 KDDNGCYIHDIVQ-DPAKSDGRLRPGDRLIMVNGVDVTNMSHTEAVSLLRAAPKEVTLVLGRA 85
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1318-1383 3.24e-06

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: 46.86  E-value: 3.24e-06
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gi 741978460 1318 RHVKLQKGSEPLGISiVSGEK---GGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd06670     5 RTITIVKGNSSLGIT-VSADKdgnGCIVKSIIHGGAVSRDGRISVGDFIVSINNESLRNVTNAQARAIL 72
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 738-804 3.35e-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: 3.35e-06
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gi 741978460  738 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLkvfpqsaSWSG 804
Cdd:cd06680    30 FFVKSIVPGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTVV-------SWPG 89
PDZ_neurabin-like cd06790
PDZ domain of neurabin-1 and neurabin-2, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1320-1379 3.54e-06

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: 47.03  E-value: 3.54e-06
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gi 741978460 1320 VKLQKGSEPLGISIV-------SG-EKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06790     5 VELEKGSEGLGISIIgmgvgadAGlEKLGIFVKTVTEGGAAQRDGrIQVNDQIVEVDGISLVGVTQAFA 73
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 705-786 3.56e-06

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


Pssm-ID: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 46.93  E-value: 3.56e-06
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gi 741978460  705 VVRR-RKSLGgkvvtplhINLSGHKDSGISLEN-----GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECE 778
Cdd:cd06671     7 LWREpGKSLG--------ISIVGGRVMGSRLSNgeeirGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEAV 78


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gi 741978460  779 SLLRSCQD 786
Cdd:cd06671    79 EAIRNAGN 86
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 1318-1393 3.72e-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: 46.57  E-value: 3.72e-06
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gi 741978460 1318 RHVKLQKGSEPLGiSIVSGEKGGVYVSKVTGGSIAHQAGLEY-GDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:cd06798     1 KIVRIEKTREPLG-ATVRNEGDSVIISRIVKGGAAEKSGLLHeGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFL 76
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 1318-1369 4.30e-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: 4.30e-06
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gi 741978460 1318 RHVKLQK-GSEPLGISIVSG---EKG-GVYVSKVTGGSIAHQAGLEY-GDQLLEFNGI 1369
Cdd:cd06718     1 RRVELIKpPGKPLGFYIRDGngvERVpGIFISRLVLGSLADSTGLLAvGDEILEVNGV 58
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 1318-1379 4.32e-06

PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467271 [Multi-domain]  Cd Length: 93  Bit Score: 46.87  E-value: 4.32e-06
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gi 741978460 1318 RHVKLQKGSEPLGISIVS-----GEKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd23058     6 LHIQLKKGPEGLGFSITSrdnptGGSGPIYIKNILPKGAAIQDGrLKAGDRLLEVNGVDVTGKTQEEV 73
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 728-773 4.49e-06

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: 46.74  E-value: 4.49e-06
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gi 741978460  728 KDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKS 773
Cdd:cd23063    22 KVSPNTKTTGIFIKGIIPDSPAHKCGRLKVGDRILSVNGNDVRNST 67
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1318-1393 4.50e-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: 4.50e-06
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gi 741978460 1318 RHVKLQKG-SEPLGISIVSGEKG-----------GVYVSKVT-GGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIG 1384
Cdd:cd06701     5 QELTIVKEpGEKLGISIRGGAKGhagnpldptdeGIFISKINpDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILR 84


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gi 741978460 1385 QQCDTITIL 1393
Cdd:cd06701    85 SVGDTLTLL 93
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 737-790 4.54e-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: 4.54e-06
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gi 741978460  737 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06701    39 GIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTL 92
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 1320-1384 4.77e-06

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: 46.58  E-value: 4.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460 1320 VKLQKGSEPLGISIvSGEKG------GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIG 1384
Cdd:cd06758     5 MHLLKEKGGLGIQI-TGGKGskrgdiGIFVAGVEEGGSADRDGrLKKGDELLMINGQSLIGLSHQEAVAILR 75
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 635-706 5.01e-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: 5.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  635 LGFDMAEGVNE----PCLPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 706
Cdd:cd06701    17 LGISIRGGAKGhagnPLDPTDEGIFISKINPDGAAarDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTLLV 94
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 709-793 5.07e-06

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: 46.45  E-value: 5.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  709 RKSLGGKVVtplhinlSGHKDSGISlENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSL 788
Cdd:cd06692     7 SKGLGIKII-------GGYRENTGE-EFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSILRSASASN 78


                  ....*
gi 741978460  789 TLSLL 793
Cdd:cd06692    79 HMSLL 83
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 ...
 1319-1385 5.26e-06

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: 46.49  E-value: 5.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460 1319 HVKLQKgsEP---LGISIVS----GEKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1385
Cdd:cd06760     6 EVTLNK--EPgvgLGIGLCClpleNDIPGIFIHHLSPGSVAHMDGrLRRGDQILEINGTSLRNVTLNEAYAILSQ 78
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 731-776 5.33e-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: 5.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 741978460  731 GISLEN--GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE 776
Cdd:cd06718    20 GNGVERvpGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDD 67
PTZ00121 PTZ00121
MAEBL; Provisional
 266-595 5.36e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  266 EDMKRLHEEDQKEIGDLRAQQQQvlkhngSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNSDLSRLEQMEEEN 345
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEER------NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  346 QRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHH---------ELNKATAQNKDLQWEMELLQSELTELRTTQAKTAK 416
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKkaeeakkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  417 ESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAE 496
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  497 ILRKQC--KALCQELKEALQE---ADVAKCRRDWAFQERDKIvAERDSIRTLCDNLRR-ERDRAVSEL--AEALRSLDDT 568
Cdd:PTZ00121 1461 EAKKKAeeAKKADEAKKKAEEakkADEAKKKAEEAKKKADEA-KKAAEAKKKADEAKKaEEAKKADEAkkAEEAKKADEA 1539

                         330       340       350
                  ....*....|....*....|....*....|.
gi 741978460  569 RK----QKNDVSRELKELKEQMESQLEKEAR 595
Cdd:PTZ00121 1540 KKaeekKKADELKKAEELKKAEEKKKAEEAK 1570
PHA03247 PHA03247
large tegument protein UL36; Provisional
 860-1287 5.50e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  860 PPGGSSSFLHKPFPGGPFSVSPQACP--SASERSLSSFRSDASGERGYGPAD--MRSRRPLLPfeTEVGPCGA-AEAPLD 934
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPrdDPAPGRVSRPRRARRLGRAAQASSppQRPRRRAAR--PTVGSLTSlADPPPP 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  935 KAEPDSAhsggtwPKAVLSSVAGPEKLSVYRKPKqrksifdPNTFKRPQTPPKIDYLLPGSGPAHSPLPSKRVGPLTPPK 1014
Cdd:PHA03247 2705 PPTPEPA------PHALVSATPLPPGPAAARQAS-------PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1015 PPRRGdsikfqhkleTSSESEATLVGSSPSTSPPSALPPDVDPGDPMHASPPRKARVRIASSYCPEGDRDSSYLPAKKSc 1094
Cdd:PHA03247 2772 PAAPA----------AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP- 2840

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1095 dedLTSQKEQKCTPASGELSP--DLQEWAPYSPGHSSrhsnpPFYPSRASVGTVPRSLAPSTVSSVLRNPIYTVRSHRVG 1172
Cdd:PHA03247 2841 ---PPPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAK-----PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1173 PCSSP-PIPREAGPHGLHPSVQHQGRLSLDLSPRACsdcsdmrashgsnslPSSARLATGSSSNLQFKAeriKIPSTPRY 1251
Cdd:PHA03247 2913 APPPPqPQPQPPPPPQPQPPPPPPPRPQPPLAPTTD---------------PAGAGEPSGAVPQPWLGA---LVPGRVAV 2974

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 741978460 1252 PRSVVGSDRGSLSHSECSTPPQSPLSVEGLSSCSQS 1287
Cdd:PHA03247 2975 PRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASS 3010
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1318-1379 6.10e-06

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: 46.09  E-value: 6.10e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1318 RHVKLQKG-SEPLGISIVSGEKGG-----VYVSKV-TGGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06679     1 KTVTIKKEpSESLGISVAGGRGSRrgdlpIYVTNVqPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEA 69
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 341-575 6.56e-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: 49.54  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  341 MEEENQRLLKqtemLtQQRDTAIQlqhqcalslrrfeAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEK 420
Cdd:COG1579     2 MPEDLRALLD----L-QELDSELD-------------RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  421 YKEERDAVY-----SEYKL--IMSERdqvisELDKLQTEVELAESKLKSSTSEKKAASEEMEALRqikdtvtmdagranK 493
Cdd:COG1579    64 LELEIEEVEarikkYEEQLgnVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELE--------------E 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  494 EAEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIVAERDSirtlcdnLRRERDRAVSELAEALRSL-DDTRKQK 572
Cdd:COG1579   125 ELAELEAELAELEAELEEKKAELD----------EELAELEAELEE-------LEAEREELAAKIPPELLALyERIRKRK 187


                  ...
gi 741978460  573 NDV 575
Cdd:COG1579   188 NGL 190
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 635-709 6.83e-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: 6.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  635 LGFDMAEGVNEPclpgdcGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 709
Cdd:cd06795    14 LGFNIVGGEDGE------GIFISFILAGGPADlsGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIAQYK 84
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 702-771 6.94e-06

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: 49.76  E-value: 6.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  702 INMVVRRRKSL--GGKV------VTPLHINLSGHKDSGISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDN 771
Cdd:COG0265   159 INLAKRVVEQLieTGRVrrgwlgVTIQPVTPELAEALGLPEPEGVLVARVEPGSPAAKAG-LRPGDVILAVDGKPVTS 235
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1320-1392 6.95e-06

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: 45.76  E-value: 6.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460 1320 VKLQKGSEPLGISIVSGEKGG--VYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1392
Cdd:cd06683     6 VELKRYGGPLGITISGTEEPFdpIVISGLTEGGLAERTGaIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTL 81
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1493-1549 7.07e-06

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: 49.76  E-value: 7.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460 1493 HGVFVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKV 1549
Cdd:COG0265   201 EGVLVARVEPGSPAaKA--GLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTV 256
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 620-711 7.15e-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: 46.23  E-value: 7.15e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  620 VVEFERETEdidlKALGFDMAEGVNEPCLpgDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd06694     4 IVTLKKDPQ----KGLGFTIVGGENSGSL--DLGIFVKSIIPGGPAdkDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQN 77

                          90
                  ....*....|....
gi 741978460  698 GEGAINMVVRRRKS 711
Cdd:cd06694    78 APDKVELIISQPKS 91
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 717-783 8.01e-06

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: 45.72  E-value: 8.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  717 VTPLHINLSGHKDSGIslenGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 783
Cdd:cd06755    11 ESPLHFSLLGGSEKGF----GIFVSKVEKGSKAAEAG-LKRGDQILEVNGQNFENITLKKALEILRN 72
PDZ_2 pfam13180
PDZ domain;
732-793 8.04e-06

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 45.34  E-value: 8.04e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460   732 ISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALdnKSLNECESLLRSC--QDSLTLSLL 793
Cdd:pfam13180    2 VDLEGGVVVVSVKSSGPAAKAG-LKAGDVILSIDGRKI--NDLTDLESALYGHkpGDTVTLQVY 62
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
 1330-1385 8.38e-06

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: 45.33  E-value: 8.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1330 GISIVSGEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNG--------INLRSATEQQARLIIGQ 1385
Cdd:cd06736    12 QITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGcirgerqsVSLEDCTKEEAHWTLQR 75
PDZ1_L-delphilin-like cd06743
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1327-1390 9.57e-06

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: 45.35  E-value: 9.57e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460 1327 EPLGISIvsGEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRS-ATEQQARLiiGQQCDTI 1390
Cdd:cd06743     9 EAFGFSI--GGSGPCYILSVEEGSSAHAAGLQPGDQILELDGQDVSSlSCEAIIAL--ARRCPSV 69
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 620-706 9.72e-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: 9.72e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  620 VVEFERETEDidlkALGFDMAEGVNEPClpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd06675     2 TVEIKRGPQD----SLGISIAGGVGSPL--GDVPVFIAMIQPNGVAaqTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKN 75


                  ....*....
gi 741978460  698 GEGAINMVV 706
Cdd:cd06675    76 ASGTIILQV 84
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 720-783 9.84e-06

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: 45.81  E-value: 9.84e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  720 LHINLSGHKDSGISlENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 783
Cdd:cd06758    14 LGIQITGGKGSKRG-DIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAILRS 76
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 1320-1383 9.96e-06

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: 45.75  E-value: 9.96e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1320 VKLQKGSEPLGISIVSGEK-----GGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd06690     6 VELERGPKGLGLGLIDGLHtplrsPGIYIRTLVPDSPAARDGrLRLGDRILAVNGTSLVGADYQSAMDLI 75
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 710-793 1.10e-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: 45.48  E-value: 1.10e-05
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  710 KSLGGKVVTPLHinlsghkdsgislengvYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLT 789
Cdd:cd23070    27 RSINGELYAPLQ-----------------HVSAVLEGGAADKAG-VRKGDRILEVNGVNVEGATHKQVVDLIKSGGDELT 88


                  ....
gi 741978460  790 LSLL 793
Cdd:cd23070    89 LTVI 92
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 731-790 1.23e-05

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


Pssm-ID: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 45.01  E-value: 1.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  731 GISLE----NGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06767    16 GISIVsgenGGIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQCGDTITM 78
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 722-793 1.27e-05

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: 45.00  E-value: 1.27e-05
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  722 INLSGHKDSGISLEN------GVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQdSLTLSLL 793
Cdd:cd06738     7 ISLVGTRGLGCSISSgptqkpGIFISNVKPGSLAEEVG-LEVGDQIVEVNGTSFTNVDHKEAVMALKSSR-HLTITVR 82
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 1316-1379 1.27e-05

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: 45.68  E-value: 1.27e-05
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gi 741978460 1316 EPRHVKLQKGSEPLGISIV-------SGEKGGVYVSKVTGGsIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06669     7 EVTVIELEKGDRGLGFSILdyqdpldPSETVIVIRSLVPGG-VAEQDGrLLPGDRLVFVNDVSLENASLDEA 77
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
231-501 1.33e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 1.33e-05
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gi 741978460  231 SRLLSDQTQLKDDVDMLRREngqllrernlLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKL 310
Cdd:COG4372    34 RKALFELDKLQEELEQLREE----------LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  311 EVVKKDYDALRKRYSEkvaiHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAI-QLQHQCALSLRRFEAIHHELNKATAQ 389
Cdd:COG4372   104 ESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELkELEEQLESLQEELAALEQELQALSEA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  390 NKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKA 469
Cdd:COG4372   180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259

                         250       260       270
                  ....*....|....*....|....*....|..
gi 741978460  470 ASEEMEALRQIKDTVTMDAGRANKEAEILRKQ 501
Cdd:COG4372   260 IEELELAILVEKDTEEEELEIAALELEALEEA 291
PDZ5_INAD-like cd23066
PDZ domain 5 of inactivation no after potential D (INAD), and related domains; PDZ (PSD-95 ...
 728-794 1.39e-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: 44.80  E-value: 1.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460  728 KDSGISL----ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 794
Cdd:cd23066    10 KELGLSLspneGIGCTIADLLPGGYAEIDGKLQKGDIITKFNGDALSGLPFQVCYALFKGANGKISLEVTR 80
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 140-590 1.42e-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: 50.21  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   140 RQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTTFDKRpyhrlnpDYERLKIQCVRAMSDLQSLQS------------ 207
Cdd:pfam10174  250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKN-------KIDQLKQELSKKESELLALQTkletltnqnsdc 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   208 -QHTNALK----------------------RCEE----VAKETDFYHTLHSRLLSDQTQLKDDVDMLRrengqlLRER-- 258
Cdd:pfam10174  323 kQHIEVLKesltakeqraailqtevdalrlRLEEkesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLD------VKERki 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   259 NLLQQSWEDMKRLHEEDQKEIGDLRaQQQQVLKHNGSSEilnklyDTAMDKLEVVKKDYDALRKRYSEKVAIHNSD-LSR 337
Cdd:pfam10174  397 NVLQKKIENLQEQLRDKDKQLAGLK-ERVKSLQTDSSNT------DTALTTLEEALSEKERIIERLKEQREREDRErLEE 469

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   338 LEQMEEENQRLLKQTEML----TQQRDTAIQLQHQcALSLRRfeaihhELNKATAQNKDLQWEMELLQSELTELRTtQAK 413
Cdd:pfam10174  470 LESLKKENKDLKEKVSALqpelTEKESSLIDLKEH-ASSLAS------SGLKKDSKLKSLEIAVEQKKEECSKLEN-QLK 541

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   414 TAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVE-----LAESKLKSSTSEKKAASEEMEALRQIKDTVTMDA 488
Cdd:pfam10174  542 KAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVErllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVA 621

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   489 -------GRANKEAEIL-----------RKQCKALCQELKEAL----QEADVAKCRrdwaFQERDKIVAERDSIRTlcdN 546
Cdd:pfam10174  622 nikhgqqEMKKKGAQLLeearrrednlaDNSQQLQLEELMGALektrQELDATKAR----LSSTQQSLAEKDGHLT---N 694

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   547 LRRERDRAVSELAE-----------------ALRSLDDTRKQKND-----VSRE----LKELKEQMESQL 590
Cdd:pfam10174  695 LRAERRKQLEEILEmkqeallaaisekdaniALLELSSSKKKKTQeevmaLKREkdrlVHQLKQQTQNRM 764
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 1483-1550 1.68e-05

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: 44.78  E-value: 1.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460 1483 LGVHLCGGNLHGVFVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVRSKTVEEVyVEMLK-PKDS-VRLKVQ 1550
Cdd:cd06782     4 IGIEIGKDDDGYLVVVSPIPGGPAeKA--GIKPGDVIVAVDGESVRGMSLDEV-VKLLRgPKGTkVKLTIR 71
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 1320-1379 1.69e-05

PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZRN4-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467199 [Multi-domain]  Cd Length: 92  Bit Score: 45.08  E-value: 1.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460 1320 VKLQKGSEPLGISIVSG------EKG----GVYVSKVT-GGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06715     5 VVLHRENGSLGFNIIGGrpcennQEGssseGIYVSKIVeNGPAADEGGLQVHDRIIEVNGKDLSKATHEEA 75
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
437-597 1.73e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  437 SERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEalrqikdtvtmdagRANKEAEILRKQCKALCQELKEALQEA 516
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE--------------QARSELEQLEEELEELNEQLQAAQAEL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  517 DVAKcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARF 596
Cdd:COG4372    97 AQAQ-------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169


                  .
gi 741978460  597 R 597
Cdd:COG4372   170 E 170
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 726-790 2.02e-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: 44.79  E-value: 2.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460  726 GHKDSGiSLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd23072    21 GGEKSG-RLDLGIFISSITPGGPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTL 84
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1319-1392 2.22e-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: 44.93  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1319 HVKLQKG-SEPLGISIV---SGEKG--GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSA-TEQQARLIIGQQCDTI 1390
Cdd:cd06689    17 YIELEKPeSGGLGFSVVglkSENRGelGIFVQEIQPGSVAARDGrLKENDQILAINGQPLDQSiSHQQAIAILQQAKGSV 96


                  ..
gi 741978460 1391 TI 1392
Cdd:cd06689    97 EL 98
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 1494-1549 2.34e-05

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: 44.78  E-value: 2.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460 1494 GVFVAEVEDDSPARgPDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKV 1549
Cdd:cd10839    26 GALVAQVLPDSPAA-KAGLKAGDVILSLNGKPITSSADLRNRVATTKPGTKVELKI 80
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1473-1540 2.35e-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: 44.19  E-value: 2.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1473 VVFIKKSQLELGVHLCGgnlHG-VFVAEVEDDSPARGPdGLVPGDLILEYGGLDVRSKTVEEVyVEMLK 1540
Cdd:cd06744     1 TVRVYRGNGSFGFTLRG---HApVYIESVDPGSAAERA-GLKPGDRILFLNGLDVRNCSHDKV-VSLLQ 64
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 706-794 2.35e-05

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


Pssm-ID: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 44.53  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  706 VRRRKSLGgkvvtplhINLSGHKDSGISLE-NGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 784
Cdd:cd06791     8 VKDEQGLG--------ITIAGYVGEKASGElSGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEAVEVLRNT 79

                          90
                  ....*....|
gi 741978460  785 QDSLTLSLLK 794
Cdd:cd06791    80 GQVVHLTLAR 89
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 1328-1379 2.38e-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: 44.66  E-value: 2.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460 1328 PLGISIVS----GEKGGVYVSKVT-GGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06717    11 FLGISIVGqsneRGDGGIYVGSIMkGGAVAADGRIEPGDMILQVNDISFENMSNDDA 67
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 1318-1392 2.40e-05

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: 44.47  E-value: 2.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460 1318 RHVKLQKGS-EPLGISIVSGEKGGVYVSKVT-GGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1392
Cdd:cd10830     1 RLVQFEKNTeEPMGITLKLNEKQSCIVARILhGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVSL 77
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 189-407 2.47e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.06  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  189 ERLKIQCVRAMSDLQSLQSQHTNALKrcEEVAKETD-FYHTL------HSRLLSDQTQLKDDVDMLRRENGQLLRERNLL 261
Cdd:PRK04778  259 QDLKEQIDENLALLEELDLDEAEEKN--EEIQERIDqLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEIDRV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  262 QQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------ALRK 322
Cdd:PRK04778  337 KQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGLRK 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  323 rySEKVAIHNsdLSRLEQMEEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATAQN 390
Cdd:PRK04778  412 --DELEAREK--LERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATEDV 485

                         250
                  ....*....|....*....
gi 741978460  391 KDLQWEMELL--QSELTEL 407
Cdd:PRK04778  486 ETLEEETEELveNATLTEQ 504
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 183-485 2.57e-05

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: 49.25  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   183 RLNPDYERLKIQCVRAMSDLQSLQSQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQL-------L 255
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeqikklQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   256 RERNLLQQSWEDMKRLHEEDQKEIGDLRAQ----QQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIH 331
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   332 NSDLSRLEQMEEENQRLLKQTEMLTQ----------QRDTAI-----------------QLQHQCALSLRRFEAIHHELN 384
Cdd:TIGR04523  499 KKLNEEKKELEEKVKDLTKKISSLKEkieklesekkEKESKIsdledelnkddfelkkeNLEKEIDEKNKEIEELKQTQK 578

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   385 KATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKsST 464
Cdd:TIGR04523  579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK-EI 657

                          330       340
                   ....*....|....*....|.
gi 741978460   465 SEKKAaseemEALRQIKDTVT 485
Cdd:TIGR04523  658 RNKWP-----EIIKKIKESKT 673
PRK01156 PRK01156
chromosome segregation protein; Provisional
 183-601 2.61e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 49.51  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  183 RLNPDYERLK--IQCVRA-MSDLQSLQSQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERN 259
Cdd:PRK01156  163 SLERNYDKLKdvIDMLRAeISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  260 LLQqSWEDMKRLHEEDQKEI-GDLRAQQQQVLKHNGSSEILNKL------------------------------------ 302
Cdd:PRK01156  243 ELS-SLEDMKNRYESEIKTAeSDLSMELEKNNYYKELEERHMKIindpvyknrnyindyfkykndienkkqilsnidaei 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  303 --YDTAMDKLEVVKKDYDALRKRYSEKVAIhNSDLSRLEQMEEENQRLLKQTEMLTQQRD----TAIQLQHQCALSLRRF 376
Cdd:PRK01156  322 nkYHAIIKKLSVLQKDYNDYIKKKSRYDDL-NNQILELEGYEMDYNSYLKSIESLKKKIEeyskNIERMSAFISEILKIQ 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  377 EAIHHELNKATAQ-NKD----------LQWEMELLQSELTELRTTQA-----------KTAKESEKYKEERDAvYSEykl 434
Cdd:PRK01156  401 EIDPDAIKKELNEiNVKlqdisskvssLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINH-YNE--- 476

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  435 imsERDQVISELDKLQTEVELAESKLKSSTS-EKKAASEEMEAL----RQIKDTVTMDAGRANKEAEILRKQCKAlcQEL 509
Cdd:PRK01156  477 ---KKSRLEEKIREIEIEVKDIDEKIVDLKKrKEYLESEEINKSineyNKIESARADLEDIKIKINELKDKHDKY--EEI 551

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  510 KE---ALQEADVAKCRRDWafqerDKIVAERDSIRTlcDNLRRERDRAVSELAEA---------------------LRSL 565
Cdd:PRK01156  552 KNrykSLKLEDLDSKRTSW-----LNALAVISLIDI--ETNRSRSNEIKKQLNDLesrlqeieigfpddksyidksIREI 624

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 741978460  566 DDTRKQKNDVSRELKELKEQMESQLEKEARFRHLMA 601
Cdd:PRK01156  625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 741-790 2.62e-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: 2.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 741978460   741 AAVVPGSPAAKEGsLAVGDRIVAINGIALdnKSLNECESLLRSCQDSLTL 790
Cdd:pfam17820    3 TAVVPGSPAERAG-LRVGDVILAVNGKPV--RSLEDVARLLQGSAGESVT 49
PDZ7_GRIP1-2-like cd06685
PDZ domain 7 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1319-1395 2.64e-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: 44.17  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1319 HVKLQK--GSEPLGISIVSG--EKGgVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1394
Cdd:cd06685     5 KVTLYKdsDTEDFGFSVSDGlyEKG-VYVNAIRPGGPADLSGLQPYDRILQVNHVRTRDFDCCLVVPLIAESGDKLELVV 83


                  .
gi 741978460 1395 Q 1395
Cdd:cd06685    84 S 84
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 339-595 2.70e-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: 48.61  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  339 EQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKES 418
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  419 EKYKEE-RDAVYSEYKLIMSERDQVISEldklQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVtmdagrANKEAEI 497
Cdd:COG4942   100 EAQKEElAELLRALYRLGRQPPLALLLS----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL------AALRAEL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  498 LRKQckalcQELKEALQEADvakcrrdwafQERDKIVAERDsirtlcdnlrrERDRAVSELAEALRSLDDTRKQKNDVSR 577
Cdd:COG4942   170 EAER-----AELEALLAELE----------EERAALEALKA-----------ERQKLLARLEKELAELAAELAELQQEAE 223

                         250
                  ....*....|....*...
gi 741978460  578 ELKELKEQMESQLEKEAR 595
Cdd:COG4942   224 ELEALIARLEAEAAAAAE 241
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 731-783 2.87e-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: 2.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  731 GISL-------ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 783
Cdd:cd06684    16 GITLststhrnKQVIVIDSIKPASIADRCGALHVGDHILSIDGTSVEHCSLAEATQLLAS 75
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 ...
 718-773 2.87e-05

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: 44.21  E-value: 2.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  718 TPLHINLSGHKD-SGISlengVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKS 773
Cdd:cd06672    11 SGLGLSLAGNKDrSRMS----VFVVGIDPDGAAGKDGRIQVGDELLEINGQVLYGRS 63
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 735-790 2.98e-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: 44.19  E-value: 2.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  735 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIalDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06716    30 DTGIYVSEVDPNSIAAKDGRIREGDQILQINGV--DVQNREEAIALLSEEEKSITL 83
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 1493-1550 3.05e-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: 44.21  E-value: 3.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1493 HGVFVAEVEDDSPARGPdGLVPGDLILEYGGLDVRSKT-VEEVYVEMlKPKDSVRLKVQ 1550
Cdd:cd06779    25 RGVLVAEVIPGSPAAKA-GLKEGDVILSVNGKPVTSFNdLRAALDTK-KPGDSLNLTIL 81
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
158-518 3.20e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  158 RERNELRKRLAFATHgTTFD-KRPYH-RLnpdYERLKIQCVRAMSDL---QSLQS---------QH----TNALKRCEEV 219
Cdd:COG4913   155 FDIRALKARLKKQGV-EFFDsFSAYLaRL---RRRLGIGSEKALRLLhktQSFKPigdlddfvrEYmleePDTFEAADAL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  220 AKETDFYHTLHSRLLSDQTQlkddVDMLR--RENGQLLRERNLLQQSWEDMKRL--HEEDQKEIGDLRAQQQQvlkhngs 295
Cdd:COG4913   231 VEHFDDLERAHEALEDAREQ----IELLEpiRELAERYAAARERLAELEYLRAAlrLWFAQRRLELLEAELEE------- 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  296 seiLNKLYDTAMDKLEVVKKDYDALRKRYSE-KVAIHNSDLSRLEQMEEENQRLLKQtemLTQQRDTAIQLQHQCAlslr 374
Cdd:COG4913   300 ---LRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERE---LEERERRRARLEALLA---- 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  375 rfeaihhelnkataqnkDLQWEMELLQSELTELRTtQAKTAKESEKykeerdavyseyklimserdqviSELDKLQTEVE 454
Cdd:COG4913   370 -----------------ALGLPLPASAEEFAALRA-EAAALLEALE-----------------------EELEALEEALA 408

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  455 LAESKLKSSTSEKKAASEEMEALRQIKDTVTmdagranKEAEILRkqcKALCQELKEAlqEADV 518
Cdd:COG4913   409 EAEAALRDLRRELRELEAEIASLERRKSNIP-------ARLLALR---DALAEALGLD--EAEL 460
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 217-500 3.25e-05

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: 48.97  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   217 EEVAKETDFYHTLHSRLLSDQTQLkDDVDMLRRENGQLLRERNllqqswEDMKRLHEEDQKEIGDlRAQQQQVLKHNGSS 296
Cdd:pfam17380  306 EEKAREVERRRKLEEAEKARQAEM-DRQAAIYAEQERMAMERE------RELERIRQEERKRELE-RIRQEEIAMEISRM 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   297 EILNKLYDTAMDKLEVVKKDYDALRKrysekvaihnsdlsrLEQMEEENQRLLKQT----EMLTQQRDTAIQLQhqcals 372
Cdd:pfam17380  378 RELERLQMERQQKNERVRQELEAARK---------------VKILEEERQRKIQQQkvemEQIRAEQEEARQRE------ 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   373 LRRFEAIH-HELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKE---------ERDAVYSEYKLIMSERDQV 442
Cdd:pfam17380  437 VRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkilEKELEERKQAMIEEERKRK 516

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460   443 ISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKD---TVTMDAGRAN---KEAEILRK 500
Cdd:pfam17380  517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEqmrKATEERSRLEameREREMMRQ 580
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 345-626 3.31e-05

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: 48.97  E-value: 3.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   345 NQRLLKQTEMLTQQRDTaiqLQHQCALSLR----RFEAIHHElnkataqnkDLQWEMELLQSELTELRT-TQAKTAKESE 419
Cdd:pfam17380  261 NGQTMTENEFLNQLLHI---VQHQKAVSERqqqeKFEKMEQE---------RLRQEKEEKAREVERRRKlEEAEKARQAE 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   420 KykEERDAVYSEYKLIMSERDQvisELDKLQTEvelaESKLKSSTSEKKAASEEMEALRQIkDTVTMDAGRAN----KEA 495
Cdd:pfam17380  329 M--DRQAAIYAEQERMAMERER---ELERIRQE----ERKRELERIRQEEIAMEISRMREL-ERLQMERQQKNervrQEL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   496 EILRKQcKALCQELKEALQEADVakcrrdwafqERDKIVAERDSIRTlcDNLRRERDRAVSELaEALRSLDDTRKQKNDV 575
Cdd:pfam17380  399 EAARKV-KILEEERQRKIQQQKV----------EMEQIRAEQEEARQ--REVRRLEEERAREM-ERVRLEEQERQQQVER 464

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 741978460   576 SRELKELKEQMESQLEKEARFRHLmAHSSHDSAIDTDSMEWETEVVEFERE 626
Cdd:pfam17380  465 LRQQEEERKRKKLELEKEKRDRKR-AEEQRRKILEKELEERKQAMIEEERK 514
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 635-706 3.31e-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: 3.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  635 LGFDMAEGvnepclPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 706
Cdd:cd23060    12 LGFSLVGG------EGGSGIFVKSISPGGVAdrDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 727-793 3.47e-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: 44.21  E-value: 3.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460  727 HKDSGISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKslNECESLLRSCQ--DSLTLSLL 793
Cdd:cd06779    16 AKELGLPVNRGVLVAEVIPGSPAAKAG-LKEGDVILSVNGKPVTSF--NDLRAALDTKKpgDSLNLTIL 81
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
326-614 3.59e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  326 EKVAIHNsdlSRLEQMEEENQRLLKQTEMLTQQRDTAiqlqhqcalslRRFEAIhhelnkatAQNKDLqwemellqseLT 405
Cdd:PRK02224  475 ERVEELE---AELEDLEEEVEEVEERLERAEDLVEAE-----------DRIERL--------EERRED----------LE 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  406 ELRTTQAKTAKESEKYKEERDAVYSEYKlimSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIkdtVT 485
Cdd:PRK02224  523 ELIAERRETIEEKRERAEELRERAAELE---AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERI---RT 596

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  486 MDAGRANKEAEILRKqckalcQELKEALQEadvakcRRDwafQERDKIVAERDSIRTLCDNL--------RRERDRAVSE 557
Cdd:PRK02224  597 LLAAIADAEDEIERL------REKREALAE------LND---ERRERLAEKRERKRELEAEFdearieeaREDKERAEEY 661

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  558 LAEALRSLDDTRKQKND-------VSRELKELKEQMESQLEKEARFRHLmaHSSHDSAIDTDSM 614
Cdd:PRK02224  662 LEQVEEKLDELREERDDlqaeigaVENELEELEELRERREALENRVEAL--EALYDEAEELESM 723
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 1318-1382 3.64e-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: 3.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460 1318 RHVKLQKGSEPLGISIvSGEKGGVyVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSAT-EQQARLI 1382
Cdd:cd06710     1 RTVEIARGRAGYGFTI-SGQAPCV-LSCVVRGSPADVAGLKAGDQILAVNGINVSKAShEDVVKLI 64
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 737-784 3.64e-05

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: 44.08  E-value: 3.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 741978460  737 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE-CESLLRSC 784
Cdd:cd06714    39 GAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEvQDIISQSK 87
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1342-1393 3.82e-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: 3.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1342 YVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII--GQQCDTITIL 1393
Cdd:cd23070    39 HVSAVLEGGAADKAGVRKGDRILEVNGVNVEGATHKQVVDLIksGGDELTLTVI 92
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 719-786 3.93e-05

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: 43.77  E-value: 3.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  719 PLHINLSGHKDsgislENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQD 786
Cdd:cd06678    12 QLGIKLVRKKD-----EPGVFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQASGE 74
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 635-707 4.05e-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: 4.05e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460   635 LGFDMAEGVNEpclpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 707
Cdd:pfam00595   12 LGFSLKGGSDQ----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 629-708 4.12e-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: 44.17  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  629 DIDLK----ALGFDMAEGVNEpcLPGDCGIFVTKV-DKG-SIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGE--G 700
Cdd:cd23058     7 HIQLKkgpeGLGFSITSRDNP--TGGSGPIYIKNIlPKGaAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKlgG 84


                  ....*...
gi 741978460  701 AINMVVRR 708
Cdd:cd23058    85 TVSLVVSR 92
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 735-790 4.21e-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: 4.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  735 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALD-NKSLNECESLLRSCQDSLTL 790
Cdd:cd06689    42 ELGIFVQEIQPGSVAARDGRLKENDQILAINGQPLDqSISHQQAIAILQQAKGSVEL 98
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 1318-1378 4.75e-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: 43.20  E-value: 4.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460 1318 RHVKLQKGSEPLGISiVSGEKG--GVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQ 1378
Cdd:cd06768     1 RLCHLVKGPEGYGFN-LHAEKGrpGHFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQ 62
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 401-595 4.77e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  401 QSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEAL--- 477
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERara 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  478 --RQIKDTVTMDA-----------GRANKEAEILRKQcKALCQELKEALQEADvakcrrdwafQERDKIVAERDSIRTLC 544
Cdd:COG3883    95 lyRSGGSVSYLDVllgsesfsdflDRLSALSKIADAD-ADLLEELKADKAELE----------AKKAELEAKLAELEALK 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 741978460  545 DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEAR 595
Cdd:COG3883   164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 653-708 4.97e-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: 43.58  E-value: 4.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  653 GIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKaLLNGEGAINMVVRR 708
Cdd:cd10833    27 GIFVSKVEEGSAAErAGLCVGDKITEVNGVSLENITMSSAVK-VLTGSNRLRMVVRR 82
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 635-708 5.10e-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: 43.87  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  635 LGFDMAEGVNE-----PCLPGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 708
Cdd:cd10822    15 LGFSIGGGIDQdpsknPFSYTDKGIYVTRVSEGGPAEkAGLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKPVLRMLVTR 94
Filament pfam00038
Intermediate filament protein;
388-591 5.86e-05

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 47.22  E-value: 5.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   388 AQNKDLQWEMELLQseltelRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEK 467
Cdd:pfam00038   25 QQNKLLETKISELR------QKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   468 KAASEEMEALRQIKDTVTM----------------DAGRANKEAEI--LRKQCK----------ALCQELKEALQ----- 514
Cdd:pfam00038   99 TSAENDLVGLRKDLDEATLarvdleakieslkeelAFLKKNHEEEVreLQAQVSdtqvnvemdaARKLDLTSALAeiraq 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   515 -EADVAKCRRD---WaFQER-----------------------------DKIVAERDSIRTLCDNLrrerDRAVSELAEA 561
Cdd:pfam00038  179 yEEIAAKNREEaeeW-YQSKleelqqaaarngdalrsakeeitelrrtiQSLEIELQSLKKQKASL----ERQLAETEER 253

                          250       260       270
                   ....*....|....*....|....*....|.
gi 741978460   562 L-RSLDDTRKQKNDVSRELKELKEQMESQLE 591
Cdd:pfam00038  254 YeLQLADYQELISELEAELQETRQEMARQLR 284
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1494-1550 5.88e-05

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: 43.70  E-value: 5.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460 1494 GVFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKVQ 1550
Cdd:cd06714    39 GAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEVQDIISQSKGEVELVVS 95
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 309-587 5.98e-05

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: 48.30  E-value: 5.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   309 KLEVVKKDYDALR---KRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEmLTQQRDTAiqlQHQcALSLRRFEAIHHELNK 385
Cdd:pfam12128  605 RLDKAEEALQSARekqAAAEEQLVQANGELEKASREETFARTALKNAR-LDLRRLFD---EKQ-SEKDKKNKALAERKDS 679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   386 ATAQNKDLQWEMELLQSELtelrttQAKTAKESEKYKEERDAVYSEYKLIMSERDqviSELDKLQTEVELAESKLKSsts 465
Cdd:pfam12128  680 ANERLNSLEAQLKQLDKKH------QAWLEEQKEQKREARTEKQAYWQVVEGALD---AQLALLKAAIAARRSGAKA--- 747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   466 EKKAASEEMEalRQIKdTVTMDAGRANKeaeiLRKQCKALCQELKEALQEADVAKCRRDWA----FQERDKIVAE----R 537
Cdd:pfam12128  748 ELKALETWYK--RDLA-SLGVDPDVIAK----LKREIRTLERKIERIAVRRQEVLRYFDWYqetwLQRRPRLATQlsniE 820

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 741978460   538 DSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQME 587
Cdd:pfam12128  821 RAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
416-631 6.07e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 6.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  416 KESEKYKEErdaVYSEYKLIMSERDQVISELDKLQTEV--------ELAESKLKSSTSEKKAASEEmEALRQIKDtvtmd 487
Cdd:PRK03918  196 KEKEKELEE---VLREINEISSELPELREELEKLEKEVkeleelkeEIEELEKELESLEGSKRKLE-EKIRELEE----- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  488 aGRANKEAEI--LRKQCKALcQELKEALQEADVAKcrrdwafQERDKIVAERDSIRTLCDNLRRER---DRAVSELAEAL 562
Cdd:PRK03918  267 -RIEELKKEIeeLEEKVKEL-KELKEKAEEYIKLS-------EFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKE 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460  563 RSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRHLMAHSSHDSAIDTDSMEWETEVVEFERE--TEDID 631
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEeiEEEIS 408
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 620-707 6.10e-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: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  620 VVEFERETEdidlkALGFDMAEGVNEpclpgDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd06796     4 VVELPKTEE-----GLGFNVMGGKEQ-----NSPIYISRIIPGGVADrhGGLKRGDQLLSVNGVSVEGEHHEKAVELLKA 73

                          90
                  ....*....|
gi 741978460  698 GEGAINMVVR 707
Cdd:cd06796    74 AQGSVKLVVR 83
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 ...
 1320-1383 6.21e-05

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: 43.05  E-value: 6.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1320 VKLQKGSEPLGISIvSGEKGG----VYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd06672     4 IELEKGSSGLGLSL-AGNKDRsrmsVFVVGIDPDGAAGKDGrIQVGDELLEINGQVLYGRSHLNASAII 71
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 722-793 6.51e-05

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: 42.94  E-value: 6.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460  722 INLSGHKDSGIslengvYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:cd06729    15 LRLAGGNDVGI------FVAGVQEGSPAEKQG-LQEGDQILKVNGVDFRNLTREEAVLFLLDLPKGEEVTIL 79
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 337-460 6.51e-05

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: 44.14  E-value: 6.51e-05
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gi 741978460   337 RLEQMEEENQRLLKQtemLTQQRDTAIQLQHqcalslrrfeaihhELNKATAQNKDLQWEMELLQSELTELRTTQAKTAK 416
Cdd:pfam20492   14 RLKQYEEETKKAQEE---LEESEETAEELEE--------------ERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAE 76

                           90       100       110       120
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gi 741978460   417 ESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKL 460
Cdd:pfam20492   77 EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 743-794 6.83e-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: 6.83e-05
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gi 741978460  743 VVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 794
Cdd:cd23068    32 VNPGSPADKAG-LRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 724-790 6.84e-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: 42.65  E-value: 6.84e-05
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gi 741978460  724 LSGHkdsgisleNGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06744    15 LRGH--------APVYIESVDPGSAAERAG-LKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMPTL 72
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 1320-1382 6.85e-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: 42.76  E-value: 6.85e-05
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gi 741978460 1320 VKLQKGSEPLGISIVSGEKggVYVSKVTGGSIAHQAGLEYGDQLLEFNGINL-RSATEQQARLI 1382
Cdd:cd06711     3 ITIQRGKDGFGFTICDDSP--VRVQAVDPGGPAEQAGLQQGDTVLQINGQPVeRSKCVELAHAI 64
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 654-708 7.10e-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: 7.10e-05
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gi 741978460  654 IFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 708
Cdd:cd23068    27 LSIQKVNPGSPADKAgLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1568-1626 7.35e-05

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: 42.06  E-value: 7.35e-05
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gi 741978460 1568 YIRALYERLAEVEPELSFKKDDILYVDDTLPQGsfgsWMAWQLDENaqkmQRGQIPSKY 1626
Cdd:cd00174     1 YARALYDYEAQDDDELSFKKGDIITVLEKDDDG----WWEGELNGG----REGLFPANY 51
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 1320-1379 7.51e-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: 43.27  E-value: 7.51e-05
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gi 741978460 1320 VKLQKG-SEPLGISIVSGEKGGVYVSKVTG--------GSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd23063     2 VVIEKTeKKSFGICIVRGEVKVSPNTKTTGifikgiipDSPAHKCGrLKVGDRILSVNGNDVRNSTEQAA 71
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 1320-1379 7.59e-05

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: 43.05  E-value: 7.59e-05
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gi 741978460 1320 VKLQKGSEPLGISIVSG-------EKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06709     3 ITLKRGPSGLGFNIVGGtdqpyipNDSGIYVAKIKEDGAAAIDGrLQEGDKILEINGQSLENLTHQDA 70
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 738-797 8.24e-05

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


Pssm-ID: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 42.62  E-value: 8.24e-05
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gi 741978460  738 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 797
Cdd:cd06799    25 IVVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQGPIT---FKLIP 81
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1483-1551 8.52e-05

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: 43.02  E-value: 8.52e-05
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gi 741978460 1483 LGVHLCGGNLH--GVFVAEVEDDSPArGPDGLVPGDLILEYGGLDVRSKTVEEVyVEMLKPKDSVRLKVQY 1551
Cdd:cd06737    15 LGFSVRGGLEHgcGLFVSHVSPGSQA-DNKGLRVGDEIVRINGYSISQCTHEEV-INLIKTKKTVSLKVRH 83
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 650-695 8.57e-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: 8.57e-05
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gi 741978460  650 GDCGIFVTKVDKGSI--ADGRLRVNDWLLRINDVDLINKDKKQAIKAL 695
Cdd:cd06717    24 GDGGIYVGSIMKGGAvaADGRIEPGDMILQVNDISFENMSNDDAVRVL 71
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 719-792 8.94e-05

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: 42.57  E-value: 8.94e-05
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gi 741978460  719 PLHINLS-GHKDSGISLENG--VYAAAVVPGSPAAKEGsLAVGDRIVAINGiaLDNK--SLNECESLLRSC-QDSLTLSL 792
Cdd:cd06712     1 PRTVHLTkEEGGFGFTLRGDspVQVASVDPGSCAAEAG-LKEGDYIVSVGG--VDCKwsKHSEVVKLLKSAgEEGLELQV 77
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 737-769 9.24e-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: 9.24e-05
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gi 741978460  737 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIAL 769
Cdd:cd06789    31 GIYIKSVVKGGAADLDGRLQAGDQLLSVDGHSL 63
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1472-1553 1.20e-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: 42.30  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1472 RVVFIKKSQLE-LGVHLCGGNLH--GVFVAEVEDDSPARGPdGLVPGDLILEYGGLDVRSKTVEEVyVEMLKPKDSVRLK 1548
Cdd:cd06752     1 RTVVLKRPPGEqLGFNIRGGKASglGIFISKVIPDSDAHRL-GLKEGDQILSVNGVDFEDIEHSEA-VKVLKTAREIQMR 78


                  ....*
gi 741978460 1549 VQYRP 1553
Cdd:cd06752    79 VRYFP 83
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 717-784 1.24e-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: 42.35  E-value: 1.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  717 VTPLHINLSGHKDSGisLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 784
Cdd:cd06717     9 VNFLGISIVGQSNER--GDGGIYVGSIMKGGAVAADGRIEPGDMILQVNDISFENMSNDDAVRVLREA 74
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 617-706 1.38e-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: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  617 ETEVVEFERETEdidlkALGFDMAEGvnepclpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKAL 695
Cdd:cd06767     2 EPRHVSIEKGSE-----PLGISIVSG-------ENGGIFVSSVTEGSLAHqAGLEYGDQLLEVNGINLRNATEQQAALIL 69

                          90
                  ....*....|.
gi 741978460  696 LNGEGAINMVV 706
Cdd:cd06767    70 RQCGDTITMLV 80
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
 1318-1381 1.40e-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: 41.83  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460 1318 RHVKLQK-GSEPLGIsIVSGEKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARL 1381
Cdd:cd10832     1 RMVGIRKnPGEPLGV-TVRLEEGELVIARILHGGMIDRQGlLHVGDIIKEVNGVPVGSPEQLQEML 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
 855-1317 1.42e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  855 RKELGPPGGSSSFLHKPFPGGPFSVSPqacpsASERSLSSFRSdASGERGYGPADMRSRRP-------LLPFEtevgPCG 927
Cdd:PHA03247 2457 RTILGAPFSLSLLLGELFPGAPVYRRP-----AEARFPFAAGA-APDPGGGGPPDPDAPPApsrlapaILPDE----PVG 2526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  928 AAEAP--------LDKAEPDSAhSGGTWPKAVLSSVAGPEKLSVYRKPKQRKSifDP---NTFKRPQTPPKIDY-LLPG- 994
Cdd:PHA03247 2527 EPVHPrmltwirgLEELASDDA-GDPPPPLPPAAPPAAPDRSVPPPRPAPRPS--EPavtSRARRPDAPPQSARpRAPVd 2603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  995 -SGPAHSPLPSKRVGPLTPPKPPRrgdsikfqhklETSSESEATLVGSSPSTSPPSALPPDVDPGdPMHASPPRKARVR- 1072
Cdd:PHA03247 2604 dRGDPRGPAPPSPLPPDTHAPDPP-----------PPSPSPAANEPDPHPPPTVPPPERPRDDPA-PGRVSRPRRARRLg 2671

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1073 --IASSYCPEGDRDSSYLPAKKSCdEDLTSQKEQKCTPASGelSPDLQEWAPYSPGHSSRHSNPPFYPsrasVGTVPRSL 1150
Cdd:PHA03247 2672 raAQASSPPQRPRRRAARPTVGSL-TSLADPPPPPPTPEPA--PHALVSATPLPPGPAAARQASPALP----AAPAPPAV 2744

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1151 APSTVSSVLRNPIYTVRSHRVGPCSSPPIPREAGPhglhpsvqhqgrlSLDLSPRACSDCSDMRASHGSNSLPSSARLAT 1230
Cdd:PHA03247 2745 PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP-------------PRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1231 GSSSNLQFKAERIKIPSTPryPRSVVGSdrgslSHSECSTPPQSPLSVEGL----SSCSQSQTSAATLPRIAVnPAAPGE 1306
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPP--PTSAQPT-----APPPPPGPPPPSLPLGGSvapgGDVRRRPPSRSPAAKPAA-PARPPV 2883

                         490
                  ....*....|.
gi 741978460 1307 RRKDRPYVEEP 1317
Cdd:PHA03247 2884 RRLARPAVSRS 2894
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 336-520 1.46e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  336 SRLEQMEEENQRLLKQTEMLTQQRDTAIQlqhqcalslrrfeaihhELNKATAQNKDLQWEMELLQSELTELRTTQAKTA 415
Cdd:COG3883    23 KELSELQAELEAAQAELDALQAELEELNE-----------------EYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  416 KESEK-----YKEERDAVYSE-----------------YKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEE 473
Cdd:COG3883    86 EELGEraralYRSGGSVSYLDvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 741978460  474 MEALRQikdtvTMDAGRANKEAEI--LRKQCKALCQELKEALQEADVAK 520
Cdd:COG3883   166 LEAAKA-----ELEAQQAEQEALLaqLSAEEAAAEAQLAELEAELAAAE 209
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 ...
 647-708 1.53e-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: 42.26  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  647 CLP---GDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN-GEGAINMVVRR 708
Cdd:cd06760    23 CLPlenDIPGIFIHHLSPGSVAhmDGRLRRGDQILEINGTSLRNVTLNEAYAILSQcKPGPVTLIISR 90
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 705-790 1.55e-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: 42.24  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  705 VVRRRKSLGgkvvtPLHINLSGHKDS-----GISlENGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECES 779
Cdd:cd06702     2 EIHLVKAGG-----PLGLSIVGGSDHsshpfGVD-EPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVS 74

                          90
                  ....*....|.
gi 741978460  780 LLRSCQDSLTL 790
Cdd:cd06702    75 ALLSPGQEIKL 85
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 247-645 1.66e-04

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: 46.74  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   247 LRRENGQLLRERNLLQQSWEDMKrLHEEDQKEIgdLRAQQQQVLKhngsseILNKLYDTAMDKleVVKKDYDALRKRYSE 326
Cdd:pfam10174  121 LQSEHERQAKELFLLRKTLEEME-LRIETQKQT--LGARDESIKK------LLEMLQSKGLPK--KSGEEDWERTRRIAE 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   327 KVAIHNSDLSRLEQMEEENQRL---------LKQTEMLTQQRDTAIQLQHQCALSLRRfeaihhelnkataQNKDLQWEM 397
Cdd:pfam10174  190 AEMQLGHLEVLLDQKEKENIHLreelhrrnqLQPDPAKTKALQTVIEMKDTKISSLER-------------NIRDLEDEV 256

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   398 ELLQSELTELRTTQAKTAKESEKYKeerdavySEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEAL 477
Cdd:pfam10174  257 QMLKTNGLLHTEDREEEIKQMEVYK-------SHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVL 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   478 rqiKDTVTMDAGRAN---------------KEAeILRKQCKALcQELKE--ALQEADVAKCRRDWAFQERdKIVAERDSI 540
Cdd:pfam10174  330 ---KESLTAKEQRAAilqtevdalrlrleeKES-FLNKKTKQL-QDLTEekSTLAGEIRDLKDMLDVKER-KINVLQKKI 403

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   541 RTLCDNLrRERDRAVSELAEALRSLD------DT-------------------RKQKN-----------DVSRELKELKE 584
Cdd:pfam10174  404 ENLQEQL-RDKDKQLAGLKERVKSLQtdssntDTalttleealsekeriierlKEQREredrerleeleSLKKENKDLKE 482

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460   585 QMESQ----LEKEARFRHLMAHSS--------HDSAIDTDSMEWETEVVEFEReTEDIDLKALGFDMAEGVNE 645
Cdd:pfam10174  483 KVSALqpelTEKESSLIDLKEHASslassglkKDSKLKSLEIAVEQKKEECSK-LENQLKKAHNAEEAVRTNP 554
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
741-776 1.72e-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: 1.72e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 741978460  741 AAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNE 776
Cdd:COG3975   499 TSVLWGSPAYKAG-LSAGDELLAIDGLRVTADNLDD 533
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1329-1387 1.73e-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: 41.88  E-value: 1.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1329 LGISIVSGEKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIgQQC 1387
Cdd:cd06667    12 LGFGIVGGKSTGVVVKTILPGGVADRDGrLRSGDHILQIGDTNLRGMGSEQVAQVL-RQC 70
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 745-792 1.82e-04

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: 42.25  E-value: 1.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 741978460  745 PGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 792
Cdd:cd06695    40 PGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSLLRGAPPEVTLLL 87
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 738-790 1.87e-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: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  738 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL----RSCQDSLTL 790
Cdd:cd06733    27 VSIGAIVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKVVDLMgnaaRNGQVNLTV 83
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 653-707 1.90e-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: 41.92  E-value: 1.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  653 GIFVTKVDKGSIAD--GrLRVNDWLLRINDVDLINKDKKQAIKALLnGEGAINMVVR 707
Cdd:cd06738    28 GIFISNVKPGSLAEevG-LEVGDQIVEVNGTSFTNVDHKEAVMALK-SSRHLTITVR 82
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 741-771 1.92e-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: 1.92e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 741978460  741 AAVVPGSPAAKEGsLAVGDRIVAINGIALDN 771
Cdd:COG0750   133 GEVVPGSPAAKAG-LQPGDRIVAINGQPVTS 162
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 1339-1376 1.97e-04

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: 42.10  E-value: 1.97e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 741978460 1339 GGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATE 1376
Cdd:cd06785    31 SGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSD 68
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 718-798 1.99e-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: 42.22  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  718 TPLHINLSGHKDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLsLLKVFP 797
Cdd:cd06691    15 GPLGIHVVPFSSSLSGRTLGLLIRGIEEGSRAERDGRFQENDCIVEINGVDLIDKSFEQAQDIFRQAMRSPEV-KLHVVP 93


                  .
gi 741978460  798 Q 798
Cdd:cd06691    94 A 94
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 737-792 1.99e-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: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  737 GVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQdSLTLSL 792
Cdd:cd06740    28 GIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKILRVSK-KLVLSV 81
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 736-793 2.02e-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: 2.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  736 NGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 793
Cdd:cd06798    21 DSVIISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFLLI 78
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 1493-1549 2.09e-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: 46.06  E-value: 2.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  1493 HGVFVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKV 1549
Cdd:TIGR02037  257 RGALVAQVLPGSPAeKA--GLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGI 312
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1329-1381 2.09e-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: 45.14  E-value: 2.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1329 LGISIVS-----------GEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1381
Cdd:COG0265   180 LGVTIQPvtpelaealglPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSARDLQRLL 243
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 745-790 2.35e-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: 2.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 741978460  745 PGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06801    34 KGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTL 79
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
469-601 2.37e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  469 AASEEMEALRQIKDTVTmdagRANKEAEILRkQCKALCQELKEALQEADVAKCRRDW-----AFQERDKIVAERDSIRTL 543
Cdd:COG4913   229 ALVEHFDDLERAHEALE----DAREQIELLE-PIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAE 303

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  544 CDNLRRERDRAVSELAEALRSLDDTRKQKNDVS--------RELKELKEQMESQLEKEARFRHLMA 601
Cdd:COG4913   304 LARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLA 369
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 1318-1375 2.44e-04

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: 41.32  E-value: 2.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1318 RHVKLQKGS-EPLGISIVSGEKGGVYVSKVT-GGSIAHQAGLEYGDQLLEFNGINLRSAT 1375
Cdd:cd10831     1 RLVQFQKNTdEPMGITLKMNEDGRCIVARIMhGGMIHRQGTLHVGDEIREINGISVANQT 60
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 739-795 2.46e-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: 2.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  739 YAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 795
Cdd:cd06746    45 YLESVDPGGVADKAG-LKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVLKVVTV 100
PRK01156 PRK01156
chromosome segregation protein; Provisional
 240-631 2.52e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.05  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  240 LKDDVDMLRRENGQLLRERNLLQQSWEDMkrlhEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDA 319
Cdd:PRK01156  171 LKDVIDMLRAEISNIDYLEEKLKSSNLEL----ENIKKQIADDEKSHSITLK---EIERLSIEYNNAMDDYNNLKSALNE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  320 L------RKRYSEKVAIHNSDLSrleQMEEENQRLLKQTEMLTQQRDTAIQLQHQcalslrrfeaihhELNKATAQNKDL 393
Cdd:PRK01156  244 LssledmKNRYESEIKTAESDLS---MELEKNNYYKELEERHMKIINDPVYKNRN-------------YINDYFKYKNDI 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  394 QWEMELLQSELTELRTTQAKTAKESEKYKEerdavYSEYKLIMSERDqvisELDKLQTEVELAESK----LKSSTSEKKA 469
Cdd:PRK01156  308 ENKKQILSNIDAEINKYHAIIKKLSVLQKD-----YNDYIKKKSRYD----DLNNQILELEGYEMDynsyLKSIESLKKK 378

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  470 ASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIV--AERDSIRTLC--- 544
Cdd:PRK01156  379 IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSrnMEMLNGQSVCpvc 458

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  545 ---------DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMES-QLEKEARFRHLMAHSSHDSaidTDSM 614
Cdd:PRK01156  459 gttlgeeksNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARADL---EDIK 535

                         410
                  ....*....|....*..
gi 741978460  615 EWETEVVEFERETEDID 631
Cdd:PRK01156  536 IKINELKDKHDKYEEIK 552
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1319-1395 2.60e-04

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: 41.41  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1319 HVKLQKGSEPLGISIVSGE---KGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1394
Cdd:cd06735     3 SVELERGPKGFGFSIRGGReynNMPLYVLRLAEDGPAQRDGrLRVGDQILEINGESTQGMTHAQAIELIRSGGSVVRLLL 82


                  .
gi 741978460 1395 Q 1395
Cdd:cd06735    83 R 83
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 653-708 2.60e-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: 2.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  653 GIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKaLLNGEGAINMVVRR 708
Cdd:cd06741    27 GIYVTGVDPGSVAENAgLKVGDQILEVNGRSFLDITHDEAVK-ILKSSKHLIMTVKD 82
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 349-603 2.73e-04

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 46.05  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   349 LKQTEMLTQQRDTAIQLQHQCALSLRrfEAIHHELNKATAQNKDLQWEMELLQSELtelrttQAKTAKESEKYKEERDAV 428
Cdd:pfam15964  319 VRSSLAEAQQRESSAYEQVKQAVQMT--EEANFEKTKALIQCEQLKSELERQKERL------EKELASQQEKRAQEKEAL 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   429 YSEYKlimSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKALCQE 508
Cdd:pfam15964  391 RKEMK---KEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDE 467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   509 LKEALQEADvAKCRRDWAF--QERDKIVAERDSIRTLCDNLRRERDRAVSE-------LAEALRSLDDTRKQKNDVSR-- 577
Cdd:pfam15964  468 AEKEHREYR-TKTGRQLEIkdQEIEKLGLELSESKQRLEQAQQDAARAREEclkltelLGESEHQLHLTRLEKESIQQsf 546

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 741978460   578 ----------------ELKELKEQMESQLEKEARFRHLMAHS 603
Cdd:pfam15964  547 sneakaqalqaqqreqELTQKMQQMEAQHDKTVNEQYSLLTS 588
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 139-586 2.75e-04

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: 45.94  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   139 DRQVNEKVENLSIQLRLMTRERNELRKRLAFATHGttfdkrpyhrlnpdyeRLKIQcvramSDLQSLQSQHTNALKRCEE 218
Cdd:pfam01576  737 DEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAA----------------KKKLE-----LDLKELEAQIDAANKGREE 795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   219 VAKEtdfyhtlhsrLLSDQTQLKDdvdmlrrengqLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEI 298
Cdd:pfam01576  796 AVKQ----------LKKLQAQMKD-----------LQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   299 LNKLYDTAMDKLEvvkkdyDALRKRYSEKVAIHNsDLSRLE----QMEEENQRLLKQTEMLTQQrdtaiqlqhqcalslr 374
Cdd:pfam01576  855 ARRQAQQERDELA------DEIASGASGKSALQD-EKRRLEariaQLEEELEEEQSNTELLNDR---------------- 911

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   375 rfeaihheLNKATAQNkdlqwemELLQSELTELRTTQAKTakESEKYKEERDAvySEYKLIMSERDQVIseldklqteve 454
Cdd:pfam01576  912 --------LRKSTLQV-------EQLTTELAAERSTSQKS--ESARQQLERQN--KELKAKLQEMEGTV----------- 961

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   455 laESKLKSSTSEKKAASEEMEalrqikDTVTMDAGRANKEAEILRKQCKalcqELKEALQEADVakcRRDWAFQERDKiv 534
Cdd:pfam01576  962 --KSKFKSSIAALEAKIAQLE------EQLEQESRERQAANKLVRRTEK----KLKEVLLQVED---ERRHADQYKDQ-- 1024

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460   535 AERDSIRTlcDNLRRERDRAVSELAEA-------LRSLDDTRKQKNDVSRELKELKEQM 586
Cdd:pfam01576 1025 AEKGNSRM--KQLKRQLEEAEEEASRAnaarrklQRELDDATESNESMNREVSTLKSKL 1081
fliJ PRK07720
flagellar biosynthesis chaperone FliJ;
310-449 2.77e-04

flagellar biosynthesis chaperone FliJ;


Pssm-ID: 181091 [Multi-domain]  Cd Length: 146  Bit Score: 43.14  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  310 LEVVKKDYDALRKRYSEKVaihnsdlSRLEQMEEENQRLLKQTEMLTQQRDTAIQ-------LQHQCALSLRRFEAIHHe 382
Cdd:PRK07720   11 LELKENEKEKALGEYEEAV-------SRFEQVAEKLYELLKQKEDLEQAKEEKLQsglsiqeIRHYQQFVTNLERTIDH- 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  383 LNKATAQNKDlqwEMELLQSELTELRTtqaktakESEKYKEERDAVYSEYKLIMSERDQviSELDKL 449
Cdd:PRK07720   83 YQLLVMQARE---QMNRKQQDLTEKNI-------EVKKYEKMKEKKQEMFALEEKAAEM--KEMDEI 137
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 735-790 2.79e-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: 2.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  735 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06674    26 DTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGKVRL 81
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 720-783 2.92e-04

PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the second PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467270 [Multi-domain]  Cd Length: 85  Bit Score: 41.22  E-value: 2.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  720 LHINLSGHKDSGIslenGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 783
Cdd:cd10834    15 LGFNIRGGSEYGL----GIYVSKVDPGGLAEQNG-IKVGDQILAVNGVSFEDITHSKAVEVLKS 73
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 713-794 2.94e-04

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: 41.50  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  713 GGKVVTPLHINlsghkDSGIslengvYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 792
Cdd:cd06704    18 GGKGSTPYKGD-----DEGI------FISRVTEGGPAAKAG-VRVGDKLLEVNGVDLVDADHHEAVEALKNSGNTVTMVV 85


                  ..
gi 741978460  793 LK 794
Cdd:cd06704    86 LR 87
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 627-793 3.08e-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: 45.29  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   627 TEDIdLKALGFDMAEGVnepclpgdcgiFVTKVDKGSIAD-GRLRVNDWLLRINDVDLIN-KDKKQAIKALLNGEGAINM 704
Cdd:TIGR02037  244 TSDL-AKSLGLEKQRGA-----------LVAQVLPGSPAEkAGLKAGDVITSVNGKPISSfADLRRAIGTLKPGKKVTLG 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   705 VVRRRKSLGGKVV--TPLHINLSGHKDS-GISLEN----------------GVYAAAVVPGSPAAKEGsLAVGDRIVAIN 765
Cdd:TIGR02037  312 ILRKGKEKTITVTlgASPEEQASSSNPFlGLTVANlspeirkelrlkgdvkGVVVTKVVSGSPAARAG-LQPGDVILSVN 390

                          170       180
                   ....*....|....*....|....*...
gi 741978460   766 GIALdnKSLNECESLLRSCQDSLTLSLL 793
Cdd:TIGR02037  391 QQPV--SSVAELRKVLARAKKGGRVALL 416
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 735-790 3.27e-04

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: 41.48  E-value: 3.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  735 ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06703    31 DEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITL 86
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1320-1375 3.38e-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: 40.72  E-value: 3.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460 1320 VKLQKGSEPLGISIVSgeKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSAT 1375
Cdd:cd06744     2 VRVYRGNGSFGFTLRG--HAPVYIESVDPGSAAERAGLKPGDRILFLNGLDVRNCS 55
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 273-496 3.39e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  273 EEDQKEIGDLRAQQQQVLKhngssEI--LNKLYDTAMDKLEVVKKDYDALRKRYSEKvaihNSDLSRLEQMEEENQRLLK 350
Cdd:COG3883    19 QAKQKELSELQAELEAAQA-----ELdaLQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  351 Q--------------TEMLTQQRDTAiQLqhqcalsLRRFEAihheLNKATAQNKDLqweMELLQSELTELRTTQAKTAK 416
Cdd:COG3883    90 EraralyrsggsvsyLDVLLGSESFS-DF-------LDRLSA----LSKIADADADL---LEELKADKAELEAKKAELEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  417 ESEKYKEERDAVyseyklimserDQVISELDKLQTEvelAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAE 496
Cdd:COG3883   155 KLAELEALKAEL-----------EAAKAELEAQQAE---QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 703-797 3.59e-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: 41.15  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  703 NMVVRRRKSlggkvVTPLHINLSGHKDSGIslenGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 782
Cdd:cd06752     1 RTVVLKRPP-----GEQLGFNIRGGKASGL----GIFISKVIPDSDAHRLG-LKEGDQILSVNGVDFEDIEHSEAVKVLK 70

                          90
                  ....*....|....*.
gi 741978460  783 ScqdSLTLSL-LKVFP 797
Cdd:cd06752    71 T---AREIQMrVRYFP 83
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 633-708 3.60e-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: 3.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  633 KALGFDMAEGVNEPclpgdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 708
Cdd:cd06678    11 EQLGIKLVRKKDEP------GVFILDLLEGGLAarDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQASGERVHFVVSR 82
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 737-790 3.73e-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: 41.09  E-value: 3.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 741978460  737 GVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRScQDSLTL 790
Cdd:cd06737    28 GLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLIKT-KKTVSL 79
PDZ_MYO18-like cd06747
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ...
 1511-1550 3.80e-04

PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467229 [Multi-domain]  Cd Length: 90  Bit Score: 41.14  E-value: 3.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 741978460 1511 GLVPGDLILEYGGLDVRSKTVEEVyVEMLKPK-DSVRLKVQ 1550
Cdd:cd06747    51 GLLPGDRLIEVNGVNVENASRDEI-IEMIRKSgDTVTLKVQ 90
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 239-599 3.80e-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: 45.45  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   239 QLKDDVDMLRRENGQLLRERnllqqswEDMKRLHEEDQKEIGDLRAQQQQ----------------VLKHngSSEILNKL 302
Cdd:pfam05622   63 LLQKQLEQLQEENFRLETAR-------DDYRIKCEELEKEVLELQHRNEEltslaeeaqalkdemdILRE--SSDKVKKL 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   303 YDTamdkLEVVKK---DYDALRKR---YSEKVAIHnsdLSRLEQMEEENQR---LLKQTEMLTQQrdtaIQ-LQHQCALS 372
Cdd:pfam05622  134 EAT----VETYKKkleDLGDLRRQvklLEERNAEY---MQRTLQLEEELKKanaLRGQLETYKRQ----VQeLHGKLSEE 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   373 LRRFEAIHHELNKATAQNKDLQWEMELLQSE-------LTELRTTQAKTAKESE----------------------KYKE 423
Cdd:pfam05622  203 SKKADKLEFEYKKLEEKLEALQKEKERLIIErdtlretNEELRCAQLQQAELSQadallspssdpgdnlaaeimpaEIRE 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   424 ERDAVYSEYKLIM-----SERDQ---VISELD-------KLQTEVELAESKLksstSEKKAASEEMEALRQIKDTVTMDA 488
Cdd:pfam05622  283 KLIRLQHENKMLRlgqegSYRERlteLQQLLEdanrrknELETQNRLANQRI----LELQQQVEELQKALQEQGSKAEDS 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   489 GRANKEAEILRKQCKALCQEL---KEALQE----ADVAKCRRDWAFQErdKIVAERDSIRTLCDNLRRERDRAvselAEA 561
Cdd:pfam05622  359 SLLKQKLEEHLEKLHEAQSELqkkKEQIEElepkQDSNLAQKIDELQE--ALRKKDEDMKAMEERYKKYVEKA----KSV 432

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 741978460   562 LRSLDDtrKQKNDVSRELKELKEQMesqLEKEARFRHL 599
Cdd:pfam05622  433 IKTLDP--KQNPASPPEIQALKNQL---LEKDKKIEHL 465
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 152-476 4.17e-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: 45.71  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  152 QLRLMTRERNELRKRLAFAThgttFDKRPYHRL----------------NPDYERLKIQCVRAMSDLQSLQSQHTNALKR 215
Cdd:COG3096   786 RLEELRAERDELAEQYAKAS----FDVQKLQRLhqafsqfvgghlavafAPDPEAELAALRQRRSELERELAQHRAQEQQ 861

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  216 CEEVAKETDFYHTLHSRLLSDQTQLKDD-----VDMLRRENGQLLRERNLLQQSWEDMKRLheEDQKEIgdLRAQQQQVl 290
Cdd:COG3096   862 LRQQLDQLKEQLQLLNKLLPQANLLADEtladrLEELREELDAAQEAQAFIQQHGKALAQL--EPLVAV--LQSDPEQF- 936

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  291 khngssEILNKLYDTAMDKLEVVKKDYDAL---RKR-----YSEKVAI--HNSDLS-----RLEQMEEEnqrllkqtemL 355
Cdd:COG3096   937 ------EQLQADYLQAKEQQRRLKQQIFALsevVQRrphfsYEDAVGLlgENSDLNeklraRLEQAEEA----------R 1000

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  356 TQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQseltelrtTQAKTAKEsEKYKEERDAVYSEYKLI 435
Cdd:COG3096  1001 REAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG--------VQADAEAE-ERARIRRDELHEELSQN 1071

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 741978460  436 MSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEA 476
Cdd:COG3096  1072 RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 1338-1392 4.45e-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: 41.08  E-value: 4.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 741978460 1338 KGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1392
Cdd:cd06781    29 NKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDTVKV 83
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
398-589 4.66e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  398 ELLQSELTELRTTQAKTAKESEKYKEERDAVYSEyklimSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEAL 477
Cdd:COG3206   178 EFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS-----EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  478 RQIKDTVTMDAGRANkeaeiLRKQCKALCQELKEALQEadvakcrrdwaFQERD-KIVAERDSIRTLCDNLRRERDRA-- 554
Cdd:COG3206   253 PDALPELLQSPVIQQ-----LRAQLAELEAELAELSAR-----------YTPNHpDVIALRAQIAALRAQLQQEAQRIla 316

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 741978460  555 ------------VSELAEALRSLDDTRKQKNDVSRELKELKEQMESQ 589
Cdd:COG3206   317 sleaelealqarEASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 628-708 4.74e-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: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  628 EDIDL----KALGFDMAEGVNEpclpgdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGA 701
Cdd:cd06667     1 EVIELvndgSGLGFGIVGGKST-------GVVVKTILPGGVAdrDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSH 73


                  ....*..
gi 741978460  702 INMVVRR 708
Cdd:cd06667    74 VRLVVAR 80
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1471-1549 4.92e-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: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1471 PRVVFIKKSQLELGVHLCGGNlhGVFVAEVEDDSPArGPDGLVPGDLILEYGGLDVRSKTVEEVyVEMLK--PKDSVRLK 1548
Cdd:cd06712     1 PRTVHLTKEEGGFGFTLRGDS--PVQVASVDPGSCA-AEAGLKEGDYIVSVGGVDCKWSKHSEV-VKLLKsaGEEGLELQ 76


                  .
gi 741978460 1549 V 1549
Cdd:cd06712    77 V 77
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 720-790 5.00e-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: 40.82  E-value: 5.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460  720 LHINLSGHKDSGISlengVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06800    13 LGISITGGKEHGVP----ILISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITL 79
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 1472-1551 5.00e-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: 40.82  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1472 RVVFIKKSQLE-LGVHLCGGNLHGV--FVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVyVEMLKPKD-SVRL 1547
Cdd:cd06800     1 RKVLLSKEPHEgLGISITGGKEHGVpiLISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEA-VTILSQQRgEITL 79


                  ....
gi 741978460 1548 KVQY 1551
Cdd:cd06800    80 EVVY 83
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1319-1367 5.17e-04

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: 40.41  E-value: 5.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 741978460 1319 HVKLQKGSEPLGISIVSGEK-GGVYVSKVT-GGSIAHQAGLEYGDQLLEFN 1367
Cdd:cd10817     1 HVELPKDQGGLGIAISEEDTeNGIVIKSLTeGGPAAKDGRLKVGDQILAVD 51
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 1343-1395 5.23e-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: 40.37  E-value: 5.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 741978460 1343 VSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1395
Cdd:cd10820    26 VAKIRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 139-558 5.34e-04

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: 44.81  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   139 DRQVN---EKVENLSIQLRLMTRERNELRKRLafathgttfdkrpyhrlnpdyerlkiqcvramsdlQSLQSQHTN---A 212
Cdd:pfam10174  393 ERKINvlqKKIENLQEQLRDKDKQLAGLKERV-----------------------------------KSLQTDSSNtdtA 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   213 LKRCEEVAKETD-FYHTLHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQqswedmkRLHEEDQKEIGDLRAQQQQVlk 291
Cdd:pfam10174  438 LTTLEEALSEKErIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQ-------PELTEKESSLIDLKEHASSL-- 508

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   292 hngSSEILNKlyDTAMDKLEV-VKKDYDALRKRYSEKVAIHNSDLS---------RLEQMEEENQR-------------- 347
Cdd:pfam10174  509 ---ASSGLKK--DSKLKSLEIaVEQKKEECSKLENQLKKAHNAEEAvrtnpeindRIRLLEQEVARykeesgkaqaever 583

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   348 ---LLKQTEMLTQQRDTAIQLQHQCALSLrrfeaiHHELNKATAQNKDLQWEMELLQSELTElrttqaktakESEKYKEE 424
Cdd:pfam10174  584 llgILREVENEKNDKDKKIAELESLTLRQ------MKEQNKKVANIKHGQQEMKKKGAQLLE----------EARRREDN 647

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   425 RDAVYSEYKLimserDQVISELDKlqTEVELAESKLKSSTSEKKAASEE--MEALRQIKdtvtmdagrankeaeilRKQC 502
Cdd:pfam10174  648 LADNSQQLQL-----EELMGALEK--TRQELDATKARLSSTQQSLAEKDghLTNLRAER-----------------RKQL 703

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460   503 kalcQELKEALQEADVAkcrrdwAFQERDKIVA-------ERDSIRTLCDNLRRERDRAVSEL 558
Cdd:pfam10174  704 ----EEILEMKQEALLA------AISEKDANIAllelsssKKKKTQEEVMALKREKDRLVHQL 756
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1319-1379 5.44e-04

PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 40.66  E-value: 5.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1319 HVKLQKGSEPLGISIVSGEKGGVY--VSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06731     3 RTSLKKSARGFGFTIIGGDEPDEFlqIKSVVPDGPAALDGkLRTGDVLVSVNDTCVLGYTHADV 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 304-463 5.55e-04

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: 43.76  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  304 DTAMDKLEVVKKD----YDALRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQcALSLRRFEAI 379
Cdd:COG1579    16 DSELDRLEHRLKElpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKEYEAL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  380 HHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVyseykliMSERDQVISELDKLQTEVELAESK 459
Cdd:COG1579    95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK-------KAELDEELAELEAELEELEAEREE 167


                  ....
gi 741978460  460 LKSS 463
Cdd:COG1579   168 LAAK 171
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 633-687 5.67e-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: 40.63  E-value: 5.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  633 KALGFDMAEGVNEPCLPGdcgIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKD 687
Cdd:cd06718    11 KPLGFYIRDGNGVERVPG---IFISRLVLGSLADstGLLAVGDEILEVNGVEVTGKS 64
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 652-707 5.68e-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: 5.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  652 CGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLNGEgAINMVVR 707
Cdd:cd06752    25 LGIFISKVIPDSDAHRLgLKEGDQILSVNGVDFEDIEHSEAVKVLKTAR-EIQMRVR 80
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 1472-1543 6.13e-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: 40.24  E-value: 6.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460 1472 RVVFIKKSQLELGVHLCGGN----LHGVFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVYVEMLKPKD 1543
Cdd:cd06718     2 RVELIKPPGKPLGFYIRDGNgverVPGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTR 77
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
 720-792 6.19e-04

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: 40.40  E-value: 6.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460  720 LHINLSGHKDSGISLENG------VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALdNKSLNECESLLRSCQDSLTLSL 792
Cdd:cd06750     3 IEVQLQGGAPWGFTLKGGlehgepLVISKIEEGGKAASVGKLQVGDEVVNINGVPL-SGSRQEAIQLVKGSHKTLKLVV 80
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 653-691 6.40e-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: 6.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 741978460  653 GIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQA 691
Cdd:cd06691    34 GLLIRGIEEGSRAerDGRFQENDCIVEINGVDLIDKSFEQA 74
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 719-785 6.61e-04

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: 40.32  E-value: 6.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  719 PLHINLSGHKDSgisleNGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQ 785
Cdd:cd06670    15 SLGITVSADKDG-----NGCIVKSIIHGGAVSRDGRISVGDFIVSINNESLRNVTNAQARAILRRAS 76
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
308-641 6.70e-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: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  308 DKLEVVKKDYDALRkrysEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQhQCALSLRRFEAihhELNKAT 387
Cdd:COG4913   610 AKLAALEAELAELE----EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEA---ELERLD 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  388 AQNKDLqwemELLQSELTELRttqaktaKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKlksSTSEK 467
Cdd:COG4913   682 ASSDDL----AALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL---ARLEL 747

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  468 KAASEEMeaLRQIKDTVTMDAGRANKEAEI--LRKQCKALCQELKEALQEAdvakcRRDWAFQERDKI--VAERDSIRTL 543
Cdd:COG4913   748 RALLEER--FAAALGDAVERELRENLEERIdaLRARLNRAEEELERAMRAF-----NREWPAETADLDadLESLPEYLAL 820

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  544 CDNLRRER-DRAVSELAEALrslddtrkqKNDVSRELKELKEQMESQLEK-EARFRHL---MAHS--SHDSAIdtdSMEW 616
Cdd:COG4913   821 LDRLEEDGlPEYEERFKELL---------NENSIEFVADLLSKLRRAIREiKERIDPLndsLKRIpfGPGRYL---RLEA 888

                         330       340
                  ....*....|....*....|....*....
gi 741978460  617 E----TEVVEFERETEDIDLKALGFDMAE 641
Cdd:COG4913   889 RprpdPEVREFRQELRAVTSGASLFDEEL 917
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
1320-1394 7.00e-04

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 44.43  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1320 VKLQKGSEP-----LGISiVSGEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSAT--EQQARLIIGqqcDTITI 1392
Cdd:COG3975   471 LKLVYEDAPslkpsLGLR-VSADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTADNldDALAAYKPG---DPIEL 546


                  ..
gi 741978460 1393 LA 1394
Cdd:COG3975   547 LV 548
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 ...
 731-783 7.08e-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: 7.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 741978460  731 GISLEN-GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 783
Cdd:cd06762    21 GSDLENkSITVHRVFPSGLAAQEGTIQKGDRILSINGKSLKGVTHGDALSVLKQ 74
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 1342-1393 7.14e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 39.43  E-value: 7.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 741978460  1342 YVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSaTEQQARLIIGQQCDTITIL 1393
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRS-LEDVARLLQGSAGESVTLT 51
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1473-1550 7.34e-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: 40.11  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1473 VVFIKKSQLE-LGVHLCGGNLHG--VFVAEVEDDSPARgPDGLVPGDLILEYGGLDVRSKTVEEVyVEMLKPKDSVRLKV 1549
Cdd:cd10833     3 TVTVEKSPDGsLGFSVRGGSEHGlgIFVSKVEEGSAAE-RAGLCVGDKITEVNGVSLENITMSSA-VKVLTGSNRLRMVV 80


                  .
gi 741978460 1550 Q 1550
Cdd:cd10833    81 R 81
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 1329-1550 7.34e-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: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1329 LGISI--VSGEK---------GGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQ---ARLIIGqqcDTITIla 1394
Cdd:TIGR02037  236 LGVTIqeVTSDLakslglekqRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRraiGTLKPG---KKVTL-- 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  1395 QYNPHMHqlsshsrssshldPVGIHSTLQGSgattPEHPsvidplmeqdegpgtppakqsipssrmvGDATKKTPEPRVV 1474
Cdd:TIGR02037  311 GILRKGK-------------EKTITVTLGAS----PEEQ----------------------------ASSSNPFLGLTVA 345

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  1475 FIKKSQLELGVHlcGGNLHGVFVAEVEDDSPARGPdGLVPGDLILEYGGLDVRSktVEEVY--VEMLKPKDSVRLKVQ 1550
Cdd:TIGR02037  346 NLSPEIRKELRL--KGDVKGVVVTKVVSGSPAARA-GLQPGDVILSVNQQPVSS--VAELRkvLARAKKGGRVALLIL 418
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 616-695 7.64e-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: 7.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  616 WETEVVEFERETEDidlKALGFDMAEgVNEPCLPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIK 693
Cdd:cd06669     4 WSDEVTVIELEKGD---RGLGFSILD-YQDPLDPSETVIVIRSLVPGGVAeqDGRLLPGDRLVFVNDVSLENASLDEAVQ 79


                  ..
gi 741978460  694 AL 695
Cdd:cd06669    80 AL 81
PDZ3_PDZD7-like cd06751
PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1320-1385 7.74e-04

PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of the Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa and can also form homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the third PDZ domain of the canonical isoform of PDZD7- isoform 1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD7-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467233 [Multi-domain]  Cd Length: 89  Bit Score: 40.11  E-value: 7.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460 1320 VKLQKGSEPLGISIVSGEKGG----VYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1385
Cdd:cd06751     4 VELSKMKQSLGISISGGIESKvqpvVKIEKIFPGGAAALSGnLKAGYELVSVDGESLQQVTHQQAVDIIRR 74
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 1466-1549 7.99e-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: 40.65  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1466 KKTPEPRVVFIKKSQLELGVHLCGGNLHGV--------------FVAEVEDDSPArgpD--GLVPGDLILEYGGLDVRSK 1529
Cdd:cd06746     1 DSIIDPRTVVLQKGDKGFGFVLRGAKAVGPileftptpafpalqYLESVDPGGVA---DkaGLKKGDFLLEINGEDVVKA 77

                          90       100
                  ....*....|....*....|.
gi 741978460 1530 TVEEVyVEMLKPK-DSVRLKV 1549
Cdd:cd06746    78 SHEQV-VNLIRQSgNTLVLKV 97
PDZ1_syntenin-like cd06721
PDZ domain 1 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1318-1371 8.45e-04

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


Pssm-ID: 467204 [Multi-domain]  Cd Length: 79  Bit Score: 39.91  E-value: 8.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 741978460 1318 RHVKLQKGSE-PLGISIVSGEKGgVYVSKVTGGSIAHQAGLEYGDQLLEFNGINL 1371
Cdd:cd06721     1 REVILCKDQDgKIGLRVKSIDKG-VFVQLVQANSPAALAGLRFGDQILQINGENV 54
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 702-783 8.50e-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: 39.94  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  702 INMVVRRRKSLGgkvvtplhINLSGHKDSGIslenGVYAAAVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLL 781
Cdd:cd06741     4 VNLVVEDGQSLG--------LMIRGGAEYGL----GIYVTGVDPGSVAENAG-LKVGDQILEVNGRSFLDITHDEAVKIL 70


                  ..
gi 741978460  782 RS 783
Cdd:cd06741    71 KS 72
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
482-633 8.78e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  482 DTVTMDAGRANKEAEILRKQCKALCQELKEALQEAdvakcrRDWAfQERDKIVAERDSIRTLCDNLRRERDRAVSELAEA 561
Cdd:COG1340     4 DELSSSLEELEEKIEELREEIEELKEKRDELNEEL------KELA-EKRDELNAQVKELREEAQELREKRDELNEKVKEL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460  562 LRSLDDTRKQKNDVSRELKELKEQMESQLEKEarfrhlmahsshdsaIDTDSMEWETEVVEFERETEDIDLK 633
Cdd:COG1340    77 KEERDELNEKLNELREELDELRKELAELNKAG---------------GSIDKLRKEIERLEWRQQTEVLSPE 133
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 430-622 8.79e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 44.22  E-value: 8.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   430 SEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEAEILRKqckalcqEL 509
Cdd:pfam05262  178 SDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRD-------EV 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   510 KEALQE-------ADVAKCRRDWAFQERDKIVAERDSIRT--LCDNLRRERDRAVSELAEALRSLDDTRKQKN-DVSREL 579
Cdd:pfam05262  251 RQKQQEaknlpkpADTSSPKEDKQVAENQKREIEKAQIEIkkNDEEALKAKDHKAFDLKQESKASEKEAEDKElEAQKKR 330

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 741978460   580 KELKEQMESQL-EKEARFRHLmahssHDSAIDTDSMEWETEVVE 622
Cdd:pfam05262  331 EPVAEDLQKTKpQVEAQPTSL-----NEDAIDSSNPVYGLKVVD 369
SH3_CAS cd11844
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins ...
 1570-1606 8.94e-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: 39.25  E-value: 8.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 741978460 1570 RALYERLAEVEPELSFKKDDILYVDDTLPQGSFGSWM 1606
Cdd:cd11844     3 RALYDNVAESPDELAFRRGDILTVLEQNTAGLEGWWL 39
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 1337-1380 9.08e-04

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


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 40.38  E-value: 9.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 741978460 1337 EKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQAR 1380
Cdd:cd10838    31 EVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRI 74
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 743-767 1.01e-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: 1.01e-03
                          10        20
                  ....*....|....*....|....*
gi 741978460  743 VVPGSPAAKEGSLAVGDRIVAINGI 767
Cdd:cd06731    32 VVPDGPAALDGKLRTGDVLVSVNDT 56
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 640-709 1.03e-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: 1.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460  640 AEGVNEPclpgDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 709
Cdd:cd06789    22 AKGAGQD----KLGIYIKSVVKGGAAdlDGRLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTLEVAKQ 89
PDZ3_harmonin cd06739
PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic ...
 719-787 1.09e-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: 39.98  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460  719 PLHINLSGHKDSgiSLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDS 787
Cdd:cd06739    13 PLDLALEGGIDS--PLGGKIVVSAVYEGGAADKHGGIVKGDQIMMVNGKSLTDVTLAEAEAALQRAMNS 79
46 PHA02562
endonuclease subunit; Provisional
 274-511 1.15e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  274 EDQKEIGDLRAQ----QQQVLKHNGSSEILNKLYDTAMDKLEVVkkdYDALRKrysEKVAIHNSDLSRLEQMEEENQRLL 349
Cdd:PHA02562  178 ELNQQIQTLDMKidhiQQQIKTYNKNIEEQRKKNGENIARKQNK---YDELVE---EAKTIKAEIEELTDELLNLVMDIE 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  350 KQTEMLTQQRDTAIQLQHQcalsLRRFEAIHHELNK-----ATAQNKDLQWEMellqseLTELRTTQAKTAKESEKYKEE 424
Cdd:PHA02562  252 DPSAALNKLNTAAAKIKSK----IEQFQKVIKMYEKggvcpTCTQQISEGPDR------ITKIKDKLKELQHSLEKLDTA 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  425 RDavysEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRqikdtvtmdAGRANKEAEIlrkqcKA 504
Cdd:PHA02562  322 ID----ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQ---------AEFVDNAEEL-----AK 383


                  ....*..
gi 741978460  505 LCQELKE 511
Cdd:PHA02562  384 LQDELDK 390
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 635-706 1.15e-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: 39.64  E-value: 1.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  635 LGFDMAEGVNEpcLPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 706
Cdd:cd06680    13 LGFSIVGGYEE--SHGNQPFFVKSIVPGTPAynDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTV 84
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 718-790 1.15e-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: 40.03  E-value: 1.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 741978460  718 TPLHINLSGHKDsgislENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06795    12 TGLGFNIVGGED-----GEGIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTI 79
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 1326-1381 1.16e-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: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460 1326 SEPLGISIVSGEKGGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1381
Cdd:cd06779    12 SPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAAL 67
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 235-472 1.16e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  235 SDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngsseilnklydtAMDKLEVVK 314
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-----------------LQAEIAEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  315 KDYDALRKRYSEkvaihnsdlsRLEQMeEENQRLLKQTEMLTQQRDTAIQLQHQCALS--LRRFEAIHHELNKATAQNKD 392
Cdd:COG3883    79 AEIEERREELGE----------RARAL-YRSGGSVSYLDVLLGSESFSDFLDRLSALSkiADADADLLEELKADKAELEA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  393 LQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKlimSERDQVISELDKLQTEVELAESKLKSSTSEKKAASE 472
Cdd:COG3883   148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS---AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 339-597 1.18e-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: 43.37  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   339 EQMEEENQRLLKQTEMLTQQRDTAIQLQHQCalslrrfeaihhelnkataqnkdlqwemelLQSELTELRttqAKTAKES 418
Cdd:pfam13868   47 EMMEEERERALEEEEEKEEERKEERKRYRQE------------------------------LEEQIEERE---QKRQEEY 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   419 EKYKEERDAVYSEYKLIMSERDQVISELDKLQTEV--ELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGR-ANKEA 495
Cdd:pfam13868   94 EEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEReEEREA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   496 EILRKQCK--ALCQELKEALQEADVAKcrrdwafQERDKIVAErdsiRTLCDNLRRERDRAVSELAEALRSLDDTRKQkN 573
Cdd:pfam13868  174 EREEIEEEkeREIARLRAQQEKAQDEK-------AERDELRAK----LYQEEQERKERQKEREEAEKKARQRQELQQA-R 241

                          250       260
                   ....*....|....*....|....
gi 741978460   574 DVSRELKELKEQMESQLEKEARFR 597
Cdd:pfam13868  242 EEQIELKERRLAEEAEREEEEFER 265
46 PHA02562
endonuclease subunit; Provisional
 265-582 1.23e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  265 WEDMKRLHEEdqKEIGDLRAQQQQVLKHN----------GSS--------------EILNKLYD----TAMDKLEVVK-- 314
Cdd:PHA02562  100 YCNGKLLDES--ASSKDFQKYFEQMLGMNyksfkqivvlGTAgyvpfmqlsaparrKLVEDLLDisvlSEMDKLNKDKir 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  315 ------KDYDALRKRYSEKVAIHNSDLSRLEqmEEENQRLLKQTEMLTQQRDTAiqlqhqcalslrrfEAIHHELNKATA 388
Cdd:PHA02562  178 elnqqiQTLDMKIDHIQQQIKTYNKNIEEQR--KKNGENIARKQNKYDELVEEA--------------KTIKAEIEELTD 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  389 QNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEErdavyseykLIMSERDQV-------ISELDKLQTEVElaeSKLK 461
Cdd:PHA02562  242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV---------IKMYEKGGVcptctqqISEGPDRITKIK---DKLK 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  462 SSTSEKKAASEEMEALRQIKDtvtmdagrankeaEILRKQCKAlcQELKealqeADVAKCRRDWAfqerdKIVAERDSIR 541
Cdd:PHA02562  310 ELQHSLEKLDTAIDELEEIMD-------------EFNEQSKKL--LELK-----NKISTNKQSLI-----TLVDKAKKVK 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 741978460  542 TLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKEL 582
Cdd:PHA02562  365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
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 ...
 708-769 1.24e-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: 39.57  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460  708 RRKSLGGKVVtplhinlsGHKDSgISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIAL 769
Cdd:cd06759    10 GGKGLGFSIV--------GGRDS-PRGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESL 62
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 718-790 1.25e-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: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  718 TPLHINLSGHKDSG-ISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06709    10 SGLGFNIVGGTDQPyIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDAVELFRNAGEDVKL 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 ...
 1324-1379 1.29e-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: 39.57  E-value: 1.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460 1324 KGSEPLGISIVSGE---KG--GVYVSKV-TGGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06759     9 AGGKGLGFSIVGGRdspRGpmGIYVKTIfPGGAAAEDGRLKEGDEILEVNGESLQGLTHQEA 70
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 ...
 618-707 1.33e-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: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  618 TEVVEFERetediDLKALGFDMAEGVNEPClpGDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQA---I 692
Cdd:cd06763     1 AVTVELEK-----GSAGLGFSLEGGKGSPL--GDRPLTIKRIFKGGAAEqsGVLQVGDEILQINGTSLQGLTRFEAwniI 73

                          90
                  ....*....|....*
gi 741978460  693 KALlnGEGAINMVVR 707
Cdd:cd06763    74 KSL--PEGPVTLLIR 86
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 1342-1393 1.35e-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: 39.53  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 741978460 1342 YVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1393
Cdd:cd06713    38 YVCRVHEDSPAYLAGLTAGDVILSVNGVSVEGASHQEIVELIRSSGNTLRLE 89
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 299-592 1.45e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 43.41  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  299 LNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQ--QRDTAIQLQHQCALSLRRF 376
Cdd:COG5185    70 LNYQNDVKKSESSVKARKFLKEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSeiVALKDELIKVEKLDEIADI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  377 EAIHHE-------LNKATAQNKDLQ--------WEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQ 441
Cdd:COG5185   150 EASYGEvetgiikDIFGKLTQELNQnlkkleifGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEII 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  442 VISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIK--DTVTMDAgRANKEAEILRKQCKALCQELKEALQEADVA 519
Cdd:COG5185   230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKlgENAESSK-RLNENANNLIKQFENTKEKIAEYTKSIDIK 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  520 KCRRDW-----AFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKN------DVSRELKELKEQMES 588
Cdd:COG5185   309 KATESLeeqlaAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVgevelsKSSEELDSFKDTIES 388


                  ....
gi 741978460  589 QLEK 592
Cdd:COG5185   389 TKES 392
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 1476-1552 1.46e-03

PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ10 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467161 [Multi-domain]  Cd Length: 86  Bit Score: 39.58  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1476 IKKSQLELGVHLCGGN---LHGVFVAEVEDDSPArGPDG-LVPGDLILEYGGLDVRSKTVEEVYVEMLKPKDSVRLKVqY 1551
Cdd:cd06673     8 INKGKKGLGLSIVGGSdtlLGAIIIHEVYEDGAA-AKDGrLWAGDQILEVNGEDLRKATHDEAINVLRQTPQKVRLLV-Y 85


                  .
gi 741978460 1552 R 1552
Cdd:cd06673    86 R 86
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 ...
 1320-1379 1.57e-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: 39.13  E-value: 1.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460 1320 VKLQKGSEPLGISIvSGEKGG------VYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06763     4 VELEKGSAGLGFSL-EGGKGSplgdrpLTIKRIFKGGAAEQSGvLQVGDEILQINGTSLQGLTRFEA 69
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1009-1307 1.59e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1009 PLTPPKPPRRGDSIKFQHKLETSSESEATLVGSSPSTSPPSALPPDVDPGDPMHASPPRKarvRIASSYCPEGDRDSSYL 1088
Cdd:PHA03307   24 PPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANE---SRSTPTWSLSTLAPASP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1089 PAKKSCDEDLTSQKE---QKCTPASGELS--PDLQEWAP--YSPGHSSRHSNP-PFYPSRASVGTVPRSLAPSTVSSVLR 1160
Cdd:PHA03307  101 AREGSPTPPGPSSPDpppPTPPPASPPPSpaPDLSEMLRpvGSPGPPPAASPPaAGASPAAVASDAASSRQAALPLSSPE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1161 NPIYTVRS--HRVGPcSSPPIPREAGPHGLHPSVQHQGRLSLDLSPR-------ACSDCSDMRASHGSNSLPSSARLATG 1231
Cdd:PHA03307  181 ETARAPSSppAEPPP-STPPAAASPRPPRRSSPISASASSPAPAPGRsaaddagASSSDSSSSESSGCGWGPENECPLPR 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1232 SSSNLQFKAERIKIPSTPRYPRSVVGSDRGSL---------SHSECSTPPQSPLSVEGLSScSQSQTSAATLPR------ 1296
Cdd:PHA03307  260 PAPITLPTRIWEASGWNGPSSRPGPASSSSSPrerspspspSSPGSGPAPSSPRASSSSSS-SRESSSSSTSSSsessrg 338

                         330
                  ....*....|.
gi 741978460 1297 IAVNPAAPGER 1307
Cdd:PHA03307  339 AAVSPGPSPSR 349
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 1493-1550 1.60e-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: 39.79  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1493 HGVFVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVrsKTVEEVYvEMLKPKDSVRLKVQ 1550
Cdd:cd06785    31 SGVYVHKVIPGSPAqRA--GLKDGDVIISINGKPV--KSSSDVY-EAVKSGSSLLVVVR 84
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 1339-1376 1.64e-03

circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Escherichia coli DegS and related domains. DegS (also known as Site-1 protease DegS, S1P protease DegS, and Site-1-type intramembrane protease) participates in the activation of the sigma(E) extracytoplasmic stress response. Initially, there is an accumulation of misfolded membrane proteins (OMPs) in the periplasm which bind by their YXF motif to the DegS PDZ domain, activating DegS-catalyzed cleavage of the RseA periplasmic domain and making RseA a substrate for cleavage by another membrane protease RseP. 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 DegS family 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: 467620 [Multi-domain]  Cd Length: 93  Bit Score: 39.30  E-value: 1.64e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 741978460 1339 GGVYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATE 1376
Cdd:cd06777    25 QGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLE 62
PDZ0_GgPro-IL-16-like cd23062
PDZ domain 0 of Gallus gallus interleukin-16, and related domains; N-terminal PDZ (PSD-95 ...
 720-783 1.65e-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: 39.10  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  720 LHINLSGHKDSGiSLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 783
Cdd:cd23062    11 SGIKLSRNPNCA-SLWKGFTGCHVPAGGTANRDGCLSPRDELLTLNGQSLKDLSSKEAESLIQS 73
PLN02939 PLN02939
transferase, transferring glycosyl groups
 298-537 1.72e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 43.35  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  298 ILNKLYDTAMDKLEVVKKDYDALRKryseKVAIHNSDLS----RLEQMEEENQRLLKQTEMLTQQRDtaiQLQHQCALSL 373
Cdd:PLN02939  146 LLNQARLQALEDLEKILTEKEALQG----KINILEMRLSetdaRIKLAAQEKIHVEILEEQLEKLRN---ELLIRGATEG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  374 RRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAK-ESEKYKEERDAVYSEYKLIMSERDqvISELDKLQTE 452
Cdd:PLN02939  219 LCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKlEKERSLLDASLRELESKFIVAQED--VSKLSPLQYD 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  453 -----VELAESKLKSSTSEKKAASEEMEALRQIKDTVtmdagrankeaeilrkqckalcQELKEALQEADVAK--CRRDW 525
Cdd:PLN02939  297 cwwekVENLQDLLDRATNQVEKAALVLDQNQDLRDKV----------------------DKLEASLKEANVSKfsSYKVE 354

                         250
                  ....*....|..
gi 741978460  526 AFQERDKIVAER 537
Cdd:PLN02939  355 LLQQKLKLLEER 366
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 1316-1393 1.75e-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: 39.40  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1316 EPRHVKLQKGSEP-LGISIVSGEKG-----GVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCD 1388
Cdd:cd23072     1 EITLVNLKKDAKYgLGFQIVGGEKSgrldlGIFISSITPGGPADLDGrLKPGDRLISVNDVSLEGLSHDAAVEILQNAPE 80


                  ....*
gi 741978460 1389 TITIL 1393
Cdd:cd23072    81 DVTLV 85
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 438-592 1.75e-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: 42.22  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  438 ERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQ-I-KDTVTMDAGRANKEAEILRKQCkalcqelkealqe 515
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArIkKYEEQLGNVRNNKEYEALQKEI------------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  516 advakcrrdwAFQERDKIVAErDSIRTL---CDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEK 592
Cdd:COG1579    99 ----------ESLKRRISDLE-DEILELmerIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
PDZ_LIMK-like cd06754
PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 754-783 1.76e-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: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 741978460  754 SLAVGDRIVAINGIALDNKSLNECESLLRS 783
Cdd:cd06754    50 SLHVGDRILEVNGTPVRDLSLEEIDDLIQS 79
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 202-595 1.77e-03

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: 43.47  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   202 LQSLQSQhtnaLKRCEEVAKETDFYHTLHSrllSDQTQLKDDVDMLRRE----NGQLLRERNLLQQSWEDMKRLHEE--- 274
Cdd:TIGR04523   42 LKTIKNE----LKNKEKELKNLDKNLNKDE---EKINNSNNKIKILEQQikdlNDKLKKNKDKINKLNSDLSKINSEikn 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   275 --DQK-----EIGDLRAQQQQVLKHNG--SSEILNKlydtaMDKLEVVKKDYDALRKRYSEkvaihnsdlSRLEQMEEEN 345
Cdd:TIGR04523  115 dkEQKnklevELNKLEKQKKENKKNIDkfLTEIKKK-----EKELEKLNNKYNDLKKQKEE---------LENELNLLEK 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   346 QRLLKQTEMLtqqrdtaiQLQHQcalsLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEER 425
Cdd:TIGR04523  181 EKLNIQKNID--------KIKNK----LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   426 DAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQikdtvtmdagraNKEAEILRkqckal 505
Cdd:TIGR04523  249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN------------QKEQDWNK------ 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   506 cqELKEALQEadvakcrrdwafQERDKIVAErdsirtlcdNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQ 585
Cdd:TIGR04523  311 --ELKSELKN------------QEKKLEEIQ---------NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367

                          410
                   ....*....|
gi 741978460   586 MESQLEKEAR 595
Cdd:TIGR04523  368 KQNEIEKLKK 377
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 1570-1628 1.94e-03

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: 38.05  E-value: 1.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1570 RALYERLAEVEPELSFKKDDILYVDDTLPQGsfgsWmaWQLDENAQKmqrGQIPSKYVM 1628
Cdd:cd11772     3 RALYDYEAQHPDELSFEEGDLLYISDKSDPN----W--WKATCGGKT---GLIPSNYVE 52
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 1320-1393 1.94e-03

PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZRN4-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467200 [Multi-domain]  Cd Length: 88  Bit Score: 39.18  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1320 VKLQKGS--EPLGISIVSG----EKGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSatEQQARLIIGQQCDTITI 1392
Cdd:cd06716     6 VTLKRSNsqEKLGLTLCYRtddeEDTGIYVSEVDPNSIAAKDGrIREGDQILQINGVDVQN--REEAIALLSEEEKSITL 83


                  .
gi 741978460 1393 L 1393
Cdd:cd06716    84 L 84
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 731-797 1.97e-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: 39.00  E-value: 1.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 741978460  731 GISL----ENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 797
Cdd:cd10831    14 GITLkmneDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSIT---FKIVP 81
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 238-423 2.32e-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: 41.04  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   238 TQLKDDVDMLRRENGQLLRERNLLQQswedMKRLHEEDQKEIGDLRAQQQQVL-KHNGSSEILNKLYDTAMDKLEVVKKd 316
Cdd:pfam15619   14 KELQNELAELQSKLEELRKENRLLKR----LQKRQEKALGKYEGTESELPQLIaRHNEEVRVLRERLRRLQEKERDLER- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   317 ydALRKRYSEkvaIH--NSDLSRLEQM--------EEENQRLLKQTEMLTQQRDTAIQ-LQHQCALSLRRFeaiHHELNK 385
Cdd:pfam15619   89 --KLKEKEAE---LLrlRDQLKRLEKLsedknlaeREELQKKLEQLEAKLEDKDEKIQdLERKLELENKSF---RRQLAA 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 741978460   386 ATAQNKDLQWEMELLQSELTELRTtqaktaKESEKYKE 423
Cdd:pfam15619  161 EKKKHKEAQEEVKILQEEIERLQQ------KLKEKERE 192
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1325-1383 2.35e-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: 38.67  E-value: 2.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460 1325 GSEPLGISIVsgekGGV------YVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1383
Cdd:cd06753     6 GPAPWGFRLQ----GGKdfnqplTISRVTPGGKAAQANLRPGDVILAINGESTEGMTHLEAQNKI 66
mukB PRK04863
chromosome partition protein MukB;
147-608 2.36e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  147 ENLSIQLRlmtRERNELRKRLAFAThgttFDKRPYHRLNPDYERLKIQCVR---------AMSDLQSLQSQHTNALKRCE 217
Cdd:PRK04863  785 EKRIEQLR---AEREELAERYATLS----FDVQKLQRLHQAFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHE 857

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  218 EVaketdfyhtlHSRLLSDQTQLKDDVDMLRRENGQL-LRERNLLQQswedmkRLhEEDQKEIGDLRAQQQQVLKHNGSS 296
Cdd:PRK04863  858 SQ----------EQQQRSQLEQAKEGLSALNRLLPRLnLLADETLAD------RV-EEIREQLDEAEEAKRFVQQHGNAL 920

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  297 EILNKLYDTamdkLEVVKKDYDALRKRYsekvaihnsdlsrlEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLrrf 376
Cdd:PRK04863  921 AQLEPIVSV----LQSDPEQFEQLKQDY--------------QQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEM--- 979

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  377 eaihheLNKATAQNKDLQWEMELLQSELTELRtTQAKTAK-ESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEV-E 454
Cdd:PRK04863  980 ------LAKNSDLNEKLRQRLEQAEQERTRAR-EQLRQAQaQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPAdS 1052

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  455 LAESKLKSSTSEkkaASEEMEALRQIKDTVTMDAGRANKEAEILRKQCKAL---CQELKEALQEADVAKC---RRDwafq 528
Cdd:PRK04863 1053 GAEERARARRDE---LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLerdYHEMREQVVNAKAGWCavlRLV---- 1125

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  529 eRDKIVAERDSIRTLC----DNLRRERDRAVSELA----------EALRSLDDTRKQKN------DVSRELK-------- 580
Cdd:PRK04863 1126 -KDNGVERRLHRRELAylsaDELRSMSDKALGALRlavadnehlrDVLRLSEDPKRPERkvqfyiAVYQHLRerirqdii 1204

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 741978460  581 ------ELKEQMESQL-----EKEARFRHLmAHSSHDSA 608
Cdd:PRK04863 1205 rtddpvEAIEQMEIELsrlteELTSREQKL-AISSESVA 1242
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 707-794 2.41e-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: 38.91  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  707 RRRKSLGGKVVTPLHINLSGHKDSgislENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQD 786
Cdd:cd06715     9 RENGSLGFNIIGGRPCENNQEGSS----SEGIYVSKIVENGPAADEGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKE 84


                  ....*...
gi 741978460  787 SLTLSLLK 794
Cdd:cd06715    85 PIVVQVLR 92
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1570-1626 2.67e-03

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: 37.56  E-value: 2.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460 1570 RALYERLAEVEPELSFKKDDILYVDDTlpqgSFGSWmaWqLDENAQKMQRGQIPSKY 1626
Cdd:cd11845     3 VALYDYEARTDDDLSFKKGDRLQILDD----SDGDW--W-LARHLSTGKEGYIPSNY 52
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 617-697 2.78e-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: 38.84  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  617 ETEVVEFERETEdidlKALGFDMAEGVNEPCLPGD----CGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQ 690
Cdd:cd06671     1 PPRRVELWREPG----KSLGISIVGGRVMGSRLSNgeeiRGIFIKHVLEDSPAGrnGTLKTGDRILEVNGVDLRNATHEE 76


                  ....*..
gi 741978460  691 AIKALLN 697
Cdd:cd06671    77 AVEAIRN 83
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 635-708 2.82e-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: 38.91  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  635 LGFDMAEGvnEPCL-----PGDCGIFVTKV-DKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 707
Cdd:cd06715    14 LGFNIIGG--RPCEnnqegSSSEGIYVSKIvENGPAADeGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKEPIVVQVL 91


                  .
gi 741978460  708 R 708
Cdd:cd06715    92 R 92
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 719-792 2.85e-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: 38.77  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  719 PLHINLSGHKDSGiSLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 792
Cdd:cd06679    12 SLGISVAGGRGSR-RGDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSIVL 84
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 742-792 2.89e-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: 38.38  E-value: 2.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 741978460  742 AVVPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 792
Cdd:cd06710    26 CVVRGSPADVAG-LKAGDQILAVNGINVSKASHEDVVKLIGKCTGVLRLVI 75
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 253-597 2.92e-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: 41.83  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   253 QLLRERNLLQqswEDMKRLHEEDQKEIGDLRAQQQQVLKhngssEIlnklydtamdklevvkKDYDALRKRYSEKVAihn 332
Cdd:pfam13868   95 EKLQEREQMD---EIVERIQEEDQAEAEEKLEKQRQLRE-----EI----------------DEFNEEQAEWKELEK--- 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   333 sdlsrlEQMEEENQRLLKQTEMLTQQRDTAIQLQhqcalsLRRFEAihhelnkataqnkdlqwemelLQSELTELRTTQA 412
Cdd:pfam13868  148 ------EEEREEDERILEYLKEKAEREEEREAER------EEIEEE---------------------KEREIARLRAQQE 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   413 KTakesEKYKEERDAVyseyklimserdqvisELDKLQTEVElAESKLKsstsEKKAASEEMEALRQIKdtvtmdagRAN 492
Cdd:pfam13868  195 KA----QDEKAERDEL----------------RAKLYQEEQE-RKERQK----EREEAEKKARQRQELQ--------QAR 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   493 KEAEILRKQCKALCQELKEALQEadvaKCRRDWAFQER-DKIVAERdsirtlcdnlRRERDRavsELAEALRSLDDTRKQ 571
Cdd:pfam13868  242 EEQIELKERRLAEEAEREEEEFE----RMLRKQAEDEEiEQEEAEK----------RRMKRL---EHRRELEKQIEEREE 304

                          330       340
                   ....*....|....*....|....*...
gi 741978460   572 --KNDVSRELKELKEQMESQLEKEARFR 597
Cdd:pfam13868  305 qrAAEREEELEEGERLREEEAERRERIE 332
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 1472-1549 2.94e-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: 38.19  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1472 RVVFIKKSQLELGVHL-CGGNLHGVFVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVRSKTVEEVyVEMLKP-KDSVRLK 1548
Cdd:cd06768     1 RLCHLVKGPEGYGFNLhAEKGRPGHFIREVDPGSPAeRA--GLKDGDRLVEVNGENVEGESHEQV-VEKIKAsGNQVTLL 77


                  .
gi 741978460 1549 V 1549
Cdd:cd06768    78 V 78
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 240-475 2.96e-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: 41.26  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   240 LKDDVDMLRRENGQLLrernllQQSWEDMKRLHEEDQKEigDLRAQQQQVLKHngSSEILNKLYDTAMDKLEVVKKDYDA 319
Cdd:pfam17078    8 LHDQIDALTKTNLQLT------VQSQNLLSKLEIAQQKE--SKFLENLASLKH--ENDNLSSMLNRKERRLKDLEDQLSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   320 LRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHqcalslRRFEAIHHELNKATAQNKDLQWEMEL 399
Cdd:pfam17078   78 LKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQN------EYKDHYQQEINTLQESLEDLKLENEK 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460   400 LQSELTELRTTQAKTAKES-EKYKEERDAVYSEYKLIMSErdqVISELDKLQTEVELAESKLKSSTSEKKA--ASEEME 475
Cdd:pfam17078  152 QLENYQQRISSNDKDIDTKlDSYNNKFKNLDNIYVNKNNK---LLTKLDSLAQLLDLPSWLNLYPESRNKIleYAEKME 227
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 737-790 2.97e-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: 2.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 741978460  737 GVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06667    23 GVVVKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRL 76
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 1320-1379 3.01e-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: 38.78  E-value: 3.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1320 VKLQKGSEPLGISIVSGE--------KGGVYVSKVTGGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1379
Cdd:cd06695     4 VKLTKGSSGLGFSFLGGEnnspedpfSGLVRIKKLFPGQPAAESGlIQEGDVILAVNGEPLKGLSYQEV 72
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
140-586 3.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  140 RQVNEKVENLsIQLRLMTRERNELRKRLAfathgtTFDKRpYHRLNPDYERLKiqcvRAMSDLQSLQSQHTNALKRCEEV 219
Cdd:COG4717   115 REELEKLEKL-LQLLPLYQELEALEAELA------ELPER-LEELEERLEELR----ELEEELEELEAELAELQEELEEL 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  220 AKETDFyhtlhsRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRlhEEDQKEIGDLRAQQQQVL--------- 290
Cdd:COG4717   183 LEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--ELEQLENELEAAALEERLkearlllli 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  291 ------------------------------------------KHNGSSEILNKLYDTAMDKLEvvKKDYDALRKRYSEKV 328
Cdd:COG4717   255 aaallallglggsllsliltiagvlflvlgllallflllareKASLGKEAEELQALPALEELE--EEELEELLAALGLPP 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  329 AIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCAL-------SLRRFEAIHHELNKAtaqnKDLQWEMELLQ 401
Cdd:COG4717   333 DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagveDEEELRAALEQAEEY----QELKEELEELE 408

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  402 SELTELrttqaktAKESEKYKEERDavyseyklimseRDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALrqik 481
Cdd:COG4717   409 EQLEEL-------LGELEELLEALD------------EEELEEELEELEEELEELEEELEELREELAELEAELEQL---- 465

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  482 dtvtmdaGRANKEAEILRKQckalcQELKEALQEAdvakcRRDWAfqerdKIVAERDSIRTLCDNLRRERDRAVSELA-E 560
Cdd:COG4717   466 -------EEDGELAELLQEL-----EELKAELREL-----AEEWA-----ALKLALELLEEAREEYREERLPPVLERAsE 523

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 741978460  561 ALRSLDDTR--------------KQKNDVSRELKEL----KEQM 586
Cdd:COG4717   524 YFSRLTDGRyrliridedlslkvDTEDGRTRPVEELsrgtREQL 567
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 431-615 3.26e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.67  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   431 EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEM-EALRQIKDTVTMD-AGRANKEAEILRKQckalcQE 508
Cdd:pfam09787   48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSrEQLQELEEQLATErSARREAEAELERLQ-----EE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   509 LKEALQEADVAKCRRDWAFQERDKIVAE-RDSIRTlcdnlRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQME 587
Cdd:pfam09787  123 LRYLEEELRRSKATLQSRIKDREAEIEKlRNQLTS-----KSQSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLV 197

                          170       180
                   ....*....|....*....|....*....
gi 741978460   588 SQLEK-EARFRHLMAHSSHDSAIDTDSME 615
Cdd:pfam09787  198 LQLERmEQQIKELQGEGSNGTSINMEGIS 226
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 738-790 3.27e-03

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: 38.57  E-value: 3.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 741978460  738 VYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 790
Cdd:cd06796    28 IYISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKL 80
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
357-516 3.43e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.17  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  357 QQRDTAIQlQHQCalslrrfeaiHHELNKATAQNKDLQWEMELLQSElTELRTTQAKTAKESEKYKEERDAVYSEYKLIM 436
Cdd:COG2268   208 AERETEIA-IAQA----------NREAEEAELEQEREIETARIAEAE-AELAKKKAEERREAETARAEAEAAYEIAEANA 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  437 SERDQVISELDKLQTEVELAESKLKSSTSEKKA---ASEEMEALRQIKdtvtmdagRANKEAEILRKQCKALCqELKEAL 513
Cdd:COG2268   276 EREVQRQLEIAEREREIELQEKEAEREEAELEAdvrKPAEAEKQAAEA--------EAEAEAEAIRAKGLAEA-EGKRAL 346


                  ...
gi 741978460  514 QEA 516
Cdd:COG2268   347 AEA 349
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 741-797 3.48e-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: 38.31  E-value: 3.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  741 AAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 797
Cdd:cd10830    28 ARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVS---LKVIP 81
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 338-456 3.75e-03

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 40.55  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   338 LEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELN-------KATAQNK-------DLQWEMELLQSE 403
Cdd:pfam14662   31 VETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNsleearrSLLAQNKqlekenqSLLQEIESLQEE 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460   404 LTELRTTQ---AKTAKESEKYKEERDAVYSEYKLIMSERDQVISEldKLQTEVELA 456
Cdd:pfam14662  111 NKKNQAERdklQKKKKELLKSKACLKEQLHSCEDLACNRETILIE--KTTQIEELK 164
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 737-766 3.77e-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: 3.77e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 741978460  737 GVYAAAVVPGSPAAkeGSLAVGDRIVAING 766
Cdd:cd23080     1 GVYVLSVVENMPAK--GILEAGDKITAIDG 28
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 245-431 3.87e-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: 41.06  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  245 DMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQqvlKHNGSSEILNKLYDTAMDKLEVVK--KDYDALRK 322
Cdd:COG1579    20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRnnKEYEALQK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  323 rysekvaihnsdlsRLEQMEEENQRLlkqtemltqqRDTAIQLQHqcalslrRFEAIHHELNKATAQNKDLQwemELLQS 402
Cdd:COG1579    97 --------------EIESLKRRISDL----------EDEILELME-------RIEELEEELAELEAELAELE---AELEE 142

                         170       180
                  ....*....|....*....|....*....
gi 741978460  403 ELTELRTTQAKTAKESEKYKEERDAVYSE 431
Cdd:COG1579   143 KKAELDEELAELEAELEELEAEREELAAK 171
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
 1570-1627 3.94e-03

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: 37.36  E-value: 3.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460 1570 RALYERLAEVEPELSFKKDDILYVDDTLPQgsfGSWMAWQLDENAQkmqrGQIPSKYV 1627
Cdd:cd11858     3 KALYDFAGSVANELSLKKDDIVYIVQKEDN---GWWLAKKLDESKE----GWVPAAYL 53
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 731-766 3.99e-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: 3.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 741978460  731 GISLENGVYAAAVVPGSPAAKEGsLAVGDRIVAING 766
Cdd:cd10839    20 GLKEPKGALVAQVLPDSPAAKAG-LKAGDVILSLNG 54
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 653-717 4.03e-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: 4.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460  653 GIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQaikallngegainmVVRRRKSLGGKVV 717
Cdd:cd06768    24 GHFIREVDPGSPAErAGLKDGDRLVEVNGENVEGESHEQ--------------VVEKIKASGNQVT 75
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 719-766 4.08e-03

PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This INAD-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467278 [Multi-domain]  Cd Length: 82  Bit Score: 37.88  E-value: 4.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 741978460  719 PLHINLSGHKDSgisLENGVYAAAVVPGSPAAKEGSLAVGDRIVAING 766
Cdd:cd23065    10 PLGVSVVGGKNH---VTTGCIITHIYPNSIVAADKRLKVFDQILDING 54
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 479-582 4.26e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 39.76  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  479 QIKDTVTmDAGRANKEAEILRKQCKalcQELKEALQEA----DVAKCR--------RDWAFQERDKIVAERDSirtlcdN 546
Cdd:PRK05759   39 KIADGLA-AAERAKKELELAQAKYE---AQLAEARAEAaeiiEQAKKRaaqiieeaKAEAEAEAARIKAQAQA------E 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 741978460  547 LRRERDRAVSEL-----------AEAL--RSLDDTrKQKNDVSRELKEL 582
Cdd:PRK05759  109 IEQERKRAREELrkqvadlavagAEKIlgRELDAA-AQSDLIDKLIAEL 156
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1330-1395 4.34e-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: 37.71  E-value: 4.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741978460 1330 GISIvsgeKGGVYVSKVTGGS-IAHQAGLEYGDQLLEFNGINL--RSATEQQARLIIGQQCDTITILAQ 1395
Cdd:cd06765    11 GISL----ENGVFISRIVPGSpAAKEGSLTVGDRIIAINGIALdnKSLSECEALLRSCRDSLSLSLMKV 75
cpPDZ_MBTPS2-like cd06775
circularly permuted PDZ domain of membrane-bound transcription factor site-2 protease (MBTPS2, ...
 1493-1528 4.40e-03

circularly permuted PDZ domain of membrane-bound transcription factor site-2 protease (MBTPS2, also known as S2P) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MBTPS2, also known as sterol regulatory element-binding protein (SREBP) Site-2 protease (S2P), and related domains. MBTPS2 is a zinc metalloprotease (MEROPS family M50A). In the Golgi, it catalyzes the second step in the proteolytic activation of sterol regulatory element-binding proteins (SREBPs), releasing the transcriptionally active N-terminal domain of SREBP, which then enters the nucleus and activates genes encoding the low density lipoprotein (LDL) receptor and enzymes for cholesterol and fatty acid biosynthesis. MBTPS2 also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF6. ATF6 is a membrane-bound transcription factor that activates genes in the endoplasmic reticulum (ER) stress response. 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. One permutation places beta-strand A on the C-terminus, another permutation places both beta-strands A and B on the C-terminus.


Pssm-ID: 467619 [Multi-domain]  Cd Length: 107  Bit Score: 38.76  E-value: 4.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 741978460 1493 HGVFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRS 1528
Cdd:cd06775    35 SGVVVTEVVENSPVSGPRGLFVGDVITSINDCPVTS 70
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 743-783 4.46e-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: 4.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 741978460  743 VVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 783
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 ...
 653-707 4.57e-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: 4.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 741978460  653 GIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 707
Cdd:cd23063    31 GIFIKGIIPDSPAHkcGRLKVGDRILSVNGNDVRNSTEQAAIDLIKEADFKIVLEIQ 87
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 1496-1550 4.64e-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: 37.12  E-value: 4.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  1496 FVAEVEDDSPA-RGpdGLVPGDLILEYGGLDVRSKtveEVYVEMLK--PKDSVRLKVQ 1550
Cdd:pfam17820    1 VVTAVVPGSPAeRA--GLRVGDVILAVNGKPVRSL---EDVARLLQgsAGESVTLTVR 53
F-BAR_srGAP1 cd07683
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
 332-453 4.72e-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: 40.82  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  332 NSDLSRLEQMEEENQRLLKQT-EMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEME--------LLQS 402
Cdd:cd07683    98 NNVIMRFMQISEDSTRMFKKSkEIAFQLHEDLMKVLNELYTVMKTYHMYHTESISAESKLKEAEKQEEkqigrsgdPVFH 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 741978460  403 ELTELRTTQAKTAKESEKYKEERDAVYSEYKL-IMSERDQVISELDKLQTEV 453
Cdd:cd07683   178 IRLEDRHQRRSSVKKIEKMKEKRQAKYSENKLkSIKARNEYLLTLEATNASV 229
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 250-480 4.73e-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: 41.76  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   250 ENGQLLRERNLLQQSWEDMKRLhEEDQKEIGDLRAQQQQVLK------HNGSSEILNKLYDTAMDKLEVVKKDYDALRKR 323
Cdd:pfam06160  170 ESGDYLEAREVLEKLEEETDAL-EELMEDIPPLYEELKTELPdqleelKEGYREMEEEGYALEHLNVDKEIQQLEEQLEE 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   324 YSEkvAIHNSDLsrlEQMEEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAihhELNKATAQNKDLQWEMELLQ-- 401
Cdd:pfam06160  249 NLA--LLENLEL---DEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIED---YLEHAEEQNKELKEELERVQqs 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   402 -----SELTELRTTQAKTAKESEKYK------EERDAVYSEyklIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAA 470
Cdd:pfam06160  321 ytlneNELERVRGLEKQLEELEKRYDeiverlEEKEVAYSE---LQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEA 397

                          250
                   ....*....|
gi 741978460   471 SEEMEALRQI 480
Cdd:pfam06160  398 REKLDEFKLE 407
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 398-594 5.02e-03

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: 41.42  E-value: 5.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   398 ELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQVISEL----DKLQTEVELAESKLKSSTSEKKAASEE 473
Cdd:pfam07888   30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELesrvAELKEELRQSREKHEELEEKYKELSAS 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   474 MEALRQIKDTVTmdAGRANKEAEI--LRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRER 551
Cdd:pfam07888  110 SEELSEEKDALL--AQRAAHEARIreLEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 741978460   552 DRAVSELAEALRSLDDTRKQ----KNDVSRELKELKEQMESQLEKEA 594
Cdd:pfam07888  188 RSLSKEFQELRNSLAQRDTQvlqlQDTITTLTQKLTTAHRKEAENEA 234
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 495-647 5.06e-03

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: 41.42  E-value: 5.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   495 AEILRKQCKALCQELKEALQEADVAKCRRdwafqERDKIVAERDsiRTLCDNLRRERDRAVSELAEALRSL----DDTRK 570
Cdd:pfam07888   29 AELLQNRLEECLQERAELLQAQEAANRQR-----EKEKERYKRD--REQWERQRRELESRVAELKEELRQSrekhEELEE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   571 QKNDVSRELKELKEQ----MESQLEKEARFRHL------MAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMA 640
Cdd:pfam07888  102 KYKELSASSEELSEEkdalLAQRAAHEARIRELeediktLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181


                   ....*..
gi 741978460   641 EGVNEPC 647
Cdd:pfam07888  182 QTEEELR 188
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 127-626 5.25e-03

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: 41.96  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   127 TGKAPSPP--PVLSD---------RQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTT------FDKRPYHRLNPDYE 189
Cdd:TIGR00606  563 TSLLGYFPnkKQLEDwlhskskeiNQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklFDVCGSQDEESDLE 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   190 RLKIQCVRAMSDLQSLQ------SQHTNALKR--------CEEV----AKETDFYHTLHSRLLSDQTQLKDdvdmLRREN 251
Cdd:TIGR00606  643 RLKEEIEKSSKQRAMLAgatavySQFITQLTDenqsccpvCQRVfqteAELQEFISDLQSKLRLAPDKLKS----TESEL 718

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   252 GQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQV------LKHNGSSEilNKLYDTAMDKLEVVKkdydalrkrys 325
Cdd:TIGR00606  719 KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVnrdiqrLKNDIEEQ--ETLLGTIMPEEESAK----------- 785

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   326 ekvaIHNSDLSRLEQMEEENQRLLKQTEMLTQQRD------TAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMEL 399
Cdd:TIGR00606  786 ----VCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH 861

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   400 LQSELTELRTTQ-------AKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASE 472
Cdd:TIGR00606  862 LKSKTNELKSEKlqigtnlQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   473 EMEALRQIKDTVTM-------------DAGRANKEAEI--LRKQCKAlCQELKEALQEaDVAKCRRDWAFQERDKivaer 537
Cdd:TIGR00606  942 KVNDIKEKVKNIHGymkdienkiqdgkDDYLKQKETELntVNAQLEE-CEKHQEKINE-DMRLMRQDIDTQKIQE----- 1014

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   538 dsiRTLCDNL-RRERDRAVSELAEALRSLDDTRKQknDVSRELKELKEQMESQLEKEARfrhlmahssHDSAIDTDSMEW 616
Cdd:TIGR00606 1015 ---RWLQDNLtLRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKR---------NHVLALGRQKGY 1080

                          570
                   ....*....|
gi 741978460   617 ETEVVEFERE 626
Cdd:TIGR00606 1081 EKEIKHFKKE 1090
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 651-710 5.26e-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: 38.03  E-value: 5.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 741978460  651 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK 710
Cdd:cd06674    26 DTGVFVSDIVKGGAAdaDGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGKVRLEVGRLK 87
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 650-686 5.28e-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: 5.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 741978460  650 GDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINK 686
Cdd:cd06714    36 GRLGAYVTKVKPGSVADtvGHLREGDEVLEWNGISLQGK 74
PDZ_ARHGAP21_23-like cd06756
PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1341-1394 5.33e-03

PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGAP21, ARHGAP23, and related domains. This subfamily includes the GAPs (GTPase activating proteins): ARHGAP21 (Rho GTPase-activating protein 21; also known as Rho GTPase-activating protein 10, Rho-type GTPase-activating protein 21) and ARHGAP23 (Rho GTPase-activating protein 23; also known as Rho-type GTPase-activating protein 23). GAPs deactivate Rho GTPases by accelerating GTP hydrolysis. ARHGAP21/23 interact with a planar cell polarity (PCP) protein Pk1 to regulate a lateral signaling pathway in migrating cells. The ARHGAP21 PDZ domain binds claudin-2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGAP21-23-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467238 [Multi-domain]  Cd Length: 109  Bit Score: 38.59  E-value: 5.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 741978460 1341 VYVSKVTGGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITILA 1394
Cdd:cd06756    55 IFVKQVKEGGPAHQAGLCTGDRIVKVNGESVIGKTYSQVIALI-QNSDSTLELS 107
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 200-427 5.72e-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: 41.29  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  200 SDLQSLQSQHTNALKRCEEVAKEtdfyhtlhsrllsdQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEI 279
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  280 GDLRAQ---QQQVLkhngsSEILNKLYDTA-MDKLEVVKKDYDAL----RKRYSEKVAihNSDLSRLEQMEEENQRLLKQ 351
Cdd:COG4942    93 AELRAEleaQKEEL-----AELLRALYRLGrQPPLALLLSPEDFLdavrRLQYLKYLA--PARREQAEELRADLAELAAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  352 TEMLTQQRDTAIQLQHQCALSLRRFEAIHHE----LNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESEKYKEERDA 427
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 218-520 6.08e-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: 41.55  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   218 EVAKETdfyhtlHSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLraqqqqVLKHNGSSE 297
Cdd:pfam05701  127 EVAKAR------HAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEEL------TIELIATKE 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   298 ILNKLYDTamdKLEVVKKDYDALRKRYSEKVAIHNSdlsrLEQMEEENQRLLKQ---TEMLTQQRDTAIQLQHqcalSLR 374
Cdd:pfam05701  195 SLESAHAA---HLEAEEHRIGAALAREQDKLNWEKE----LKQAEEELQRLNQQllsAKDLKSKLETASALLL----DLK 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   375 RfeaihhELNkATAQNK--DLQWEMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLI-------MSERDQVISE 445
Cdd:pfam05701  264 A------ELA-AYMESKlkEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLrvaaaslRSELEKEKAE 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460   446 LDKLQTEVELA-------ESKLKSSTSE-------KKAASEEMEALRQIKDTVTMDAGRANKEAEILRkqckalcQELKE 511
Cdd:pfam05701  337 LASLRQREGMAsiavsslEAELNRTKSEialvqakEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAR-------EELRK 409


                   ....*....
gi 741978460   512 ALQEADVAK 520
Cdd:pfam05701  410 AKEEAEQAK 418
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 655-708 6.29e-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: 6.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 741978460   655 FVTKVDKGSIAD-GRLRVNDWLLRINDVDLinKDKKQAIKALLNGEGA-INMVVRR 708
Cdd:pfam17820    1 VVTAVVPGSPAErAGLRVGDVILAVNGKPV--RSLEDVARLLQGSAGEsVTLTVRR 54
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 296-595 7.22e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 41.36  E-value: 7.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  296 SEILNKLYDTAMDKLEVVKKDYD----ALRKRYSEKVAIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTA-----IQLQ 366
Cdd:PTZ00440 1086 VEALLKKIDENKNKLIEIKNKSHehvvNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLnevneIEIE 1165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  367 HQCALslrrfeaIHHELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKESE------KYKEERDAVYSEYKLIM---- 436
Cdd:PTZ00440 1166 YERIL-------IDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNdhlttfEYNAYYDKATASYENIEeltt 1238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  437 --------SERDQVISELDKLQTEVelaESKLKSSTSEkkaaSEEME-ALRQIKDT----VTMDAGRANKEAEILRKQCK 503
Cdd:PTZ00440 1239 eakglkgeANRSTNVDELKEIKLQV---FSYLQQVIKE----NNKMEnALHEIKNMyeflISIDSEKILKEILNSTKKAE 1311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  504 ALCQELKEALQEADvakcrrDWAFQERDKIVAERDSIRTLCDNLRRER-DRAVSELAEALRSLDDTRKQKNDVSRELKEL 582
Cdd:PTZ00440 1312 EFSNDAKKELEKTD------NLIKQVEAKIEQAKEHKNKIYGSLEDKQiDDEIKKIEQIKEEISNKRKEINKYLSNIKSN 1385

                         330
                  ....*....|...
gi 741978460  583 KEQMESQLEKEAR 595
Cdd:PTZ00440 1386 KEKCDLHVRNASR 1398
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1472-1551 7.25e-03

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: 37.17  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460 1472 RVVFIKKSQLE-LGVHLCGGNLHG--VFVAEVEDDSPARGPDGLVPGDLILEYGGLDVRSKTVEEVyVEMLK-PKDSVRL 1547
Cdd:cd06801     1 RTVRVVKQDVGgLGISIKGGAEHKmpILISKIFKGQAADQTGQLFVGDAILSVNGENLEDATHDEA-VQALKnAGDEVTL 79


                  ....
gi 741978460 1548 KVQY 1551
Cdd:cd06801    80 TVKY 83
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 635-708 7.36e-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: 7.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 741978460  635 LGFDMAEGVNepclpgDCGIFVTK-VDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 708
Cdd:cd06696    16 LGFTVTKGKD------DNGCYIHDiVQDPAKSDGRLRPGDRLIMVNGVDVTNMSHTEAVSLLRAAPKEVTLVLGR 84
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 634-695 7.37e-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: 37.62  E-value: 7.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 741978460  634 ALGFDMAEGVNEPclPGDCGIFVTKVD-KGSIA-DGRLRVNDWLLRINDVDLINKDKKQAIKAL 695
Cdd:cd06679    12 SLGISVAGGRGSR--RGDLPIYVTNVQpDGCLGrDGRIKKGDVLLSINGISLTNLSHSEAVAVL 73
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
140-442 7.64e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 7.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  140 RQVNEKVENLSIQLRLMTRERNELRKRLAfathgttfdkrpyhRLNPDYERLKIQCVRAMSDLQSLQSQHTNALKRCEEV 219
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREELE--------------QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  220 AKETdfyhtlhSRLLSDQTQLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQ------------ 287
Cdd:COG4372   100 QEEL-------ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEslqeelaaleqe 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  288 -QVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKV--AIHNSDLSRLEQMEEENQRLLKQTEMLTQQRDTAIQ 364
Cdd:COG4372   173 lQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRelAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  365 LQHQCALSLRRFEAIHHELNKATAQNKDLQW--EMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEYKLIMSERDQV 442
Cdd:COG4372   253 EEVILKEIEELELAILVEKDTEEEELEIAALelEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
Cep57_CLD_2 pfam14197
Centrosome localization domain of PPC89; The N-terminal region of the fission yeast spindle ...
 545-585 7.74e-03

Centrosome localization domain of PPC89; The N-terminal region of the fission yeast spindle pole body protein PPC89 has low similarity to the human Cep57 protein. The CLD or centrosome localization domain of Cep57 and PPC89 is found at the N-terminus. This region localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57 and PPC89.


Pssm-ID: 372959 [Multi-domain]  Cd Length: 67  Bit Score: 36.88  E-value: 7.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 741978460   545 DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQ 585
Cdd:pfam14197   27 KRLRRERDSAVRQLGVAYLEIQELKAENEALRKELKEQRAQ 67
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 653-695 7.85e-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: 7.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 741978460  653 GIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 695
Cdd:cd06740    28 GIYVSLVEPGSLAEKEgLRVGDQILRVNDVSFEKVTHAEAVKIL 71
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 737-766 8.01e-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: 8.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 741978460  737 GVYAAAVVPGSPAAKEGsLAVGDRIVAING 766
Cdd:cd06785    32 GVYVHKVIPGSPAQRAG-LKDGDVIISING 60
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 743-771 8.05e-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: 8.05e-03
                          10        20
                  ....*....|....*....|....*....
gi 741978460  743 VVPGSPAAKEGsLAVGDRIVAINGIALDN 771
Cdd:cd23081     6 VVANSPAAEAG-LKPGDRILKIDGQKVRT 33
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 651-697 8.39e-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: 37.16  E-value: 8.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 741978460  651 DCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLN 697
Cdd:cd06729    22 DVGIFVAGVQEGSPAEKQgLQEGDQILKVNGVDFRNLTREEAVLFLLD 69
46 PHA02562
endonuclease subunit; Provisional
 304-430 8.42e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  304 DTAMDKLEVVKKDYDALRKRYsEKVAIHNSDLSrlEQMEEENQRLLKQTEMLTQqrdtaIQLQHQcALSLRRFEA--IHH 381
Cdd:PHA02562  295 SEGPDRITKIKDKLKELQHSL-EKLDTAIDELE--EIMDEFNEQSKKLLELKNK-----ISTNKQ-SLITLVDKAkkVKA 365

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 741978460  382 ELNKATAQNKDLQWEMELLQSELTELRTTQAKTAKEsekyKEERDAVYS 430
Cdd:PHA02562  366 AIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE----KYHRGIVTD 410
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 ...
 633-707 8.71e-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: 8.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 741978460  633 KALGFDMAEGVNEPclPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN-GEGAINMVVR 707
Cdd:cd06759    12 KGLGFSIVGGRDSP--RGPMGIYVKTIFPGGAAaeDGRLKEGDEILEVNGESLQGLTHQEAIQKFKQiKKGLVVLTVR 87
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 396-563 9.63e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 9.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  396 EMELLQSELTELRTTQAKTAKESEKYKEERDAVYSEyklimserdqvisELDKLQTEVELAESKLKsstsEKKAASEEME 475
Cdd:COG0542   412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRD-------------ELAELEEELEALKARWE----AEKELIEEIQ 474

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741978460  476 ALRQIKDTVTMDAGRANKEAEILRKQCKALCQELKEALQEADVAkcrrdwafqerdKIVA-------------ERDSIRT 542
Cdd:COG0542   475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIA------------EVVSrwtgipvgkllegEREKLLN 542

                         170       180
                  ....*....|....*....|....*
gi 741978460  543 LCDNLrRER----DRAVSELAEALR 563
Cdd:COG0542   543 LEEEL-HERvigqDEAVEAVADAIR 566
 
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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