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Conserved domains on  [gi|2462521864|ref|XP_054223128|]
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disks large homolog 5 isoform X4 [Homo sapiens]

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 ...
 521-615 9.79e-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: 196.85  E-value: 9.79e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  521 EWETEVVEFQRETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 600
Cdd:cd06764      1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                           90
                   ....*....|....*
gi 2462521864  601 LLNGEGAINMVVRRR 615
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 ...
 1252-1333 2.41e-49

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: 169.81  E-value: 2.41e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1252 EEPRHVKVQKGSEPLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1331
Cdd:cd06767      1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                   ..
gi 2462521864 1332 QY 1333
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 ...
 1405-1485 5.25e-49

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: 168.72  E-value: 5.25e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1405 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1484
Cdd:cd06766      1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                   .
gi 2462521864 1485 Q 1485
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 ...
 627-703 4.58e-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: 151.34  E-value: 4.58e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  627 HINLSGQKDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 703
Cdd:cd06765      1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1638-1814 1.84e-42

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: 153.60  E-value: 1.84e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1638 QKVDCTALRPVLILG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1714
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1715 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylRDKVTQRHSKEQFEAAQKLEQEYsRYFTGVI 1794
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 2462521864  1795 QGGALSSICTQILAMVNQEQ 1814
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1503-1565 1.07e-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: 127.07  E-value: 1.07e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864 1503 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1565
Cdd:cd11860      1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 35-119 5.99e-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: 114.28  E-value: 5.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   35 KAPSPPPLLTDRQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 114
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 2462521864  115 HTNAL 119
Cdd:pfam04822   81 ISEAL 85
dbPDZ_assoc super family cl24984
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1333-1405 1.50e-25

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: 101.90  E-value: 1.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1333 YNPHVHQLSSHSRSSSHLDPAGTHSTLQGSGTTTPEHPSVIDPLMEQDEGPSTPPAKQS--------SSRIAGDANKKTL 1404
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTtpatsphnSFRMPGDANKRVP 80


                   .
gi 2462521864 1405 E 1405
Cdd:pfam16610   81 E 81
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-542 1.24e-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: 89.73  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  244 LEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTtqvk 319
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEE---- 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  320 TAKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAANEEMEALRQIKDTVTM 392
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  393 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 472
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  473 DTRKQKNDVSRELKELKEQMESQLEK--EARFRQLMAHSSHDSAIDTDSMEWETEVVEFQREtedidLKALG 542
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
PRK04778 super family cl32064
septation ring formation regulator EzrA; Provisional
 105-313 2.05e-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: 49.45  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  105 MSDLQSLQNQHTNALK-----RCEEVAKE--------TDFYHTL------HSRLLSDQTRLKDDVDMLRRENGQLLRERN 165
Cdd:PRK04778   255 EKEIQDLKEQIDENLAlleelDLDEAEEKneeiqeriDQLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEID 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  166 LLQQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------AL 226
Cdd:PRK04778   335 RVKQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  227 RKrySEKVAihNADLSRLEQLGEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATA 294
Cdd:PRK04778   410 RK--DELEA--REKLERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATE 483

                          250       260
                   ....*....|....*....|.
gi 2462521864  295 QNKDLQWEMELL--QSELTEL 313
Cdd:PRK04778   484 DVETLEEETEELveNATLTEQ 504
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 780-1209 1.58e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  780 GGPLQVCPQACPSASERSLSSFRSDASGDRGFGLVD---VRGRRPLLPFETEVGPCGVGEAsldKADSEGSNSGGTWPka 856
Cdd:PHA03307    17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAvtvVAGAAACDRFEPPTGPPPGPGT---EAPANESRSTPTWS-- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  857 mlSSTAVPEKlsvykkPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGPAHSPQPSKRAGPLTPPKPPRRSDSIKFQHR--- 933
Cdd:PHA03307    92 --LSTLAPAS------PAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAava 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  934 ------------LETSSESEATLVGSSPSTSppsalpPDVDPGEPMHASPPRKARVRIASSYYPEGDGDSSHLPAKKSCD 1001
Cdd:PHA03307   164 sdaassrqaalpLSSPEETARAPSSPPAEPP------PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1002 EDLTSQKVD-ELGQKRRRPKSAPSFRPKLAPVVIPAQFLEEQKCVPASGELSPELQEWAPYSPGHSSRHSNPPLYPSRPS 1080
Cdd:PHA03307   238 DSSSSESSGcGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1081 VGTVPRSLTPSTTVSSILRNPIYTVRS---HRVGPCSSPPAARDAGPQGLHPSVQHQGRLSldlshrtcsdysemRATHG 1157
Cdd:PHA03307   318 SSSSRESSSSSTSSSSESSRGAAVSPGpspSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP--------------AASAG 383

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1158 SNSLPSSARLGSSSNLQfkaeRIKIPSTPRYPRSVVGSERGSVSHSECSTPP 1209
Cdd:PHA03307   384 RPTRRRARAAVAGRARR----RDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
 
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 ...
 521-615 9.79e-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: 196.85  E-value: 9.79e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  521 EWETEVVEFQRETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 600
Cdd:cd06764      1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                           90
                   ....*....|....*
gi 2462521864  601 LLNGEGAINMVVRRR 615
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 ...
 1252-1333 2.41e-49

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: 169.81  E-value: 2.41e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1252 EEPRHVKVQKGSEPLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1331
Cdd:cd06767      1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                   ..
gi 2462521864 1332 QY 1333
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 ...
 1405-1485 5.25e-49

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: 168.72  E-value: 5.25e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1405 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1484
Cdd:cd06766      1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                   .
gi 2462521864 1485 Q 1485
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 ...
 627-703 4.58e-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: 151.34  E-value: 4.58e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  627 HINLSGQKDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 703
Cdd:cd06765      1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1638-1814 1.84e-42

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: 153.60  E-value: 1.84e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1638 QKVDCTALRPVLILG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1714
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1715 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylRDKVTQRHSKEQFEAAQKLEQEYsRYFTGVI 1794
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 2462521864  1795 QGGALSSICTQILAMVNQEQ 1814
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1503-1565 1.07e-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: 127.07  E-value: 1.07e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864 1503 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1565
Cdd:cd11860      1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 35-119 5.99e-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: 114.28  E-value: 5.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   35 KAPSPPPLLTDRQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 114
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 2462521864  115 HTNAL 119
Cdd:pfam04822   81 ISEAL 85
dbPDZ_assoc pfam16610
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1333-1405 1.50e-25

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: 101.90  E-value: 1.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1333 YNPHVHQLSSHSRSSSHLDPAGTHSTLQGSGTTTPEHPSVIDPLMEQDEGPSTPPAKQS--------SSRIAGDANKKTL 1404
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTtpatsphnSFRMPGDANKRVP 80


                   .
gi 2462521864 1405 E 1405
Cdd:pfam16610   81 E 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1253-1335 7.58e-19

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 82.81  E-value: 7.58e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1253 EPRHVKVQKGSEPLGISIVSG--EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....*
gi 2462521864  1331 AQYNP 1335
Cdd:smart00228   81 VLRGG 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-542 1.24e-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: 89.73  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  244 LEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTtqvk 319
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEE---- 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  320 TAKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAANEEMEALRQIKDTVTM 392
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  393 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 472
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  473 DTRKQKNDVSRELKELKEQMESQLEK--EARFRQLMAHSSHDSAIDTDSMEWETEVVEFQREtedidLKALG 542
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
Guanylate_kin pfam00625
Guanylate kinase;
1646-1813 3.49e-16

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 78.58  E-value: 3.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1646 RPVLILGPLL---DVVKEMLVNEAPGKFCRC---------PLEVMK-----ASQQAIERGVKDCLFVDYKRRSGHFDVTT 1708
Cdd:pfam00625    3 RPVVLSGPSGvgkSHIKKALLSEYPDKFGYSvphttrpprKGEVDGkdyyfVSKEEMERDISANEFLEYAQFSGNMYGTS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1709 VASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSakhIKEQRDPIYLRDKVTQRHSKEQFEAAQKLEQEYSr 1788
Cdd:pfam00625   83 VETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPS---LKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE- 158

                          170       180
                   ....*....|....*....|....*
gi 2462521864 1789 yFTGVIQGGALSSICTQILAMVNQE 1813
Cdd:pfam00625  159 -FDVIIVNDDLEEAYKKLKEALEAE 182
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1405-1488 1.46e-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: 67.79  E-value: 1.46e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1405 EPRVVFIKKSQLELGVHLCGG--NLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRL 1482
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79


                    ....*.
gi 2462521864  1483 KVQYRP 1488
Cdd:smart00228   80 TVLRGG 85
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 621-699 9.39e-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: 65.48  E-value: 9.39e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864   621 KVVTPLHINLSGQKDSGisleNGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:smart00228    9 KGGGGLGFSLVGGKDEG----GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
53-520 1.99e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 72.38  E-value: 1.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   53 ENLSIQLRLMTRERNELRKRLAFATHGTAFDkrpyhrlNPDYERLKIQcvraMSDLQslqnqhtnalKRCEEVAKETDFY 132
Cdd:PRK02224   275 EELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEAR----REELE----------DRDEELRDRLEEC 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  133 HTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILnklYDTA 212
Cdd:PRK02224   334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD---LGNA 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  213 MDKLEVVKKDYDALRkrysEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAiQLQHQCALSLRRfeaihHELNKA 292
Cdd:PRK02224   411 EDFLEELREERDELR----EREAELEATLRTARERVEEAEALLEAGKCPECGQPVE-GSPHVETIEEDR-----ERVEEL 480

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  293 TAQNKDLQWEMELLQSELTELrTTQVKTAKESEKYREERDAV---YSEYKLIMSERDQVISEL----DKLQTEVELAESK 365
Cdd:PRK02224   481 EAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELreraAELEAEAEEKREA 559

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  366 LKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILrkqckALCQELKEALQEadVAKCRRDWAF---QERDKIVAE 442
Cdd:PRK02224   560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-----AAIADAEDEIER--LREKREALAElndERRERLAEK 632

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  443 RDSIRTLCDNL--------RRERDRAVSELAEALRSLDDTRKQKND-------VSRELKELKEQMESQLEKEARFRQLma 507
Cdd:PRK02224   633 RERKRELEAEFdearieeaREDKERAEEYLEQVEEKLDELREERDDlqaeigaVENELEELEELRERREALENRVEAL-- 710

                          490
                   ....*....|...
gi 2462521864  508 HSSHDSAIDTDSM 520
Cdd:PRK02224   711 EALYDEAEELESM 723
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 121-505 5.10e-12

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: 71.36  E-value: 5.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  121 RCEEVAKETDFYHTLHSRLLSDQTRLKDDVDmlrRENGQLLRERNLLQQSWEDM-KRLHE-EDQKeigdlRAQQQQVLKH 198
Cdd:pfam01576  626 RAEAEAREKETRALSLARALEEALEAKEELE---RTNKQLRAEMEDLVSSKDDVgKNVHElERSK-----RALEQQVEEM 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  199 NGSSEILNKLYDTAMD---KLEVvkkDYDALRkrysekvAIHNADLSRLEQLGEENQR-LLKQT-EMLTQ------QRDT 267
Cdd:pfam01576  698 KTQLEELEDELQATEDaklRLEV---NMQALK-------AQFERDLQARDEQGEEKRRqLVKQVrELEAElederkQRAQ 767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  268 AIQLQHQCALSLRRFEAIHHELNK----ATAQNKDLQWEMELLQSELTELRTTQ---VKTAKESEKYRE--ERDAVYSEY 338
Cdd:pfam01576  768 AVAAKKKLELDLKELEAQIDAANKgreeAVKQLKKLQAQMKDLQRELEEARASRdeiLAQSKESEKKLKnlEAELLQLQE 847

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  339 KLIMSER--DQVISELDKLQTEVELAESKlKSSTSEKKaaneemealRQIKDTVTMdagrankeveilrkqckaLCQELK 416
Cdd:pfam01576  848 DLAASERarRQAQQERDELADEIASGASG-KSALQDEK---------RRLEARIAQ------------------LEEELE 899

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  417 EALQEADVAKCRRDWAFQERDKIVAERDSIRTLC---DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK-EQM 492
Cdd:pfam01576  900 EEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSqksESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKiAQL 979

                          410
                   ....*....|...
gi 2462521864  493 ESQLEKEARFRQL 505
Cdd:pfam01576  980 EEQLEQESRERQA 992
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 154-491 1.67e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  154 RRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngsseilnklydtamdKLEVVKKDYDALRKRYSEK 233
Cdd:COG1196    224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-----------------ELEELRLELEELELELEEA 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  234 VAIHNADLSRLEQLGEENQRllkQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTEL 313
Cdd:COG1196    287 QAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  314 RTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMD 393
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  394 AGRANKEVEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIvaerdsirtlcDNLRRERDRAVSELaEALRSLDD 473
Cdd:COG1196    444 LEEAAEEEAELEEEEEALLELLAELLEEAA----------LLEAAL-----------AELLEELAEAAARL-LLLLEAEA 501

                          330
                   ....*....|....*...
gi 2462521864  474 TRKQKNDVSRELKELKEQ 491
Cdd:COG1196    502 DYEGFLEGVKAALLLAGL 519
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1262-1332 1.63e-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: 1.63e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1262 GSEPLGISIVSGEKG---GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1332
Cdd:pfam00595    8 GRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1500-1562 2.77e-09

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


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 54.47  E-value: 2.77e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  1500 DSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWMAWQLDENaqkiQRGQIPSKYV 1562
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG----WWKGRLGRG----KEGLFPSNYV 55
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 523-616 3.68e-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: 55.08  E-value: 3.68e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   523 ETEVVEFQRETEDidlkaLGFDMAEGVNEpcfpgDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 601
Cdd:smart00228    1 EPRLVELEKGGGG-----LGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                            90
                    ....*....|....*
gi 2462521864   602 LNGEGAINMVVRRRK 616
Cdd:smart00228   71 KKAGGKVTLTVLRGG 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
50-421 6.12e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 6.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   50 EKVENLSIQLRLMTRERNELRKRLAfathgtafDKRPYHRLnpdYERLK--------IQCVRAMSDLQSLQNQHTNALKR 121
Cdd:PRK03918   331 KELEEKEERLEELKKKLKELEKRLE--------ELEERHEL---YEEAKakkeelerLKKRLTGLTPEKLEKELEELEKA 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  122 CEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRREN------GQLLRE---RNLLQQSWEDMKRLhEEDQKEIG----DL 188
Cdd:PRK03918   400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEehrKELLEEYTAELKRI-EKELKEIEekerKL 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  189 RAQQQQVLKHNGSSEILNKLYDTA--------------MDKLEVVKKDYDALRKRYSE---KVAIHNADLSRLEQLGEEN 251
Cdd:PRK03918   479 RKELRELEKVLKKESELIKLKELAeqlkeleeklkkynLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEELKKKL 558

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  252 QRLLKQ--------TEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQW---EMELLQSELTELRTTQVKT 320
Cdd:PRK03918   559 AELEKKldeleeelAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEReekELKKLEEELDKAFEELAET 638

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  321 AKESEKYREERDAV---YS--EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTmDAG 395
Cdd:PRK03918   639 EKRLEELRKELEELekkYSeeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLE 717

                          410       420
                   ....*....|....*....|....*..
gi 2462521864  396 RANKEVEILRKQCKALCQELKE-ALQE 421
Cdd:PRK03918   718 KALERVEELREKVKKYKALLKErALSK 744
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-391 1.08e-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: 60.46  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   46 RQVNEKVENLSIQLRLMTRERNELRKRLAfathgtafdkrpyhRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEV 125
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  126 AKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngsseiL 205
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------L 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  206 NKLYDTAMDKLEVVKKDYDALRKRY----------SEKVAIHNADLSRLEQLGEEnqrLLKQTEMLTQQRDtaiQLQHQC 275
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEE---LESELEALLNERA---SLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  276 ALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRT----TQVKTAKESEKYREErdavYS-EYKLIMSERDQVIS 350
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELrlegLEVRIDNLQERLSEE----YSlTLEEAEALENKIED 965

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2462521864  351 ELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 391
Cdd:TIGR02168  966 DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 625-699 4.85e-08

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 51.90  E-value: 4.85e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  625 PLHINLSGQKDSGIsleNGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:pfam00595   11 GLGFSLKGGSDQGD---PGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 323-507 4.34e-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: 52.74  E-value: 4.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  323 ESEKYREERDAVySEYKLIMSERDQVISELDKLQTEV-----ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRA 397
Cdd:cd07596      2 EDQEFEEAKDYI-LKLEEQLKKLSKQAQRLVKRRRELgsalgEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  398 NKEVeilRKQCKALCQELKEALQEADVAKCrrdwAFQERDKIVAERDSIRTLCDNLRRERDRAVS-------ELAEALRS 470
Cdd:cd07596     81 EAQA---NQELVKLLEPLKEYLRYCQAVKE----TLDDRADALLTLQSLKKDLASKKAQLEKLKAapgikpaKVEELEEE 153

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462521864  471 LDDTRKQKNDVSRELKELKEQMESQLE--KEARFRQLMA 507
Cdd:cd07596    154 LEEAESALEEARKRYEEISERLKEELKrfHEERARDLKA 192
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 618-688 4.88e-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: 53.72  E-value: 4.88e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  618 LGGKVVTPLHINLSGQKDS-GISL---ENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 688
Cdd:COG0793     43 LDPEEYEDFQESTSGEFGGlGAELgeeDGKVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLLR 116
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1407-1485 6.02e-06

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 46.12  E-value: 6.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1407 RVVFIKKSQLELGVHLCGGN---LHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLK 1483
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79


                   ..
gi 2462521864 1484 VQ 1485
Cdd:pfam00595   80 IL 81
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 105-313 2.05e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.45  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  105 MSDLQSLQNQHTNALK-----RCEEVAKE--------TDFYHTL------HSRLLSDQTRLKDDVDMLRRENGQLLRERN 165
Cdd:PRK04778   255 EKEIQDLKEQIDENLAlleelDLDEAEEKneeiqeriDQLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEID 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  166 LLQQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------AL 226
Cdd:PRK04778   335 RVKQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  227 RKrySEKVAihNADLSRLEQLGEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATA 294
Cdd:PRK04778   410 RK--DELEA--REKLERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATE 483

                          250       260
                   ....*....|....*....|.
gi 2462521864  295 QNKDLQWEMELL--QSELTEL 313
Cdd:PRK04778   484 DVETLEEETEELveNATLTEQ 504
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 58-382 2.99e-05

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: 49.18  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   58 QLRLMTRERNELRKRLAFAthgtAFDKRPYHRL----------------NPDYERLKIQCVRAMSDLQSLQNQHTNALKR 121
Cdd:COG3096    786 RLEELRAERDELAEQYAKA----SFDVQKLQRLhqafsqfvgghlavafAPDPEAELAALRQRRSELERELAQHRAQEQQ 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  122 CEEVAKETDFYHTLHSRLLSDQTRLKDD-----VDMLRRENGQLLRERNLLQQSWEDMKRLheEDQKEIgdLRAQQQQVl 196
Cdd:COG3096    862 LRQQLDQLKEQLQLLNKLLPQANLLADEtladrLEELREELDAAQEAQAFIQQHGKALAQL--EPLVAV--LQSDPEQF- 936

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  197 khngssEILNKLYDTAMDKLEVVKKDYDAL---RKR-----YSEKVAIHNADLSRLEQLgeeNQRLLKQTEMLTQQRDTA 268
Cdd:COG3096    937 ------EQLQADYLQAKEQQRRLKQQIFALsevVQRrphfsYEDAVGLLGENSDLNEKL---RARLEQAEEARREAREQL 1007

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  269 IQLQHQCALSLRRFEAIhhelnKATAQNKdlqweMELLQSELTELRTTQVKTAKESE-KYREERDAVYSEYKLIMSERDQ 347
Cdd:COG3096   1008 RQAQAQYSQYNQVLASL-----KSSRDAK-----QQTLQELEQELEELGVQADAEAEeRARIRRDELHEELSQNRSRRSQ 1077

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2462521864  348 VISELDKLQTEVELAESKLKSSTSEKKAANEEMEA 382
Cdd:COG3096   1078 LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 541-613 4.35e-05

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 43.42  E-value: 4.35e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  541 LGFDMAEGVNEpcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 613
Cdd:pfam00595   12 LGFSLKGGSDQ----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 89-391 2.30e-04

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: 46.17  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   89 RLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQL-------L 161
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeqikklQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  162 RERNLLQQSWEDMKRLHEEDQKEIGDLRAQ----QQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVaih 237
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE--- 495

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  238 nadlSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcaLSLR------------------------------------R 281
Cdd:TIGR04523  496 ----KELKKLNEEKKELEEKVKDLTKKISSLKEKIEK--LESEkkekeskisdledelnkddfelkkenlekeideknkE 569

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  282 FEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVEL 361
Cdd:TIGR04523  570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649

                          330       340       350
                   ....*....|....*....|....*....|
gi 2462521864  362 AESKLksstseKKAANEEMEALRQIKDTVT 391
Cdd:TIGR04523  650 IKETI------KEIRNKWPEIIKKIKESKT 673
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
1266-1331 5.21e-04

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 44.81  E-value: 5.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1266 LGISiVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSAT--EQQARLIIGqqcDTITILA 1331
Cdd:COG3975    485 LGLR-VSADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTADNldDALAAYKPG---DPIELLV 548
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1428-1484 6.09e-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: 43.60  E-value: 6.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1428 HGVFVAEVEDDSPA-KGpdGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1484
Cdd:COG0265    201 EGVLVARVEPGSPAaKA--GLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTV 256
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 780-1209 1.58e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  780 GGPLQVCPQACPSASERSLSSFRSDASGDRGFGLVD---VRGRRPLLPFETEVGPCGVGEAsldKADSEGSNSGGTWPka 856
Cdd:PHA03307    17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAvtvVAGAAACDRFEPPTGPPPGPGT---EAPANESRSTPTWS-- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  857 mlSSTAVPEKlsvykkPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGPAHSPQPSKRAGPLTPPKPPRRSDSIKFQHR--- 933
Cdd:PHA03307    92 --LSTLAPAS------PAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAava 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  934 ------------LETSSESEATLVGSSPSTSppsalpPDVDPGEPMHASPPRKARVRIASSYYPEGDGDSSHLPAKKSCD 1001
Cdd:PHA03307   164 sdaassrqaalpLSSPEETARAPSSPPAEPP------PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1002 EDLTSQKVD-ELGQKRRRPKSAPSFRPKLAPVVIPAQFLEEQKCVPASGELSPELQEWAPYSPGHSSRHSNPPLYPSRPS 1080
Cdd:PHA03307   238 DSSSSESSGcGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1081 VGTVPRSLTPSTTVSSILRNPIYTVRS---HRVGPCSSPPAARDAGPQGLHPSVQHQGRLSldlshrtcsdysemRATHG 1157
Cdd:PHA03307   318 SSSSRESSSSSTSSSSESSRGAAVSPGpspSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP--------------AASAG 383

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1158 SNSLPSSARLGSSSNLQfkaeRIKIPSTPRYPRSVVGSERGSVSHSECSTPP 1209
Cdd:PHA03307   384 RPTRRRARAAVAGRARR----RDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 144-329 1.88e-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: 41.43  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  144 TRLKDDVDMLRRENGQLLRERNLLQQswedMKRLHEEDQKEIGDLRAQQQQVL-KHNGSSEILNKLYDTAMDKLEVVKKd 222
Cdd:pfam15619   14 KELQNELAELQSKLEELRKENRLLKR----LQKRQEKALGKYEGTESELPQLIaRHNEEVRVLRERLRRLQEKERDLER- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  223 ydALRKRYSEkvaIH--NADLSRLEQLG--------EENQRLLKQTEMLTQQRDTAIQ-LQHQCALSLRRFeaiHHELNK 291
Cdd:pfam15619   89 --KLKEKEAE---LLrlRDQLKRLEKLSedknlaerEELQKKLEQLEAKLEDKDEKIQdLERKLELENKSF---RRQLAA 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462521864  292 ATAQNKDLQWEMELLQSELTELRTtqvktaKESEKYRE 329
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 ...
 521-615 9.79e-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: 196.85  E-value: 9.79e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  521 EWETEVVEFQRETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 600
Cdd:cd06764      1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                           90
                   ....*....|....*
gi 2462521864  601 LLNGEGAINMVVRRR 615
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 ...
 1252-1333 2.41e-49

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: 169.81  E-value: 2.41e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1252 EEPRHVKVQKGSEPLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1331
Cdd:cd06767      1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                   ..
gi 2462521864 1332 QY 1333
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 ...
 1405-1485 5.25e-49

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: 168.72  E-value: 5.25e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1405 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1484
Cdd:cd06766      1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                   .
gi 2462521864 1485 Q 1485
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 ...
 627-703 4.58e-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: 151.34  E-value: 4.58e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  627 HINLSGQKDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 703
Cdd:cd06765      1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1638-1814 1.84e-42

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: 153.60  E-value: 1.84e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1638 QKVDCTALRPVLILG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1714
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1715 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylRDKVTQRHSKEQFEAAQKLEQEYsRYFTGVI 1794
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 2462521864  1795 QGGALSSICTQILAMVNQEQ 1814
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1503-1565 1.07e-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: 127.07  E-value: 1.07e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864 1503 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1565
Cdd:cd11860      1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 35-119 5.99e-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: 114.28  E-value: 5.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   35 KAPSPPPLLTDRQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 114
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 2462521864  115 HTNAL 119
Cdd:pfam04822   81 ISEAL 85
dbPDZ_assoc pfam16610
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1333-1405 1.50e-25

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: 101.90  E-value: 1.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1333 YNPHVHQLSSHSRSSSHLDPAGTHSTLQGSGTTTPEHPSVIDPLMEQDEGPSTPPAKQS--------SSRIAGDANKKTL 1404
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTtpatsphnSFRMPGDANKRVP 80


                   .
gi 2462521864 1405 E 1405
Cdd:pfam16610   81 E 81
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1253-1335 7.58e-19

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 82.81  E-value: 7.58e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1253 EPRHVKVQKGSEPLGISIVSG--EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....*
gi 2462521864  1331 AQYNP 1335
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) ...
 1253-1335 1.15e-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: 1.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1253 EPRHVKVQKGSEPLGISIVSGEKG-GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
Cdd:cd06795      1 EPRKIVLHKGSTGLGFNIVGGEDGeGIFISFILAGGPADLSGeLRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTII 80


                   ....*
gi 2462521864 1331 AQYNP 1335
Cdd:cd06795     81 AQYKP 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-542 1.24e-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: 89.73  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  244 LEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTtqvk 319
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEE---- 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  320 TAKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAANEEMEALRQIKDTVTM 392
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  393 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 472
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  473 DTRKQKNDVSRELKELKEQMESQLEK--EARFRQLMAHSSHDSAIDTDSMEWETEVVEFQREtedidLKALG 542
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1256-1330 7.66e-17

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: 76.81  E-value: 7.66e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1256 HVKVQKGS-EPLGISIVSGE--KGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
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 ...
 1253-1332 1.85e-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: 75.89  E-value: 1.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1253 EPRHVKVQKGSEPLGISIVSGEKGGIYVSKVTVGSIAHQA-GLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1331
Cdd:cd06766      1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPdGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                   .
gi 2462521864 1332 Q 1332
Cdd:cd06766     81 Q 81
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 608-696 2.72e-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: 2.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  608 INMVVRRRKSLGgkvvtplhINLSGQKDSGIslenGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL 687
Cdd:cd00136      2 VTLEKDPGGGLG--------FSIRGGKDGGG----GIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELL 69


                   ....*....
gi 2462521864  688 RSCQDSLTL 696
Cdd:cd00136     70 KSAGGEVTL 78
Guanylate_kin pfam00625
Guanylate kinase;
1646-1813 3.49e-16

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 78.58  E-value: 3.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1646 RPVLILGPLL---DVVKEMLVNEAPGKFCRC---------PLEVMK-----ASQQAIERGVKDCLFVDYKRRSGHFDVTT 1708
Cdd:pfam00625    3 RPVVLSGPSGvgkSHIKKALLSEYPDKFGYSvphttrpprKGEVDGkdyyfVSKEEMERDISANEFLEYAQFSGNMYGTS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1709 VASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSakhIKEQRDPIYLRDKVTQRHSKEQFEAAQKLEQEYSr 1788
Cdd:pfam00625   83 VETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPS---LKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE- 158

                          170       180
                   ....*....|....*....|....*
gi 2462521864 1789 yFTGVIQGGALSSICTQILAMVNQE 1813
Cdd:pfam00625  159 -FDVIIVNDDLEEAYKKLKEALEAE 182
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 534-615 8.45e-16

PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467206 [Multi-domain]  Cd Length: 89  Bit Score: 74.27  E-value: 8.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  534 EDIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGA 607
Cdd:cd06723      2 EEITLergnSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAaaDGRLRVNDIILRVNDVDVRNVTHSVAVEALKEAGSI 81


                   ....*...
gi 2462521864  608 INMVVRRR 615
Cdd:cd06723     82 VRLYVKRR 89
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 526-613 6.21e-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: 6.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  526 VVEFQRETEdidlKALGFDMAEGVNepcfpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 603
Cdd:cd00136      1 TVTLEKDPG----GGLGFSIRGGKD-----GGGGIFVSRVEPGGPAarDGRLRVGDRILEVNGVSLEGLTHEEAVELLKS 71

                           90
                   ....*....|
gi 2462521864  604 GEGAINMVVR 613
Cdd:cd00136     72 AGGEVTLTVR 81
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 203-504 1.43e-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: 79.72  E-value: 1.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  203 EILNKLYDTA--MDKLEVV----KKDYDALRK------RYSE-KVAIHNADLS----RLEQLGEENQRLLKQTEMLTQQR 265
Cdd:TIGR02168  176 ETERKLERTRenLDRLEDIlnelERQLKSLERqaekaeRYKElKAELRELELAllvlRLEELREELEELQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  266 DTAIQLQHQCALSLRRFEAIHHELNKataqnkdlqwEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSER 345
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEE----------EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  346 DQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKdtvtmdagrankeveilrkqckalcQELKEALQEADV- 424
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL-------------------------EELESRLEELEEq 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  425 ---AKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDdtRKQKNDVSRELKELKEQMESQLEKEAR 501
Cdd:TIGR02168  381 letLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELER 458


                   ...
gi 2462521864  502 FRQ 504
Cdd:TIGR02168  459 LEE 461
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1262-1329 1.65e-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: 70.43  E-value: 1.65e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1262 GSEPLGISIVSG--EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITI 1329
Cdd:cd06738     11 GTRGLGCSISSGptQKPGIFISNVKPGSLAEEVGLEVGDQIVEVNGTSFTNVDHKEAVMAL-KSSRHLTI 79
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 137-501 3.82e-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: 3.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  137 SRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMK-RLHE------EDQKEIGDLRAQQQQVLK-HNGSSEILNKL 208
Cdd:TIGR02169  663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEnRLDElsqelsDASRKIGEIEKEIEQLEQeEEKLKERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  209 yDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLE-QLGEENQRLLKQTEMLTQQRDTAIQLQHQcalSLR-RFEAIH 286
Cdd:TIGR02169  743 -EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEeALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEaRLREIE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  287 HELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKL 366
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  367 KSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKcrrdwafqERDKIVAErdsI 446
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA--------ELQRVEEE---I 967

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  447 RTLCD-NLrrerdRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEAR 501
Cdd:TIGR02169  968 RALEPvNM-----LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE-EYEKKKR 1017
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 154-503 7.30e-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: 77.40  E-value: 7.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  154 RRENGQLLRERNL--LQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDALRKRyS 231
Cdd:TIGR02168  667 KTNSSILERRREIeeLEEKIEELEEKIAELEKALAELRKELEELEE---ELEQLRKELEELSRQISALRKDLARLEAE-V 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  232 EKVAihnadlSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAihhELNKATAQNKDLQWEMELLQSELT 311
Cdd:TIGR02168  743 EQLE------ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA---QIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  312 ELRTTQvkTAKESEKYREERDAVYSEYKLIMSE------RDQVIS---ELDKLQTEVELAESKLKSSTSEKKAANEEMEA 382
Cdd:TIGR02168  814 LLNEEA--ANLRERLESLERRIAATERRLEDLEeqieelSEDIESlaaEIEELEELIEELESELEALLNERASLEEALAL 891

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  383 LRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDwAFQER----------------DKIVAERDSI 446
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-NLQERlseeysltleeaealeNKIEDDEEEA 970

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  447 RTLCDNLRRERDR-------AVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEARFR 503
Cdd:TIGR02168  971 RRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE-EIDREARER 1033
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
 1503-1560 9.74e-14

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: 67.31  E-value: 9.74e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1503 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSK 1560
Cdd:cd11859      1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGTVGSWQAVRVGRNHQELERGVIPNK 58
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 1405-1488 1.46e-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: 67.79  E-value: 1.46e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  1405 EPRVVFIKKSQLELGVHLCGG--NLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRL 1482
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79


                    ....*.
gi 2462521864  1483 KVQYRP 1488
Cdd:smart00228   80 TVLRGG 85
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 146-493 1.57e-13

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: 76.26  E-value: 1.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  146 LKDDVDMLRRENGQLLRERNLLqqswedmKRLHEEDQ----KEIGDLRAQQQQVLKhngssEIlnklyDTAMDKLEVVKK 221
Cdd:TIGR02169  196 KRQQLERLRREREKAERYQALL-------KEKREYEGyellKEKEALERQKEAIER-----QL-----ASLEEELEKLTE 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  222 DYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLkQTEMLtqqrdtaiQLQHQCALSLRRFEAIHHELNKATAQNKDLQW 301
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIG--------ELEAEIASLERSIAEKERELEDAEERLAKLEA 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  302 EMELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEME 381
Cdd:TIGR02169  330 EIDKLLAEIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  382 ALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAV 461
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482

                          330       340       350
                   ....*....|....*....|....*....|..
gi 2462521864  462 SELAEALRSLDDTRKQKNDVSRELKELKEQME 493
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARASEERVRGGRAVEE 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 89-456 8.22e-13

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: 73.95  E-value: 8.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   89 RLNPDYERLKIQCVRAMSDLQSLQNqHTNALKRCEEVAKETdfyhtlHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQ 168
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEN-RLDELSQELSDASRK------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  169 QSWEDMKRLHEEDQKEIGDLRAQQQQVlkhngsSEILNKLYDT-AMDKLEVVKKDYDALRKRYSEKVAIhnadLSRLEQl 247
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKL------EEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEAR----LREIEQ- 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  248 gEENQRLLKQtEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNkatAQNKDLQWEMELLQSELTELRTTQVKTAKEseky 327
Cdd:TIGR02169  820 -KLNRLTLEK-EYLEKEIQELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEAALRDLESRLGDLKKE---- 890

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  328 REERDAVYSEYKlimserdqviSELDKLQTEVELAESKLKSSTSEKKAANEEmeaLRQIKDTVTMDAGRANKE--VEILR 405
Cdd:TIGR02169  891 RDELEAQLRELE----------RKIEELEAQIEKKRKRLSELKAKLEALEEE---LSEIEDPKGEDEEIPEEElsLEDVQ 957

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  406 KQCKALCQELKE-------ALQEADVAKCRRDWAFQERDKIVAERDSIRTL---CDNLRRE 456
Cdd:TIGR02169  958 AELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERieeYEKKKRE 1018
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 621-699 9.39e-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: 65.48  E-value: 9.39e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864   621 KVVTPLHINLSGQKDSGisleNGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:smart00228    9 KGGGGLGFSLVGGKDEG----GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 535-603 1.47e-12

PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467207 [Multi-domain]  Cd Length: 85  Bit Score: 64.98  E-value: 1.47e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  535 DIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 603
Cdd:cd06724      1 EIKLvkgpKGLGFSIAGGVGNQHIPGDNGIYVTKIIEGGAAqkDGRLQVGDKLLAVNDVSLEEVTHEEAVAALKN 75
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
53-520 1.99e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 72.38  E-value: 1.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   53 ENLSIQLRLMTRERNELRKRLAFATHGTAFDkrpyhrlNPDYERLKIQcvraMSDLQslqnqhtnalKRCEEVAKETDFY 132
Cdd:PRK02224   275 EELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEAR----REELE----------DRDEELRDRLEEC 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  133 HTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILnklYDTA 212
Cdd:PRK02224   334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD---LGNA 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  213 MDKLEVVKKDYDALRkrysEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAiQLQHQCALSLRRfeaihHELNKA 292
Cdd:PRK02224   411 EDFLEELREERDELR----EREAELEATLRTARERVEEAEALLEAGKCPECGQPVE-GSPHVETIEEDR-----ERVEEL 480

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  293 TAQNKDLQWEMELLQSELTELrTTQVKTAKESEKYREERDAV---YSEYKLIMSERDQVISEL----DKLQTEVELAESK 365
Cdd:PRK02224   481 EAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELreraAELEAEAEEKREA 559

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  366 LKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILrkqckALCQELKEALQEadVAKCRRDWAF---QERDKIVAE 442
Cdd:PRK02224   560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-----AAIADAEDEIER--LREKREALAElndERRERLAEK 632

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  443 RDSIRTLCDNL--------RRERDRAVSELAEALRSLDDTRKQKND-------VSRELKELKEQMESQLEKEARFRQLma 507
Cdd:PRK02224   633 RERKRELEAEFdearieeaREDKERAEEYLEQVEEKLDELREERDDlqaeigaVENELEELEELRERREALENRVEAL-- 710

                          490
                   ....*....|...
gi 2462521864  508 HSSHDSAIDTDSM 520
Cdd:PRK02224   711 EALYDEAEELESM 723
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 649-696 3.97e-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: 3.97e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462521864  649 VLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06681     37 VRPGGPADREGTIKPGDRLLSVDGISLHGATHAEAMSILKQCGQEATL 84
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 121-505 5.10e-12

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: 71.36  E-value: 5.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  121 RCEEVAKETDFYHTLHSRLLSDQTRLKDDVDmlrRENGQLLRERNLLQQSWEDM-KRLHE-EDQKeigdlRAQQQQVLKH 198
Cdd:pfam01576  626 RAEAEAREKETRALSLARALEEALEAKEELE---RTNKQLRAEMEDLVSSKDDVgKNVHElERSK-----RALEQQVEEM 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  199 NGSSEILNKLYDTAMD---KLEVvkkDYDALRkrysekvAIHNADLSRLEQLGEENQR-LLKQT-EMLTQ------QRDT 267
Cdd:pfam01576  698 KTQLEELEDELQATEDaklRLEV---NMQALK-------AQFERDLQARDEQGEEKRRqLVKQVrELEAElederkQRAQ 767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  268 AIQLQHQCALSLRRFEAIHHELNK----ATAQNKDLQWEMELLQSELTELRTTQ---VKTAKESEKYRE--ERDAVYSEY 338
Cdd:pfam01576  768 AVAAKKKLELDLKELEAQIDAANKgreeAVKQLKKLQAQMKDLQRELEEARASRdeiLAQSKESEKKLKnlEAELLQLQE 847

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  339 KLIMSER--DQVISELDKLQTEVELAESKlKSSTSEKKaaneemealRQIKDTVTMdagrankeveilrkqckaLCQELK 416
Cdd:pfam01576  848 DLAASERarRQAQQERDELADEIASGASG-KSALQDEK---------RRLEARIAQ------------------LEEELE 899

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  417 EALQEADVAKCRRDWAFQERDKIVAERDSIRTLC---DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK-EQM 492
Cdd:pfam01576  900 EEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSqksESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKiAQL 979

                          410
                   ....*....|...
gi 2462521864  493 ESQLEKEARFRQL 505
Cdd:pfam01576  980 EEQLEQESRERQA 992
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1257-1332 6.24e-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: 63.04  E-value: 6.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1257 VKVQKGSEPLGISIVSG----------EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1326
Cdd:cd06702      3 IHLVKAGGPLGLSIVGGsdhsshpfgvDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPGQE 82


                   ....*.
gi 2462521864 1327 ITILAQ 1332
Cdd:cd06702     83 IKLLVR 88
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 103-447 7.80e-12

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: 70.92  E-value: 7.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  103 RAMSDLQ-SLQNQHTNALKRCEEVAKetdfyhtLHSRL---LSDQTRLKDDVDMLRRENGQL------LRERN----LLQ 168
Cdd:pfam15921  496 RTVSDLTaSLQEKERAIEATNAEITK-------LRSRVdlkLQELQHLKNEGDHLRNVQTECealklqMAEKDkvieILR 568

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  169 QSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngssEILNKLYDtaMDKLEVVKKDYDA----LRKRYS----EKVAIHNAD 240
Cdd:pfam15921  569 QQIENMTQLVGQHGRTAGAMQVEKAQLEK-----EINDRRLE--LQEFKILKDKKDAkireLEARVSdlelEKVKLVNAG 641

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  241 LSRL---EQLGEENQRLLKQTEmltQQRDTAIQLQHQCALSLRRFEAIHHELNKATaqNKdLQWEMELLQSELTELRTTq 317
Cdd:pfam15921  642 SERLravKDIKQERDQLLNEVK---TSRNELNSLSEDYEVLKRNFRNKSEEMETTT--NK-LKMQLKSAQSELEQTRNT- 714

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  318 VKTAKESEKYREErdAVYSEYKLIMSERDQViselDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRA 397
Cdd:pfam15921  715 LKSMEGSDGHAMK--VAMGMQKQITAKRGQI----DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM 788

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  398 NKEVEILRKQCKalcqELKEALQEADVAKCRRDWAFQERDKIV--AERDSIR 447
Cdd:pfam15921  789 AGELEVLRSQER----RLKEKVANMEVALDKASLQFAECQDIIqrQEQESVR 836
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 626-698 1.24e-11

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: 62.23  E-value: 1.24e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  626 LHINLSGQKDSGISLeNGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 698
Cdd:cd06792     14 LGISVTGGINTSVRH-GGIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVL 85
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1253-1333 1.58e-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: 61.81  E-value: 1.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1253 EPRHVKVQKGSEpLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIG--QQCDTITIL 1330
Cdd:cd06729      1 DTRLVSFRKGGS-VGLRLAGGNDVGIFVAGVQEGSPAEKQGLQEGDQILKVNGVDFRNLTREEAVLFLLdlPKGEEVTIL 79


                   ...
gi 2462521864 1331 AQY 1333
Cdd:cd06729     80 AQS 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 154-491 1.67e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  154 RRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngsseilnklydtamdKLEVVKKDYDALRKRYSEK 233
Cdd:COG1196    224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-----------------ELEELRLELEELELELEEA 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  234 VAIHNADLSRLEQLGEENQRllkQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTEL 313
Cdd:COG1196    287 QAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  314 RTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMD 393
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  394 AGRANKEVEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIvaerdsirtlcDNLRRERDRAVSELaEALRSLDD 473
Cdd:COG1196    444 LEEAAEEEAELEEEEEALLELLAELLEEAA----------LLEAAL-----------AELLEELAEAAARL-LLLLEAEA 501

                          330
                   ....*....|....*...
gi 2462521864  474 TRKQKNDVSRELKELKEQ 491
Cdd:COG1196    502 DYEGFLEGVKAALLLAGL 519
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 223-542 4.47e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 68.17  E-value: 4.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  223 YDALRKRYSEKVAihnaDLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSL-----------RRFEAIHHELNK 291
Cdd:TIGR02169  659 SRAPRGGILFSRS----EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdasrkigeieKEIEQLEQEEEK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  292 ATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREE----RDAVYS-EYKLIMSERDQVISELDKLQTEV------- 359
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDlhklEEALNDlEARLSHSRIPEIQAELSKLEEEVsriearl 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  360 ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEalqeadvakcrrdwafqerdKI 439
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE--------------------LE 874

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  440 VAERDSIRTLCDnLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDs 519
Cdd:TIGR02169  875 AALRDLESRLGD-LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS- 952

                          330       340
                   ....*....|....*....|...
gi 2462521864  520 meweTEVVEFQRETEDIDLKALG 542
Cdd:TIGR02169  953 ----LEDVQAELQRVEEEIRALE 971
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1407-1485 4.62e-11

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: 60.25  E-value: 4.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1407 RVVFIKKSQLELGVHLCGGNLH--GVFVAEVEDDSPAKgPDG-LVPGDLILEYGSLDVRNKTVEEVyVEMLK-PRDGVRL 1482
Cdd:cd00136      1 TVTLEKDPGGGLGFSIRGGKDGggGIFVSRVEPGGPAA-RDGrLRVGDRILEVNGVSLEGLTHEEA-VELLKsAGGEVTL 78


                   ...
gi 2462521864 1483 KVQ 1485
Cdd:cd00136     79 TVR 81
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 108-525 4.85e-11

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: 67.23  E-value: 4.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  108 LQSLQNQHTNALKRCE----EVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQK 183
Cdd:pfam07888   36 LEECLQERAELLQAQEaanrQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  184 EIGDLRAQQ----QQVLKHNGSSEILNK---LYDTAMDKL-EVVKKDYDALRKRYSEKVAIHnadlSRLEQLGEENQRLL 255
Cdd:pfam07888  116 EKDALLAQRaaheARIRELEEDIKTLTQrvlERETELERMkERAKKAGAQRKEEEAERKQLQ----AKLQQTEEELRSLS 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  256 KQTEMLTQ---QRDT-AIQLQHQCAlslrrfeAIHHELNkaTAQNKDLqwEMELLQSELTELRTTQVKTAKESEKYREER 331
Cdd:pfam07888  192 KEFQELRNslaQRDTqVLQLQDTIT-------TLTQKLT--TAHRKEA--ENEALLEELRSLQERLNASERKVEGLGEEL 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  332 DAVyseykliMSERDQVISELDKL-----QTEVELAESKLKssTSEKKAA-NEEMEALRQikdtvtmdagRANKEVEILR 405
Cdd:pfam07888  261 SSM-------AAQRDRTQAELHQArlqaaQLTLQLADASLA--LREGRARwAQERETLQQ----------SAEADKDRIE 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  406 KQCKALcQELKEALQEADVakcrrdwafqERDKIVAE----RDSIRTLCDNLRRErdraVSELAEALRSLDDTRKQKNDV 481
Cdd:pfam07888  322 KLSAEL-QRLEERLQEERM----------EREKLEVElgreKDCNRVQLSESRRE----LQELKASLRVAQKEKEQLQAE 386

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2462521864  482 SRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWETE 525
Cdd:pfam07888  387 KQELLEYIRQLEQRLETVADAKWSEAALTSTERPDSPLSDSEDE 430
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 145-535 7.83e-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: 67.51  E-value: 7.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  145 RLKDDVDMLRRENGQLLRERNLLQQSWEDMK-RLHEEDQK--EIGDLRAQQQQVLkhngsSEILNKLYDTAMDKLEVVKk 221
Cdd:pfam01576  135 KLEEDILLLEDQNSKLSKERKLLEERISEFTsNLAEEEEKakSLSKLKNKHEAMI-----SDLEERLKKEEKGRQELEK- 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  222 dydALRKRYSEKVAIHN--ADL-SRLEQLG-------EENQRLLKQTEMLTQQRDTAI----QLQHQCALSLRRFEAIHH 287
Cdd:pfam01576  209 ---AKRKLEGESTDLQEqiAELqAQIAELRaqlakkeEELQAALARLEEETAQKNNALkkirELEAQISELQEDLESERA 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  288 ELNKATAQNKDLQWEMELLQselTELRTTQVKTAKESEkYREERDAVYSEYKLIMSER----DQVISELDKLQTEV---- 359
Cdd:pfam01576  286 ARNKAEKQRRDLGEELEALK---TELEDTLDTTAAQQE-LRSKREQEVTELKKALEEEtrshEAQLQEMRQKHTQAleel 361

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  360 --ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRAnkEVEILRKQCKALCQELKEALQEADVAKCRRdwafQER- 436
Cdd:pfam01576  362 teQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ--DSEHKRKKLEGQLQELQARLSESERQRAEL----AEKl 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  437 DKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTR-------KQKNDVS---RELKE----LKEQMESQLEKEARF 502
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLStrlRQLEDernsLQEQLEEEEEAKRNV 515

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2462521864  503 -RQLMAHSSHDSAIDTdSMEWETEVVE--------FQRETED 535
Cdd:pfam01576  516 eRQLSTLQAQLSDMKK-KLEEDAGTLEaleegkkrLQRELEA 556
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 42-518 8.70e-11

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: 67.05  E-value: 8.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   42 LLTDRQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKR 121
Cdd:pfam05483  246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  122 CEEVAKE-------------------TDFYHT---LHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQ---------- 169
Cdd:pfam05483  326 ICQLTEEkeaqmeelnkakaahsfvvTEFEATtcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnkev 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  170 SWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDT---AMDKLEVVKKDYDALRKRYSEKVA-----IHNADL 241
Cdd:pfam05483  406 ELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekEIHDLEIQLTAIKTSEEHYLKEVEdlkteLEKEKL 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  242 SRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcalslrrfeaiHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTA 321
Cdd:pfam05483  486 KNIELTAHCDKLLLENKELTQEASDMTLELKKH-----------QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  322 KESEKYREE---------RDAVYSEYKLIMSERDQVISEL--DKLQTEVE---------LAESKL--KSSTSEKKAANE- 378
Cdd:pfam05483  555 EEFIQKGDEvkckldkseENARSIEYEVLKKEKQMKILENkcNNLKKQIEnknknieelHQENKAlkKKGSAENKQLNAy 634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  379 ---------EMEALRQIKDTVTmdaGRANKEVEILRKQCKALCQELKEALQEADVA---------KCRRDWA----FQER 436
Cdd:pfam05483  635 eikvnklelELASAKQKFEEII---DNYQKEIEDKKISEEKLLEEVEKAKAIADEAvklqkeidkRCQHKIAemvaLMEK 711

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  437 -----DKIVAERDSIRTLCDNLRRERDRAVSELAEALrslddtrkqkNDVSRELKELKEQMEsqLEKEARfRQLMAHSSH 511
Cdd:pfam05483  712 hkhqyDKIIEERDSELGLYKNKEQEQSSAKAALEIEL----------SNIKAELLSLKKQLE--IEKEEK-EKLKMEAKE 778


                   ....*..
gi 2462521864  512 DSAIDTD 518
Cdd:pfam05483  779 NTAILKD 785
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 534-603 1.12e-10

PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467193 [Multi-domain]  Cd Length: 86  Bit Score: 59.61  E-value: 1.12e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  534 EDIDLK----ALGFDMAEGVNEPCFPGDCGIFVTKV-DKGSIA-DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 603
Cdd:cd06709      1 EEITLKrgpsGLGFNIVGGTDQPYIPNDSGIYVAKIkEDGAAAiDGRLQEGDKILEINGQSLENLTHQDAVELFRN 76
PDZ2_ZO1-like_ds cd06728
PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form ...
 635-700 1.13e-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: 1.13e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  635 DSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 700
Cdd:cd06728     13 EYGLRLGSRIFVKEITPDSLAAKDGNLQEGDIILKINGTPVENLSLSEAKKLIEKSKDKLQLVVLR 78
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 633-688 1.15e-10

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: 60.05  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  633 QKDSGISLENGVYAAAVL----------PGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLR 688
Cdd:cd06686     17 LKGFGIQLQGGVFATETLsspplisfiePDSPAERCGVLQVGDRVLSINGIPTEDRTLEEANQLLR 82
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 212-539 1.31e-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: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  212 AMDKLEVVKKDYDALRKRYSEKvaihnadLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQhqcalsLRRFEAIHHELNK 291
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEK-------RQQLERLRREREKAERYQALLKEKREYEGYEL------LKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  292 ATAQNKDLQWEMELLQSELTELrttqvktAKESEKYREERDAVYSEYKLIMSERD-QVISELDKLQTEVELAESKLKsst 370
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIA--- 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  371 sekkaaneemEALRQIKDtvtMDAGRANKEVEILRKQCKAlcQELKEALQEADVakcrrdwafqERDKIVAERDSIRTLC 450
Cdd:TIGR02169  312 ----------EKERELED---AEERLAKLEAEIDKLLAEI--EELEREIEEERK----------RRDKLTEEYAELKEEL 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  451 DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHsshdsaIDTDSMEWETEVVEFQ 530
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD------LNAAIAGIEAKINELE 440


                   ....*....
gi 2462521864  531 RETEDIDLK 539
Cdd:TIGR02169  441 EEKEDKALE 449
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1405-1486 1.35e-10

PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins , and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467211 [Multi-domain]  Cd Length: 82  Bit Score: 59.12  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1405 EPRVV-FIKKSQLelGVHLCGGNLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEV--YVEMLKPRDGVR 1481
Cdd:cd06729      1 DTRLVsFRKGGSV--GLRLAGGNDVGIFVAGVQEGSPAEK-QGLQEGDQILKVNGVDFRNLTREEAvlFLLDLPKGEEVT 77


                   ....*
gi 2462521864 1482 LKVQY 1486
Cdd:cd06729     78 ILAQS 82
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 1257-1329 1.44e-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: 1.44e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1257 VKVQKGSEPLGISIVSG-----EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1329
Cdd:cd06789      6 VTLKKVGNGMGLSIVAAkgagqDKLGIYIKSVVKGGAADLDGrLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTL 84
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 1255-1320 1.45e-10

PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RapGEF2 and RapGEF6 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467237 [Multi-domain]  Cd Length: 83  Bit Score: 59.20  E-value: 1.45e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1255 RHVKVQKGS--EPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06755      1 RTVTLTRPSreSPLHFSLLGGsEKGfGIFVSKVEKGSKAAEAGLKRGDQILEVNGQNFENITLKKALEIL 70
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1262-1332 1.63e-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: 1.63e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1262 GSEPLGISIVSGEKG---GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1332
Cdd:pfam00595    8 GRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 541-614 2.62e-10

PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This densin and erbin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467231 [Multi-domain]  Cd Length: 87  Bit Score: 58.49  E-value: 2.62e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  541 LGFDMAEGVN---EPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 614
Cdd:cd06749     11 LGFSISGGIGsqgNPFRPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVNIEHGQAVSLLKSFQNTVDLVVER 87
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 52-503 3.11e-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: 65.52  E-value: 3.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   52 VENLSIQLRLMTR---ERNELRKRLAFATHGTAFDkrpyhrLNPDYERLKIQcVRAMSDLQSLQNQHTNALK-RCEEVAK 127
Cdd:pfam15921   80 LEEYSHQVKDLQRrlnESNELHEKQKFYLRQSVID------LQTKLQEMQME-RDAMADIRRRESQSQEDLRnQLQNTVH 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  128 ETDFYHTLHSRLLSDQTrlkDDVDMLRRengQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGS--SEIL 205
Cdd:pfam15921  153 ELEAAKCLKEDMLEDSN---TQIEQLRK---MMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSaiSKIL 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  206 NKLyDTAMDKLE----VVKKDYDALRKRYSEKVAI---HNADlsRLEQLGEENQ-RLLKQTEMLTQQRDTAIQLQHQcal 277
Cdd:pfam15921  227 REL-DTEISYLKgrifPVEDQLEALKSESQNKIELllqQHQD--RIEQLISEHEvEITGLTEKASSARSQANSIQSQ--- 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  278 slrrFEAIHHELNKATA----QNKDLQWEMELLQSELTELRTTQVKTAKESEKY-----------REERDAVYSEYKLIM 342
Cdd:pfam15921  301 ----LEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanselteaRTERDQFSQESGNLD 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  343 SERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRankeVEILRKQCKALCQELKEalqea 422
Cdd:pfam15921  377 DQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQR----LEALLKAMKSECQGQME----- 447

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  423 dvakcRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARF 502
Cdd:pfam15921  448 -----RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL 522


                   .
gi 2462521864  503 R 503
Cdd:pfam15921  523 R 523
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
228-498 4.30e-10

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 63.01  E-value: 4.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  228 KRYSEKVAIHNADLSRLEqlgEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEmelLQ 307
Cdd:COG1340     11 EELEEKIEELREEIEELK---EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE---LN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  308 SELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEV-------ELAEsKLKSSTSEKKAANEEM 380
Cdd:COG1340     85 EKLNELR-------EELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekELVE-KIKELEKELEKAKKAL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  381 EALRQIKDTVTmdagrankEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDS-------IRTLCDNL 453
Cdd:COG1340    157 EKNEKLKELRA--------ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADElhkeiveAQEKADEL 228

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462521864  454 RRERDRAVSELAEALRSLDDTRKQKNDVSR-----ELKELKEQMESQLEK 498
Cdd:COG1340    229 HEEIIELQKELRELRKELKKLRKKQRALKRekekeELEEKAEEIFEKLKK 278
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 1255-1333 4.88e-10

PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GOPC-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467261 [Multi-domain]  Cd Length: 83  Bit Score: 57.77  E-value: 4.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1255 RHVKVQKG-SEPLGISIVSGEKGG--IYVSKVTVGSIAHQ-AGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
Cdd:cd06800      1 RKVLLSKEpHEGLGISITGGKEHGvpILISEIHEGQPADRcGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITLE 80


                   ...
gi 2462521864 1331 AQY 1333
Cdd:cd06800     81 VVY 83
SH3_ZO-1 cd12026
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ...
 1500-1560 6.00e-10

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


Pssm-ID: 212959  Cd Length: 65  Bit Score: 57.01  E-value: 6.00e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1500 DSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSK 1560
Cdd:cd12026      1 DSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNK 61
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 1257-1330 6.45e-10

PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 57.22  E-value: 6.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1257 VKVQKGSEPLGISIVSG-----EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
Cdd:cd06792      5 VELSKKDGSLGISVTGGintsvRHGGIYVKSLVPGGAAEQDGrIQKGDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLV 84
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1257-1320 6.90e-10

PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 57.27  E-value: 6.90e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864 1257 VKVQKGSePLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06741      6 LVVEDGQ-SLGLMIRGGaEYGlGIYVTGVDPGSVAENAGLKVGDQILEVNGRSFLDITHDEAVKIL 70
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 537-614 7.57e-10

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 57.27  E-value: 7.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  537 DLKALGFDMAEGVNEPCF-PGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 613
Cdd:cd06703     10 DGKGLGFSIAGGKGSTPFrDGDEGIFISRITEGGAAdrDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITLVVE 89


                   .
gi 2462521864  614 R 614
Cdd:cd06703     90 R 90
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 641-696 8.65e-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: 56.92  E-value: 8.65e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06690     29 SPGIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMDLIRTSGDKLRF 84
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 106-541 9.10e-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: 63.98  E-value: 9.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  106 SDLQSLQNQ--HTNALKRCEEVAKETDFYHtLHSRLLSDQTRLKDDVDMLRRE----NGQLLRERNLLQQSWEDMKRLHE 179
Cdd:pfam15921  299 SQLEIIQEQarNQNSMYMRQLSDLESTVSQ-LRSELREAKRMYEDKIEELEKQlvlaNSELTEARTERDQFSQESGNLDD 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  180 EDQKEIGDLRAQQQQVlkhNGSSEILNKLYDTAMDKLEVVkkdyDALRKRYSEKvaihNADLSRLEQLgeenqrllkqte 259
Cdd:pfam15921  378 QLQKLLADLHKREKEL---SLEKEQNKRLWDRDTGNSITI----DHLRRELDDR----NMEVQRLEAL------------ 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  260 MLTQQRDTAIQLQHQCAlslrRFEAIHHELNKATAQNKDLQWEMELLQSELTELrttqvkTAKESEKYREERdaVYSEYK 339
Cdd:pfam15921  435 LKAMKSECQGQMERQMA----AIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL------TAKKMTLESSER--TVSDLT 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  340 LIMSERDQVI----SELDKLQTEVELAESKLKSSTSEK---KAANEEMEALRqikdtvtMDAGRANKEVEILRKQCKALC 412
Cdd:pfam15921  503 ASLQEKERAIeatnAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALK-------LQMAEKDKVIEILRQQIENMT 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  413 Q------------ELKEALQEADVAKCRRDwaFQERDKIVAERDS-IRTL---CDNLRRERDRAVSELAEALRSLDDTRK 476
Cdd:pfam15921  576 QlvgqhgrtagamQVEKAQLEKEINDRRLE--LQEFKILKDKKDAkIRELearVSDLELEKVKLVNAGSERLRAVKDIKQ 653

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  477 QKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFQRETEDIDLKAL 541
Cdd:pfam15921  654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1257-1316 1.07e-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: 56.67  E-value: 1.07e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864 1257 VKVQKGS-EPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd10833      4 VTVEKSPdGSLGFSVRGGsEHGlGIFVSKVEEGSAAERAGLCVGDKITEVNGVSLENITMSSA 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
124-508 1.16e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.25  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  124 EVAKETdFYHTLHSRLLSdqtRLKDDVDMLRRENGQL----LRERNLLQQSWEDMKRLHEE---DQKEIGDLRAQQQQVl 196
Cdd:COG4717     33 EAGKST-LLAFIRAMLLE---RLEKEADELFKPQGRKpelnLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEEL- 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  197 khngssEILNKLYDTAMDKLEVVKKDYDALRKRysEKVAIHNADL-SRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQC 275
Cdd:COG4717    108 ------EAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELpERLEELEERLEELRELEEELEELEAELAELQEEL 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  276 ALSLRRF-EAIHHELNKATAQNKDLQWEMELLQSELTELR-------------TTQVKTAKESEKYREER---------- 331
Cdd:COG4717    180 EELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQeeleeleeeleqlENELEAAALEERLKEARlllliaaall 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  332 ------DAVYSEYKLIM---------------------SERDQVISELDKLQTEVELAESKLKS-----STSEKKAANEE 379
Cdd:COG4717    260 allglgGSLLSLILTIAgvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEEL 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  380 MEALRQIKDTVTMDAGRANKEVEIlrkQCKALCQELKEALQEADV-------AKCRRdwaFQERDKIVAERDSIRTLCDN 452
Cdd:COG4717    340 LELLDRIEELQELLREAEELEEEL---QLEELEQEIAALLAEAGVedeeelrAALEQ---AEEYQELKEELEELEEQLEE 413

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  453 LRRERDRAVS---------ELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEARFRQLMAH 508
Cdd:COG4717    414 LLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAELEAELE-QLEEDGELAELLQE 477
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1254-1335 1.23e-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: 1.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1254 PRHVKVQKGSEPLGISIVSG--EKGGIYVSKVTVGSIA-HQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
Cdd:cd06796      2 PRVVELPKTEEGLGFNVMGGkeQNSPIYISRIIPGGVAdRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLV 81


                   ....*
gi 2462521864 1331 AQYNP 1335
Cdd:cd06796     82 VRYTP 86
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1405-1491 1.38e-09

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: 56.59  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1405 EPRVVFIKKSQLELGVHLCGG-NLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLK 1483
Cdd:cd06795      1 EPRKIVLHKGSTGLGFNIVGGeDGEGIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTII 80


                   ....*...
gi 2462521864 1484 VQYRPEEF 1491
Cdd:cd06795     81 AQYKPEEY 88
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 639-696 1.49e-09

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: 56.63  E-value: 1.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  639 SLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06694     27 SLDLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 557-615 1.58e-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: 1.58e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  557 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKAL-------LNGEGAINMVVRRR 615
Cdd:cd23059     36 DLGIFIKSIIHGGAAskDGRLRVNDQLIAVNGESLLGLTNSEAMETLrramsteGNIRGMIQLVVARR 103
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 106-501 1.65e-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: 62.73  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  106 SDLQSLQNQHTNALKrceevaKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQK-- 183
Cdd:TIGR04523  221 SELKKQNNQLKDNIE------KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlk 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  184 -EIGDLRAQQQQVLKHNGSSEI----------------LNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQ 246
Cdd:TIGR04523  295 sEISDLNNQKEQDWNKELKSELknqekkleeiqnqisqNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  247 LGEENQRLLKQTEMLTQQ-RDTAIQLQHQcalslrrfeaihHELNKATAQN-KDLQWEMELLQSELTELRTTQVKTAKES 324
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQiNDLESKIQNQ------------EKLNQQKDEQiKKLQQEKELLEKEIERLKETIIKNNSEI 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  325 EKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALrqikdtvtmdagraNKEVEIL 404
Cdd:TIGR04523  443 KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL--------------NEEKKEL 508

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  405 RKQCKALCQELKEALQEADVAKCRRDwafQERDKIVAERDSIRTLCDNLRR--------ERDRAVSELAEALRSLDDTRK 476
Cdd:TIGR04523  509 EEKVKDLTKKISSLKEKIEKLESEKK---EKESKISDLEDELNKDDFELKKenlekeidEKNKEIEELKQTQKSLKKKQE 585

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2462521864  477 QKNDV----SRELKELKEQME------SQLEKEAR 501
Cdd:TIGR04523  586 EKQELidqkEKEKKDLIKEIEekekkiSSLEKELE 620
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
235-539 2.19e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 62.75  E-value: 2.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  235 AIHNADL-SRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEaihhelnkataqnkDLQWEMELLQSELTEL 313
Cdd:PRK02224   198 EKEEKDLhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE--------------ERREELETLEAEIEDL 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  314 RTTQVKTAKESEKYREErdavyseykliMSERDQVISELDKLQTEVeLAESKLKSSTSEKKAA-----NEEMEALRQIKD 388
Cdd:PRK02224   264 RETIAETEREREELAEE-----------VRDLRERLEELEEERDDL-LAEAGLDDADAEAVEArreelEDRDEELRDRLE 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  389 TVTMDAGRANKEVEILRKQCKALCQELKEALQEA-----DVAKCRRDWAfQERDKIVAERDSIRTL---CDNLRRERDRA 460
Cdd:PRK02224   332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAaelesELEEAREAVE-DRREEIEELEEEIEELrerFGDAPVDLGNA 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  461 VSELAEALRSLDDTRKQKNDVSRELKELKEQMEsqlEKEARFR--------QLMAHSSHDSAIDtdsmEWETEVVEFQRE 532
Cdd:PRK02224   411 EDFLEELREERDELREREAELEATLRTARERVE---EAEALLEagkcpecgQPVEGSPHVETIE----EDRERVEELEAE 483


                   ....*..
gi 2462521864  533 TEDIDLK 539
Cdd:PRK02224   484 LEDLEEE 490
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1500-1562 2.77e-09

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


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 54.47  E-value: 2.77e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  1500 DSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWMAWQLDENaqkiQRGQIPSKYV 1562
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSDDG----WWKGRLGRG----KEGLFPSNYV 55
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 1253-1332 3.08e-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: 55.79  E-value: 3.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1253 EPRHVKVQK-GSEPLGISIVSG-----------EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLI 1319
Cdd:cd06671      1 PPRRVELWRePGKSLGISIVGGrvmgsrlsngeEIRGIFIKHVLEDSPAGRNGtLKTGDRILEVNGVDLRNATHEEAVEA 80

                           90
                   ....*....|...
gi 2462521864 1320 IGQQCDTITILAQ 1332
Cdd:cd06671     81 IRNAGNPVVFLVQ 93
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 523-616 3.68e-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: 55.08  E-value: 3.68e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   523 ETEVVEFQRETEDidlkaLGFDMAEGVNEpcfpgDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 601
Cdd:smart00228    1 EPRLVELEKGGGG-----LGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                            90
                    ....*....|....*
gi 2462521864   602 LNGEGAINMVVRRRK 616
Cdd:smart00228   71 KKAGGKVTLTVLRGG 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
50-421 6.12e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 6.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   50 EKVENLSIQLRLMTRERNELRKRLAfathgtafDKRPYHRLnpdYERLK--------IQCVRAMSDLQSLQNQHTNALKR 121
Cdd:PRK03918   331 KELEEKEERLEELKKKLKELEKRLE--------ELEERHEL---YEEAKakkeelerLKKRLTGLTPEKLEKELEELEKA 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  122 CEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRREN------GQLLRE---RNLLQQSWEDMKRLhEEDQKEIG----DL 188
Cdd:PRK03918   400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEehrKELLEEYTAELKRI-EKELKEIEekerKL 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  189 RAQQQQVLKHNGSSEILNKLYDTA--------------MDKLEVVKKDYDALRKRYSE---KVAIHNADLSRLEQLGEEN 251
Cdd:PRK03918   479 RKELRELEKVLKKESELIKLKELAeqlkeleeklkkynLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEELKKKL 558

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  252 QRLLKQ--------TEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQW---EMELLQSELTELRTTQVKT 320
Cdd:PRK03918   559 AELEKKldeleeelAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEReekELKKLEEELDKAFEELAET 638

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  321 AKESEKYREERDAV---YS--EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTmDAG 395
Cdd:PRK03918   639 EKRLEELRKELEELekkYSeeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLE 717

                          410       420
                   ....*....|....*....|....*..
gi 2462521864  396 RANKEVEILRKQCKALCQELKE-ALQE 421
Cdd:PRK03918   718 KALERVEELREKVKKYKALLKErALSK 744
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1257-1316 6.71e-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: 54.55  E-value: 6.71e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1257 VKVQKGSEPLGISIV-------SGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06791      5 VELVKDEQGLGITIAgyvgekaSGELSGIFVKSIIPGSAADQDGrIQVNDQIIAVDGVNLQGFTNQEA 72
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
 1500-1560 7.62e-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: 53.72  E-value: 7.62e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1500 DSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSK 1560
Cdd:cd12028      1 DSFYIRTHFDYEPDPPSGLSFTRGEVFHVLDTMHRGKLGSWLAVRMGRDLREMEKGIIPNQ 61
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 649-696 1.06e-08

PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467216 [Multi-domain]  Cd Length: 84  Bit Score: 53.77  E-value: 1.06e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462521864  649 VLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06734     33 IIPGSPADRCGQLKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTL 80
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-391 1.08e-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: 60.46  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   46 RQVNEKVENLSIQLRLMTRERNELRKRLAfathgtafdkrpyhRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEV 125
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  126 AKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngsseiL 205
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------L 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  206 NKLYDTAMDKLEVVKKDYDALRKRY----------SEKVAIHNADLSRLEQLGEEnqrLLKQTEMLTQQRDtaiQLQHQC 275
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEE---LESELEALLNERA---SLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  276 ALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRT----TQVKTAKESEKYREErdavYS-EYKLIMSERDQVIS 350
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELrlegLEVRIDNLQERLSEE----YSlTLEEAEALENKIED 965

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2462521864  351 ELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 391
Cdd:TIGR02168  966 DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 47-385 1.24e-08

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: 60.47  E-value: 1.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   47 QVNEKVENLSI-------QLRLMTRERN------ELRKRLAfathgtafDKRPYHRLNpDYERLKIQCVRAMSDLQSLQN 113
Cdd:TIGR02169  181 EVEENIERLDLiidekrqQLERLRREREkaeryqALLKEKR--------EYEGYELLK-EKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  114 QHTNALKRCEEVAKEtdfYHTLHSRLLSDQTRLKDdvdMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQ 193
Cdd:TIGR02169  252 ELEKLTEEISELEKR---LEEIEQLLEELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  194 QvlkhnGSSEILNKLYD-TAMDK-LEVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLL-------KQTEMLTQQ 264
Cdd:TIGR02169  326 K-----LEAEIDKLLAEiEELEReIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelkdyrEKLEKLKRE 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  265 RDTAIQLQHQCALSLRRFEA----IHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKL 340
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2462521864  341 IMSERDQVISELDKLQTEVELAESKLKSStsekKAANEEMEALRQ 385
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERVRGG----RAVEEVLKASIQ 521
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1255-1320 1.31e-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: 53.52  E-value: 1.31e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1255 RHV--KVQKGSEPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06740      2 RQVtlKRSKSHEGLGFSIRGGaEHGvGIYVSLVEPGSLAEKEGLRVGDQILRVNDVSFEKVTHAEAVKIL 71
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 556-615 1.37e-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: 1.37e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  556 GDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 615
Cdd:cd06758     27 GDIGIFVAGVEEGGSAdrDGRLKKGDELLMINGQSLIGLSHQEAVAILRSSASPVQLVIASK 88
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1253-1330 1.55e-08

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


Pssm-ID: 467165 [Multi-domain]  Cd Length: 89  Bit Score: 53.40  E-value: 1.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1253 EPRHVKVQKGS--EPLGISIVSGEK---GGIYVSKV-TVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1326
Cdd:cd06677      2 EITTIEIHRSDpyEELGISIVGGNDtplINIVIQEVyRDGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLRQPCPV 81


                   ....*.
gi 2462521864 1327 --ITIL 1330
Cdd:cd06677     82 lrLTVL 87
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 531-614 1.60e-08

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


Pssm-ID: 467176 [Multi-domain]  Cd Length: 102  Bit Score: 53.79  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  531 RETEDIDL-----KALGFDMAeGVNEPCfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDL-INKDKKQAIKALL 602
Cdd:cd06689     13 RQVEYIELekpesGGLGFSVV-GLKSEN-RGELGIFVQEIQPGSVAarDGRLKENDQILAINGQPLdQSISHQQAIAILQ 90

                           90
                   ....*....|..
gi 2462521864  603 NGEGAINMVVRR 614
Cdd:cd06689     91 QAKGSVELVVAR 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-395 1.90e-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: 59.69  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   46 RQVNEKVENLSIQLRLMTR------ERNELRKRLAfATHGTAFDKRpYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNAL 119
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERykelkaELRELELALL-VLRLEELREE-LEELQEELKEAEEELEELTAELQELEEKLEELR 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  120 KRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhn 199
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE-- 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  200 gSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcalsl 279
Cdd:TIGR02168  352 -ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE----- 425

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  280 rrfeaihHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEV 359
Cdd:TIGR02168  426 -------LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2462521864  360 ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAG 395
Cdd:TIGR02168  499 ENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 1262-1320 2.38e-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: 52.74  E-value: 2.38e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1262 GSEPLGISIVSGEKG-GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd23060      8 ANGGLGFSLVGGEGGsGIFVKSISPGGVADRDGrLQVGDRLLQVNGESVIGLSHSKAVNIL 68
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1255-1329 2.96e-08

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 52.65  E-value: 2.96e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1255 RHVKVQK-GSEPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQcDTITI 1329
Cdd:cd06737      3 RLVRLDRrGPESLGFSVRGGlEHGcGLFVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINLIKTK-KTVSL 79
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
188-547 3.54e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 3.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  188 LRAQQQQVLKHNGSSEILNKlydTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDT 267
Cdd:COG4717     51 LEKEADELFKPQGRKPELNL---KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  268 AIQLQHQCALS---------LRRFEAIHHELNKATAQNKDLQWEMELLQSELTEL-RTTQVKTAKESEKYREERDAVYSE 337
Cdd:COG4717    128 LPLYQELEALEaelaelperLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQR 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  338 YKLIMSERDQVISELDKLQTEVELAESKLKS------------------------------------------------- 368
Cdd:COG4717    208 LAELEEELEEAQEELEELEEELEQLENELEAaaleerlkearlllliaaallallglggsllsliltiagvlflvlglla 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  369 -----STSEKKAANEEMEA--------------LRQIKDTVTMDAGRANKEVEILRKQCKALCQ---ELKEALQEADVAK 426
Cdd:COG4717    288 llfllLAREKASLGKEAEElqalpaleeleeeeLEELLAALGLPPDLSPEELLELLDRIEELQEllrEAEELEEELQLEE 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  427 CRRDW-------------AFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDT--RKQKNDVSRELKELKEQ 491
Cdd:COG4717    368 LEQEIaallaeagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEE 447

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  492 MESQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFQRETEDIDLKALGFDMAE 547
Cdd:COG4717    448 LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1261-1335 3.66e-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: 52.32  E-value: 3.66e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1261 KGSEPLGISIVSGEKG--GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITILAQYNP 1335
Cdd:cd06752      8 PPGEQLGFNIRGGKASglGIFISKVIPDSDAHRLGLKEGDQILSVNGVDFEDIEHSEAVKVL-KTAREIQMRVRYFP 83
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1266-1316 4.13e-08

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


Pssm-ID: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 52.28  E-value: 4.13e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1266 LGISIVSGeKG---------GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06704     12 LGISIAGG-KGstpykgddeGIFISRVTEGGPAAKAGVRVGDKLLEVNGVDLVDADHHEA 70
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 541-614 4.17e-08

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


Pssm-ID: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 52.28  E-value: 4.17e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  541 LGFDMAEGVNEPCFPG-DCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 614
Cdd:cd06704     12 LGISIAGGKGSTPYKGdDEGIFISRVTEGGPAAkAGVRVGDKLLEVNGVDLVDADHHEAVEALKNSGNTVTMVVLR 87
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1253-1330 4.28e-08

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 52.56  E-value: 4.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1253 EPRHVKVQKGSEP-------LGISIVSGEKG-----GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLI 1319
Cdd:cd06714      3 LIGRIILQRDPKDgsvsgngLGLKVVGGKMTesgrlGAYVTKVKPGSVADTVGhLREGDEVLEWNGISLQGKTFEEVQDI 82

                           90
                   ....*....|.
gi 2462521864 1320 IGQQCDTITIL 1330
Cdd:cd06714     83 ISQSKGEVELV 93
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 625-699 4.85e-08

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 51.90  E-value: 4.85e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  625 PLHINLSGQKDSGIsleNGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:pfam00595   11 GLGFSLKGGSDQGD---PGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 625-700 4.87e-08

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


Pssm-ID: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 51.92  E-value: 4.87e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  625 PLHINLSGQKDsgisLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 700
Cdd:cd06683     14 PLGITISGTEE----PFDPIVISGLTEGGLAERTGAIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTLKISR 85
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 1279-1329 5.69e-08

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: 52.21  E-value: 5.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1279 YVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1329
Cdd:cd06746     45 YLESVDPGGVADKAGLKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVL 95
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
304-506 6.27e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.72  E-value: 6.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  304 ELLQSELTELRTtQVKTA-KESEKYREERDAVYSEyklimSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEA 382
Cdd:COG3206    178 EFLEEQLPELRK-ELEEAeAALEEFRQKNGLVDLS-----EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  383 LRQIKDTVTmdagrANKEVEILRKQCKALCQELKEALQEadvakcrrdwaFQERD-KIVAERDSIRTLCDNLRRERDRAV 461
Cdd:COG3206    252 GPDALPELL-----QSPVIQQLRAQLAELEAELAELSAR-----------YTPNHpDVIALRAQIAALRAQLQQEAQRIL 315

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462521864  462 SELAEALRSLddtRKQKNDVSRELKELKEQMESQLEKEARFRQLM 506
Cdd:COG3206    316 ASLEAELEAL---QAREASLQAQLAQLEARLAELPELEAELRRLE 357
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1405-1486 6.35e-08

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


Pssm-ID: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 51.56  E-value: 6.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1405 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPAKgPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1484
Cdd:cd06767      2 EPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAH-QAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                   ..
gi 2462521864 1485 QY 1486
Cdd:cd06767     81 QY 82
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 557-614 6.36e-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: 6.36e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  557 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDkkQAIKALLNGEGAINMVVRR 614
Cdd:cd06716     30 DTGIYVSEVDPNSIAakDGRIREGDQILQINGVDVQNRE--EAIALLSEEEKSITLLVAR 87
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
293-500 6.91e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 56.07  E-value: 6.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  293 TAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSE 372
Cdd:COG1340      7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  373 KKAANEEMEALRQIKDTvtmdAGRANKEVEILRKQCKAL-------------------------------------CQEL 415
Cdd:COG1340     87 LNELREELDELRKELAE----LNKAGGSIDKLRKEIERLewrqqtevlspeeekelvekikelekelekakkalekNEKL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  416 KEALQEADVAKCRRDWAFQ-------ERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKEL 488
Cdd:COG1340    163 KELRAELKELRKEAEEIHKkikelaeEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242

                          250
                   ....*....|..
gi 2462521864  489 KEQMESQLEKEA 500
Cdd:COG1340    243 RKELKKLRKKQR 254
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 90-499 7.29e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 57.72  E-value: 7.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   90 LNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRL---LSDQTRLKDDVDMLRRENGQLLRERNL 166
Cdd:TIGR04523  157 LNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkkIQKNKSLESQISELKKQNNQLKDNIEK 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  167 LQQSWEDMKRLHEEDQKEIGDLRAQQQqvlkhngssEILNKLYDTAMDkLEVVKKDYDALRKRYSEkvaiHNADLSRLEQ 246
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQN---------KIKKQLSEKQKE-LEQNNKKIKELEKQLNQ----LKSEISDLNN 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  247 lgEENQRLLKQ-TEMLTQQRDTAIQLQHQcalsLRRFEAIHHELNKATAQnkdlqwemelLQSELTELRTTQVKTAKESE 325
Cdd:TIGR04523  303 --QKEQDWNKElKSELKNQEKKLEEIQNQ----ISQNNKIISQLNEQISQ----------LKKELTNSESENSEKQRELE 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  326 KYReerdavySEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVtmdagraNKEVEILR 405
Cdd:TIGR04523  367 EKQ-------NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL-------EKEIERLK 432

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  406 KQCKALCQELKEaLQEADVAK--------CRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSElaealrsLDDTRKQ 477
Cdd:TIGR04523  433 ETIIKNNSEIKD-LTNQDSVKeliiknldNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE-------LKKLNEE 504

                          410       420
                   ....*....|....*....|..
gi 2462521864  478 KNDVSRELKELKEQMESQLEKE 499
Cdd:TIGR04523  505 KKELEEKVKDLTKKISSLKEKI 526
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 205-519 7.39e-08

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 57.67  E-value: 7.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  205 LNKLYDTAMDKLEV------VKKDYDALRKRysEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQhqcALS 278
Cdd:pfam02463  175 LKKLIEETENLAELiidleeLKLQELKLKEQ--AKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL---RDE 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  279 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDavysEYKLIMSERDQVISELDKLQTE 358
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL----KLERRKVDDEEKLKESEKEKKK 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  359 VELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVakcRRDWAFQERDK 438
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK---LKEEELELKSE 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  439 IVAERDSI----RTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKEL------KEQMESQLEKEARFRQLMAH 508
Cdd:pfam02463  403 EEKEAQLLlelaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelkllkDELELKKSEDLLKETQLVKL 482

                          330
                   ....*....|.
gi 2462521864  509 SSHDSAIDTDS 519
Cdd:pfam02463  483 QEQLELLLSRQ 493
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 630-700 7.40e-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: 51.38  E-value: 7.40e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  630 LSGQKDSGISLengvYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 700
Cdd:cd06753     14 LQGGKDFNQPL----TISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLER 79
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 534-614 8.94e-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: 51.49  E-value: 8.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  534 EDIDLK----ALGFDMAEGVNEPCFP---GDCGIFVTKVDKGSIAdGR--LRVNDWLLRINDVDLINKDKKQAIKALLNG 604
Cdd:cd06702      1 EEIHLVkaggPLGLSIVGGSDHSSHPfgvDEPGIFISKVIPDGAA-AKsgLRIGDRILSVNGKDLRHATHQEAVSALLSP 79

                           90
                   ....*....|
gi 2462521864  605 EGAINMVVRR 614
Cdd:cd06702     80 GQEIKLLVRH 89
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 ...
 633-691 9.93e-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: 51.12  E-value: 9.93e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  633 QKDSGISL------------ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQ 691
Cdd:cd06760     10 NKEPGVGLgiglcclplendIPGIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLNEAYAILSQCK 80
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 1256-1330 1.03e-07

PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467207 [Multi-domain]  Cd Length: 85  Bit Score: 51.11  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1256 HVKVQKGSEPLGISIVSGeKG--------GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1326
Cdd:cd06724      1 EIKLVKGPKGLGFSIAGG-VGnqhipgdnGIYVTKIIEGGAAQKDGrLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDV 79


                   ....
gi 2462521864 1327 ITIL 1330
Cdd:cd06724     80 VYLK 83
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1256-1320 1.05e-07

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


Pssm-ID: 467166 [Multi-domain]  Cd Length: 82  Bit Score: 51.09  E-value: 1.05e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1256 HVKVQK-GSEPLGISIVS-GEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06678      2 HVTLNKrDGEQLGIKLVRkKDEPGVFILDLLEGGLAARDGrLKSDDRVLAINGQDLRHGTPEQAAQII 69
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-542 1.05e-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: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   42 LLTDRQVNEKVENLSIQLRLMTRERNELRKRLAfathgtafdkrpyhRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKR 121
Cdd:COG1196    231 LLKLRELEAELEELEAELEELEAELEELEAELA--------------ELEAELEELRLELEELELELEEAQAEEYELLAE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  122 CEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhnGS 201
Cdd:COG1196    297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--EL 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  202 SEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNAdLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRR 281
Cdd:COG1196    375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  282 FEAihhELNKATAQNKDLQWEMELLQSELTELRTtQVKTAKESEKYREERDAVYSEY---------KLIMSERDQVISEL 352
Cdd:COG1196    454 LEE---EEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFlegvkaallLAGLRGLAGAVAVL 529

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  353 DKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRAN--------------------------KEVEILRK 406
Cdd:COG1196    530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpldkiraraalaaalargaigaavDLVASDLR 609

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  407 QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAE------------------RDSIRTLCDNLRRERDRAVSELAEAL 468
Cdd:COG1196    610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrevtlegeggsaggsltGGSRRELLAALLEAEAELEELAERLA 689

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  469 RSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAI----------------------DTDSMEWETEV 526
Cdd:COG1196    690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREElleelleeeelleeealeelpePPDLEELEREL 769

                          570
                   ....*....|....*.
gi 2462521864  527 VEFQREtedidLKALG 542
Cdd:COG1196    770 ERLERE-----IEALG 780
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 634-699 1.05e-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: 51.49  E-value: 1.05e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  634 KDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:cd23058     24 RDNPTGGSGPIYIKNILPKGAAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKLGGTVSLV 89
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
222-489 1.06e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  222 DYDALRKRYSEKVAIHN-------ADLSRLEQLGEEN-QRLLKQT---------------EMLTQQR--DTAIQLQHQca 276
Cdd:COG4913    156 DIRALKARLKKQGVEFFdsfsaylARLRRRLGIGSEKaLRLLHKTqsfkpigdlddfvreYMLEEPDtfEAADALVEH-- 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  277 lsLRRFEAIHHELNKATAQnkdlqweMELLQsELTELRTTQVKTAKESEKYREERDAVysEYKLIMSERDQVISELDKLQ 356
Cdd:COG4913    234 --FDDLERAHEALEDAREQ-------IELLE-PIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELR 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  357 TEVELAESKLKSSTSEKKAANEEMEALRQIKdtvtmdAGRANKEVEILRKQCKALCQELKEALQEAD--VAKCRR-DWAF 433
Cdd:COG4913    302 AELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRArlEALLAAlGLPL 375

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  434 -QERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK 489
Cdd:COG4913    376 pASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 648-700 1.10e-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: 51.19  E-value: 1.10e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  648 AVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 700
Cdd:cd06682     33 DVKKGSVAHRTGTLEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIRK 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-507 1.27e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   95 ERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDM 174
Cdd:COG1196    382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  175 KRLHEEDQKEIGDLRAQQQQVLKHNGSS----EILNKLYDTAMDKLEVVKKDYDALRKR-------------YSEKVAIH 237
Cdd:COG1196    462 LELLAELLEEAALLEAALAELLEELAEAaarlLLLLEAEADYEGFLEGVKAALLLAGLRglagavavligveAAYEAALE 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  238 NADLSRLEQLGEEN-QRLLKQTEMLTQQ---RDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSEL--T 311
Cdd:COG1196    542 AALAAALQNIVVEDdEVAAAAIEYLKAAkagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdT 621

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  312 ELRTTQVKTAKESEKYREERDAVyseyklimsERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 391
Cdd:COG1196    622 LLGRTLVAARLEAALRRAVTLAG---------RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  392 MDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRD------------------WAFQERDKIVAERDSIRTLCDNL 453
Cdd:COG1196    693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEaereelleelleeeelleEEALEELPEPPDLEELERELERL 772

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  454 RRERDR-------AVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEARfRQLMA 507
Cdd:COG1196    773 EREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIE-EIDRETR-ERFLE 831
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
288-604 1.31e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.06  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  288 ELNKATAQNKDLQWEMELLQSELTELrttqvktakesekyREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLK 367
Cdd:COG4372     32 QLRKALFELDKLQEELEQLREELEQA--------------REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  368 SSTSEKKAANEEMEALRQikdtvtmDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDwafQERDKIVAERDSIR 447
Cdd:COG4372     98 QAQEELESLQEEAEELQE-------ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK---ELEEQLESLQEELA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  448 TLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVV 527
Cdd:COG4372    168 ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  528 EFQRETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNG 604
Cdd:COG4372    248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 626-688 1.51e-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: 51.13  E-value: 1.51e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  626 LHINLSGQ---KDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLR 688
Cdd:cd23059     18 LGVSVKGKtskEDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETLR 83
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 648-688 1.91e-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: 50.56  E-value: 1.91e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462521864  648 AVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 688
Cdd:cd06782     20 SPIPGGPAEKAG-IKPGDVIVAVDGESVRGMSLDEVVKLLR 59
SH3_ZO-2 cd12027
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a ...
 1499-1560 2.30e-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: 49.53  E-value: 2.30e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1499 GDSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLdenAQKIQRGQIPSK 1560
Cdd:cd12027      1 GDSFFIRTHFEYEKELPQSLAFTRGEIFRVVDTLYDGKLGNWLAVRI---GNELEKGLIPNK 59
PDZ_PICK1-like cd06722
PDZ domain of PICK1 (protein interacting with C-kinase 1) and similar domains; PDZ (PSD-95 ...
 633-700 2.35e-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: 50.11  E-value: 2.35e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  633 QKDS----GISLENG------VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 700
Cdd:cd06722      6 KKDAqnliGISIGGGapycpcLYIVQVFDNTPAAKDGTLAAGDEIVGVNGKSVKGKTKVEVAKMIQAVKGEVTIHYNK 83
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
 638-699 2.44e-07

PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467250 [Multi-domain]  Cd Length: 75  Bit Score: 49.55  E-value: 2.44e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  638 ISLENGVYAAAVLPGSPAakEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:cd06769     16 AGSERPVVVRSVTPGGPS--EGKLLPGDQILKINNEPVEDLPRERVIDLIRECKDSIVLTVL 75
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 1255-1329 2.67e-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: 49.57  E-value: 2.67e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1255 RHVKVQKG-SEPLGISIvSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1329
Cdd:cd06726      1 RLVEFEKArDEPLGATI-KMEEDSVIVARILHGGMAHRSGlLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTF 76
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 641-699 2.80e-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: 49.57  E-value: 2.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:cd06726     21 EDSVIVARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLI 79
PDZ1_APBA1_3-like cd06720
PDZ domain 1 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ...
 644-690 3.02e-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: 49.95  E-value: 3.02e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2462521864  644 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 690
Cdd:cd06720     29 VVVANMMPGGPAARSGKLNIGDQIMSINGTSLVGLPLSTCQAIIKNL 75
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
209-501 3.25e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 3.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  209 YDTAMDKLEVVKKDYDALRKRYsEKVAIHNADLSrlEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCAL---SLRRFEAI 285
Cdd:PRK03918   160 YENAYKNLGEVIKEIKRRIERL-EKFIKRTENIE--ELIKEKEKELEEVLREINEISSELPELREELEKlekEVKELEEL 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  286 HHELNKATAQNKDLQWEMELLQSELTELRT-------------TQVKTAKESEKYREERDAVYSEYKLIMSERDQVISEL 352
Cdd:PRK03918   237 KEEIEELEKELESLEGSKRKLEEKIRELEErieelkkeieeleEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  353 DKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTM---------DAGRANKEVEILRKQCKalCQELKEALQEAD 423
Cdd:PRK03918   317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyeEAKAKKEELERLKKRLT--GLTPEKLEKELE 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  424 VAKCRRDWAFQERDKIVAERDSIRtlcdNLRRERDRAVSELAEAL-------RSLDDTRKQK---------NDVSRELKE 487
Cdd:PRK03918   395 ELEKAKEEIEEEISKITARIGELK----KEIKELKKAIEELKKAKgkcpvcgRELTEEHRKElleeytaelKRIEKELKE 470

                          330
                   ....*....|....
gi 2462521864  488 LKEQmESQLEKEAR 501
Cdd:PRK03918   471 IEEK-ERKLRKELR 483
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 1263-1316 3.34e-07

PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains. Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467179 [Multi-domain]  Cd Length: 88  Bit Score: 49.91  E-value: 3.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1263 SEPLGISIV------SGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06692      7 SKGLGIKIIggyrenTGEEFGIFIKRILPGGLAATDGrLKEGDLILEVNGESLQGVTNERA 67
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1256-1330 3.44e-07

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


Pssm-ID: 467170 [Multi-domain]  Cd Length: 85  Bit Score: 49.65  E-value: 3.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1256 HVKVQKGSEP-LGISIVSGEK----GGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITI 1329
Cdd:cd06682      2 HVKLPKRSGVgLGITISAPKNrkpgDPLIISDVKKGSVAHRTGtLEPGDKLLAIDNIRLDNCSMEDAAQIL-QQAEDIVK 80


                   .
gi 2462521864 1330 L 1330
Cdd:cd06682     81 L 81
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 1257-1340 3.46e-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: 49.60  E-value: 3.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1257 VKVQKGSEPLGISIVSGEK---GGIYVSKV-TVGSIAHQAGLEYGDQLLEFNGINLRSATEQQArliigqqcdtITILAQ 1332
Cdd:cd06673      6 IEINKGKKGLGLSIVGGSDtllGAIIIHEVyEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEA----------INVLRQ 75


                   ....*...
gi 2462521864 1333 YNPHVHQL 1340
Cdd:cd06673     76 TPQKVRLL 83
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 306-501 3.79e-07

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: 54.38  E-value: 3.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  306 LQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALR- 384
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKe 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  385 ----QIKDTVTM-------------DAGRANKEVEILR---KQCKALCQELKEALQEADvakcrrdwafQERDKIVAERD 444
Cdd:COG4942    105 elaeLLRALYRLgrqpplalllspeDFLDAVRRLQYLKylaPARREQAEELRADLAELA----------ALRAELEAERA 174

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  445 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQmESQLEKEAR 501
Cdd:COG4942    175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIA 230
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 628-696 3.85e-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: 49.58  E-value: 3.85e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  628 INLSGQKDS--GISLENGVYAAAVLPGSPAakEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06727     15 IAVSGGRDNphFQSGDTSIVISDVLKGGPA--EGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANI 83
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
279-542 3.91e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.52  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  279 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTE 358
Cdd:COG4372     37 LFELDKLQEELEQLREELEQAREELEQLEEELEQAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  359 VELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEAlqEADVAKCRRDWAFQERDK 438
Cdd:COG4372    110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDE 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  439 IVAER----DSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSA 514
Cdd:COG4372    188 LLKEAnrnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267

                          250       260
                   ....*....|....*....|....*...
gi 2462521864  515 IDTDSMEWETEVVEFQRETEDIDLKALG 542
Cdd:COG4372    268 LVEKDTEEEELEIAALELEALEEAALEL 295
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 345-532 3.95e-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: 55.03  E-value: 3.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  345 RDQVISELDKLQTEVelAESKLKSSTSE--KKAANEEMEALRQIKDTVTMDAGRANKEvEILRKQCKALCQ-ELKE---- 417
Cdd:pfam05701   37 RKLVELELEKVQEEI--PEYKKQSEAAEaaKAQVLEELESTKRLIEELKLNLERAQTE-EAQAKQDSELAKlRVEEmeqg 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  418 --------ALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK 489
Cdd:pfam05701  114 iadeasvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATK 193

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  490 EQMESqlekearfrqlmAHSSHDSA----------IDTDSMEWETEVVEFQRE 532
Cdd:pfam05701  194 ESLES------------AHAAHLEAeehrigaalaREQDKLNWEKELKQAEEE 234
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 323-507 4.34e-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: 52.74  E-value: 4.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  323 ESEKYREERDAVySEYKLIMSERDQVISELDKLQTEV-----ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRA 397
Cdd:cd07596      2 EDQEFEEAKDYI-LKLEEQLKKLSKQAQRLVKRRRELgsalgEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  398 NKEVeilRKQCKALCQELKEALQEADVAKCrrdwAFQERDKIVAERDSIRTLCDNLRRERDRAVS-------ELAEALRS 470
Cdd:cd07596     81 EAQA---NQELVKLLEPLKEYLRYCQAVKE----TLDDRADALLTLQSLKKDLASKKAQLEKLKAapgikpaKVEELEEE 153

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462521864  471 LDDTRKQKNDVSRELKELKEQMESQLE--KEARFRQLMA 507
Cdd:cd07596    154 LEEAESALEEARKRYEEISERLKEELKrfHEERARDLKA 192
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1256-1329 4.70e-07

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: 49.31  E-value: 4.70e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1256 HVKVQKGSEPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA-RLIIGQQCDTITI 1329
Cdd:cd10834      5 HLYTTSDDYCLGFNIRGGsEYGlGIYVSKVDPGGLAEQNGIKVGDQILAVNGVSFEDITHSKAvEVLKSQTHLMLTI 81
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 618-688 4.88e-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: 53.72  E-value: 4.88e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  618 LGGKVVTPLHINLSGQKDS-GISL---ENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 688
Cdd:COG0793     43 LDPEEYEDFQESTSGEFGGlGAELgeeDGKVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLLR 116
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 1260-1331 5.24e-07

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: 49.32  E-value: 5.24e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1260 QKGsepLGISIVSGEKG-----GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1331
Cdd:cd06694     12 QKG---LGFTIVGGENSgsldlGIFVKSIIPGGPADKDGrIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVELII 86
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 611-692 5.61e-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: 49.24  E-value: 5.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  611 VVRR-RKSLGgkvvtplhINLSGQKDSGISLEN-----GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECE 684
Cdd:cd06671      7 LWREpGKSLG--------ISIVGGRVMGSRLSNgeeirGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEAV 78


                   ....*...
gi 2462521864  685 SLLRSCQD 692
Cdd:cd06671     79 EAIRNAGN 86
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
154-416 5.81e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 53.38  E-value: 5.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  154 RRE-NGQLLRERNLLQQswedMKRLHEEDQKEIGDLRAQQQQVLkhngssEILNKLYDTA------MDKLEVVKKDYDAL 226
Cdd:COG1340     45 RDElNAQVKELREEAQE----LREKRDELNEKVKELKEERDELN------EKLNELREELdelrkeLAELNKAGGSIDKL 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  227 RKRYsekvaihnadlsrlEQLgEENQrllkQTEMLTQQRDTAIQLQhqcalsLRRFEAIHHELNKATAQNKDLQW---EM 303
Cdd:COG1340    115 RKEI--------------ERL-EWRQ----QTEVLSPEEEKELVEK------IKELEKELEKAKKALEKNEKLKElraEL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  304 ELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEAL 383
Cdd:COG1340    170 KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL 249

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462521864  384 RQIKdtvtmDAGRANKEVEILRKQCKALCQELK 416
Cdd:COG1340    250 RKKQ-----RALKREKEKEELEEKAEEIFEKLK 277
PDZ5_PTPN13-like cd06697
PDZ domain 5 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 625-696 6.03e-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: 48.88  E-value: 6.03e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  625 PLHINLSGQKDSgisLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06697     14 QLGLKLTGGSDS---KYQVIYVLEIVPGSAAAEEGSLQPLDIIHYINGVSTQGMTLEDAVRALEASLPTVVL 82
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1255-1316 6.04e-07

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: 48.72  E-value: 6.04e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1255 RHVKVQKgsEP---LGISIvsgeKGG------IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06801      1 RTVRVVK--QDvggLGISI----KGGaehkmpILISKIFKGQAADQTGqLFVGDAILSVNGENLEDATHDEA 66
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1253-1332 7.06e-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: 48.80  E-value: 7.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1253 EPRHVKVQKGSEPLGISIVSGeKG---------GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1322
Cdd:cd06703      1 ETITTTLIRDGKGLGFSIAGG-KGstpfrdgdeGIFISRITEGGAADRDGkLQVGDRVLSINGVDVTEARHDQAVALLTS 79

                           90
                   ....*....|
gi 2462521864 1323 QCDTITILAQ 1332
Cdd:cd06703     80 SSPTITLVVE 89
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
120-505 8.33e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 8.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  120 KRCEEVAKETDFYHTLhSRLLSDqtrLKDDVDMLRRENGQLLRERNLLQQSWEDMkrlhEEDQKEIGDLRAQQQQVLKHN 199
Cdd:PRK03918   283 KELKELKEKAEEYIKL-SEFYEE---YLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRL 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  200 GSSEILNKLYDTAMDKL---------------EVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQ 264
Cdd:PRK03918   355 EELEERHELYEEAKAKKeelerlkkrltgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  265 RDTA------IQLQHQCALsLRRFEA----IHHELNKATAQNKDL-----QWEMELL-QSELTELRTT--QVKTAKES-E 325
Cdd:PRK03918   435 KGKCpvcgreLTEEHRKEL-LEEYTAelkrIEKELKEIEEKERKLrkelrELEKVLKkESELIKLKELaeQLKELEEKlK 513

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  326 KYR-EERDAVYSEYKLIMSERDQVISELDKLQTEVE---LAESKLKSSTSEKKAANEEM-EALRQIKDTVTMDAGRANKE 400
Cdd:PRK03918   514 KYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEELaELLKELEELGFESVEELEER 593

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  401 VEILRK------QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCD------------NLRRERDRAVS 462
Cdd:PRK03918   594 LKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseeeyeELREEYLELSR 673

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2462521864  463 ELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQL 505
Cdd:PRK03918   674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
 632-696 8.54e-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: 48.64  E-value: 8.54e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  632 GQKDSGiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd23071     21 GGENTG-KLDLGIFIASIIPGGPAEKDGRIKPGGRLISLNNISLEGVTFNTAVKILQNSPDEVEL 84
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 1405-1485 8.61e-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: 48.86  E-value: 8.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1405 EPRVVFIKK-SQLELGVHLCGGN-----------LHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVyVE 1472
Cdd:cd06671      1 PPRRVELWRePGKSLGISIVGGRvmgsrlsngeeIRGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEA-VE 79

                           90
                   ....*....|....
gi 2462521864 1473 MLK-PRDGVRLKVQ 1485
Cdd:cd06671     80 AIRnAGNPVVFLVQ 93
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 279-481 8.77e-07

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: 52.23  E-value: 8.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  279 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMS--ERDQ-----VIS- 350
Cdd:COG1579      9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEeqlgnVRNn 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  351 -ELDKLQTEVELAESKLKSSTSEKKAANEEMEALRqikdtvtmdagranKEVEILRKQCKALCQELKEALQEADvakcrr 429
Cdd:COG1579     89 kEYEALQKEIESLKRRISDLEDEILELMERIEELE--------------EELAELEAELAELEAELEEKKAELD------ 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  430 dwafQERDKIVAERDSirtlcdnLRRERDRAVSELAEALRSL-DDTRKQKNDV 481
Cdd:COG1579    149 ----EELAELEAELEE-------LEAEREELAAKIPPELLALyERIRKRKNGL 190
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 540-614 9.17e-07

PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467209 [Multi-domain]  Cd Length: 87  Bit Score: 48.42  E-value: 9.17e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  540 ALGFDMA--EGVNEPCFP-GDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 614
Cdd:cd06727     10 GFGFGIAvsGGRDNPHFQsGDTSIVISDVLKGGPAEGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANITVKR 87
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 137-421 9.40e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.87  E-value: 9.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  137 SRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQ---QVLKHNgssEILNKLYDTam 213
Cdd:TIGR04523  338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdleSKIQNQ---EKLNQQKDE-- 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  214 dKLEVVKKDYDALRKRY---SEKVAIHNADLSRLEqlgEENQRLLKQTEMLTQQRDtaiQLQHQCALSLRRFEAIHH--- 287
Cdd:TIGR04523  413 -QIKKLQQEKELLEKEIerlKETIIKNNSEIKDLT---NQDSVKELIIKNLDNTRE---SLETQLKVLSRSINKIKQnle 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  288 -----------ELNKATAQNKDLQWEMELLQSELTELRTTQVK------------TAKESEKYREERDAVYSEYKLIMSE 344
Cdd:TIGR04523  486 qkqkelkskekELKKLNEEKKELEEKVKDLTKKISSLKEKIEKlesekkekeskiSDLEDELNKDDFELKKENLEKEIDE 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  345 RDQVISEL----DKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALcQELKEALQ 420
Cdd:TIGR04523  566 KNKEIEELkqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI-KSKKNKLK 644


                   .
gi 2462521864  421 E 421
Cdd:TIGR04523  645 Q 645
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 47-540 9.63e-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: 54.20  E-value: 9.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   47 QVNEKVENLSIQLRLMTRERNELRKRLAFATHgtafdkrpyHRLNPDYERLKIQCVRAMSDLqsLQNQHTNALKRCEEVA 126
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK---------QQSSIEEQRRLLQTLHSQEIH--IRDAHEVATSIREISC 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  127 KETDFYHTLHSrLLSDQTRLKD-------DVDMLRRENGQ---LLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVL 196
Cdd:TIGR00618  373 QQHTLTQHIHT-LQQQKTTLTQklqslckELDILQREQATidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  197 KHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEqlgeENQRLLKQTEMLTQQRDTAI------- 269
Cdd:TIGR00618  452 QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ----EEPCPLCGSCIHPNPARQDIdnpgplt 527

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  270 ----QLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELrTTQVKTAKES-EKYREERDAVYSEYKLIMSE 344
Cdd:TIGR00618  528 rrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL-TQCDNRSKEDiPNLQNITVRLQDLTEKLSEA 606

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  345 RDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADV 424
Cdd:TIGR00618  607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  425 AKCRRDWAFQErdkIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRE-LKELKEQMESQLEKEArfr 503
Cdd:TIGR00618  687 SEKEQLTYWKE---MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQsLKELMHQARTVLKART--- 760

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2462521864  504 qlmahsshdsaiDTDSMEWETEVVEFQRETEDIDLKA 540
Cdd:TIGR00618  761 ------------EAHFNNNEEVTAALQTGAELSHLAA 785
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 286-547 9.70e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 54.21  E-value: 9.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  286 HHELNKATAQNKDLQwemELLQSELTEL----------RTTQVKTAKESEKYREERDAVYSEYKLIMSER----DQVISE 351
Cdd:pfam02463  108 EYYINGKNVTKKEVA---ELLESQGISPeaynflvqggKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEAlkklIEETEN 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  352 LDKLQTEVELAESKLKSstsEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRdw 431
Cdd:pfam02463  185 LAELIIDLEELKLQELK---LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE-- 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  432 aFQERDKIVAERDSIRTLC----DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMA 507
Cdd:pfam02463  260 -IEKEEEKLAQVLKENKEEekekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2462521864  508 HSSHDSAIDTDSMEWETEVVEFQRETEDIDLKALGFDMAE 547
Cdd:pfam02463  339 ELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 1256-1330 1.13e-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: 48.49  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1256 HVKVQKGSEPLGISIVSG------------EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQ 1323
Cdd:cd10822      5 HKLRQGENLILGFSIGGGidqdpsknpfsyTDKGIYVTRVSEGGPAEKAGLQVGDKILQVNGWDMTMVTHKQAVKRLTKK 84


                   ....*..
gi 2462521864 1324 CDTITIL 1330
Cdd:cd10822     85 KPVLRML 91
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 1266-1316 1.31e-06

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: 48.05  E-value: 1.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462521864 1266 LGISIVSGEKG-GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06674     16 LGLSIVGKRNDtGVFVSDIVKGGAADADGrLMQGDQILSVNGEDVRNASQEAA 68
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 198-551 1.54e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 53.19  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  198 HNGSSEILNKLYDTAMDKLEVVKKDYDALrkrYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCal 277
Cdd:pfam05483   55 NSGDCHYQEGLKDSDFENSEGLSRLYSKL---YKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFEN-- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  278 slrrfEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQT 357
Cdd:pfam05483  130 -----EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRV 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  358 EVELA--ESKLKSSTSEKKAANEEMEALRQIKDTvtmdagraNKEVEILRKQCKALCQELKE---ALQEAdvakcrRDWA 432
Cdd:pfam05483  205 QAENArlEMHFKLKEDHEKIQHLEEEYKKEINDK--------EKQVSLLLIQITEKENKMKDltfLLEES------RDKA 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  433 FQERDKIVAERDSIRTLCDnlrrERDRAVSELAEALRSLDDTRKQKNDVSRELK-------ELKEQMESQLEKEARFRQl 505
Cdd:pfam05483  271 NQLEEKTKLQDENLKELIE----KKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKA- 345

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2462521864  506 mAHSSHDSAIDTDSMEWETEV-VEFQR-ETEDIDLKALGFDMAEGVNE 551
Cdd:pfam05483  346 -AHSFVVTEFEATTCSLEELLrTEQQRlEKNEDQLKIITMELQKKSSE 392
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-354 1.56e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   46 RQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNaLKrcEEV 125
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LN--EEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  126 AKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEdQKEIGDLRAQQQQVLkhngssEIL 205
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-LEALLNERASLEEAL------ALL 892

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  206 NKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQLgeeNQRLLKQTEMLT-QQRDTaiqlqhqcalslrrFEA 284
Cdd:TIGR02168  893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSeEYSLT--------------LEE 955

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  285 IHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSER---DQVISELDK 354
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKetlEEAIEEIDR 1028
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 528-614 1.58e-06

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: 47.59  E-value: 1.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  528 EFQRETEDIDlKALGFDMAEGVNEPCFPGdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGE 605
Cdd:cd06792      2 VFEVELSKKD-GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAeqDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAG 78


                   ....*....
gi 2462521864  606 GAINMVVRR 614
Cdd:cd06792     79 QVVTLVLER 87
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 1257-1328 1.65e-06

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


Pssm-ID: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 47.62  E-value: 1.65e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1257 VKVQKGSEPLGISIVSGEKGG-IYVSKVTVGSIAHQAGLEY-GDQLLEFNGINLRSATEQQARLIIGQQCDTIT 1328
Cdd:cd06799      3 VRLVKNNEPLGATIKRDEKTGaIVVARIMRGGAADRSGLIHvGDELREVNGISVEGKDPEEVIQILANSQGPIT 76
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1255-1316 1.65e-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: 47.63  E-value: 1.65e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1255 RHVKVQKG-SEPLGISIVSGEKGG-----IYVSKV-TVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06679      1 KTVTIKKEpSESLGISVAGGRGSRrgdlpIYVTNVqPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEA 69
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
50-513 1.82e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   50 EKVENLSiQLRLMTRERNELRKRLAF-----ATHGTAFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEE 124
Cdd:COG4913    249 EQIELLE-PIRELAERYAAARERLAEleylrAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  125 vaketdfyhtLHSRLLSDQTrlkDDVDMLRRENGQLLRERNLLQQSWEDMKRL-------HEEDQKEIGDLRAQ-QQQVL 196
Cdd:COG4913    328 ----------LEAQIRGNGG---DRLEQLEREIERLERELEERERRRARLEALlaalglpLPASAEEFAALRAEaAALLE 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  197 KHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSE----KVAIHNADLSRLEQLGEE---------------------- 250
Cdd:COG4913    395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrKSNIPARLLALRDALAEAlgldeaelpfvgelievrpeee 474

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  251 -----------NQRL------------------LKQTEMLTQQR-------------------------DTAIQ--LQHQ 274
Cdd:COG4913    475 rwrgaiervlgGFALtllvppehyaaalrwvnrLHLRGRLVYERvrtglpdperprldpdslagkldfkPHPFRawLEAE 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  275 --------CALS---LRRFE-AI-----------HHELNK-------------ATAQNKDLQWEMELLQSELTELRTTQV 318
Cdd:COG4913    555 lgrrfdyvCVDSpeeLRRHPrAItragqvkgngtRHEKDDrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLE 634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  319 KTAKESEKYREERDA-----VYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMD 393
Cdd:COG4913    635 ALEAELDALQERREAlqrlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGE 714

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  394 AGRANKEveilRKQCKALCQELKEALQEA-DVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 472
Cdd:COG4913    715 IGRLEKE----LEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  473 DTRKQ--------KNDVSREL-------KELKEQMESQL-EKEARFRQLMAHSSHDS 513
Cdd:COG4913    791 RAMRAfnrewpaeTADLDADLeslpeylALLDRLEEDGLpEYEERFKELLNENSIEF 847
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 632-699 1.85e-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: 47.74  E-value: 1.85e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  632 GQKDS-GISLENG---------VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:cd06675      8 GPQDSlGISIAGGvgsplgdvpVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKNASGTIILQVV 85
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 644-699 1.94e-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: 1.94e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  644 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:cd06676     28 IYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTLTVL 83
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 641-698 2.17e-06

PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 9 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ9 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ9 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467263 [Multi-domain]  Cd Length: 79  Bit Score: 46.96  E-value: 2.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 698
Cdd:cd10817     21 ENGIVIKSLTEGGPAAKDGRLKVGDQILAVDDESVVGCPYEKAISLLKTAKGTVKLTV 78
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 532-603 2.24e-06

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


Pssm-ID: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 47.23  E-value: 2.24e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  532 ETEDIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 603
Cdd:cd06791      1 ETFEVELvkdeQGLGITIAGYVGEKASGELSGIFVKSIIPGSAAdqDGRIQVNDQIIAVDGVNLQGFTNQEAVEVLRN 78
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 642-698 2.27e-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: 46.96  E-value: 2.27e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  642 NGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 698
Cdd:cd23060     23 SGIFVKSISPGGVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 616-699 2.49e-06

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: 47.40  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  616 KSLGGKVVTPLHinlsgqkdsgislengvYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLT 695
Cdd:cd23070     27 RSINGELYAPLQ-----------------HVSAVLEGGAADKAG-VRKGDRILEVNGVNVEGATHKQVVDLIKSGGDELT 88


                   ....
gi 2462521864  696 LSLL 699
Cdd:cd23070     89 LTVI 92
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1503-1561 2.59e-06

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


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 45.92  E-value: 2.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1503 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWMAWQLDENaqkiQRGQIPSKY 1561
Cdd:cd00174      1 YARALYDYEAQDDDELSFKKGDIITVLEKDDDG----WWEGELNGG----REGLFPANY 51
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 93-523 2.74e-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: 52.48  E-value: 2.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   93 DYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAketdfyHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWE 172
Cdd:pfam01576  423 ESERQRAELAEKLSKLQSELESVSSLLNEAEGKN------IKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLED 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  173 DMKRLHEEDQKEIGDLRAQQQQVLKHNGS-SEILNKLYDTA--MDKLEVVKK----DYDALRKRYSEKVAIHN------- 238
Cdd:pfam01576  497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQlSDMKKKLEEDAgtLEALEEGKKrlqrELEALTQQLEEKAAAYDklektkn 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  239 ----------ADLSRLEQLG---EENQRLLKQteMLTQQRDTAIQLQHQ-------------CALSL-RRFEAIHHELNK 291
Cdd:pfam01576  577 rlqqelddllVDLDHQRQLVsnlEKKQKKFDQ--MLAEEKAISARYAEErdraeaeareketRALSLaRALEEALEAKEE 654

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  292 ATAQNKDLQWEME---------------------LLQSELTELRTtQVK------TAKESEKYREERD--AVYSEYKLIM 342
Cdd:pfam01576  655 LERTNKQLRAEMEdlvsskddvgknvhelerskrALEQQVEEMKT-QLEeledelQATEDAKLRLEVNmqALKAQFERDL 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  343 SERD--------QVISELDKLQTEVElAESKLKS--STSEKKAANEEMEALRQIKDtvtmdagrANKEVEILRKQCKALC 412
Cdd:pfam01576  734 QARDeqgeekrrQLVKQVRELEAELE-DERKQRAqaVAAKKKLELDLKELEAQIDA--------ANKGREEAVKQLKKLQ 804

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  413 QELKEALQEADVAKCRRDWAF-----QERDKIVAERDSIR-----TLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVS 482
Cdd:pfam01576  805 AQMKDLQRELEEARASRDEILaqskeSEKKLKNLEAELLQlqedlAASERARRQAQQERDELADEIASGASGKSALQDEK 884

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2462521864  483 RELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWE 523
Cdd:pfam01576  885 RRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTE 925
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 1262-1332 3.02e-06

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


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 46.75  E-value: 3.02e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864 1262 GSEPLGISIVSGEKGG--IYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1332
Cdd:cd23068      9 SNTPWGFRLQGGADFGqpLSIQKVNPGSPADKAGLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQ 81
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
343-504 3.18e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 3.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  343 SERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEalrqikdtvtmdagRANKEVEILRKQCKALCQELKEALQEA 422
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE--------------QARSELEQLEEELEELNEQLQAAQAEL 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  423 DVAKcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARF 502
Cdd:COG4372     97 AQAQ-------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169


                   ..
gi 2462521864  503 RQ 504
Cdd:COG4372    170 EQ 171
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 626-689 3.30e-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: 46.96  E-value: 3.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  626 LHINLSGQKDSGISlENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 689
Cdd:cd06758     14 LGIQITGGKGSKRG-DIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAILRS 76
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
239-468 3.40e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 3.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  239 ADLSRLEQLGEenqRLLKQTEMLTQQRDTAIQLQHQcALSLRRFEAIHHELNKATAQNKDLQWEMEL--LQSELTELRTT 316
Cdd:COG4913    235 DDLERAHEALE---DAREQIELLEPIRELAERYAAA-RERLAELEYLRAALRLWFAQRRLELLEAELeeLRAELARLEAE 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  317 QVKTAKESEKYREERDAVYSEYklimseRDQVISELDKLQTEVELAESKLKSStseKKAANEEMEALRQIKDTVTMDAgr 396
Cdd:COG4913    311 LERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEER---ERRRARLEALLAALGLPLPASA-- 379

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  397 anKEVEILRKQCKALCQELKEALQEADV----AKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEAL 468
Cdd:COG4913    380 --EEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
242-492 3.41e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  242 SRLEQLGEENQRLLKQTEMLTQQRDTAiqlqhqcalsLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTA 321
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREELEQA----------REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  322 KESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQikdtvTMDAGRANKEV 401
Cdd:COG4372    101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE-----ELAALEQELQA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  402 EILRKQCKALCQELKEALQEADV--AKCRRDWAFQERDKIVAERDSIRTlcDNLRRERDRAVSELAEALRSLDDTRKQKN 479
Cdd:COG4372    176 LSEAEAEQALDELLKEANRNAEKeeELAEAEKLIESLPRELAEELLEAK--DSLEAKLGLALSALLDALELEEDKEELLE 253

                          250
                   ....*....|...
gi 2462521864  480 DVSRELKELKEQM 492
Cdd:COG4372    254 EVILKEIEELELA 266
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 641-696 3.86e-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: 46.49  E-value: 3.86e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06724     27 DNGIYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYL 82
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 1257-1321 4.30e-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: 4.30e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1257 VKVQKGSEPLGISIvSGEKG------GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIG 1321
Cdd:cd06758      5 MHLLKEKGGLGIQI-TGGKGskrgdiGIFVAGVEEGGSADRDGrLKKGDELLMINGQSLIGLSHQEAVAILR 75
PDZ_neurabin-like cd06790
PDZ domain of neurabin-1 and neurabin-2, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1257-1316 4.45e-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: 46.64  E-value: 4.45e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1257 VKVQKGSEPLGISIV-------SG-EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06790      5 VELEKGSEGLGISIIgmgvgadAGlEKLGIFVKTVTEGGAAQRDGrIQVNDQIVEVDGISLVGVTQAFA 73
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 608-677 4.66e-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: 50.15  E-value: 4.66e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  608 INMVVRRRKSL--GGKV------VTPLHINLSGQKDSGISLENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDN 677
Cdd:COG0265    159 INLAKRVVEQLieTGRVrrgwlgVTIQPVTPELAEALGLPEPEGVLVARVEPGSPAAKAG-LRPGDVILAVDGKPVTS 235
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 641-699 4.66e-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: 4.66e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:cd06692     25 EFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSILRSASASNHMSLL 83
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1255-1330 4.79e-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: 4.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1255 RHVKVQKG-SEPLGISIVSGEKG-----------GIYVSKVT-VGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIG 1321
Cdd:cd06701      5 QELTIVKEpGEKLGISIRGGAKGhagnpldptdeGIFISKINpDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILR 84


                   ....*....
gi 2462521864 1322 QQCDTITIL 1330
Cdd:cd06701     85 SVGDTLTLL 93
PDZ5_INAD-like cd23066
PDZ domain 5 of inactivation no after potential D (INAD), and related domains; PDZ (PSD-95 ...
 634-700 4.79e-06

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: 46.34  E-value: 4.79e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  634 KDSGISL----ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 700
Cdd:cd23066     10 KELGLSLspneGIGCTIADLLPGGYAEIDGKLQKGDIITKFNGDALSGLPFQVCYALFKGANGKISLEVTR 80
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
46-492 4.95e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 4.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   46 RQVNEKVENLsIQLRLMTRERNELRKRLAfathgtAFDKRpYHRLNPDYERLKiqcvRAMSDLQSLQNQHTNALKRCEEV 125
Cdd:COG4717    115 REELEKLEKL-LQLLPLYQELEALEAELA------ELPER-LEELEERLEELR----ELEEELEELEAELAELQEELEEL 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  126 AKETDFyhtlhsRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRlhEEDQKEIGDLRAQQQQVLKHNGSSEIl 205
Cdd:COG4717    183 LEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--ELEQLENELEAAALEERLKEARLLLL- 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  206 nklydtAMDKLEVVKKDYDALrkrYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAI 285
Cdd:COG4717    254 ------IAAALLALLGLGGSL---LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  286 HHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKES--EKYREERDAVYSEYKliMSERDQVISELDKLQTEVELAE 363
Cdd:COG4717    325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAG--VEDEEELRAALEQAEEYQELKE 402

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  364 sKLKSSTSEKKAANEEMEALRQI--KDTVTMDAGRANKEVEILRKQCKALCQELK----------------EALQEADVA 425
Cdd:COG4717    403 -ELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAeleaeleqleedgelaELLQELEEL 481

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  426 KCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELA-EALRSLDDTR--------------KQKNDVSRELKEL-- 488
Cdd:COG4717    482 KAELRELAEEWAALKLALELLEEAREEYREERLPPVLERAsEYFSRLTDGRyrliridedlslkvDTEDGRTRPVEELsr 561


                   ....*.
gi 2462521864  489 --KEQM 492
Cdd:COG4717    562 gtREQL 567
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 629-696 5.12e-06

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: 45.89  E-value: 5.12e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  629 NLSGQKDsgislENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06768     15 NLHAEKG-----RPGHFIREVDPGSPAERAG-LKDGDRLVEVNGENVEGESHEQVVEKIKASGNQVTL 76
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
 1267-1322 5.41e-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: 45.72  E-value: 5.41e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1267 GISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNG--------INLRSATEQQARLIIGQ 1322
Cdd:cd06736     12 QITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGcirgerqsVSLEDCTKEEAHWTLQR 75
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 ...
 1256-1322 5.94e-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: 46.11  E-value: 5.94e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864 1256 HVKVQKgsEP---LGISIVS----GEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1322
Cdd:cd06760      6 EVTLNK--EPgvgLGIGLCClpleNDIPGIFIHHLSPGSVAHMDGrLRRGDQILEINGTSLRNVTLNEAYAILSQ 78
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1407-1485 6.02e-06

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 46.12  E-value: 6.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1407 RVVFIKKSQLELGVHLCGGN---LHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLK 1483
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79


                   ..
gi 2462521864 1484 VQ 1485
Cdd:pfam00595   80 IL 81
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 639-701 6.19e-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: 46.15  E-value: 6.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  639 SLENGVYAAAVLPgSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 701
Cdd:cd06696     24 KDDNGCYIHDIVQ-DPAKSDGRLRPGDRLIMVNGVDVTNMSHTEAVSLLRAAPKEVTLVLGRA 85
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1257-1329 6.21e-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: 45.79  E-value: 6.21e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1257 VKVQKGSEPLGISIVSGEKGG-----IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1329
Cdd:cd06676      2 ITLERGSDGLGFSIVGGFGSPhgdlpIYVKTVFEKGAAAEDGrLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTL 80
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 63-539 6.41e-06

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: 51.59  E-value: 6.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   63 TRERNELRKRLAFATHGTAFDKRPYHRLNPD-YERLKIqcvRAMSDLQSLQNQHTNALKRCEEVAKETdfYHTLHSRLLS 141
Cdd:TIGR00606  363 IRARDSLIQSLATRLELDGFERGPFSERQIKnFHTLVI---ERQEDEAKTAAQLCADLQSKERLKQEQ--ADEIRDEKKG 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  142 DQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRaqQQQVLKHNGSSEILNKlydtAMDKLEVVKK 221
Cdd:TIGR00606  438 LGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAER--ELSKAEKNSLTETLKK----EVKSLQNEKA 511

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  222 DYDALRKRYSEKvaihnadlsrLEQLGEENQRlLKQTEMLTQQRDTA------IQLQHQCALS--------LRRFEAIHH 287
Cdd:TIGR00606  512 DLDRKLRKLDQE----------MEQLNHHTTT-RTQMEMLTKDKMDKdeqirkIKSRHSDELTsllgyfpnKKQLEDWLH 580

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  288 ELNKATAQNKDlqwEMELLQSELTELRTTQVKTAKEsEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLK 367
Cdd:TIGR00606  581 SKSKEINQTRD---RLAKLNKELASLEQNKNHINNE-LESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA 656

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  368 SSTSEKKAANEEMEALRQ-------IKDTVTMDAGRANKEVEILRKQCKALCQELKEAlqEADVAKCRRdwafqerdkiv 440
Cdd:TIGR00606  657 MLAGATAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST--ESELKKKEK----------- 723

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  441 aERDSIRTLCDNLRRERDRAVSELAEalrslddTRKQKNDVSRELKELKEQMEsqlEKEARFRQLMA--HSSHDSAIDTD 518
Cdd:TIGR00606  724 -RRDEMLGLAPGRQSIIDLKEKEIPE-------LRNKLQKVNRDIQRLKNDIE---EQETLLGTIMPeeESAKVCLTDVT 792

                          490       500
                   ....*....|....*....|.
gi 2462521864  519 SMEwetevvEFQRETEDIDLK 539
Cdd:TIGR00606  793 IME------RFQMELKDVERK 807
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 1255-1306 6.57e-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: 46.02  E-value: 6.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1255 RHVKVQK-GSEPLGISIVSG---EKG-GIYVSKVTVGSIAHQAGLEY-GDQLLEFNGI 1306
Cdd:cd06718      1 RRVELIKpPGKPLGFYIRDGngvERVpGIFISRLVLGSLADSTGLLAvGDEILEVNGV 58
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 541-615 6.59e-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: 6.59e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  541 LGFDMAEGVNEPcfpgdcGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 615
Cdd:cd06795     14 LGFNIVGGEDGE------GIFISFILAGGPADlsGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIAQYK 84
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
127-547 7.91e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 7.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  127 KETDFYHTLHSRLLSDQTRLK-DDVDMLRRENGQLLRERnLLQQSwedmKRLHEEDqkeiGDLRAQQQQVLkhnGSSeil 205
Cdd:COG4913    543 KPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRAITRAG-QVKGN----GTRHEKD----DRRRIRSRYVL---GFD--- 607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  206 nklydtAMDKLEVVKKDYDALRkrysEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQhQCALSLRRFEAi 285
Cdd:COG4913    608 ------NRAKLAALEAELAELE----EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEA- 675

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  286 hhELNKATAQNKDLqwemELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESK 365
Cdd:COG4913    676 --ELERLDASSDDL----AALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  366 LKSSTS---EKKAANEEMEAL-----RQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAkcrrdwafqerd 437
Cdd:COG4913    743 ARLELRallEERFAAALGDAVerelrENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAD------------ 810

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  438 kiVAERDSIRTLCDNLRRER-DRAVSELAEALrslddtrkqKNDVSRELKELKEQMESQLEK-EARFRQL---MAHS--S 510
Cdd:COG4913    811 --LESLPEYLALLDRLEEDGlPEYEERFKELL---------NENSIEFVADLLSKLRRAIREiKERIDPLndsLKRIpfG 879

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2462521864  511 HDSAIdtdSMEWE----TEVVEFQRETEDIDLKALGFDMAE 547
Cdd:COG4913    880 PGRYL---RLEARprpdPEVREFRQELRAVTSGASLFDEEL 917
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 46-496 8.40e-06

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: 50.98  E-value: 8.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   46 RQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ------HTNAL 119
Cdd:pfam10174  250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQnsdckqHIEVL 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  120 KrcEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLR---ERNLLQQSWEDMKRLHEEDQKEIGDLRAQ---QQ 193
Cdd:pfam10174  330 K--ESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDlteEKSTLAGEIRDLKDMLDVKERKINVLQKKienLQ 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  194 QVLKH-----NGSSEILNKLY------DTAMDKLEVVKKDYDALRKRYSEKVAIHN-ADLSRLEQLGEENQRLLKQTEML 261
Cdd:pfam10174  408 EQLRDkdkqlAGLKERVKSLQtdssntDTALTTLEEALSEKERIIERLKEQREREDrERLEELESLKKENKDLKEKVSAL 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  262 ----TQQRDTAIQLQHQcALSLRRfeaihhELNKATAQNKDLQWEMELLQSELTELRTtQVKTAKESEKYREERDAVYSE 337
Cdd:pfam10174  488 qpelTEKESSLIDLKEH-ASSLAS------SGLKKDSKLKSLEIAVEQKKEECSKLEN-QLKKAHNAEEAVRTNPEINDR 559

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  338 YKLIMSERDQVISELDKLQTEVE-----LAESKLKSSTSEKKAANEEMEALRQIKDTVT-----------MDAGRANKEV 401
Cdd:pfam10174  560 IRLLEQEVARYKEESGKAQAEVErllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKkvanikhgqqeMKKKGAQLLE 639

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  402 EILR-----------KQCKALCQELKEALQEADVAKCRrdwaFQERDKIVAERDSIRTlcdNLRRERDRAVSELAE---- 466
Cdd:pfam10174  640 EARRrednladnsqqLQLEELMGALEKTRQELDATKAR----LSSTQQSLAEKDGHLT---NLRAERRKQLEEILEmkqe 712

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  467 -------------ALRSLDDTRKQKND-----VSRE----LKELKEQMESQL 496
Cdd:pfam10174  713 allaaisekdaniALLELSSSKKKKTQeevmaLKREkdrlVHQLKQQTQNRM 764
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 138-493 9.17e-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: 50.94  E-value: 9.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  138 RLLSDQTRLKD-DVDMLRRENGQLLRERN--LLQ-----QSWEDMKRLHEEDQKEI-GDLRAQQQQvlkhNGSSEILNKL 208
Cdd:pfam01576  334 KALEEETRSHEaQLQEMRQKHTQALEELTeqLEQakrnkANLEKAKQALESENAELqAELRTLQQA----KQDSEHKRKK 409

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  209 YDTAMDKLEVVKKDYDALRKRYSEKVAIHNADL----SRLEQLGEENQRLLKQTEMLTQQ-RDTAIQLQhqcalslrrfE 283
Cdd:pfam01576  410 LEGQLQELQARLSESERQRAELAEKLSKLQSELesvsSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQ----------E 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  284 AIHHELNKATaQNKDLQWEMELLQSELTElrttQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELD----KLQTEV 359
Cdd:pfam01576  480 ETRQKLNLST-RLRQLEDERNSLQEQLEE----EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEegkkRLQREL 554

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  360 ELAESKLKsstsEKKAANEEMEA----LRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEalQEADVAKcrrdwAFQE 435
Cdd:pfam01576  555 EALTQQLE----EKAAAYDKLEKtknrLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE--EKAISAR-----YAEE 623

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  436 RDKivAERDSirtlcdnlrRERDRAVSELAealRSLDDTRKQKNDVSRELKELKEQME 493
Cdd:pfam01576  624 RDR--AEAEA---------REKETRALSLA---RALEEALEAKEELERTNKQLRAEME 667
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 634-679 9.57e-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: 45.58  E-value: 9.57e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462521864  634 KDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKS 679
Cdd:cd23063     22 KVSPNTKTTGIFIKGIIPDSPAHKCGRLKVGDRILSVNGNDVRNST 67
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
295-507 9.71e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.52  E-value: 9.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  295 QNKDLQWEMELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQtevelaeSKLKSSTSEKK 374
Cdd:COG1340      2 KTDELSSSLEELEEKIEELR-------EEIEELKEKRDELNEELKELAEKRDELNAQVKELR-------EEAQELREKRD 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  375 AANEEMEALRQIKDTVtmdagraNKEVEILRKQCKALCQELKEA-LQEADVAKCRRD-----WAFQERDkivaerdsirt 448
Cdd:COG1340     68 ELNEKVKELKEERDEL-------NEKLNELREELDELRKELAELnKAGGSIDKLRKEierleWRQQTEV----------- 129

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  449 lcdnLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMA 507
Cdd:COG1340    130 ----LSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIK 184
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1408-1485 9.90e-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: 45.71  E-value: 9.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1408 VVFIKKSQLELGVHLCGGNLH----------GVFVAEVEDDSPAkGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPR 1477
Cdd:cd06702      2 EIHLVKAGGPLGLSIVGGSDHsshpfgvdepGIFISKVIPDGAA-AKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPG 80


                   ....*...
gi 2462521864 1478 DGVRLKVQ 1485
Cdd:cd06702     81 QEIKLLVR 88
PDZ1_L-delphilin-like cd06743
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1264-1327 1.11e-05

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


Pssm-ID: 467225 [Multi-domain]  Cd Length: 76  Bit Score: 44.96  E-value: 1.11e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864 1264 EPLGISIvsGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRS-ATEQQARLiiGQQCDTI 1327
Cdd:cd06743      9 EAFGFSI--GGSGPCYILSVEEGSSAHAAGLQPGDQILELDGQDVSSlSCEAIIAL--ARRCPSV 69
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 623-689 1.15e-05

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: 45.33  E-value: 1.15e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  623 VTPLHINLSGQKDSGIslenGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 689
Cdd:cd06755     11 ESPLHFSLLGGSEKGF----GIFVSKVEKGSKAAEAG-LKRGDQILEVNGQNFENITLKKALEILRN 72
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 643-696 1.20e-05

PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467185 [Multi-domain]  Cd Length: 98  Bit Score: 45.68  E-value: 1.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  643 GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06701     39 GIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTL 92
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 1255-1330 1.22e-05

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


Pssm-ID: 467259 [Multi-domain]  Cd Length: 79  Bit Score: 45.03  E-value: 1.22e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1255 RHVKVQKGSEPLGiSIVSGEKGGIYVSKVTVGSIAHQAGLEY-GDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
Cdd:cd06798      1 KIVRIEKTREPLG-ATVRNEGDSVIISRIVKGGAAEKSGLLHeGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFL 76
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 625-692 1.24e-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: 44.93  E-value: 1.24e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  625 PLHINLSGQKDsgislENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQD 692
Cdd:cd06678     12 QLGIKLVRKKD-----EPGVFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQASGE 74
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 1255-1316 1.26e-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: 45.33  E-value: 1.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1255 RHVKVQKGSEPLGISIVS-----GEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd23058      6 LHIQLKKGPEGLGFSITSrdnptGGSGPIYIKNILPKGAAIQDGrLKAGDRLLEVNGVDVTGKTQEEV 73
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 628-699 1.29e-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: 1.29e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  628 INLSGQKDSGISLEN------GVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQdSLTLSLL 699
Cdd:cd06738      7 ISLVGTRGLGCSISSgptqkpGIFISNVKPGSLAEEVG-LEVGDQIVEVNGTSFTNVDHKEAVMALKSSR-HLTITVR 82
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 541-612 1.54e-05

PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467185 [Multi-domain]  Cd Length: 98  Bit Score: 45.29  E-value: 1.54e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  541 LGFDMAEGVNE----PCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 612
Cdd:cd06701     17 LGISIRGGAKGhagnPLDPTDEGIFISKINPDGAAarDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTLLV 94
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 637-689 1.58e-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: 44.94  E-value: 1.58e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  637 GISL-------ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 689
Cdd:cd06684     16 GITLststhrnKQVIVIDSIKPASIADRCGALHVGDHILSIDGTSVEHCSLAEATQLLAS 75
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 526-612 1.62e-05

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: 45.05  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  526 VVEFQRETEDidlkALGFDMAEGVNEPCfpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 603
Cdd:cd06675      2 TVEIKRGPQD----SLGISIAGGVGSPL--GDVPVFIAMIQPNGVAaqTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKN 75


                   ....*....
gi 2462521864  604 GEGAINMVV 612
Cdd:cd06675     76 ASGTIILQV 84
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1257-1329 1.73e-05

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


Pssm-ID: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 44.60  E-value: 1.73e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864 1257 VKVQKGSEPLGISIVSGEKGG--IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1329
Cdd:cd06683      6 VELKRYGGPLGITISGTEEPFdpIVISGLTEGGLAERTGaIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTL 81
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 632-696 1.76e-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: 44.62  E-value: 1.76e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  632 GQKDSGISLE----NGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06767     11 GSEPLGISIVsgenGGIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQCGDTITM 78
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 251-505 1.77e-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: 49.74  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  251 NQRLLKQTEMLTQQRDTaiqLQHQCALSLR----RFEAIHHElnkataqnkDLQWEMELLQSELTELRTTQvktakESEK 326
Cdd:pfam17380  261 NGQTMTENEFLNQLLHI---VQHQKAVSERqqqeKFEKMEQE---------RLRQEKEEKAREVERRRKLE-----EAEK 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  327 YR----EERDAVYSEYKLIMSERDQvisELDKLQTEvelaesklksstsEKKaanEEMEALRQIKDTVTMDAGRANKEVE 402
Cdd:pfam17380  324 ARqaemDRQAAIYAEQERMAMERER---ELERIRQE-------------ERK---RELERIRQEEIAMEISRMRELERLQ 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  403 ILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKivaERDSIRTLCDNLRRERDRAVSElaEALRSLDDTRKQKNDVS 482
Cdd:pfam17380  385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKV---EMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQERQ 459

                          250       260
                   ....*....|....*....|....*....
gi 2462521864  483 RELKELKEQMESQ------LEKEARFRQL 505
Cdd:pfam17380  460 QQVERLRQQEEERkrkkleLEKEKRDRKR 488
PDZ_2 pfam13180
PDZ domain;
638-699 1.86e-05

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 44.18  E-value: 1.86e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  638 ISLENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALdnKSLNECESLLRSC--QDSLTLSLL 699
Cdd:pfam13180    2 VDLEGGVVVVSVKSSGPAAKAG-LKAGDVILSIDGRKI--NDLTDLESALYGHkpGDTVTLQVY 62
PTZ00121 PTZ00121
MAEBL; Provisional
 172-540 2.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  172 EDMKRLHEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEkvAIHNADlsRLEQLGEEN 251
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAAKKKAEEAKK---AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--AKKKAD--AAKKKAEEK 1390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  252 QRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH--HELNKATAQNKDLQwemELLQSELTELRTTQVKTAKESEKYRE 329
Cdd:PTZ00121  1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKkaEEKKKADEAKKKAE---EAKKADEAKKKAEEAKKAEEAKKKAE 1467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  330 E-RDAVYSEYKlimSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQC 408
Cdd:PTZ00121  1468 EaKKADEAKKK---AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  409 KALCQELKEA--LQEADVAKCRRDWAFQERDKIVAERdsirtlcdnlRRERDRAVSE--LAEALRSLDDTRKQKNDVSRE 484
Cdd:PTZ00121  1545 KKKADELKKAeeLKKAEEKKKAEEAKKAEEDKNMALR----------KAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKK 1614

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  485 LKELKEQMEsQLEKEARFRQLMAHSSHDSAIDTDSMEwetevvEFQRETEDIDLKA 540
Cdd:PTZ00121  1615 AEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAE------ELKKAEEENKIKA 1663
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 105-313 2.05e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.45  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  105 MSDLQSLQNQHTNALK-----RCEEVAKE--------TDFYHTL------HSRLLSDQTRLKDDVDMLRRENGQLLRERN 165
Cdd:PRK04778   255 EKEIQDLKEQIDENLAlleelDLDEAEEKneeiqeriDQLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEID 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  166 LLQQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------AL 226
Cdd:PRK04778   335 RVKQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  227 RKrySEKVAihNADLSRLEQLGEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATA 294
Cdd:PRK04778   410 RK--DELEA--REKLERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATE 483

                          250       260
                   ....*....|....*....|.
gi 2462521864  295 QNKDLQWEMELL--QSELTEL 313
Cdd:PRK04778   484 DVETLEEETEELveNATLTEQ 504
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 1265-1316 2.46e-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: 44.28  E-value: 2.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1265 PLGISIVS----GEKGGIYVSKVT-VGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06717     11 FLGISIVGqsneRGDGGIYVGSIMkGGAVAADGRIEPGDMILQVNDISFENMSNDDA 67
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
297-537 2.51e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  297 KDLQWEMELLQSELTelRTTQVKTA-KESEKYREErdaVYSEYKLIMSERDQVISELDKLQTEV--------ELAESKLK 367
Cdd:PRK03918   172 KEIKRRIERLEKFIK--RTENIEELiKEKEKELEE---VLREINEISSELPELREELEKLEKEVkeleelkeEIEELEKE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  368 SSTSEKKAANEEmEALRQIKDTVTmdagRANKEVEILRKQCKALcQELKEALQEADVAKcrrdwafQERDKIVAERDSIR 447
Cdd:PRK03918   247 LESLEGSKRKLE-EKIRELEERIE----ELKKEIEELEEKVKEL-KELKEKAEEYIKLS-------EFYEEYLDELREIE 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  448 TLCDNLRRER---DRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWET 524
Cdd:PRK03918   314 KRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393

                          250
                   ....*....|....*
gi 2462521864  525 EVVEFQRE--TEDID 537
Cdd:PRK03918   394 EELEKAKEeiEEEIS 408
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 644-710 2.52e-05

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: 44.26  E-value: 2.52e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  644 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLkvfpqssSWSG 710
Cdd:cd06680     30 FFVKSIVPGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTVV-------SWPG 89
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 1257-1320 2.53e-05

PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Radil (also known as protein KIAA1849) and related domains. Radil is required for cell adhesion and migration of neural crest precursors during development. Radil is a component of a Rasip1-Radil-ARHGAP29 complex at endothelial cell-cell junctions. Rap1, via its effectors Radil and Rasip1 and their binding partner ArhGAP29, controls the endothelial barrier by decreasing Rho-mediated radial tension on cell-cell junctions. ArhGAP29 binds the Radil PDZ domain. The Radil PDZ domain also binds kinesin family protein 14 (KIF14); KIF14 negatively regulates Rap1-mediated inside-out integrin activation by tethering Radil on microtubules. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Radil-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467177 [Multi-domain]  Cd Length: 88  Bit Score: 44.59  E-value: 2.53e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1257 VKVQKGSEPLGISIVSGEK-----GGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06690      6 VELERGPKGLGLGLIDGLHtplrsPGIYIRTLVPDSPAARDGrLRLGDRILAVNGTSLVGADYQSAMDLI 75
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 644-703 2.58e-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: 44.16  E-value: 2.58e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  644 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 703
Cdd:cd06799     25 IVVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQGPIT---FKLIP 81
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 1257-1316 2.58e-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: 44.69  E-value: 2.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1257 VKVQKGSEPLGISIVSG------EKG----GIYVSKVT-VGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06715      5 VVLHRENGSLGFNIIGGrpcennQEGssseGIYVSKIVeNGPAADEGGLQVHDRIIEVNGKDLSKATHEEA 75
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 632-696 2.61e-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: 44.40  E-value: 2.61e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  632 GQKDSGiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
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) ...
 1256-1329 2.81e-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: 44.54  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1256 HVKVQKG-SEPLGISIV---SGEKG--GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSA-TEQQARLIIGQQCDTI 1327
Cdd:cd06689     17 YIELEKPeSGGLGFSVVglkSENRGelGIFVQEIQPGSVAARDGrLKENDQILAINGQPLDQSiSHQQAIAILQQAKGSV 96


                   ..
gi 2462521864 1328 TI 1329
Cdd:cd06689     97 EL 98
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 128-537 2.95e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  128 ETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngSSEILNK 207
Cdd:TIGR00618  174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ------SHAYLTQ 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  208 LYDTAMDKlevvkkdyDALRKRYSEKVAihnadlsRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcalslrrfEAIHH 287
Cdd:TIGR00618  248 KREAQEEQ--------LKKQQLLKQLRA-------RIEELRAQEAVLEETQERINRARKAAPLAAHI--------KAVTQ 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  288 ELNKATAQNKDLQWEMELLQSELTElRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELaESKLK 367
Cdd:TIGR00618  305 IEQQAQRIHTELQSKMRSRAKLLMK-RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIH 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  368 SSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRK-QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERdsi 446
Cdd:TIGR00618  383 TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI--- 459

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  447 rtlcdnLRRERDRAVSELAEALRSLDDTRKQKNDVSR-ELKELKEQMESQLEKEARFRQLMAH--SSHDSAIDTDSME-W 522
Cdd:TIGR00618  460 ------HLQESAQSLKEREQQLQTKEQIHLQETRKKAvVLARLLELQEEPCPLCGSCIHPNPArqDIDNPGPLTRRMQrG 533

                          410
                   ....*....|....*
gi 2462521864  523 ETEVVEFQRETEDID 537
Cdd:TIGR00618  534 EQTYAQLETSEEDVY 548
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 58-382 2.99e-05

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: 49.18  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   58 QLRLMTRERNELRKRLAFAthgtAFDKRPYHRL----------------NPDYERLKIQCVRAMSDLQSLQNQHTNALKR 121
Cdd:COG3096    786 RLEELRAERDELAEQYAKA----SFDVQKLQRLhqafsqfvgghlavafAPDPEAELAALRQRRSELERELAQHRAQEQQ 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  122 CEEVAKETDFYHTLHSRLLSDQTRLKDD-----VDMLRRENGQLLRERNLLQQSWEDMKRLheEDQKEIgdLRAQQQQVl 196
Cdd:COG3096    862 LRQQLDQLKEQLQLLNKLLPQANLLADEtladrLEELREELDAAQEAQAFIQQHGKALAQL--EPLVAV--LQSDPEQF- 936

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  197 khngssEILNKLYDTAMDKLEVVKKDYDAL---RKR-----YSEKVAIHNADLSRLEQLgeeNQRLLKQTEMLTQQRDTA 268
Cdd:COG3096    937 ------EQLQADYLQAKEQQRRLKQQIFALsevVQRrphfsYEDAVGLLGENSDLNEKL---RARLEQAEEARREAREQL 1007

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  269 IQLQHQCALSLRRFEAIhhelnKATAQNKdlqweMELLQSELTELRTTQVKTAKESE-KYREERDAVYSEYKLIMSERDQ 347
Cdd:COG3096   1008 RQAQAQYSQYNQVLASL-----KSSRDAK-----QQTLQELEQELEELGVQADAEAEeRARIRRDELHEELSQNRSRRSQ 1077

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2462521864  348 VISELDKLQTEVELAESKLKSSTSEKKAANEEMEA 382
Cdd:COG3096   1078 LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 343-507 3.04e-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: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  343 SERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEAL--------RQIKDT------VTMDAGRANKEVEILRKQC 408
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriaalaRRIRALeqelaaLEAELAELEKEIAELRAEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  409 KALCQELKEALQEADVAKCRRDWAF-------------------------QERDKIVAERDSIRTLCDNLRRERDR---A 460
Cdd:COG4942    100 EAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaparrEQAEELRADLAELAALRAELEAERAEleaL 179

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  461 VSELAEALRSLDDTRKQKNDV----SRELKELKEQMESQLEKEARFRQLMA 507
Cdd:COG4942    180 LAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEALIA 230
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 1255-1319 3.12e-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: 3.12e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864 1255 RHVKVQKGSEPLGISIvSGEKGGIyVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSAT-EQQARLI 1319
Cdd:cd06710      1 RTVEIARGRAGYGFTI-SGQAPCV-LSCVVRGSPADVAGLKAGDQILAVNGINVSKAShEDVVKLI 64
Filament pfam00038
Intermediate filament protein;
294-498 3.12e-05

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 47.99  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  294 AQNKDLQWEMELLQsELTELRTTQVKTAKESEkYREERDAVYSeyklIMSERDQVISELDKLQTEVELAESKLKSSTSEK 373
Cdd:pfam00038   25 QQNKLLETKISELR-QKKGAEPSRLYSLYEKE-IEDLRRQLDT----LTVERARLQLELDNLRLAAEDFRQKYEDELNLR 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  374 KAANEEMEALRQIKDTVTMdagraNKeVEiLRKQCKALCQELK--EALQEADVAKCRRDWAFQERdkiVAERDSIRTLcd 451
Cdd:pfam00038   99 TSAENDLVGLRKDLDEATL-----AR-VD-LEAKIESLKEELAflKKNHEEEVRELQAQVSDTQV---NVEMDAARKL-- 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462521864  452 nlrrerdravsELAEALRsldDTRKQKND-VSRELKELKEQMESQLEK 498
Cdd:pfam00038  167 -----------DLTSALA---EIRAQYEEiAAKNREEAEEWYQSKLEE 200
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 541-612 3.19e-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: 3.19e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  541 LGFDMAEGvnepcfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 612
Cdd:cd23060     12 LGFSLVGG------EGGSGIFVKSISPGGVAdrDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 643-690 3.28e-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: 44.47  E-value: 3.28e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2462521864  643 GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE-CESLLRSC 690
Cdd:cd06714     39 GAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEvQDIISQSK 87
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 143-526 3.40e-05

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: 49.02  E-value: 3.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  143 QTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVlkhngsSEILNKLyDTAMDKLEVVKKD 222
Cdd:pfam01576   21 QQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQEL------EEILHEL-ESRLEEEEERSQQ 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  223 YDALRKRYSEkvaiHNADLSrlEQLGEEN---QRLlkQTEMLTqqrdtaiqlqhqCALSLRRFEAihhELNKATAQNKDL 299
Cdd:pfam01576   94 LQNEKKKMQQ----HIQDLE--EQLDEEEaarQKL--QLEKVT------------TEAKIKKLEE---DILLLEDQNSKL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  300 QWEMELLQSELTELRTT---QVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAA 376
Cdd:pfam01576  151 SKERKLLEERISEFTSNlaeEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  377 NEEMEALRQIKDTVTMDA-GRANKEV---EILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRT-LCD 451
Cdd:pfam01576  231 IAELRAQLAKKEEELQAAlARLEEETaqkNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTeLED 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  452 N---------LRRERDRAVSELAEALRslDDTRK---QKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHdsAIDTDS 519
Cdd:pfam01576  311 TldttaaqqeLRSKREQEVTELKKALE--EETRSheaQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ--ALESEN 386


                   ....*..
gi 2462521864  520 MEWETEV 526
Cdd:pfam01576  387 AELQAEL 393
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 637-682 3.78e-05

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: 43.71  E-value: 3.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462521864  637 GISLEN--GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE 682
Cdd:cd06718     20 GNGVERvpGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDD 67
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 641-696 3.80e-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: 3.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALD-NKSLNECESLLRSCQDSLTL 696
Cdd:cd06689     42 ELGIFVQEIQPGSVAARDGRLKENDQILAINGQPLDqSISHQQAIAILQQAKGSVEL 98
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 628-699 3.97e-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: 43.71  E-value: 3.97e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  628 INLSGQKDSGIslengvYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:cd06729     15 LRLAGGNDVGI------FVAGVQEGSPAEKQG-LQEGDQILKVNGVDFRNLTREEAVLFLLDLPKGEEVTIL 79
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 641-696 4.13e-05

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


Pssm-ID: 467200 [Multi-domain]  Cd Length: 88  Bit Score: 43.80  E-value: 4.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIalDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06716     30 DTGIYVSEVDPNSIAAKDGRIREGDQILQINGV--DVQNREEAIALLSEEEKSITL 83
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 632-696 4.20e-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: 43.42  E-value: 4.20e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  632 GQKDSGISL--ENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06744      7 GNGSFGFTLrgHAPVYIESVDPGSAAERAG-LKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMPTL 72
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 541-613 4.35e-05

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 43.42  E-value: 4.35e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  541 LGFDMAEGVNEpcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 613
Cdd:pfam00595   12 LGFSLKGGSDQ----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1279-1330 4.39e-05

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


Pssm-ID: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 43.94  E-value: 4.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1279 YVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII--GQQCDTITIL 1330
Cdd:cd23070     39 HVSAVLEGGAADKAGVRKGDRILEVNGVNVEGATHKQVVDLIksGGDELTLTVI 92
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 527-614 4.42e-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: 4.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  527 VEFQRETEDIDLKaLGFDMAEGVNE-----PCFPGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKA 600
Cdd:cd10822      2 IEIHKLRQGENLI-LGFSIGGGIDQdpsknPFSYTDKGIYVTRVSEGGPAEkAGLQVGDKILQVNGWDMTMVTHKQAVKR 80

                           90
                   ....*....|....
gi 2462521864  601 LLNGEGAINMVVRR 614
Cdd:cd10822     81 LTKKKPVLRMLVTR 94
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1255-1320 4.78e-05

PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 6 of multi-PDZ-domain protein 1 (MUPP1). MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ6 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467158 [Multi-domain]  Cd Length: 87  Bit Score: 43.40  E-value: 4.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1255 RHVKVQKGSEPLGISIVSGEKG-GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06670      5 RTITIVKGNSSLGITVSADKDGnGCIVKSIIHGGAVSRDGrISVGDFIVSINNESLRNVTNAQARAIL 72
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 559-614 4.80e-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: 4.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  559 GIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKaLLNGEGAINMVVRR 614
Cdd:cd10833     27 GIFVSKVEEGSAAErAGLCVGDKITEVNGVSLENITMSSAVK-VLTGSNRLRMVVRR 82
PRK01156 PRK01156
chromosome segregation protein; Provisional
 89-493 4.99e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 48.36  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   89 RLNPDYERLK--IQCVRA-MSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERN 165
Cdd:PRK01156   163 SLERNYDKLKdvIDMLRAeISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  166 LLQqSWEDMKRLHEEDQKEI-GDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKR---YSEKVAIHNADL 241
Cdd:PRK01156   243 ELS-SLEDMKNRYESEIKTAeSDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDienKKQILSNIDAEI 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  242 SRLEQlgeenqrLLKQTEMLTQQRDTAIQLQhqcalslRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTA 321
Cdd:PRK01156   322 NKYHA-------IIKKLSVLQKDYNDYIKKK-------SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  322 KESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEAL------------------ 383
Cdd:PRK01156   388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeeks 467

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  384 RQIKDTVTMDAGRANKEVEILRKQCKALCQE------LKEALQEADVAKCRRDWAFQE--RDKIVAERDSIRTLCD---- 451
Cdd:PRK01156   468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKivdlkkRKEYLESEEINKSINEYNKIEsaRADLEDIKIKINELKDkhdk 547

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  452 --------------NLRRERDRAVSELAE-ALRSLDDTRKQKNDVSRELKELKEQME 493
Cdd:PRK01156   548 yeeiknrykslkleDLDSKRTSWLNALAViSLIDIETNRSRSNEIKKQLNDLESRLQ 604
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 288-501 5.28e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 5.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  288 ELNKATAQNKDLQWEMELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLK 367
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAELDALQ-------AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  368 ---SSTSEKKAANEEMEALRQIKDTVTMdAGRANKeVEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIVAERD 444
Cdd:COG3883     90 eraRALYRSGGSVSYLDVLLGSESFSDF-LDRLSA-LSKIADADADLLEELKADKAELE----------AKKAELEAKLA 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  445 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEAR 501
Cdd:COG3883    158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 1276-1313 5.31e-05

circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of HtrA family serine proteases including human HtrA1, HtrA2 (mitochondrial), HtrA3, and HtrA4, and related domains. These proteases are key enzymes associated with pregnancy. Their diverse biological functions include cell growth proliferation, migration and apoptosis. They are also implicated in disorders including Alzheimer's, Parkinson's, arthritis and cancer. HtrA1 (also known as high-temperature requirement A serine peptidase 1, L56, and serine protease 11) substrates include extracellular matrix proteins, proteoglycans, and insulin-like growth factor (IGF)-binding proteins. HtrA1 also inhibits signaling by members of the transforming growth factor beta (TGF-beta) family. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467624 [Multi-domain]  Cd Length: 98  Bit Score: 43.64  E-value: 5.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462521864 1276 GGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATE 1313
Cdd:cd06785     31 SGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSD 68
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 1258-1485 5.96e-05

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


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 47.60  E-value: 5.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1258 KVQKGSepLGISI--VSGEK---------GGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARliigqqcdt 1326
Cdd:TIGR02037  230 KVKRGW--LGVTIqeVTSDLakslglekqRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRA--------- 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1327 itilaqynphVHQLsshsrssshldPAGTHSTLQgsgtttpehpsvidplMEQDEGPSTPPAK-QSSSRIAGDANKKTLE 1405
Cdd:TIGR02037  299 ----------IGTL-----------KPGKKVTLG----------------ILRKGKEKTITVTlGASPEEQASSSNPFLG 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1406 PRVVFIKKSQLELGVHlcGGNLHGVFVAEVEDDSPAKGPdGLVPGDLILEYGSLDVRNktVEEVY--VEMLKPRDGVRLK 1483
Cdd:TIGR02037  342 LTVANLSPEIRKELRL--KGDVKGVVVTKVVSGSPAARA-GLQPGDVILSVNQQPVSS--VAELRkvLARAKKGGRVALL 416


                   ..
gi 2462521864 1484 VQ 1485
Cdd:TIGR02037  417 IL 418
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 1262-1316 6.32e-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: 6.32e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1262 GSEPLGISIVSGE--------KGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd23063      8 EKKSFGICIVRGEvkvspntkTTGIFIKGIIPDSPAHKCGrLKVGDRILSVNGNDVRNSTEQAA 71
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 623-690 6.60e-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: 43.12  E-value: 6.60e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  623 VTPLHINLSGQKDSGisLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 690
Cdd:cd06717      9 VNFLGISIVGQSNER--GDGGIYVGSIMKGGAVAADGRIEPGDMILQVNDISFENMSNDDAVRVLREA 74
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 1407-1486 6.61e-05

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: 43.13  E-value: 6.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1407 RVVFIKKSQLE-LGVHLCGGNLHGV--FVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVyVEMLKPRDG-VRL 1482
Cdd:cd06800      1 RKVLLSKEPHEgLGISITGGKEHGVpiLISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEA-VTILSQQRGeITL 79


                   ....
gi 2462521864 1483 KVQY 1486
Cdd:cd06800     80 EVVY 83
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1408-1475 6.66e-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: 6.66e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1408 VVFIKKSQLELGVHLCGgnlHG-VFVAEVEDDSPAKGPdGLVPGDLILEYGSLDVRNKTVEEVyVEMLK 1475
Cdd:cd06744      1 TVRVYRGNGSFGFTLRG---HApVYIESVDPGSAAERA-GLKPGDRILFLNGLDVRNCSHDKV-VSLLQ 64
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 560-614 6.85e-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: 6.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  560 IFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 614
Cdd:cd23068     27 LSIQKVNPGSPADKAgLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 1255-1315 6.99e-05

PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 42.81  E-value: 6.99e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864 1255 RHVKVQKGSEPLGISiVSGEKG--GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQ 1315
Cdd:cd06768      1 RLCHLVKGPEGYGFN-LHAEKGrpGHFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQ 62
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 539-617 7.62e-05

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


Pssm-ID: 467180 [Multi-domain]  Cd Length: 92  Bit Score: 43.15  E-value: 7.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  539 KALGFDMAEGVNEPCFpgDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK 616
Cdd:cd06694     13 KGLGFTIVGGENSGSL--DLGIFVKSIIPGGPAdkDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVELIISQPK 90


                   .
gi 2462521864  617 S 617
Cdd:cd06694     91 S 91
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 647-696 7.84e-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: 41.74  E-value: 7.84e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462521864  647 AAVLPGSPAAKEGsLAVGDRIVAINGIALdnKSLNECESLLRSCQDSLTL 696
Cdd:pfam17820    3 TAVVPGSPAERAG-LRVGDVILAVNGKPV--RSLEDVARLLQGSAGESVT 49
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 556-601 8.27e-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: 8.27e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462521864  556 GDCGIFVTKVDKGSI--ADGRLRVNDWLLRINDVDLINKDKKQAIKAL 601
Cdd:cd06717     24 GDGGIYVGSIMKGGAvaADGRIEPGDMILQVNDISFENMSNDDAVRVL 71
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 634-699 9.06e-05

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


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 43.05  E-value: 9.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  634 KDSGISLENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKslNECESLLRSCQ--DSLTLSLL 699
Cdd:cd06779     17 KELGLPVNRGVLVAEVIPGSPAAKAG-LKEGDVILSVNGKPVTSF--NDLRAALDTKKpgDSLNLTIL 81
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 1503-1561 9.07e-05

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 41.88  E-value: 9.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1503 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWmaWQ--LDENAQKIQRGQIPSKY 1561
Cdd:cd11883      1 VVVALYDFTPKSKNQLSFKAGDIIYVLNKDPSG----W--WDgvIISSSGKVKRGWFPSNY 55
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 1257-1319 9.41e-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: 42.38  E-value: 9.41e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1257 VKVQKGSEPLGISIVSGEKggIYVSKVTVGSIAHQAGLEYGDQLLEFNGINL-RSATEQQARLI 1319
Cdd:cd06711      3 ITIQRGKDGFGFTICDDSP--VRVQAVDPGGPAEQAGLQQGDTVLQINGQPVeRSKCVELAHAI 64
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 555-614 9.57e-05

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


Pssm-ID: 467271 [Multi-domain]  Cd Length: 93  Bit Score: 43.01  E-value: 9.57e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  555 PGDCGIFVTKV-DKG-SIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGE--GAINMVVRR 614
Cdd:cd23058     29 GGSGPIYIKNIlPKGaAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKlgGTVSLVVSR 92
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 1255-1329 9.95e-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: 42.54  E-value: 9.95e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1255 RHVKVQKGS-EPLGISIVSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1329
Cdd:cd10830      1 RLVQFEKNTeEPMGITLKLNEKQSCIVARILHGGMIHRQGsLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVSL 77
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
647-682 9.98e-05

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 47.12  E-value: 9.98e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462521864  647 AAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNE 682
Cdd:COG3975    499 TSVLWGSPAYKAG-LSAGDELLAIDGLRVTADNLDD 533
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 1253-1316 1.00e-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: 42.99  E-value: 1.00e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1253 EPRHVKVQKGSEPLGISI------VSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06669      7 EVTVIELEKGDRGLGFSIldyqdpLDPSETVIVIRSLVPGGVAEQDGrLLPGDRLVFVNDVSLENASLDEA 77
PTZ00121 PTZ00121
MAEBL; Provisional
 172-537 1.04e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  172 EDMKRLHE----EDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTamdKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQL 247
Cdd:PTZ00121  1549 DELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA---RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  248 GEENQrllkqtemltqQRDTAIQLQHQCALSLRRFEAIH--HELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESE 325
Cdd:PTZ00121  1626 KKAEE-----------EKKKVEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  326 KYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILR 405
Cdd:PTZ00121  1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  406 KQCKALcqeLKEALQEADvAKCRRDWAFQERD-----KIVAERDSIRTLCDNLRRERDraVSELAEALrsldDTRKQKND 480
Cdd:PTZ00121  1775 KEKEAV---IEEELDEED-EKRRMEVDKKIKDifdnfANIIEGGKEGNLVINDSKEME--DSAIKEVA----DSKNMQLE 1844

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  481 VSRELKELKEQMESQLEKEarfrqlmAHSSHDSAIDTDSMEWETEVVEFQRETEDID 537
Cdd:PTZ00121  1845 EADAFEKHKFNKNNENGED-------GNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 153-551 1.08e-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: 47.12  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  153 LRRENGQLLRERNLLQQSWEDMKrLHEEDQKEIgdLRAQQQQVLKhngsseILNKLYDTAMDKleVVKKDYDALRKRyse 232
Cdd:pfam10174  121 LQSEHERQAKELFLLRKTLEEME-LRIETQKQT--LGARDESIKK------LLEMLQSKGLPK--KSGEEDWERTRR--- 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  233 kVAIHNADLSRLEQLgeenqrlLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTE 312
Cdd:pfam10174  187 -IAEAEMQLGHLEVL-------LDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQM 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  313 LRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALrqiKDTVTM 392
Cdd:pfam10174  259 LKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVL---KESLTA 335

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  393 DAGRAN---KEVEILR-----------KQCKALcQELKE--ALQEADVAKCRRDWAFQERdKIVAERDSIRTLCDNLrRE 456
Cdd:pfam10174  336 KEQRAAilqTEVDALRlrleekesflnKKTKQL-QDLTEekSTLAGEIRDLKDMLDVKER-KINVLQKKIENLQEQL-RD 412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  457 RDRAVSELAEALRSLD------DT-------------------RKQKN-----------DVSRELKELKEQMESQ----L 496
Cdd:pfam10174  413 KDKQLAGLKERVKSLQtdssntDTalttleealsekeriierlKEQREredrerleeleSLKKENKDLKEKVSALqpelT 492

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  497 EKEARFRQLMAHSS--------HDSAIDTDSMEWETEVVEFQReTEDIDLKALGFDMAEGVNE 551
Cdd:pfam10174  493 EKESSLIDLKEHASslassglkKDSKLKSLEIAVEQKKEECSK-LENQLKKAHNAEEAVRTNP 554
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 612-698 1.19e-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: 42.63  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  612 VRRRKSLGGkvvtpLHINLSGQKDSGISLENG--VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 689
Cdd:cd06695      4 VKLTKGSSG-----LGFSFLGGENNSPEDPFSglVRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSLLRG 78


                   ....*....
gi 2462521864  690 CQDSLTLSL 698
Cdd:cd06695     79 APPEVTLLL 87
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 238-509 1.21e-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: 46.82  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  238 NADLSRLEQLGEENQRL------LKQTEMLTQQRDTAIQLQHQCALSLRrfEAIHHELNKATAQNKDLQWEMELLQSELT 311
Cdd:pfam15964  296 NVHMQTIERLTKERDDLmsalvsVRSSLAEAQQRESSAYEQVKQAVQMT--EEANFEKTKALIQCEQLKSELERQKERLE 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  312 ElrttqvKTAKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 391
Cdd:pfam15964  374 K------ELASQQEKRAQEKEALRKEMK---KEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQE 444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  392 MDAGRANKEVEILRKQCKALCQELKEALQEADvAKCRRDWAF--QERDKIVAERDSIRTLCDNLRRERDRAVSE------ 463
Cdd:pfam15964  445 MDVTKVCGEMRYQLNQTKMKKDEAEKEHREYR-TKTGRQLEIkdQEIEKLGLELSESKQRLEQAQQDAARAREEclklte 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  464 -LAEALRSLDDTRKQKNDVSR------------------ELKELKEQMESQLEKEARFRQLMAHS 509
Cdd:pfam15964  524 lLGESEHQLHLTRLEKESIQQsfsneakaqalqaqqreqELTQKMQQMEAQHDKTVNEQYSLLTS 588
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
 1255-1318 1.29e-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: 42.21  E-value: 1.29e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864 1255 RHVKVQK-GSEPLGIsIVSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARL 1318
Cdd:cd10832      1 RMVGIRKnPGEPLGV-TVRLEEGELVIARILHGGMIDRQGlLHVGDIIKEVNGVPVGSPEQLQEML 65
SH3_CAS cd11844
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins ...
 1505-1541 1.29e-04

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


Pssm-ID: 212778  Cd Length: 56  Bit Score: 41.56  E-value: 1.29e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462521864 1505 RALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWM 1541
Cdd:cd11844      3 RALYDNVAESPDELAFRRGDILTVLEQNTAGLEGWWL 39
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 526-613 1.33e-04

PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 42.42  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  526 VVEFQRETEdidlkALGFDMAEGVNEpcfpgDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLN 603
Cdd:cd06796      4 VVELPKTEE-----GLGFNVMGGKEQ-----NSPIYISRIIPGGVADrhGGLKRGDQLLSVNGVSVEGEHHEKAVELLKA 73

                           90
                   ....*....|
gi 2462521864  604 GEGAINMVVR 613
Cdd:cd06796     74 AQGSVKLVVR 83
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 649-700 1.37e-04

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: 42.13  E-value: 1.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  649 VLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 700
Cdd:cd23068     32 VNPGSPADKAG-LRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 249-501 1.39e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  249 EENQRLLKQT-EMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKY 327
Cdd:COG4942     23 AEAEAELEQLqQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  328 REE-RDAVYSEYKLIMSERDQVISEldklQTEVELAESKLKSSTSEKKAANEEMEALRQIKdtvtmdagranKEVEILRK 406
Cdd:COG4942    103 KEElAELLRALYRLGRQPPLALLLS----PEDFLDAVRRLQYLKYLAPARREQAEELRADL-----------AELAALRA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  407 QCKALCQELKEALQEADvakcrrdwafQERDKIVAERDsirtlcdnlrrERDRAVSELAEALRSLDDTRKQKNDVSRELK 486
Cdd:COG4942    168 ELEAERAELEALLAELE----------EERAALEALKA-----------ERQKLLARLEKELAELAAELAELQQEAEELE 226

                          250
                   ....*....|....*
gi 2462521864  487 ELKEQMESQLEKEAR 501
Cdd:COG4942    227 ALIARLEAEAAAAAE 241
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 527-699 1.41e-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: 46.45  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  527 VEFQRETEDIdLKALGFDMAEGVnepcfpgdcgiFVTKVDKGSIAD-GRLRVNDWLLRINDVDLIN-KDKKQAIKALLNG 604
Cdd:TIGR02037  238 VTIQEVTSDL-AKSLGLEKQRGA-----------LVAQVLPGSPAEkAGLKAGDVITSVNGKPISSfADLRRAIGTLKPG 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  605 EGAINMVVRRRKSLGGKVV--TPLHINLSGQKDS-GISLEN----------------GVYAAAVLPGSPAAKEGsLAVGD 665
Cdd:TIGR02037  306 KKVTLGILRKGKEKTITVTlgASPEEQASSSNPFlGLTVANlspeirkelrlkgdvkGVVVTKVVSGSPAARAG-LQPGD 384

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462521864  666 RIVAINGIALdnKSLNECESLLRSCQDSLTLSLL 699
Cdd:TIGR02037  385 VILSVNQQPV--SSVAELRKVLARAKKGGRVALL 416
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
378-507 1.47e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  378 EEMEALRQIKDTVT--MDAGRANKEVEILRKQCKAL------CQELKEALQEADVAKCRRDW-----AFQERDKIVAERD 444
Cdd:COG4913    219 EEPDTFEAADALVEhfDDLERAHEALEDAREQIELLepirelAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELE 298

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  445 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVS--------RELKELKEQMESQLEKEARFRQLMA 507
Cdd:COG4913    299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLA 369
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 1257-1316 1.63e-04

PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467193 [Multi-domain]  Cd Length: 86  Bit Score: 41.89  E-value: 1.63e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1257 VKVQKGSEPLGISIVSG-------EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06709      3 ITLKRGPSGLGFNIVGGtdqpyipNDSGIYVAKIKEDGAAAIDGrLQEGDKILEINGQSLENLTHQDA 70
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 1505-1563 1.64e-04

Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212706 [Multi-domain]  Cd Length: 53  Bit Score: 41.13  E-value: 1.64e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1505 RALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWmaWQLDENAQKiqrGQIPSKYVM 1563
Cdd:cd11772      3 RALYDYEAQHPDELSFEEGDLLYISDKSDPN----W--WKATCGGKT---GLIPSNYVE 52
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 215-539 1.65e-04

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: 46.76  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  215 KLEVVKKDYDALR---KRYSEKVAIHNADLSRLeQLGEENQRllkqtEMLTQQRDTAIQL--QHQcALSLRRFEAIHHEL 289
Cdd:pfam12128  605 RLDKAEEALQSARekqAAAEEQLVQANGELEKA-SREETFAR-----TALKNARLDLRRLfdEKQ-SEKDKKNKALAERK 677

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  290 NKATAQNKDLQWEMELLQSELtelrttQVKTAKESEKYREERDAVYSEYKLIMSERDqviSELDKLQTEVELAESKLKSs 369
Cdd:pfam12128  678 DSANERLNSLEAQLKQLDKKH------QAWLEEQKEQKREARTEKQAYWQVVEGALD---AQLALLKAAIAARRSGAKA- 747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  370 tsekkaaneEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWA----FQERDKIVAE--- 442
Cdd:pfam12128  748 ---------ELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYqetwLQRRPRLATQlsn 818

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  443 -RDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMesqlEKEARFRqlmahsshdsaIDTDSME 521
Cdd:pfam12128  819 iERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM----SKLATLK-----------EDANSEQ 883

                          330
                   ....*....|....*...
gi 2462521864  522 WETEVVEFQRETEDIDLK 539
Cdd:pfam12128  884 AQGSIGERLAQLEDLKLK 901
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 626-696 1.68e-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: 41.97  E-value: 1.68e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  626 LHINLSGQKDSGISlengVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06800     13 LGISITGGKEHGVP----ILISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITL 79
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 624-696 1.72e-04

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: 41.96  E-value: 1.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  624 TPLHINLSGQKDsgislENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06795     12 TGLGFNIVGGED-----GEGIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTI 79
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 649-696 1.78e-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: 41.79  E-value: 1.78e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2462521864  649 VLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06801     32 IFKGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTL 79
PDZ7_GRIP1-2-like cd06685
PDZ domain 7 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1256-1332 1.78e-04

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: 41.86  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1256 HVKVQK--GSEPLGISIVSG--EKGgIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1331
Cdd:cd06685      5 KVTLYKdsDTEDFGFSVSDGlyEKG-VYVNAIRPGGPADLSGLQPYDRILQVNHVRTRDFDCCLVVPLIAESGDKLELVV 83


                   .
gi 2462521864 1332 Q 1332
Cdd:cd06685     84 S 84
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 559-613 1.83e-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: 1.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  559 GIFVTKVDKGSIAD--GrLRVNDWLLRINDVDLINKDKKQAIKALLnGEGAINMVVR 613
Cdd:cd06738     28 GIFISNVKPGSLAEevG-LEVGDQIVEVNGTSFTNVDHKEAVMALK-SSRHLTITVR 82
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1505-1561 2.12e-04

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 40.64  E-value: 2.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1505 RALYDRLADVEQELSFKKDDILYVDDTlpqgTFGSWmaWqLDENAQKIQRGQIPSKY 1561
Cdd:cd11845      3 VALYDYEARTDDDLSFKKGDRLQILDD----SDGDW--W-LARHLSTGKEGYIPSNY 52
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 95-505 2.12e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 46.27  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   95 ERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDdvdmlrrengqlLRERNLLQQSWEDM 174
Cdd:pfam05557  121 QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE------------LEFEIQSQEQDSEI 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  175 KRLHEEDQKEIGDLRAQQQQVLKHN-------GSSEILN--------KLY--DTAMDKLEVVKKDYDALRKRYSEKVAI- 236
Cdd:pfam05557  189 VKNSKSELARIPELEKELERLREHNkhlneniENKLLLKeevedlkrKLEreEKYREEAATLELEKEKLEQELQSWVKLa 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  237 --HNADL-------SRLEQLGEENQRLLKQTEMLTQQ----RDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEM 303
Cdd:pfam05557  269 qdTGLNLrspedlsRRIEQLQQREIVLKEENSSLTSSarqlEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  304 ELL--------------QSELTELRTTQVKTA--KESEKYREERDAVYSEYKLIMSE-RDQVISELDKLQT-EVELAESK 365
Cdd:pfam05557  349 LLLtkerdgyrailesyDKELTMSNYSPQLLEriEEAEDMTQKMQAHNEEMEAQLSVaEEELGGYKQQAQTlERELQALR 428

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  366 LKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDS 445
Cdd:pfam05557  429 QQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEK 508

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  446 IRTLCDNLRReRDRAVSELAEALRSLDDTRKQKNDvsRELKELKEQMESqleKEARFRQL 505
Cdd:pfam05557  509 LQAEIERLKR-LLKKLEDDLEQVLRLPETTSTMNF--KEVLDLRKELES---AELKNQRL 562
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 611-696 2.15e-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: 41.86  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  611 VVRRRKSLGgkvvtPLHINLSGQKDS-----GISlENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECES 685
Cdd:cd06702      2 EIHLVKAGG-----PLGLSIVGGSDHsshpfGVD-EPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVS 74

                           90
                   ....*....|.
gi 2462521864  686 LLRSCQDSLTL 696
Cdd:cd06702     75 ALLSPGQEIKL 85
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 643-698 2.16e-04

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


Pssm-ID: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 41.58  E-value: 2.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  643 GVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQdSLTLSL 698
Cdd:cd06740     28 GIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKILRVSK-KLVLSV 81
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 89-391 2.30e-04

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: 46.17  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   89 RLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQL-------L 161
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeqikklQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  162 RERNLLQQSWEDMKRLHEEDQKEIGDLRAQ----QQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVaih 237
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE--- 495

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  238 nadlSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcaLSLR------------------------------------R 281
Cdd:TIGR04523  496 ----KELKKLNEEKKELEEKVKDLTKKISSLKEKIEK--LESEkkekeskisdledelnkddfelkkenlekeideknkE 569

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  282 FEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVEL 361
Cdd:TIGR04523  570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649

                          330       340       350
                   ....*....|....*....|....*....|
gi 2462521864  362 AESKLksstseKKAANEEMEALRQIKDTVT 391
Cdd:TIGR04523  650 IKETI------KEIRNKWPEIIKKIKESKT 673
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 ...
 624-679 2.41e-04

PDZ domain 8 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 7 of protein-associated tight junction (PATJ), PDZ domain 2 of Drosophila melanogaster inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 8 of MUPP1, PDZ domain 7 of PATJ, and PDZ domain 2 of Drosophila melanogaster INAD, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ8 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467160 [Multi-domain]  Cd Length: 84  Bit Score: 41.51  E-value: 2.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  624 TPLHINLSGQKD-SGISlengVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKS 679
Cdd:cd06672     11 SGLGLSLAGNKDrSRMS----VFVVGIDPDGAAGKDGRIQVGDELLEINGQVLYGRS 63
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 1407-1478 2.45e-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: 41.40  E-value: 2.45e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864 1407 RVVFIKKSQLELGVHLCGGN----LHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRD 1478
Cdd:cd06718      2 RVELIKPPGKPLGFYIRDGNgverVPGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMVAPTR 77
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 ...
 1257-1320 2.45e-04

PDZ domain 8 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 7 of protein-associated tight junction (PATJ), PDZ domain 2 of Drosophila melanogaster inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 8 of MUPP1, PDZ domain 7 of PATJ, and PDZ domain 2 of Drosophila melanogaster INAD, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ8 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467160 [Multi-domain]  Cd Length: 84  Bit Score: 41.51  E-value: 2.45e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864 1257 VKVQKGSEPLGISIvSGEKGG----IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06672      4 IELEKGSSGLGLSL-AGNKDRsrmsVFVVGIDPDGAAGKDGrIQVGDELLEINGQVLYGRSHLNASAII 71
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 343-507 2.47e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  343 SERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALR-QIKDTVTmDAGRANKEVEILRKQCKALCQELKEALQE 421
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQaELEALQA-EIDKLQAEIAEAEAEIEERREELGERARA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  422 ADVAKCRRDW-----------AFQER----DKIV-AERDSIRTLcdnlrrERDRAvsELAEALRSLDDTRKQKNDVSREL 485
Cdd:COG3883     95 LYRSGGSVSYldvllgsesfsDFLDRlsalSKIAdADADLLEEL------KADKA--ELEAKKAELEAKLAELEALKAEL 166

                          170       180
                   ....*....|....*....|...
gi 2462521864  486 KELKEQMESQL-EKEARFRQLMA 507
Cdd:COG3883    167 EAAKAELEAQQaEQEALLAQLSA 189
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 559-614 2.51e-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: 2.51e-04
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                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  559 GIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKaLLNGEGAINMVVRR 614
Cdd:cd06741     27 GIYVTGVDPGSVAENAgLKVGDQILEVNGRSFLDITHDEAVK-ILKSSKHLIMTVKD 82
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 1279-1330 2.55e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 40.59  E-value: 2.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1279 YVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSaTEQQARLIIGQQCDTITIL 1330
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRS-LEDVARLLQGSAGESVTLT 51
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 523-612 2.59e-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: 41.54  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  523 ETEVVEFQRETEdidlkALGFDMAEGvnepcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKAL 601
Cdd:cd06767      2 EPRHVSIEKGSE-----PLGISIVSG-------ENGGIFVSSVTEGSLAHqAGLEYGDQLLEVNGINLRNATEQQAALIL 69

                           90
                   ....*....|.
gi 2462521864  602 LNGEGAINMVV 612
Cdd:cd06767     70 RQCGDTITMLV 80
fliJ PRK07720
flagellar biosynthesis chaperone FliJ;
216-355 2.88e-04

flagellar biosynthesis chaperone FliJ;


Pssm-ID: 181091 [Multi-domain]  Cd Length: 146  Bit Score: 43.14  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  216 LEVVKKDYDALRKRYSEKVaihnadlSRLEQLGEENQRLLKQTEMLTQQRDTAIQ-------LQHQCALSLRRFEAIHHe 288
Cdd:PRK07720    11 LELKENEKEKALGEYEEAV-------SRFEQVAEKLYELLKQKEDLEQAKEEKLQsglsiqeIRHYQQFVTNLERTIDH- 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  289 LNKATAQNKDlqwEMELLQSELTELRTtqvktakESEKYREERDAVYSEYKLIMSERDQviSELDKL 355
Cdd:PRK07720    83 YQLLVMQARE---QMNRKQQDLTEKNI-------EVKKYEKMKEKKQEMFALEEKAAEM--KEMDEI 137
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 624-704 2.97e-04

PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP) and related domains; Drosophila bazooka PDZ1 belongs to a different PDZ family. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include: Par-3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467178 [Multi-domain]  Cd Length: 98  Bit Score: 41.83  E-value: 2.97e-04
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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  624 TPLHINLSGQKDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLsLLKVFP 703
Cdd:cd06691     15 GPLGIHVVPFSSSLSGRTLGLLIRGIEEGSRAERDGRFQENDCIVEINGVDLIDKSFEQAQDIFRQAMRSPEV-KLHVVP 93


                   .
gi 2462521864  704 Q 704
Cdd:cd06691     94 A 94
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 626-689 3.05e-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: 3.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  626 LHINLSGQKDSGIslenGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 689
Cdd:cd10834     15 LGFNIRGGSEYGL----GIYVSKVDPGGLAEQNG-IKVGDQILAVNGVSFEDITHSKAVEVLKS 73
PDZ3_PDZD2-PDZ1_hPro-IL-16-like cd06759
PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 ...
 614-675 3.08e-04

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: 41.11  E-value: 3.08e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  614 RRKSLGGKVVtplhinlsGQKDSgISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIAL 675
Cdd:cd06759     10 GGKGLGFSIV--------GGRDS-PRGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESL 62
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 ...
 552-614 3.29e-04

PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the second PDZ domain (PDZ2) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467241 [Multi-domain]  Cd Length: 90  Bit Score: 41.49  E-value: 3.29e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  552 PCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN-GEGAINMVVRR 614
Cdd:cd06760     25 PLENDIPGIFIHHLSPGSVAhmDGRLRRGDQILEINGTSLRNVTLNEAYAILSQcKPGPVTLIISR 90
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 647-677 3.35e-04

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 45.08  E-value: 3.35e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462521864  647 AAVLPGSPAAKEGsLAVGDRIVAINGIALDN 677
Cdd:COG0750    133 GEVVPGSPAAKAG-LQPGDRIVAINGQPVTS 162
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 ...
 637-689 3.41e-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: 41.09  E-value: 3.41e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  637 GISLEN-GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 689
Cdd:cd06762     21 GSDLENkSITVHRVFPSGLAAQEGTIQKGDRILSINGKSLKGVTHGDALSVLKQ 74
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 123-425 3.63e-04

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: 45.50  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  123 EEVAKETDFYHTLHSRLLSDQTRLkDDVDMLRRENGQLLRERNllqqswEDMKRLHEEDQKEIGDlRAQQQQVLKHNGSS 202
Cdd:pfam17380  306 EEKAREVERRRKLEEAEKARQAEM-DRQAAIYAEQERMAMERE------RELERIRQEERKRELE-RIRQEEIAMEISRM 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  203 EILNKLYDTAMDKLEVVKKDYDALRKrysekvaihnadlsrLEQLGEENQRLLKQT----EMLTQQRDTAIQLQhqcals 278
Cdd:pfam17380  378 RELERLQMERQQKNERVRQELEAARK---------------VKILEEERQRKIQQQkvemEQIRAEQEEARQRE------ 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  279 LRRFEAIH-HELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYRE---------ERDAVYSEYKLIMSERDQV 348
Cdd:pfam17380  437 VRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkilEKELEERKQAMIEEERKRK 516

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  349 ISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVtMDAGRANKEVEILRKQCKALCQ--ELKEALQEADVA 425
Cdd:pfam17380  517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRLEAMEREREMMRQivESEKARAEYEAT 594
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 1275-1329 3.85e-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: 41.47  E-value: 3.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864 1275 KGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1329
Cdd:cd06781     29 NKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDTVKV 83
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 539-614 3.86e-04

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


Pssm-ID: 467166 [Multi-domain]  Cd Length: 82  Bit Score: 40.69  E-value: 3.86e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  539 KALGFDMAEGVNEPcfpgdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 614
Cdd:cd06678     11 EQLGIKLVRKKDEP------GVFILDLLEGGLAarDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQASGERVHFVVSR 82
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 1272-1332 4.07e-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: 40.76  E-value: 4.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1272 SGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1332
Cdd:cd10820     18 SEQKKPLQVAKIRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 609-703 4.17e-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: 40.76  E-value: 4.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  609 NMVVRRRKSlggkvVTPLHINLSGQKDSGIslenGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 688
Cdd:cd06752      1 RTVVLKRPP-----GEQLGFNIRGGKASGL----GIFISKVIPDSDAHRLG-LKEGDQILSVNGVDFEDIEHSEAVKVLK 70

                           90
                   ....*....|....*.
gi 2462521864  689 ScqdSLTLSL-LKVFP 703
Cdd:cd06752     71 T---AREIQMrVRYFP 83
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 625-691 4.23e-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: 41.09  E-value: 4.23e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  625 PLHINLSGQKDSgisleNGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQ 691
Cdd:cd06670     15 SLGITVSADKDG-----NGCIVKSIIHGGAVSRDGRISVGDFIVSINNESLRNVTNAQARAILRRAS 76
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1257-1312 4.38e-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: 40.34  E-value: 4.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864 1257 VKVQKGSEPLGISIVSgeKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSAT 1312
Cdd:cd06744      2 VRVYRGNGSFGFTLRG--HAPVYIESVDPGSAAERAGLKPGDRILFLNGLDVRNCS 55
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 534-614 4.58e-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: 4.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  534 EDIDL----KALGFDMAEGVNEpcfpgdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGA 607
Cdd:cd06667      1 EVIELvndgSGLGFGIVGGKST-------GVVVKTILPGGVAdrDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSH 73


                   ....*..
gi 2462521864  608 INMVVRR 614
Cdd:cd06667     74 VRLVVAR 80
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 631-675 4.65e-04

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: 40.73  E-value: 4.65e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462521864  631 SGQKDSGIslengvYAAAVLPGSPAAKEGSLAVGDRIVAINGIAL 675
Cdd:cd06789     25 AGQDKLGI------YIKSVVKGGAADLDGRLQAGDQLLSVDGHSL 63
PDZ3_harmonin cd06739
PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic ...
 625-693 4.97e-04

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: 40.76  E-value: 4.97e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  625 PLHINLSGQKDSgiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDS 693
Cdd:cd06739     13 PLDLALEGGIDS--PLGGKIVVSAVYEGGAADKHGGIVKGDQIMMVNGKSLTDVTLAEAEAALQRAMNS 79
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 625-698 5.03e-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: 40.26  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  625 PLHINLS-GQKDSGISLENG--VYAAAVLPGSPAAKEGsLAVGDRIVAINGiaLDNK--SLNECESLLRSC-QDSLTLSL 698
Cdd:cd06712      1 PRTVHLTkEEGGFGFTLRGDspVQVASVDPGSCAAEAG-LKEGDYIVSVGG--VDCKwsKHSEVVKLLKSAgEEGLELQV 77
mukB PRK04863
chromosome partition protein MukB;
53-514 5.19e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   53 ENLSIQLRlmtRERNELRKRLAFAthgtAFDKRPYHRLNPDYERLKIQCVR---------AMSDLQSLQNQHTNALKRCE 123
Cdd:PRK04863   785 EKRIEQLR---AEREELAERYATL----SFDVQKLQRLHQAFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHE 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  124 EvaketdfyHTLHSRLLSDQtrLKDDVDMLRRENGQL-LRERNLLQQswedmkRLhEEDQKEIGDLRAQQQQVLKHNGSS 202
Cdd:PRK04863   858 S--------QEQQQRSQLEQ--AKEGLSALNRLLPRLnLLADETLAD------RV-EEIREQLDEAEEAKRFVQQHGNAL 920

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  203 EILNKLYDTAM---DKLEVVKKDYDALRKR----------------------YSEKVAIHNADLSRLEQLgeeNQRLLKQ 257
Cdd:PRK04863   921 AQLEPIVSVLQsdpEQFEQLKQDYQQAQQTqrdakqqafaltevvqrrahfsYEDAAEMLAKNSDLNEKL---RQRLEQA 997

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  258 TEMLTQQRDTAIQLQHQcalsLRRFEAIHHELNKA-TAQNKDLQwemELLQsELTELrTTQVkTAKESEKYREERDAVYS 336
Cdd:PRK04863   998 EQERTRAREQLRQAQAQ----LAQYNQVLASLKSSyDAKRQMLQ---ELKQ-ELQDL-GVPA-DSGAEERARARRDELHA 1067

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  337 EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVtMDAGRANKEVEILRKqckalcQELk 416
Cdd:PRK04863  1068 RLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHR------REL- 1139

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  417 eALQEADVAKCRRDWAFQERDKIVAE----RDSIRTLCDNLRRERD-----RAVSELAEALRslddtrkqkNDVSR--EL 485
Cdd:PRK04863  1140 -AYLSADELRSMSDKALGALRLAVADnehlRDVLRLSEDPKRPERKvqfyiAVYQHLRERIR---------QDIIRtdDP 1209

                          490       500       510
                   ....*....|....*....|....*....|....
gi 2462521864  486 KELKEQMESQL-----EKEARFRQLmAHSSHDSA 514
Cdd:PRK04863  1210 VEAIEQMEIELsrlteELTSREQKL-AISSESVA 1242
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
1266-1331 5.21e-04

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 44.81  E-value: 5.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1266 LGISiVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSAT--EQQARLIIGqqcDTITILA 1331
Cdd:COG3975    485 LGLR-VSADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTADNldDALAAYKPG---DPIELLV 548
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 612-700 5.32e-04

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: 40.68  E-value: 5.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  612 VRRRKSLGgkvvtplhINLSGQKDSGISLE-NGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 690
Cdd:cd06791      8 VKDEQGLG--------ITIAGYVGEKASGElSGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEAVEVLRNT 79

                           90
                   ....*....|
gi 2462521864  691 QDSLTLSLLK 700
Cdd:cd06791     80 GQVVHLTLAR 89
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
146-407 5.53e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 5.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  146 LKDDVDMLRRENGQLLRERNL----LQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKK 221
Cdd:COG4372     29 LSEQLRKALFELDKLQEELEQlreeLEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  222 DYDALRKRYSEkvaiHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAI-QLQHQCALSLRRFEAIHHELNKATAQNKDLQ 300
Cdd:COG4372    109 EAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELkELEEQLESLQEELAALEQELQALSEAEAEQA 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  301 WEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEM 380
Cdd:COG4372    185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264

                          250       260
                   ....*....|....*....|....*..
gi 2462521864  381 EALRQIKDTVTMDAGRANKEVEILRKQ 407
Cdd:COG4372    265 LAILVEKDTEEEELEIAALELEALEEA 291
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1428-1484 6.09e-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: 43.60  E-value: 6.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1428 HGVFVAEVEDDSPA-KGpdGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1484
Cdd:COG0265    201 EGVLVARVEPGSPAaKA--GLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTV 256
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
 626-698 6.16e-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: 6.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  626 LHINLSGQKDSGISLENG------VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALdNKSLNECESLLRSCQDSLTLSL 698
Cdd:cd06750      3 IEVQLQGGAPWGFTLKGGlehgepLVISKIEEGGKAASVGKLQVGDEVVNINGVPL-SGSRQEAIQLVKGSHKTLKLVV 80
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 45-464 6.24e-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: 6.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   45 DRQVN---EKVENLSIQLRLMTRERNELRKRL------------AFATHGTAFDKRpyHRLnpdYERLKIQcvRAMSDLQ 109
Cdd:pfam10174  393 ERKINvlqKKIENLQEQLRDKDKQLAGLKERVkslqtdssntdtALTTLEEALSEK--ERI---IERLKEQ--REREDRE 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  110 SLQNQHTnaLKRCEEVAKETdfYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLR 189
Cdd:pfam10174  466 RLEELES--LKKENKDLKEK--VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  190 AQQQQVLKHNGSSEILnklydtamDKLEVVKKDYdalrKRYSEKVAIHNADLSRLeqLGeenqrLLKQTEMLTQQRDTAI 269
Cdd:pfam10174  542 KAHNAEEAVRTNPEIN--------DRIRLLEQEV----ARYKEESGKAQAEVERL--LG-----ILREVENEKNDKDKKI 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  270 QLQHQCALSLrrfeaiHHELNKATAQNKDLQWEMELLQSELTElrttqvktakesEKYREERDAVYSEYKLIMSErdqVI 349
Cdd:pfam10174  603 AELESLTLRQ------MKEQNKKVANIKHGQQEMKKKGAQLLE------------EARRREDNLADNSQQLQLEE---LM 661

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  350 SELDKlqTEVELAESKLKSSTSEKKAANEE--MEALRQIKdtvtmdagrankeveilRKQCkalcQELKEALQEADVAkc 427
Cdd:pfam10174  662 GALEK--TRQELDATKARLSSTQQSLAEKDghLTNLRAER-----------------RKQL----EEILEMKQEALLA-- 716

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2462521864  428 rrdwAFQERDKIVA-------ERDSIRTLCDNLRRERDRAVSEL 464
Cdd:pfam10174  717 ----AISEKDANIAllelsssKKKKTQEEVMALKREKDRLVHQL 756
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 558-613 6.29e-04

PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD11-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 40.37  E-value: 6.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  558 CGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLNGEgAINMVVR 613
Cdd:cd06752     25 LGIFISKVIPDSDAHRLgLKEGDQILSVNGVDFEDIEHSEAVKVLKTAR-EIQMRVR 80
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 619-700 6.33e-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: 40.34  E-value: 6.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  619 GGKVVTPLHINlsgqkDSGIslengvYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 698
Cdd:cd06704     18 GGKGSTPYKGD-----DEGI------FISRVTEGGPAAKAG-VRVGDKLLEVNGVDLVDADHHEAVEALKNSGNTVTMVV 85


                   ..
gi 2462521864  699 LK 700
Cdd:cd06704     86 LR 87
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 344-498 6.47e-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: 43.37  E-value: 6.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  344 ERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQ-I-KDTVTMDAGRANKEVEILRKQCkalcqelkealqe 421
Cdd:COG1579     32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArIkKYEEQLGNVRNNKEYEALQKEI------------- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  422 advakcrrdwAFQERDKIVAErDSIRTL---CDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEK 498
Cdd:COG1579     99 ----------ESLKRRISDLE-DEILELmerIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 1429-1484 6.51e-04

circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do) and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for combining with other DegP monomers to form a stable oligomer structure. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegP family PDZ domain 1 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467630 [Multi-domain]  Cd Length: 91  Bit Score: 40.54  E-value: 6.51e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1429 GVFVAEVEDDSPAKgPDGLVPGDLILEY------GSLDVRNKtveevyVEMLKPRDGVRLKV 1484
Cdd:cd10839     26 GALVAQVLPDSPAA-KAGLKAGDVILSLngkpitSSADLRNR------VATTKPGTKVELKI 80
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1266-1324 6.51e-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: 40.34  E-value: 6.51e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1266 LGISIVSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIgQQC 1324
Cdd:cd06667     12 LGFGIVGGKSTGVVVKTILPGGVADRDGrLRSGDHILQIGDTNLRGMGSEQVAQVL-RQC 70
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1266-1318 6.66e-04

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


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 43.60  E-value: 6.66e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1266 LGISIVS-----------GEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1318
Cdd:COG0265    180 LGVTIQPvtpelaealglPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSARDLQRLL 243
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
 1505-1562 6.66e-04

Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212792 [Multi-domain]  Cd Length: 55  Bit Score: 39.29  E-value: 6.66e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1505 RALYDRLADVEQELSFKKDDILYVDDTLPQGTfgsWMAWQLDENAQkiqrGQIPSKYV 1562
Cdd:cd11858      3 KALYDFAGSVANELSLKKDDIVYIVQKEDNGW---WLAKKLDESKE----GWVPAAYL 53
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 559-597 6.68e-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: 6.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462521864  559 GIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQA 597
Cdd:cd06691     34 GLLIRGIEEGSRAerDGRFQENDCIVEINGVDLIDKSFEQA 74
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 1418-1485 7.07e-04

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: 40.16  E-value: 7.07e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1418 LGVHLCGGNLHGVFVAEVEDDSPA-KGpdGLVPGDLILEYGSLDVRNKTVEEVyVEMLKPRDG--VRLKVQ 1485
Cdd:cd06782      4 IGIEIGKDDDGYLVVVSPIPGGPAeKA--GIKPGDVIVAVDGESVRGMSLDEV-VKLLRGPKGtkVKLTIR 71
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 633-703 7.28e-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: 40.16  E-value: 7.28e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  633 QKDS----GISL----ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 703
Cdd:cd10831      6 QKNTdepmGITLkmneDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSIT---FKIVP 81
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 641-696 7.67e-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: 40.32  E-value: 7.67e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06703     31 DEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITL 86
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 539-593 8.34e-04

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


Pssm-ID: 467202 [Multi-domain]  Cd Length: 84  Bit Score: 39.86  E-value: 8.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  539 KALGFDMAEGVNEPCFPGdcgIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKD 593
Cdd:cd06718     11 KPLGFYIRDGNGVERVPG---IFISRLVLGSLADstGLLAVGDEILEVNGVEVTGKS 64
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 611-698 8.50e-04

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: 39.54  E-value: 8.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  611 VVRRRKSLGgkvvtplhINLSGQKDSGISlengvyaaAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSC 690
Cdd:cd06710      5 IARGRAGYG--------FTISGQAPCVLS--------CVVRGSPADVAG-LKAGDQILAVNGINVSKASHEDVVKLIGKC 67


                   ....*...
gi 2462521864  691 QDSLTLSL 698
Cdd:cd06710     68 TGVLRLVI 75
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
241-503 8.88e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 8.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  241 LSRLEQLGE---------ENQRLLK---QTEMLtqqrDT---AIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMEL 305
Cdd:COG0497    115 LSQLRELGEllvdihgqhEHQSLLDpdaQRELL----DAfagLEELLEEYREAYRAWRALKKELEELRADEAERARELDL 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  306 LQSELTELRTTQVKtAKESEKYREER----------DAVYSEYKLIMSERDQVISELDKLQTEVE-LAE--SKLKSSTSE 372
Cdd:COG0497    191 LRFQLEELEAAALQ-PGEEEELEEERrrlsnaeklrEALQEALEALSGGEGGALDLLGQALRALErLAEydPSLAELAER 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  373 KKAANEEME----ALRQIKDTVTMDAGRANkEVE----ILRKQCK----------ALCQELKEALQEADvakcRRDWAFQ 434
Cdd:COG0497    270 LESALIELEeaasELRRYLDSLEFDPERLE-EVEerlaLLRRLARkygvtveellAYAEELRAELAELE----NSDERLE 344

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  435 ERDKIVAE-RDSIRTLCDNLRRERDRAVSELAEAlrslddtrkqkndVSRELKELKeqMESqlekeARFR 503
Cdd:COG0497    345 ELEAELAEaEAELLEAAEKLSAARKKAAKKLEKA-------------VTAELADLG--MPN-----ARFE 394
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 279-366 8.96e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.06  E-value: 8.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  279 LRRFEAIHHELNKataQNKDLQWEMELLQS-------ELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISE 351
Cdd:pfam20492   29 LEESEETAEELEE---ERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEE 105

                           90
                   ....*....|....*
gi 2462521864  352 LDKLQTEVELAESKL 366
Cdd:pfam20492  106 ARRLQEELEEAREEE 120
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 608-689 9.14e-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: 9.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  608 INMVVRRRKSLGgkvvtplhINLSGQKDSGIslenGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLL 687
Cdd:cd06741      4 VNLVVEDGQSLG--------LMIRGGAEYGL----GIYVTGVDPGSVAENAG-LKVGDQILEVNGRSFLDITHDEAVKIL 70


                   ..
gi 2462521864  688 RS 689
Cdd:cd06741     71 KS 72
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1408-1485 9.22e-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: 39.72  E-value: 9.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1408 VVFIKKSQLE-LGVHLCGGNLHG--VFVAEVEDDSPAKgPDGLVPGDLILEYGSLDVRNKTVEEVyVEMLKPRDGVRLKV 1484
Cdd:cd10833      3 TVTVEKSPDGsLGFSVRGGSEHGlgIFVSKVEEGSAAE-RAGLCVGDKITEVNGVSLENITMSSA-VKVLTGSNRLRMVV 80


                   .
gi 2462521864 1485 Q 1485
Cdd:cd10833     81 R 81
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 310-539 9.78e-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: 43.84  E-value: 9.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  310 LTELRTTQVKTAKESEKYREERDavyseyklimserdqviSELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDT 389
Cdd:pfam05262  169 VSDVDTDSISDKKVVEALREDNE-----------------KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  390 VTMDAGRANKEVEILRKqckalcqELKEALQE-------ADVAKCRRDWAFQERDKIVAERDSIRT--LCDNLRRERDRA 460
Cdd:pfam05262  232 AQQKADFAQDNADKQRD-------EVRQKQQEaknlpkpADTSSPKEDKQVAENQKREIEKAQIEIkkNDEEALKAKDHK 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  461 VSELAEALRSLDDTRKQKN-DVSRELKELKEQMESQL-EKEARfrqlmAHSSHDSAIDTDSMEWETEVVEFQR---ETED 535
Cdd:pfam05262  305 AFDLKQESKASEKEAEDKElEAQKKREPVAEDLQKTKpQVEAQ-----PTSLNEDAIDSSNPVYGLKVVDPITnlsELVL 379


                   ....
gi 2462521864  536 IDLK 539
Cdd:pfam05262  380 IDLK 383
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 644-696 9.80e-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: 39.90  E-value: 9.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  644 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL----RSCQDSLTL 696
Cdd:cd06733     27 VSIGAIVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKVVDLMgnaaRNGQVNLTV 83
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 546-615 9.97e-04

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: 9.97e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  546 AEGVNEPcfpgDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 615
Cdd:cd06789     22 AKGAGQD----KLGIYIKSVVKGGAAdlDGRLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTLEVAKQ 89
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 645-701 1.06e-03

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: 40.27  E-value: 1.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  645 YAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 701
Cdd:cd06746     45 YLESVDPGGVADKAG-LKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVLKVVTV 100
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 624-696 1.09e-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: 1.09e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  624 TPLHINLSGQKDSG-ISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06709     10 SGLGFNIVGGTDQPyIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDAVELFRNAGEDVKL 83
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 647-703 1.11e-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: 39.46  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  647 AAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 703
Cdd:cd10830     28 ARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVS---LKVIP 81
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 146-375 1.13e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 42.42  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  146 LKDDVDMLRRENGQLLrernllQQSWEDMKRLHEEDQKEigDLRAQQQQVLKHngSSEILNKLYDTAMDKLEVVKKDYDA 225
Cdd:pfam17078    8 LHDQIDALTKTNLQLT------VQSQNLLSKLEIAQQKE--SKFLENLASLKH--ENDNLSSMLNRKERRLKDLEDQLSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  226 LRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHqcalslRRFEAIHHELNKATAQNKDLQWEMEl 305
Cdd:pfam17078   78 LKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQN------EYKDHYQQEINTLQESLEDLKLENE- 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864  306 lqSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQ-VISELDKLQTEVELAESKLKSSTSEKKA 375
Cdd:pfam17078  151 --KQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKI 219
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1256-1332 1.14e-03

PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 39.48  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1256 HVKVQKGSEPLGISIVSGE---KGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1331
Cdd:cd06735      3 SVELERGPKGFGFSIRGGReynNMPLYVLRLAEDGPAQRDGrLRVGDQILEINGESTQGMTHAQAIELIRSGGSVVRLLL 82


                   .
gi 2462521864 1332 Q 1332
Cdd:cd06735     83 R 83
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1429-1485 1.21e-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: 39.84  E-value: 1.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1429 GVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKVQ 1485
Cdd:cd06714     39 GAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEVQDIISQSKGEVELVVS 95
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 642-699 1.24e-03

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


Pssm-ID: 467259 [Multi-domain]  Cd Length: 79  Bit Score: 39.25  E-value: 1.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  642 NGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 699
Cdd:cd06798     21 DSVIISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFLLI 78
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1406-1484 1.38e-03

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: 39.10  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1406 PRVVFIKKSQLELGVHLCGGNlhGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVyVEMLK--PRDGVRLK 1483
Cdd:cd06712      1 PRTVHLTKEEGGFGFTLRGDS--PVQVASVDPGSCAAE-AGLKEGDYIVSVGGVDCKWSKHSEV-VKLLKsaGEEGLELQ 76


                   .
gi 2462521864 1484 V 1484
Cdd:cd06712     77 V 77
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1262-1320 1.43e-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: 39.05  E-value: 1.43e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864 1262 GSEPLGISIVsgekGG------IYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06753      6 GPAPWGFRLQ----GGkdfnqpLTISRVTPGGKAAQANLRPGDVILAINGESTEGMTHLEAQNKI 66
PLN02939 PLN02939
transferase, transferring glycosyl groups
 74-443 1.45e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 43.74  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   74 AFATHGTAFDKRPYHRLNPDYERLKIQCV---RAMSDLQSLQNQHTNALKRCEEVAK---ETDFYHTLHSRLL------- 140
Cdd:PLN02939     8 ALLSHGCGPIRSRAPFYLPSRRRLAVSCRarrRGFSSQQKKKRGKNIAPKQRSSNSKlqsNTDENGQLENTSLrtvmelp 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  141 SDQTRLKDDVDMLRRENGQLLRERNLLQQswEDMKRLHEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVK 220
Cdd:PLN02939    88 QKSTSSDDDHNRASMQRDEAIAAIDNEQQ--TNSKDGEQLSDFQLEDLVGMIQNAEK---NILLLNQARLQALEDLEKIL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  221 KDYDALRKryseKVAIHNADLS----RLEQLGEENQRLLKQTEMLTQQRDtaiQLQHQCALSLRRFEAIHHELNKATAQN 296
Cdd:PLN02939   163 TEKEALQG----KINILEMRLSetdaRIKLAAQEKIHVEILEEQLEKLRN---ELLIRGATEGLCVHSLSKELDVLKEEN 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  297 KDLQWEMELLQSELTELRTTQVKTAKeSEKYREERDAVYS--EYKLIMSERDqvISELDKLQTE-----VELAESKLKSS 369
Cdd:PLN02939   236 MLLKDDIQFLKAELIEVAETEERVFK-LEKERSLLDASLRelESKFIVAQED--VSKLSPLQYDcwwekVENLQDLLDRA 312

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  370 TSEKKAANEEMEALRQIKDTVtmdagrankeveilrkqckalcQELKEALQEADVAK--CRRDWAFQERDKIVAER 443
Cdd:PLN02939   313 TNQVEKAALVLDQNQDLRDKV----------------------DKLEASLKEANVSKfsSYKVELLQQKLKLLEER 366
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 1253-1330 1.46e-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: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1253 EPRHVKVQKGSEP-LGISIVSGEKG-----GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCD 1325
Cdd:cd23072      1 EITLVNLKKDAKYgLGFQIVGGEKSgrldlGIFISSITPGGPADLDGrLKPGDRLISVNDVSLEGLSHDAAVEILQNAPE 80


                   ....*
gi 2462521864 1326 TITIL 1330
Cdd:cd23072     81 DVTLV 85
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
 1255-1320 1.53e-03

PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains. Human STXBP4 (also known as Synip) includes a single PDZ domain, a coiled-coil domain, and a WW domain (named for its two conserved tryptophans); Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). Human STXBP4 plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane: insulin induces the dissociation of the STXBP4 and STX4 complex liberating STX4 to interact with Vamp2, and to form the SNARE complex thereby promoting vesicle fusion. It may also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose. Human STXBP4 is also known to physically associate with a prominent isoform of TP63 (deltaNp63alpha 9) whose overexpression promotes squamous cell carcinoma development, and in doing so prevents degradation of this isoform by the Cdc20-APC/C complex, Itch, and RACK1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467184 [Multi-domain]  Cd Length: 89  Bit Score: 39.21  E-value: 1.53e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462521864 1255 RHVKVQKGSEpLGISIVSG----EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1320
Cdd:cd06698      3 QLITVAKSTG-LGLSIVGGinrpEGPMVFIQEVIPGGDCYKDGrLRPGDQLVSINKESLIGVTLEEAKSIL 72
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 780-1209 1.58e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  780 GGPLQVCPQACPSASERSLSSFRSDASGDRGFGLVD---VRGRRPLLPFETEVGPCGVGEAsldKADSEGSNSGGTWPka 856
Cdd:PHA03307    17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAvtvVAGAAACDRFEPPTGPPPGPGT---EAPANESRSTPTWS-- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  857 mlSSTAVPEKlsvykkPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGPAHSPQPSKRAGPLTPPKPPRRSDSIKFQHR--- 933
Cdd:PHA03307    92 --LSTLAPAS------PAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAava 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  934 ------------LETSSESEATLVGSSPSTSppsalpPDVDPGEPMHASPPRKARVRIASSYYPEGDGDSSHLPAKKSCD 1001
Cdd:PHA03307   164 sdaassrqaalpLSSPEETARAPSSPPAEPP------PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1002 EDLTSQKVD-ELGQKRRRPKSAPSFRPKLAPVVIPAQFLEEQKCVPASGELSPELQEWAPYSPGHSSRHSNPPLYPSRPS 1080
Cdd:PHA03307   238 DSSSSESSGcGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1081 VGTVPRSLTPSTTVSSILRNPIYTVRS---HRVGPCSSPPAARDAGPQGLHPSVQHQGRLSldlshrtcsdysemRATHG 1157
Cdd:PHA03307   318 SSSSRESSSSSTSSSSESSRGAAVSPGpspSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP--------------AASAG 383

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1158 SNSLPSSARLGSSSNLQfkaeRIKIPSTPRYPRSVVGSERGSVSHSECSTPP 1209
Cdd:PHA03307   384 RPTRRRARAAVAGRARR----RDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 1255-1312 1.59e-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: 1.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1255 RHVKVQKGS-EPLGISIVSGEKGGIYVSKVTVGSIAH-QAGLEYGDQLLEFNGINLRSAT 1312
Cdd:cd10831      1 RLVQFQKNTdEPMGITLKMNEDGRCIVARIMHGGMIHrQGTLHVGDEIREINGISVANQT 60
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 299-505 1.61e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  299 LQWEMELLQSELTE-LRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEV--ELAESKLKSSTSEKKA 375
Cdd:pfam13868   67 RKEERKRYRQELEEqIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELE 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  376 ANEEMEALRQIKDTVTMDAGR-ANKEVEILRKQCK--ALCQELKEALQEADVAKcrrdwafQERDKIVAERdsirTLCDN 452
Cdd:pfam13868  147 KEEEREEDERILEYLKEKAEReEEREAEREEIEEEkeREIARLRAQQEKAQDEK-------AERDELRAKL----YQEEQ 215

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  453 LRRERDRAVSELAEALRSLDDTRKQkNDVSRELKELKEQMESQLEKEARFRQL 505
Cdd:pfam13868  216 ERKERQKEREEAEKKARQRQELQQA-REEQIELKERRLAEEAEREEEEFERML 267
SH3_DLG-like cd11861
Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding ...
 1503-1560 1.66e-03

Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding proteins that cluster at synapses and are also called PSD (postsynaptic density)-95 proteins or SAPs (synapse-associated proteins). They play important roles in synaptic development and plasticity, cell polarity, migration and proliferation. They are 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. DLG-like proteins contain three PDZ domains and varying N-terminal regions. All DLG proteins exist as alternatively-spliced isoforms. Vertebrates contain four DLG proteins from different genes, called DLG1-4. DLG4 and DLG2 are found predominantly at postsynaptic sites and they mediate surface ion channel and receptor clustering. DLG3 is found axons and some presynaptic terminals. DLG1 interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. The SH3 domain of DLG4 binds and clusters the kainate subgroup of glutamate receptors via two proline-rich sequences in their C-terminal tail. It also binds AKAP79/150 (A-kinase anchoring protein). 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: 212795 [Multi-domain]  Cd Length: 61  Bit Score: 38.46  E-value: 1.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1503 YIRALYDRLADVE-----QELSFKKDDILYV----DDTLpqgtfgsWMAWQLDENAQKIQRGQIPSK 1560
Cdd:cd11861      1 YVRALFDYDPSRDsglpsQGLSFKFGDILHVtnasDDEW-------WQARRVTPNGEEEEVGVIPSK 60
PDZ0_GgPro-IL-16-like cd23062
PDZ domain 0 of Gallus gallus interleukin-16, and related domains; N-terminal PDZ (PSD-95 ...
 626-689 1.68e-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: 1.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  626 LHINLSGQKDSGiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 689
Cdd:cd23062     11 SGIKLSRNPNCA-SLWKGFTGCHVPAGGTANRDGCLSPRDELLTLNGQSLKDLSSKEAESLIQS 73
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 643-696 1.71e-03

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: 39.16  E-value: 1.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  643 GVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRScQDSLTL 696
Cdd:cd06737     28 GLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLIKT-KKTVSL 79
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 625-698 1.72e-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: 39.16  E-value: 1.72e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  625 PLHINLSGQKDSGiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 698
Cdd:cd06679     12 SLGISVAGGRGSR-RGDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSIVL 84
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 ...
 524-613 1.74e-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: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  524 TEVVEFQRetediDLKALGFDMAEGVNEPCfpGDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQA---I 598
Cdd:cd06763      1 AVTVELEK-----GSAGLGFSLEGGKGSPL--GDRPLTIKRIFKGGAAEqsGVLQVGDEILQINGTSLQGLTRFEAwniI 73

                           90
                   ....*....|....*
gi 2462521864  599 KALlnGEGAINMVVR 613
Cdd:cd06763     74 KSL--PEGPVTLLIR 86
PDZ_LIMK-like cd06754
PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 660-689 1.77e-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: 1.77e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462521864  660 SLAVGDRIVAINGIALDNKSLNECESLLRS 689
Cdd:cd06754     50 SLHVGDRILEVNGTPVRDLSLEEIDDLIQS 79
PDZ_ARHGAP21_23-like cd06756
PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1278-1331 1.82e-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: 39.75  E-value: 1.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462521864 1278 IYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITILA 1331
Cdd:cd06756     55 IFVKQVKEGGPAHQAGLCTGDRIVKVNGESVIGKTYSQVIALI-QNSDSTLELS 107
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 637-672 1.85e-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: 39.00  E-value: 1.85e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462521864  637 GISLENGVYAAAVLPGSPAAKEGsLAVGDRIVAING 672
Cdd:cd10839     20 GLKEPKGALVAQVLPDSPAAKAG-LKAGDVILSLNG 54
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 402-553 1.85e-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: 42.96  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  402 EILRKQCKALCQELKEALQEADVAKCRRdwafqERDKIVAERDsiRTLCDNLRRERDRAVSELAEALRSL----DDTRKQ 477
Cdd:pfam07888   30 ELLQNRLEECLQERAELLQAQEAANRQR-----EKEKERYKRD--REQWERQRRELESRVAELKEELRQSrekhEELEEK 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  478 KNDVSRELKELKEQ----MESQLEKEARFRQL------MAHSSHDSAIDTDSMEWETEVVEFQRETEDIDLKALGFDMAE 547
Cdd:pfam07888  103 YKELSASSEELSEEkdalLAQRAAHEARIRELeediktLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182


                   ....*.
gi 2462521864  548 GVNEPC 553
Cdd:pfam07888  183 TEEELR 188
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 144-329 1.88e-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: 41.43  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  144 TRLKDDVDMLRRENGQLLRERNLLQQswedMKRLHEEDQKEIGDLRAQQQQVL-KHNGSSEILNKLYDTAMDKLEVVKKd 222
Cdd:pfam15619   14 KELQNELAELQSKLEELRKENRLLKR----LQKRQEKALGKYEGTESELPQLIaRHNEEVRVLRERLRRLQEKERDLER- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  223 ydALRKRYSEkvaIH--NADLSRLEQLG--------EENQRLLKQTEMLTQQRDTAIQ-LQHQCALSLRRFeaiHHELNK 291
Cdd:pfam15619   89 --KLKEKEAE---LLrlRDQLKRLEKLSedknlaerEELQKKLEQLEAKLEDKDEKIQdLERKLELENKSF---RRQLAA 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462521864  292 ATAQNKDLQWEMELLQSELTELRTtqvktaKESEKYRE 329
Cdd:pfam15619  161 EKKKHKEAQEEVKILQEEIERLQQ------KLKEKERE 192
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 541-612 1.93e-03

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


Pssm-ID: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 39.25  E-value: 1.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  541 LGFDMAEGVNEpcFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 612
Cdd:cd06680     13 LGFSIVGGYEE--SHGNQPFFVKSIVPGTPAynDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTV 84
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
388-539 1.94e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  388 DTVTMDAGRANKEVEILRKQCKALCQELKEALQEAdvakcrRDWAfQERDKIVAERDSIRTLCDNLRRERDRAVSELAEA 467
Cdd:COG1340      4 DELSSSLEELEEKIEELREEIEELKEKRDELNEEL------KELA-EKRDELNAQVKELREEAQELREKRDELNEKVKEL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  468 lrslddtRKQKNDVSRELKELKEQMESQLEKEARFRQlmahsshdSAIDTDSMEWETEVVEFQRETEDIDLK 539
Cdd:COG1340     77 -------KEERDELNEKLNELREELDELRKELAELNK--------AGGSIDKLRKEIERLEWRQQTEVLSPE 133
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 ...
 1257-1316 1.97e-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: 1.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864 1257 VKVQKGSEPLGISIvSGEKGG------IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06763      4 VELEKGSAGLGFSL-EGGKGSplgdrpLTIKRIFKGGAAEQSGvLQVGDEILQINGTSLQGLTRFEA 69
PHA03247 PHA03247
large tegument protein UL36; Provisional
 881-1254 2.01e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  881 DPNTFKRPQTPPKIDYLLPGPGPAHSPQPSKRAGPLTPPKPPRRSDSI-----KFQHRLETSSESEATLVGSSPSTSPPS 955
Cdd:PHA03247  2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDdpapgRVSRPRRARRLGRAAQASSPPQRPRRR 2686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  956 ALPPDV---------DPGEPMHASPPRKARVRIASSYYPEGDGDSSHLPAKKSCDEDLTSQKVDELGQKRRRPKSAPSFR 1026
Cdd:PHA03247  2687 AARPTVgsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP 2766

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1027 PKLAPVVIPAQFLEEQKCVPASGELSPELQE----WAPYSPGHSSRHSNPPLYPSRPSVGTVPRSLTPSTTVSSILRNPI 1102
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESlpspWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1103 YTVRS-----------HRVGPCSSPPAARDAGPqglHPSVQHQGRLSLDLSHRtcsdysemrathgSNSLPssarlgsss 1171
Cdd:PHA03247  2847 PPSLPlggsvapggdvRRRPPSRSPAAKPAAPA---RPPVRRLARPAVSRSTE-------------SFALP--------- 2901

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1172 nlQFKAERIKIPSTPRYPRSVVGSERGSVSHSECSTP--PQSPLNIDTLSSCSQSQTSASTLPRI-AVNPASLGERR--- 1245
Cdd:PHA03247  2902 --PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPprPQPPLAPTTDPAGAGEPSGAVPQPWLgALVPGRVAVPRfrv 2979

                          410
                   ....*....|
gi 2462521864 1246 -KDRPYVEEP 1254
Cdd:PHA03247  2980 pQPAPSREAP 2989
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 141-378 2.04e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  141 SDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngsseilnklydtAMDKLEVVK 220
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-----------------LQAEIAEAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  221 KDYDALRKRYSEKVA---IHNADLSRLEQL--GEENQRLLKQTEMLTQ--QRDTAIqlqhqcalsLRRFEAIHHELNKAT 293
Cdd:COG3883     79 AEIEERREELGERARalyRSGGSVSYLDVLlgSESFSDFLDRLSALSKiaDADADL---------LEELKADKAELEAKK 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  294 AQNKDLQWEMELLQSELTELRttqvktaKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVELAESKLKSSTSEK 373
Cdd:COG3883    150 AELEAKLAELEALKAELEAAK-------AELEAQQAEQEALLAQLS---AEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219


                   ....*
gi 2462521864  374 KAANE 378
Cdd:COG3883    220 AAAAA 224
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 633-696 2.19e-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: 38.80  E-value: 2.19e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  633 QKDSGISL---------ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06674      9 QKKPGRGLglsivgkrnDTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGKVRL 81
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 ...
 1261-1316 2.24e-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: 38.79  E-value: 2.24e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1261 KGSEPLGISIVSGE---KG--GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06759      9 AGGKGLGFSIVGGRdspRGpmGIYVKTIFPGGAAAEDGrLKEGDEILEVNGESLQGLTHQEA 70
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 649-673 2.37e-03

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


Pssm-ID: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 38.73  E-value: 2.37e-03
                           10        20
                   ....*....|....*....|....*
gi 2462521864  649 VLPGSPAAKEGSLAVGDRIVAINGI 673
Cdd:cd06731     32 VVPDGPAALDGKLRTGDVLVSVNDT 56
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 261-426 2.43e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  261 LTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRtTQVKTAKESEKYREER--DAVYSEY 338
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-AEIAEAEAEIEERREElgERARALY 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  339 K----------------------------LIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQikdtv 390
Cdd:COG3883     97 RsggsvsyldvllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA----- 171

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462521864  391 TMDAGRANKEVEI--LRKQCKALCQELKEALQEADVAK 426
Cdd:COG3883    172 ELEAQQAEQEALLaqLSAEEAAAEAQLAELEAELAAAE 209
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 1274-1317 2.43e-03

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


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 39.22  E-value: 2.43e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462521864 1274 EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQAR 1317
Cdd:cd10838     31 EVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRI 74
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 1276-1313 2.68e-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: 38.91  E-value: 2.68e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462521864 1276 GGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATE 1313
Cdd:cd06777     25 QGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLE 62
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 1279-1330 2.74e-03

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 38.76  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1279 YVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1330
Cdd:cd06713     38 YVCRVHEDSPAYLAGLTAGDVILSVNGVSVEGASHQEIVELIRSSGNTLRLE 89
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 523-603 2.79e-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: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  523 ETEVVEFQRETEdidlKALGFDMAEGVNEPCFPGD----CGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQ 596
Cdd:cd06671      1 PPRRVELWREPG----KSLGISIVGGRVMGSRLSNgeeiRGIFIKHVLEDSPAGrnGTLKTGDRILEVNGVDLRNATHEE 76


                   ....*..
gi 2462521864  597 AIKALLN 603
Cdd:cd06671     77 AVEAIRN 83
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 1263-1318 2.85e-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: 38.81  E-value: 2.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864 1263 SEPLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1318
Cdd:cd06779     12 SPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAAL 67
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 541-614 3.00e-03

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


Pssm-ID: 467199 [Multi-domain]  Cd Length: 92  Bit Score: 38.53  E-value: 3.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521864  541 LGFDMAEG---VNEPCFPGDCGIFVTKV-DKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 614
Cdd:cd06715     14 LGFNIIGGrpcENNQEGSSSEGIYVSKIvENGPAADeGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKEPIVVQVLR 92
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 643-696 3.16e-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: 38.03  E-value: 3.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  643 GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06667     23 GVVVKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRL 76
46 PHA02562
endonuclease subunit; Provisional
 171-488 3.31e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  171 WEDMKRLHEEdqKEIGDLRAQQQQVLKHN----------GSS--------------EILNKLYD----TAMDKLEVVK-- 220
Cdd:PHA02562   100 YCNGKLLDES--ASSKDFQKYFEQMLGMNyksfkqivvlGTAgyvpfmqlsaparrKLVEDLLDisvlSEMDKLNKDKir 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  221 ------KDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKqtEMLTQQRDTAiqlqhqcalslrrfEAIHHELNKATA 294
Cdd:PHA02562   178 elnqqiQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQ--NKYDELVEEA--------------KTIKAEIEELTD 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  295 QNKDLQWEMELLQSELTELRTTQVKTAKESEKYreERDAVYSEYKLIMSERDQVISELDKLQTEVElaeSKLKSSTSEKK 374
Cdd:PHA02562   242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF--QKVIKMYEKGGVCPTCTQQISEGPDRITKIK---DKLKELQHSLE 316

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  375 AANEEMEALRQIKDtvtmdagrankevEILRKQCKAlcQELKealqeADVAKCRRDWAfqerdKIVAERDSIRTLCDNLR 454
Cdd:PHA02562   317 KLDTAIDELEEIMD-------------EFNEQSKKL--LELK-----NKISTNKQSLI-----TLVDKAKKVKAAIEELQ 371

                          330       340       350
                   ....*....|....*....|....*....|....
gi 2462521864  455 RERDRAVSELAEALRSLDDTRKQKNDVSRELKEL 488
Cdd:PHA02562   372 AEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 153-535 3.34e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.98  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  153 LRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQ----------------VLKHngSSEILNKLYDTamdkL 216
Cdd:pfam05622   64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEEltslaeeaqalkdemdILRE--SSDKVKKLEAT----V 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  217 EVVKK---DYDALRKR---YSEKVAIHnadLSRLEQLGEENQR---LLKQTEMLTQQrdtaIQ-LQHQCALSLRRFEAIH 286
Cdd:pfam05622  138 ETYKKkleDLGDLRRQvklLEERNAEY---MQRTLQLEEELKKanaLRGQLETYKRQ----VQeLHGKLSEESKKADKLE 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  287 HELNKATAQNKDLQWEMELLQSE-------LTELRTTQVKTAKESE----------------------KYREERDAVYSE 337
Cdd:pfam05622  211 FEYKKLEEKLEALQKEKERLIIErdtlretNEELRCAQLQQAELSQadallspssdpgdnlaaeimpaEIREKLIRLQHE 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  338 YK-LIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAAN----------EEMEALRQIKDTVTMDAGRANKEVEILRK 406
Cdd:pfam05622  291 NKmLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANqrilelqqqvEELQKALQEQGSKAEDSSLLKQKLEEHLE 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  407 QCKALCQEL---KEALQE----ADVAKCRRDWAFQErdKIVAERDSIRTLCDNLRRERDRAvselAEALRSLDDtrKQKN 479
Cdd:pfam05622  371 KLHEAQSELqkkKEQIEElepkQDSNLAQKIDELQE--ALRKKDEDMKAMEERYKKYVEKA----KSVIKTLDP--KQNP 442

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  480 DVSRELKELKEQMesqLEKEARFrqlmahsshdsaidtDSMEWETEVVEFQRETED 535
Cdd:pfam05622  443 ASPPEIQALKNQL---LEKDKKI---------------EHLERDFEKSKLQREQEE 480
SH3_NEDD9 cd12002
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, ...
 1505-1541 3.64e-03

Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, Neural precursor cell Expressed, Developmentally Down-regulated 9; NEDD9 is also called human enhancer of filamentation 1 (HEF1) or CAS-L (Crk-associated substrate in lymphocyte). It was first described as a gene predominantly expressed in early embryonic brain, and was also isolated from a screen of human proteins that regulate filamentous budding in yeast, and as a tyrosine phosphorylated protein in lymphocytes. It promotes metastasis in different solid tumors. NEDD9 localizes in focal adhesions and associates with FAK and Abl kinase. It also interacts with SMAD3 and the proteasomal machinery which allows its rapid turnover; these interactions are not shared by other CAS proteins. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212935  Cd Length: 57  Bit Score: 37.27  E-value: 3.64e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462521864 1505 RALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWM 1541
Cdd:cd12002      3 RALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWL 39
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 1263-1330 3.68e-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: 38.41  E-value: 3.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864 1263 SEPLGISIVSG----EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSatEQQARLIIGQQCDTITIL 1330
Cdd:cd06716     14 QEKLGLTLCYRtddeEDTGIYVSEVDPNSIAAKDGrIREGDQILQINGVDVQN--REEAIALLSEEEKSITLL 84
SH3_CRK_N cd11758
N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ...
 1503-1562 3.87e-03

N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The N-terminal SH3 domain of CRK binds a number of target proteins including DOCK180, C3G, SOS, and cABL. The CRK family includes two alternatively spliced protein forms, CRKI and CRKII, that are expressed by the CRK gene, and the CRK-like (CRKL) protein, which is expressed by a distinct gene (CRKL). 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: 212692 [Multi-domain]  Cd Length: 55  Bit Score: 37.34  E-value: 3.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1503 YIRALYDRLADVEQELSFKKDDILYVDDTlPQGTFgsWMAwqldENAQKiQRGQIPSKYV 1562
Cdd:cd11758      2 YVRALFDFPGNDDEDLPFKKGEILTVIRK-PEEQW--WNA----RNSEG-KTGMIPVPYV 53
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 559-623 3.89e-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: 3.89e-03
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gi 2462521864  559 GIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQaikallngegainmVVRRRKSLGGKVV 623
Cdd:cd06768     24 GHFIREVDPGSPAErAGLKDGDRLVEVNGENVEGESHEQ--------------VVEKIKASGNQVT 75
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 1428-1492 4.01e-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: 38.43  E-value: 4.01e-03
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gi 2462521864 1428 HGVFVAEVEDDSPAKGPdGLVPGDLILEYGSLDVRNKT-VEEVYVEMlKPRDGVRLKVQYRPEEFT 1492
Cdd:cd06779     25 RGVLVAEVIPGSPAAKA-GLKEGDVILSVNGKPVTSFNdLRAALDTK-KPGDSLNLTILRDGKTLT 88
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1267-1332 4.28e-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: 4.28e-03
                           10        20        30        40        50        60
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gi 2462521864 1267 GISIvsgeKGGIYVSKVTVGS-IAHQAGLEYGDQLLEFNGINL--RSATEQQARLIIGQQCDTITILAQ 1332
Cdd:cd06765     11 GISL----ENGVFISRIVPGSpAAKEGSLTVGDRIIAINGIALdnKSLSECEALLRSCRDSLSLSLMKV 75
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 613-700 4.31e-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: 38.14  E-value: 4.31e-03
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gi 2462521864  613 RRRKSLGGKVVTPlhiNLSGQKDSGISLEnGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQD 692
Cdd:cd06715      9 RENGSLGFNIIGG---RPCENNQEGSSSE-GIYVSKIVENGPAADEGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKE 84


                   ....*...
gi 2462521864  693 SLTLSLLK 700
Cdd:cd06715     85 PIVVQVLR 92
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 625-672 4.34e-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: 4.34e-03
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gi 2462521864  625 PLHINLSGQKDSgisLENGVYAAAVLPGSPAAKEGSLAVGDRIVAING 672
Cdd:cd23065     10 PLGVSVVGGKNH---VTTGCIITHIYPNSIVAADKRLKVFDQILDING 54
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 156-386 4.40e-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: 4.40e-03
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gi 2462521864  156 ENGQLLRERNLLQQSWEDMKRLhEEDQKEIGDLRAQQQQVLK------HNGSSEILNKLYDTAMDKLEVVKKDYDALRKR 229
Cdd:pfam06160  170 ESGDYLEAREVLEKLEEETDAL-EELMEDIPPLYEELKTELPdqleelKEGYREMEEEGYALEHLNVDKEIQQLEEQLEE 248

                           90       100       110       120       130       140       150       160
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gi 2462521864  230 YSEkvAIHNADLSRLEqlgEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAihhELNKATAQNKDLQWEMELLQ-- 307
Cdd:pfam06160  249 NLA--LLENLELDEAE---EALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIED---YLEHAEEQNKELKEELERVQqs 320

                          170       180       190       200       210       220       230       240
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gi 2462521864  308 -----SELTELR--TTQVKTAK----ESEKYREERDAVYSEyklIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAA 376
Cdd:pfam06160  321 ytlneNELERVRglEKQLEELEkrydEIVERLEEKEVAYSE---LQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEA 397

                          250
                   ....*....|
gi 2462521864  377 NEEMEALRQI 386
Cdd:pfam06160  398 REKLDEFKLE 407
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 559-613 4.41e-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: 4.41e-03
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gi 2462521864  559 GIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 613
Cdd:cd23063     31 GIFIKGIIPDSPAHkcGRLKVGDRILSVNGNDVRNSTEQAAIDLIKEADFKIVLEIQ 87
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 644-696 4.45e-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: 38.19  E-value: 4.45e-03
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gi 2462521864  644 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 696
Cdd:cd06796     28 IYISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKL 80
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1256-1304 4.76e-03

PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 9 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ9 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ9 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467263 [Multi-domain]  Cd Length: 79  Bit Score: 37.71  E-value: 4.76e-03
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gi 2462521864 1256 HVKVQKGSEPLGISIVSGEK-GGIYVSKVTVGSIAHQAG-LEYGDQLLEFN 1304
Cdd:cd10817      1 HVELPKDQGGLGIAISEEDTeNGIVIKSLTEGGPAAKDGrLKVGDQILAVD 51
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 523-603 4.77e-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: 37.93  E-value: 4.77e-03
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gi 2462521864  523 ETEVVEFQREtedidlKALGFDMAEGvnepcfpGDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 601
Cdd:cd06729      1 DTRLVSFRKG------GSVGLRLAGG-------NDVGIFVAGVQEGSPAEKQgLQEGDQILKVNGVDFRNLTREEAVLFL 67


                   ..
gi 2462521864  602 LN 603
Cdd:cd06729     68 LD 69
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 643-672 4.88e-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: 37.86  E-value: 4.88e-03
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gi 2462521864  643 GVYAAAVLPGSPAAkeGSLAVGDRIVAING 672
Cdd:cd23080      1 GVYVLSVVENMPAK--GILEAGDKITAIDG 28
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1256-1316 4.99e-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: 37.96  E-value: 4.99e-03
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gi 2462521864 1256 HVKVQKGSEPLGISIVSGEKGG--IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1316
Cdd:cd06731      3 RTSLKKSARGFGFTIIGGDEPDefLQIKSVVPDGPAALDGkLRTGDVLVSVNDTCVLGYTHADV 66
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 279-507 5.03e-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: 41.06  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  279 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVY-SEYKLIMSERDQVISELDKLQT 357
Cdd:pfam13868   33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRqEEYEEKLQEREQMDEIVERIQE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  358 EvELAESKLKSStsEKKAANEEM-EALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQE- 435
Cdd:pfam13868  113 E-DQAEAEEKLE--KQRQLREEIdEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARl 189

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  436 RDKIVAERDSIRTLcDNLRRERDRAVSELAEALRSLDDTRKQKndvsRELKELKEQMESQLEKEARFRQLMA 507
Cdd:pfam13868  190 RAQQEKAQDEKAER-DELRAKLYQEEQERKERQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEA 256
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 1252-1329 5.07e-03

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: 41.01  E-value: 5.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1252 EEPRHVKVQKGSEPLGISI-VSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA-RLIIGQQCDTITI 1329
Cdd:COG0793     46 EEYEDFQESTSGEFGGLGAeLGEEDGKVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAGLTLDDAvKLLRGKAGTKVTL 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 556-592 5.09e-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: 5.09e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462521864  556 GDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINK 592
Cdd:cd06714     36 GRLGAYVTKVKPGSVADtvGHLREGDEVLEWNGISLQGK 74
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 202-501 5.13e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 42.13  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  202 SEILNKLYDTAMDKLEVVKKDYD----ALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTA-----IQLQ 272
Cdd:PTZ00440  1086 VEALLKKIDENKNKLIEIKNKSHehvvNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLnevneIEIE 1165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  273 HQCALslrrfeaIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESE------KYREERDAVYSEYKLIM---- 342
Cdd:PTZ00440  1166 YERIL-------IDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNdhlttfEYNAYYDKATASYENIEeltt 1238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  343 --------SERDQVISELDKLQTEVelaESKLKSSTSEkkaaNEEME-ALRQIKDT----VTMDAGRANKEVEILRKQCK 409
Cdd:PTZ00440  1239 eakglkgeANRSTNVDELKEIKLQV---FSYLQQVIKE----NNKMEnALHEIKNMyeflISIDSEKILKEILNSTKKAE 1311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  410 ALCQELKEALQEADvakcrrDWAFQERDKIVAERDSIRTLCDNLRRER-DRAVSELAEALRSLDDTRKQKNDVSRELKEL 488
Cdd:PTZ00440  1312 EFSNDAKKELEKTD------NLIKQVEAKIEQAKEHKNKIYGSLEDKQiDDEIKKIEQIKEEISNKRKEINKYLSNIKSN 1385

                          330
                   ....*....|...
gi 2462521864  489 KEQMESQLEKEAR 501
Cdd:PTZ00440  1386 KEKCDLHVRNASR 1398
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 557-616 5.43e-03

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


Pssm-ID: 467162 [Multi-domain]  Cd Length: 87  Bit Score: 37.65  E-value: 5.43e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864  557 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK 616
Cdd:cd06674     26 DTGVFVSDIVKGGAAdaDGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGKVRLEVGRLK 87
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 151-316 6.07e-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: 40.29  E-value: 6.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  151 DMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQqvlKHNGSSEILNKLYDTAMDKLEVVK--KDYDALRK 228
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRnnKEYEALQK 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  229 ryseKVAIHNADLSRLEqlgEENQRLLKQTEMLTQQRDtaiQLQHQCALSLRRFEAIHHELNKATAqnkDLQWEMELLQS 308
Cdd:COG1579     97 ----EIESLKRRISDLE---DEILELMERIEELEEELA---ELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163


                   ....*...
gi 2462521864  309 ELTELRTT 316
Cdd:COG1579    164 EREELAAK 171
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 561-614 6.07e-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: 6.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521864  561 FVTKVDKGSIAD-GRLRVNDWLLRINDVDLinKDKKQAIKALLNGEGA-INMVVRR 614
Cdd:pfam17820    1 VVTAVVPGSPAErAGLRVGDVILAVNGKPV--RSLEDVARLLQGSAGEsVTLTVRR 54
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 1411-1487 6.60e-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: 37.66  E-value: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1411 IKKSQLELGVHLCGGN---LHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKVqYR 1487
Cdd:cd06673      8 INKGKKGLGLSIVGGSdtlLGAIIIHEVYEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEAINVLRQTPQKVRLLV-YR 86
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 541-616 6.62e-03

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


Pssm-ID: 467285 [Multi-domain]  Cd Length: 92  Bit Score: 37.86  E-value: 6.62e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  541 LGFDMAEGvnEPCFPGDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK 616
Cdd:cd23072     15 LGFQIVGG--EKSGRLDLGIFISSITPGGPADldGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVSQPK 90
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 434-506 6.82e-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: 40.29  E-value: 6.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462521864  434 QERDKivaERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLM 506
Cdd:COG1579     13 QELDS---ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 522-601 6.93e-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: 37.59  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  522 WETEVVEFQRETEDidlKALGFDMAEgVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIK 599
Cdd:cd06669      4 WSDEVTVIELEKGD---RGLGFSILD-YQDPLDPSETVIVIRSLVPGGVAeqDGRLLPGDRLVFVNDVSLENASLDEAVQ 79


                   ..
gi 2462521864  600 AL 601
Cdd:cd06669     80 AL 81
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 227-540 7.09e-03

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: 41.48  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  227 RKRYSEKVAIHNADL-SRLEQLGEENQRLLKQTEMLTQQ--RDTAIQLQHQCALS-LRRFeaihheLNKATAQNKDLQWE 302
Cdd:COG3096    280 RRELSERALELRRELfGARRQLAEEQYRLVEMARELEELsaRESDLEQDYQAASDhLNLV------QTALRQQEKIERYQ 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  303 MELlqSELT---ELRTTQVKTAKES-EKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKsstsekkaANE 378
Cdd:COG3096    354 EDL--EELTerlEEQEEVVEEAAEQlAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ--------ALE 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  379 EMEALRQIKDtvtMDAGRANKEVEILRKQCKALCQELKEA---LQEADVAKCRRDWAFQERDKIVAErdsirtlcdnlrR 455
Cdd:COG3096    424 KARALCGLPD---LTPENAEDYLAAFRAKEQQATEEVLELeqkLSVADAARRQFEKAYELVCKIAGE------------V 488

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  456 ERDRAVSELAEALRSLDDTRKQKNDVS---RELKELKEQMESQleKEARfRQLMAHSSHDSAIDTDSMEWETEVVEFQRE 532
Cdd:COG3096    489 ERSQAWQTARELLRRYRSQQALAQRLQqlrAQLAELEQRLRQQ--QNAE-RLLEEFCQRIGQQLDAAEELEELLAELEAQ 565


                   ....*...
gi 2462521864  533 TEDIDLKA 540
Cdd:COG3096    566 LEELEEQA 573
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 541-614 7.10e-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: 7.10e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462521864  541 LGFDMAEGVNepcfpgDCGIFVTK-VDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 614
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 ...
 540-601 7.25e-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: 7.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462521864  540 ALGFDMAEGVNEPcfPGDCGIFVTKVD-KGSIA-DGRLRVNDWLLRINDVDLINKDKKQAIKAL 601
Cdd:cd06679     12 SLGISVAGGRGSR--RGDLPIYVTNVQpDGCLGrDGRIKKGDVLLSINGISLTNLSHSEAVAVL 73
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 559-601 7.50e-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: 7.50e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462521864  559 GIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 601
Cdd:cd06740     28 GIYVSLVEPGSLAEKEgLRVGDQILRVNDVSFEKVTHAEAVKIL 71
Cep57_CLD_2 pfam14197
Centrosome localization domain of PPC89; The N-terminal region of the fission yeast spindle ...
 451-491 7.69e-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: 7.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2462521864  451 DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQ 491
Cdd:pfam14197   27 KRLRRERDSAVRQLGVAYLEIQELKAENEALRKELKEQRAQ 67
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 1266-1309 7.92e-03

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


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 37.46  E-value: 7.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462521864 1266 LGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLR 1309
Cdd:cd06782      4 IGIEIGKDDDGYLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVR 47
COG5022 COG5022
Myosin heavy chain [General function prediction only];
227-490 8.08e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 8.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  227 RKRYSEKVAIhNADLsrleQLGEENQRLLKQTEmltqqrdtAIQLQHQCALSLRRFEAIHHELNKATAQNKDL-----QW 301
Cdd:COG5022    809 RKEYRSYLAC-IIKL----QKTIKREKKLRETE--------EVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETiylqsAQ 875

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  302 EMELLQSELTELRTTqvktakesekyREERDAVYseykLIMSERDQVISELDKLQTEVELAESKLKS--STSEKKAANEe 379
Cdd:COG5022    876 RVELAERQLQELKID-----------VKSISSLK----LVNLELESEIIELKKSLSSDLIENLEFKTelIARLKKLLNN- 939

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  380 mealRQIKDTVTMDAGRaNKEVEILRKQCKalcqELKEALQEadvakcrrdwafqerdkivaeRDSIRTLCDNLRRERDR 459
Cdd:COG5022    940 ----IDLEEGPSIEYVK-LPELNKLHEVES----KLKETSEE---------------------YEDLLKKSTILVREGNK 989

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2462521864  460 AVSELAEALRSLDDTRKQKNDVSRELKELKE 490
Cdd:COG5022    990 ANSELKNFKKELAELSKQYGALQESTKQLKE 1020
PDZ1_syntenin-like cd06721
PDZ domain 1 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1276-1308 8.25e-03

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: 36.83  E-value: 8.25e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462521864 1276 GGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINL 1308
Cdd:cd06721     22 KGVFVQLVQANSPAALAGLRFGDQILQINGENV 54
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 106-333 8.27e-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: 40.52  E-value: 8.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  106 SDLQSLQNQHTNALKRCEEVAKEtdfyhtlhsrllsdQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEI 185
Cdd:COG4942     27 AELEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  186 GDLRAQ---QQQVLkhngsSEILNKLYDTA-MDKLEVVKKDYDAL----RKRYSEKVAihNADLSRLEQLGEENQRLLKQ 257
Cdd:COG4942     93 AELRAEleaQKEEL-----AELLRALYRLGrQPPLALLLSPEDFLdavrRLQYLKYLA--PARREQAEELRADLAELAAL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  258 TEMLTQQRDTAIQLQHQCALSLRRFEAIHHE----LNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDA 333
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
46-348 8.38e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864   46 RQVNEKVENLSIQLRLMTRERNELRKRLAfathgtafdkrpyhRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEV 125
Cdd:COG4372     34 RKALFELDKLQEELEQLREELEQAREELE--------------QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  126 AKETdfyhtlhSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQ------------ 193
Cdd:COG4372    100 QEEL-------ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEslqeelaaleqe 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  194 -QVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKV--AIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQ 270
Cdd:COG4372    173 lQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRelAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  271 LQHQCALSLRRFEAIHHELNKATAQNKDLQW--EMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQV 348
Cdd:COG4372    253 EEVILKEIEELELAILVEKDTEEEELEIAALelEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
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 ...
 539-613 8.40e-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: 8.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864  539 KALGFDMAEGVNEPcfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN-GEGAINMVVR 613
Cdd:cd06759     12 KGLGFSIVGGRDSP--RGPMGIYVKTIFPGGAAaeDGRLKEGDEILEVNGESLQGLTHQEAIQKFKQiKKGLVVLTVR 87
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1257-1320 8.45e-03

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: 37.23  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864 1257 VKVQK--GSEpLGISIVSG---EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGIN------------LRSATEQQARL 1318
Cdd:cd06684      5 VEIEKtpGSS-LGITLSTSthrNKQVIVIDSIKPASIADRCGaLHVGDHILSIDGTSvehcslaeatqlLASNSGDQVKL 83


                   ..
gi 2462521864 1319 II 1320
Cdd:cd06684     84 EI 85
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 159-493 8.81e-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: 40.78  E-value: 8.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  159 QLLRERNLLQQSWEDMKRL-HEEDQ----KEIGDLRAQQ-QQVLKHNGSSEilnklydtAMDKLEVVKkdydalrkryse 232
Cdd:pfam05701   71 ELESTKRLIEELKLNLERAqTEEAQakqdSELAKLRVEEmEQGIADEASVA--------AKAQLEVAK------------ 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  233 kvAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCAL---------------------SLRRFEAIHHE--- 288
Cdd:pfam05701  131 --ARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSaskeiektveeltieliatkeSLESAHAAHLEaee 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  289 --LNKATAQNKD-LQWEMELLQSEltelrttqvktaKESEKYREErdavyseyklIMSERDqVISELD-------KLQTE 358
Cdd:pfam05701  209 hrIGAALAREQDkLNWEKELKQAE------------EELQRLNQQ----------LLSAKD-LKSKLEtasalllDLKAE 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  359 V-ELAESKLKSSTS----EKKAANEEMEALRQIK---DTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRD 430
Cdd:pfam05701  266 LaAYMESKLKEEADgegnEKKTSTSIQAALASAKkelEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAELASLRQREG 345

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  431 WAF-------QERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQME 493
Cdd:pfam05701  346 MASiavssleAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAE 415
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
 641-699 8.84e-03

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: 36.82  E-value: 8.84e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  641 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDN-KSLNEcesLLRSCQDSLTLSLL 699
Cdd:cd10832     21 EGELVIARILHGGMIDRQGLLHVGDIIKEVNGVPVGSpEQLQE---MLKNASGSVTLKIL 77
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 284-523 8.98e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 39.66  E-value: 8.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  284 AIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKesEKYREERDAvyseyklimsERDQVISEldKLQTEVELAE 363
Cdd:pfam04012   12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIA--RQKQLERRL----------EQQTEQAK--KLEEKAQAAL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  364 SKlksstsekkaANEEM--EALRQIKDtvtmdagrankeveiLRKQCKALCQELKEalQEADVAKCRRDWAFQERdKIVA 441
Cdd:pfam04012   78 TK----------GNEELarEALAEKKS---------------LEKQAEALETQLAQ--QRSAVEQLRKQLAALET-KIQQ 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521864  442 ERDSIRTLcdNLRRERDRAVSELAEALRSLDdtrkqKNDVSRELKELKEQmesQLEKEARFrQLMAHSSHDSAIDTDSME 521
Cdd:pfam04012  130 LKAKKNLL--KARLKAAKAQEAVQTSLGSLS-----TSSATDSFERIEEK---IEEREARA-DAAAELASAVDLDAKLEQ 198


                   ..
gi 2462521864  522 WE 523
Cdd:pfam04012  199 AG 200
PDZ3_harmonin cd06739
PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1255-1317 9.75e-03

PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of harmonin isoforms a and b, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467221 [Multi-domain]  Cd Length: 94  Bit Score: 37.29  E-value: 9.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521864 1255 RHVKVQKgSEPLGISIVSGE----KGGIYVSKVTVGSIAH-QAGLEYGDQLLEFNGINLRSATEQQAR 1317
Cdd:cd06739      4 RLLRIKK-NGPLDLALEGGIdsplGGKIVVSAVYEGGAADkHGGIVKGDQIMMVNGKSLTDVTLAEAE 70
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
 623-687 9.89e-03

PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains. Human STXBP4 (also known as Synip) includes a single PDZ domain, a coiled-coil domain, and a WW domain (named for its two conserved tryptophans); Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). Human STXBP4 plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane: insulin induces the dissociation of the STXBP4 and STX4 complex liberating STX4 to interact with Vamp2, and to form the SNARE complex thereby promoting vesicle fusion. It may also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose. Human STXBP4 is also known to physically associate with a prominent isoform of TP63 (deltaNp63alpha 9) whose overexpression promotes squamous cell carcinoma development, and in doing so prevents degradation of this isoform by the Cdc20-APC/C complex, Itch, and RACK1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467184 [Multi-domain]  Cd Length: 89  Bit Score: 36.90  E-value: 9.89e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462521864  623 VTPLHINLSGqkdsGISLENG--VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL 687
Cdd:cd06698     10 STGLGLSIVG----GINRPEGpmVFIQEVIPGGDCYKDGRLRPGDQLVSINKESLIGVTLEEAKSIL 72
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 1505-1562 9.95e-03

Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. 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: 212753 [Multi-domain]  Cd Length: 54  Bit Score: 36.14  E-value: 9.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462521864 1505 RALYDRLADVEQELSFKKDDILY----VDDtlpqgtfgswmAWQLDENAQKiQRGQIPSKYV 1562
Cdd:cd11819      3 KALYDYQAAEDNEISFVEGDIITqieqIDE-----------GWWLGVNAKG-QKGLFPANYV 52
 
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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