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Conserved domains on  [gi|767964245|ref|XP_011538646|]
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disks large homolog 5 isoform X6 [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 ...
 503-597 2.05e-59

PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


:

Pssm-ID: 467245 [Multi-domain]  Cd Length: 95  Bit Score: 198.78  E-value: 2.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  503 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 582
Cdd:cd06764     1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                          90
                  ....*....|....*
gi 767964245  583 LLNGEGAINMVVRRR 597
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 ...
 1234-1315 2.38e-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: 2.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1234 EEPRHVKVQKGSEPLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1313
Cdd:cd06767     1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                  ..
gi 767964245 1314 QY 1315
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 ...
 1387-1467 5.19e-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: 5.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1387 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1466
Cdd:cd06766     1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                  .
gi 767964245 1467 Q 1467
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 ...
 609-685 4.12e-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: 151.73  E-value: 4.12e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  609 HINLSGQKDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 685
Cdd:cd06765     1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1620-1796 1.97e-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: 1.97e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1620 QKVDCTALRPVLILG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1696
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1697 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylRDKVTQRHSKEQFEAAQKLEQEYsRYFTGVI 1776
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 767964245   1777 QGGALSSICTQILAMVNQEQ 1796
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1485-1547 1.05e-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: 1.05e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245 1485 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1547
Cdd:cd11860     1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 17-101 6.80e-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: 6.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    17 KAPSPPPLLTDQQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 96
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 767964245    97 HTNAL 101
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 ...
 1315-1387 1.67e-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: 101.52  E-value: 1.67e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1315 YNPHVHQLSSHSRSSSHLDPAGTHSTLQGSGTTTPEHPSVIDPLMEQDEGPSTPPAKQS--------SSRIAGDANKKTL 1386
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTtpatsphnSFRMPGDANKRVP 80


                   .
gi 767964245  1387 E 1387
Cdd:pfam16610   81 E 81
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-524 9.30e-18

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: 90.12  E-value: 9.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   226 LEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTtqvk 301
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEE---- 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   302 TAKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAANEEMEALRQIKDTVTM 374
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   375 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 454
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245   455 DTRKQKNDVSRELKELKEQMESQLEK--EARFRQLMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 524
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
PRK04778 super family cl32064
septation ring formation regulator EzrA; Provisional
 87-295 2.23e-05

septation ring formation regulator EzrA; Provisional


The actual alignment was detected with superfamily member PRK04778:

Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.06  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   87 MSDLQSLQNQHTNALK-----RCEEVAKE--------TDFYHTL------HSRLLSDQTRLKDDVDMLRRENGQLLRERN 147
Cdd:PRK04778  255 EKEIQDLKEQIDENLAlleelDLDEAEEKneeiqeriDQLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEID 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  148 LLQQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------AL 208
Cdd:PRK04778  335 RVKQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGL 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  209 RKrySEKVAihNADLSRLEQLGEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATA 276
Cdd:PRK04778  410 RK--DELEA--REKLERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATE 483

                         250       260
                  ....*....|....*....|.
gi 767964245  277 QNKDLQWEMELL--QSELTEL 295
Cdd:PRK04778  484 DVETLEEETEELveNATLTEQ 504
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 762-1191 1.88e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  762 GGPLQVCPQACPSASERSLSSFRSDASGDRGFGLVD---VRGRRPLLPFETEVGPCGVGEAsldKADSEGSNSGGTWPka 838
Cdd:PHA03307   17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAvtvVAGAAACDRFEPPTGPPPGPGT---EAPANESRSTPTWS-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  839 mlSSTAVPEKlsvykkPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGPAHSPQPSKRAGPLTPPKPPRRSDSIKFQHR--- 915
Cdd:PHA03307   92 --LSTLAPAS------PAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAava 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  916 ------------LETSSESEATLVGSSPSTSppsalpPDVDPGEPMHASPPRKARVRIASSYYPEGDGDSSHLPAKKSCD 983
Cdd:PHA03307  164 sdaassrqaalpLSSPEETARAPSSPPAEPP------PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  984 EDLTSQKVD-ELGQKRRRPKSAPSFRPKLAPVVIPAQFLEEQKCVPASGELSPELQEWAPYSPGHSSRHSNPPLYPSRPS 1062
Cdd:PHA03307  238 DSSSSESSGcGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1063 VGTVPRSLTPSTTVSSILRNPIYTVRS---HRVGPCSSPPAARDAGPQGLHPSVQHQGRLSldlshrtcsdysemRATHG 1139
Cdd:PHA03307  318 SSSSRESSSSSTSSSSESSRGAAVSPGpspSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP--------------AASAG 383

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1140 SNSLPSSARLGSSSNLQfkaeRIKIPSTPRYPRSVVGSERGSVSHSECSTPP 1191
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 ...
 503-597 2.05e-59

PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467245 [Multi-domain]  Cd Length: 95  Bit Score: 198.78  E-value: 2.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  503 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 582
Cdd:cd06764     1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                          90
                  ....*....|....*
gi 767964245  583 LLNGEGAINMVVRRR 597
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 ...
 1234-1315 2.38e-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: 2.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1234 EEPRHVKVQKGSEPLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1313
Cdd:cd06767     1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                  ..
gi 767964245 1314 QY 1315
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 ...
 1387-1467 5.19e-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: 5.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1387 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1466
Cdd:cd06766     1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                  .
gi 767964245 1467 Q 1467
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 ...
 609-685 4.12e-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: 151.73  E-value: 4.12e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  609 HINLSGQKDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 685
Cdd:cd06765     1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1620-1796 1.97e-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: 1.97e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1620 QKVDCTALRPVLILG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1696
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1697 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylRDKVTQRHSKEQFEAAQKLEQEYsRYFTGVI 1776
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 767964245   1777 QGGALSSICTQILAMVNQEQ 1796
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1485-1547 1.05e-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: 1.05e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245 1485 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1547
Cdd:cd11860     1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 17-101 6.80e-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: 6.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    17 KAPSPPPLLTDQQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 96
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 767964245    97 HTNAL 101
Cdd:pfam04822   81 ISEAL 85
dbPDZ_assoc pfam16610
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1315-1387 1.67e-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: 101.52  E-value: 1.67e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1315 YNPHVHQLSSHSRSSSHLDPAGTHSTLQGSGTTTPEHPSVIDPLMEQDEGPSTPPAKQS--------SSRIAGDANKKTL 1386
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTtpatsphnSFRMPGDANKRVP 80


                   .
gi 767964245  1387 E 1387
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 ...
 1235-1317 7.36e-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: 7.36e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1235 EPRHVKVQKGSEPLGISIVSG--EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....*
gi 767964245   1313 AQYNP 1317
Cdd:smart00228   81 VLRGG 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-524 9.30e-18

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: 90.12  E-value: 9.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   226 LEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTtqvk 301
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEE---- 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   302 TAKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAANEEMEALRQIKDTVTM 374
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   375 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 454
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245   455 DTRKQKNDVSRELKELKEQMESQLEK--EARFRQLMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 524
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
Guanylate_kin pfam00625
Guanylate kinase;
1628-1795 3.62e-16

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 78.19  E-value: 3.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1628 RPVLILGPLL---DVVKEMLVNEAPGKFCRC---------PLEVMK-----ASQQAIERGVKDCLFVDYKRRSGHFDVTT 1690
Cdd:pfam00625    3 RPVVLSGPSGvgkSHIKKALLSEYPDKFGYSvphttrpprKGEVDGkdyyfVSKEEMERDISANEFLEYAQFSGNMYGTS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1691 VASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSakhIKEQRDPIYLRDKVTQRHSKEQFEAAQKLEQEYSr 1770
Cdd:pfam00625   83 VETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPS---LKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE- 158

                          170       180
                   ....*....|....*....|....*
gi 767964245  1771 yFTGVIQGGALSSICTQILAMVNQE 1795
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 ...
 1387-1470 1.40e-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: 1.40e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1387 EPRVVFIKKSQLELGVHLCGG--NLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRL 1464
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79


                    ....*.
gi 767964245   1465 KVQYRP 1470
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 ...
 603-681 9.30e-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: 9.30e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245    603 KVVTPLHINLSGQKDSGisleNGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:smart00228    9 KGGGGLGFSLVGGKDEG----GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-502 2.21e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 72.38  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   35 ENLSIQLRLMTRERNELRKRLAFATHGTAFDkrpyhrlNPDYERLKIQcvraMSDLQslqnqhtnalKRCEEVAKETDFY 114
Cdd:PRK02224  275 EELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEAR----REELE----------DRDEELRDRLEEC 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  115 HTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILnklYDTA 194
Cdd:PRK02224  334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD---LGNA 410

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  195 MDKLEVVKKDYDALRkrysEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAiQLQHQCALSLRRfeaihHELNKA 274
Cdd:PRK02224  411 EDFLEELREERDELR----EREAELEATLRTARERVEEAEALLEAGKCPECGQPVE-GSPHVETIEEDR-----ERVEEL 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  275 TAQNKDLQWEMELLQSELTELrTTQVKTAKESEKYREERDAV---YSEYKLIMSERDQVISEL----DKLQTEVELAESK 347
Cdd:PRK02224  481 EAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELreraAELEAEAEEKREA 559

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  348 LKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILrkqckALCQELKEALQEadVAKCRRDWAF---QERDKIVAE 424
Cdd:PRK02224  560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-----AAIADAEDEIER--LREKREALAElndERRERLAEK 632

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  425 RDSIRTLCDNL--------RRERDRAVSELAEALRSLDDTRKQKND-------VSRELKELKEQMESQLEKEARFRQLma 489
Cdd:PRK02224  633 RERKRELEAEFdearieeaREDKERAEEYLEQVEEKLDELREERDDlqaeigaVENELEELEELRERREALENRVEAL-- 710

                         490
                  ....*....|...
gi 767964245  490 HSSHDSAIDTDSM 502
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 ...
 103-487 6.89e-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: 70.97  E-value: 6.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   103 RCEEVAKETDFYHTLHSRLLSDQTRLKDDVDmlrRENGQLLRERNLLQQSWEDM-KRLHE-EDQKeigdlRAQQQQVLKH 180
Cdd:pfam01576  626 RAEAEAREKETRALSLARALEEALEAKEELE---RTNKQLRAEMEDLVSSKDDVgKNVHElERSK-----RALEQQVEEM 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   181 NGSSEILNKLYDTAMD---KLEVvkkDYDALRkrysekvAIHNADLSRLEQLGEENQR-LLKQT-EMLTQ------QRDT 249
Cdd:pfam01576  698 KTQLEELEDELQATEDaklRLEV---NMQALK-------AQFERDLQARDEQGEEKRRqLVKQVrELEAElederkQRAQ 767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   250 AIQLQHQCALSLRRFEAIHHELNK----ATAQNKDLQWEMELLQSELTELRTTQ---VKTAKESEKYRE--ERDAVYSEY 320
Cdd:pfam01576  768 AVAAKKKLELDLKELEAQIDAANKgreeAVKQLKKLQAQMKDLQRELEEARASRdeiLAQSKESEKKLKnlEAELLQLQE 847

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   321 KLIMSER--DQVISELDKLQTEVELAESKlKSSTSEKKaaneemealRQIKDTVTMdagrankeveilrkqckaLCQELK 398
Cdd:pfam01576  848 DLAASERarRQAQQERDELADEIASGASG-KSALQDEK---------RRLEARIAQ------------------LEEELE 899

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   399 EALQEADVAKCRRDWAFQERDKIVAERDSIRTLC---DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK-EQM 474
Cdd:pfam01576  900 EEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSqksESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKiAQL 979

                          410
                   ....*....|...
gi 767964245   475 ESQLEKEARFRQL 487
Cdd:pfam01576  980 EEQLEQESRERQA 992
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 136-473 1.66e-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: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  136 RRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngsseilnklydtamdKLEVVKKDYDALRKRYSEK 215
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-----------------ELEELRLELEELELELEEA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  216 VAIHNADLSRLEQLGEENQRllkQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTEL 295
Cdd:COG1196   287 QAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  296 RTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMD 375
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  376 AGRANKEVEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIvaerdsirtlcDNLRRERDRAVSELaEALRSLDD 455
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAA----------LLEAAL-----------AELLEELAEAAARL-LLLLEAEA 501

                         330
                  ....*....|....*...
gi 767964245  456 TRKQKNDVSRELKELKEQ 473
Cdd:COG1196   502 DYEGFLEGVKAALLLAGL 519
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1244-1314 1.61e-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: 1.61e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  1244 GSEPLGISIVSGEKG---GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1314
Cdd:pfam00595    8 GRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1482-1544 2.74e-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: 2.74e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245   1482 DSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWMAWQLDENaqkiQRGQIPSKYV 1544
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 ...
 505-598 3.31e-09

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 55.46  E-value: 3.31e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    505 ETEVVEFERETEDidlkaLGFDMAEGVNEpcfpgDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 583
Cdd:smart00228    1 EPRLVELEKGGGG-----LGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                            90
                    ....*....|....*
gi 767964245    584 LNGEGAINMVVRRRK 598
Cdd:smart00228   71 KKAGGKVTLTVLRGG 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-403 7.05e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   28 QQVNEKVENLSIQLRLMTRERNELRKRLAfathgtafDKRPYHRLnpdYERLK--------IQCVRAMSDLQSLQNQHTN 99
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKELEKRLE--------ELEERHEL---YEEAKakkeelerLKKRLTGLTPEKLEKELEE 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  100 ALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRREN------GQLLRE---RNLLQQSWEDMKRLhEEDQKEIG-- 168
Cdd:PRK03918  396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEehrKELLEEYTAELKRI-EKELKEIEek 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  169 --DLRAQQQQVLKHNGSSEILNKLYDTA--------------MDKLEVVKKDYDALRKRYSE---KVAIHNADLSRLEQL 229
Cdd:PRK03918  475 erKLRKELRELEKVLKKESELIKLKELAeqlkeleeklkkynLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEEL 554

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  230 GEENQRLLKQ--------TEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQW---EMELLQSELTELRTT 298
Cdd:PRK03918  555 KKKLAELEKKldeleeelAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEReekELKKLEEELDKAFEE 634

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  299 QVKTAKESEKYREERDAV---YS--EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 373
Cdd:PRK03918  635 LAETEKRLEELRKELEELekkYSeeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714

                         410       420       430
                  ....*....|....*....|....*....|.
gi 767964245  374 mDAGRANKEVEILRKQCKALCQELKE-ALQE 403
Cdd:PRK03918  715 -KLEKALERVEELREKVKKYKALLKErALSK 744
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-373 8.85e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 8.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    10 HPGGTTGKAPSPPPLLTDQQVNEkVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPYHRLNPDYERLKIQCVRAMSD 89
Cdd:TIGR02168  656 RPGGVITGGSAKTNSSILERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    90 LQSLQNQHTNALKRCEEVAKETdfyhtlhSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGD 169
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKEL-------TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   170 LRAQQQQvlkhngsseiLNKLYDTAMDKLEVVKKDYDALRKRY----------SEKVAIHNADLSRLEQLGEEnqrLLKQ 239
Cdd:TIGR02168  808 LRAELTL----------LNEEAANLRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEE---LESE 874

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   240 TEMLTQQRDtaiQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRT----TQVKTAKESEKYREErda 315
Cdd:TIGR02168  875 LEALLNERA---SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELrlegLEVRIDNLQERLSEE--- 948

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245   316 vYS-EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 373
Cdd:TIGR02168  949 -YSlTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 607-681 4.94e-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: 4.94e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245   607 PLHINLSGQKDSGIsleNGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:pfam00595   11 GLGFSLKGGSDQGD---PGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 305-489 4.54e-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: 4.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  305 ESEKYREERDAVySEYKLIMSERDQVISELDKLQTEV-----ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRA 379
Cdd:cd07596     2 EDQEFEEAKDYI-LKLEEQLKKLSKQAQRLVKRRRELgsalgEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  380 NKEVeilRKQCKALCQELKEALQEADVAKCrrdwAFQERDKIVAERDSIRTLCDNLRRERDRAVS-------ELAEALRS 452
Cdd:cd07596    81 EAQA---NQELVKLLEPLKEYLRYCQAVKE----TLDDRADALLTLQSLKKDLASKKAQLEKLKAapgikpaKVEELEEE 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767964245  453 LDDTRKQKNDVSRELKELKEQMESQLE--KEARFRQLMA 489
Cdd:cd07596   154 LEEAESALEEARKRYEEISERLKEELKrfHEERARDLKA 192
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 600-670 4.82e-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: 4.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245  600 LGGKVVTPLHINLSGQKDS-GISL---ENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 670
Cdd:COG0793    43 LDPEEYEDFQESTSGEFGGlGAELgeeDGKVVVVSVIPGSPAEKAG-IKPGDIILAIDGKSVAGLTLDDAVKLLR 116
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1389-1467 6.08e-06

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 45.73  E-value: 6.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1389 RVVFIKKSQLELGVHLCGGN---LHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLK 1465
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79


                   ..
gi 767964245  1466 VQ 1467
Cdd:pfam00595   80 IL 81
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 87-295 2.23e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.06  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   87 MSDLQSLQNQHTNALK-----RCEEVAKE--------TDFYHTL------HSRLLSDQTRLKDDVDMLRRENGQLLRERN 147
Cdd:PRK04778  255 EKEIQDLKEQIDENLAlleelDLDEAEEKneeiqeriDQLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEID 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  148 LLQQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------AL 208
Cdd:PRK04778  335 RVKQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGL 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  209 RKrySEKVAihNADLSRLEQLGEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATA 276
Cdd:PRK04778  410 RK--DELEA--REKLERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATE 483

                         250       260
                  ....*....|....*....|.
gi 767964245  277 QNKDLQWEMELL--QSELTEL 295
Cdd:PRK04778  484 DVETLEEETEELveNATLTEQ 504
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 40-364 3.50e-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: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   40 QLRLMTRERNELRKRLAFAthgtAFDKRPYHRL----------------NPDYERLKIQCVRAMSDLQSLQNQHTNALKR 103
Cdd:COG3096   786 RLEELRAERDELAEQYAKA----SFDVQKLQRLhqafsqfvgghlavafAPDPEAELAALRQRRSELERELAQHRAQEQQ 861

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  104 CEEVAKETDFYHTLHSRLLSDQTRLKDD-----VDMLRRENGQLLRERNLLQQSWEDMKRLheEDQKEIgdLRAQQQQVl 178
Cdd:COG3096   862 LRQQLDQLKEQLQLLNKLLPQANLLADEtladrLEELREELDAAQEAQAFIQQHGKALAQL--EPLVAV--LQSDPEQF- 936

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  179 khngssEILNKLYDTAMDKLEVVKKDYDAL---RKR-----YSEKVAIHNADLSRLEQLgeeNQRLLKQTEMLTQQRDTA 250
Cdd:COG3096   937 ------EQLQADYLQAKEQQRRLKQQIFALsevVQRrphfsYEDAVGLLGENSDLNEKL---RARLEQAEEARREAREQL 1007

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  251 IQLQHQCALSLRRFEAIhhelnKATAQNKdlqweMELLQSELTELRTTQVKTAKESE-KYREERDAVYSEYKLIMSERDQ 329
Cdd:COG3096  1008 RQAQAQYSQYNQVLASL-----KSSRDAK-----QQTLQELEQELEELGVQADAEAEeRARIRRDELHEELSQNRSRRSQ 1077

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 767964245  330 VISELDKLQTEVELAESKLKSSTSEKKAANEEMEA 364
Cdd:COG3096  1078 LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 523-595 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 767964245   523 LGFDMAEGVNEpcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 595
Cdd:pfam00595   12 LGFSLKGGSDQ----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 71-373 2.72e-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: 45.78  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    71 RLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQL-------L 143
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeqikklQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   144 RERNLLQQSWEDMKRLHEEDQKEIGDLRAQ----QQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVaih 219
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE--- 495

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   220 nadlSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcaLSLR------------------------------------R 263
Cdd:TIGR04523  496 ----KELKKLNEEKKELEEKVKDLTKKISSLKEKIEK--LESEkkekeskisdledelnkddfelkkenlekeideknkE 569

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   264 FEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVEL 343
Cdd:TIGR04523  570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649

                          330       340       350
                   ....*....|....*....|....*....|
gi 767964245   344 AESKLksstseKKAANEEMEALRQIKDTVT 373
Cdd:TIGR04523  650 IKETI------KEIRNKWPEIIKKIKESKT 673
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
1248-1313 5.16e-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: 5.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1248 LGISiVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSAT--EQQARLIIGqqcDTITILA 1313
Cdd:COG3975   485 LGLR-VSADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTADNldDALAAYKPG---DPIELLV 548
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1410-1466 6.03e-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: 6.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1410 HGVFVAEVEDDSPA-KGpdGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1466
Cdd:COG0265   201 EGVLVARVEPGSPAaKA--GLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTV 256
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 762-1191 1.88e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  762 GGPLQVCPQACPSASERSLSSFRSDASGDRGFGLVD---VRGRRPLLPFETEVGPCGVGEAsldKADSEGSNSGGTWPka 838
Cdd:PHA03307   17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAvtvVAGAAACDRFEPPTGPPPGPGT---EAPANESRSTPTWS-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  839 mlSSTAVPEKlsvykkPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGPAHSPQPSKRAGPLTPPKPPRRSDSIKFQHR--- 915
Cdd:PHA03307   92 --LSTLAPAS------PAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAava 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  916 ------------LETSSESEATLVGSSPSTSppsalpPDVDPGEPMHASPPRKARVRIASSYYPEGDGDSSHLPAKKSCD 983
Cdd:PHA03307  164 sdaassrqaalpLSSPEETARAPSSPPAEPP------PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  984 EDLTSQKVD-ELGQKRRRPKSAPSFRPKLAPVVIPAQFLEEQKCVPASGELSPELQEWAPYSPGHSSRHSNPPLYPSRPS 1062
Cdd:PHA03307  238 DSSSSESSGcGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1063 VGTVPRSLTPSTTVSSILRNPIYTVRS---HRVGPCSSPPAARDAGPQGLHPSVQHQGRLSldlshrtcsdysemRATHG 1139
Cdd:PHA03307  318 SSSSRESSSSSTSSSSESSRGAAVSPGpspSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP--------------AASAG 383

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1140 SNSLPSSARLGSSSNLQfkaeRIKIPSTPRYPRSVVGSERGSVSHSECSTPP 1191
Cdd:PHA03307  384 RPTRRRARAAVAGRARR----RDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 126-311 2.28e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 41.04  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   126 TRLKDDVDMLRRENGQLLRERNLLQQswedMKRLHEEDQKEIGDLRAQQQQVL-KHNGSSEILNKLYDTAMDKLEVVKKd 204
Cdd:pfam15619   14 KELQNELAELQSKLEELRKENRLLKR----LQKRQEKALGKYEGTESELPQLIaRHNEEVRVLRERLRRLQEKERDLER- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   205 ydALRKRYSEkvaIH--NADLSRLEQLG--------EENQRLLKQTEMLTQQRDTAIQ-LQHQCALSLRRFeaiHHELNK 273
Cdd:pfam15619   89 --KLKEKEAE---LLrlRDQLKRLEKLSedknlaerEELQKKLEQLEAKLEDKDEKIQdLERKLELENKSF---RRQLAA 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 767964245   274 ATAQNKDLQWEMELLQSELTELRTtqvktaKESEKYRE 311
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 ...
 503-597 2.05e-59

PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467245 [Multi-domain]  Cd Length: 95  Bit Score: 198.78  E-value: 2.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  503 EWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKA 582
Cdd:cd06764     1 EWETETVEFEKVRDDMDLKALGFDIAGGVNDPQFPGDCSIFVTKVDKGSIADGRLRVNDCLLRINDVDLTNKDKKQAIQA 80

                          90
                  ....*....|....*
gi 767964245  583 LLNGEGAINMVVRRR 597
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 ...
 1234-1315 2.38e-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: 2.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1234 EEPRHVKVQKGSEPLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1313
Cdd:cd06767     1 EEPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                  ..
gi 767964245 1314 QY 1315
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 ...
 1387-1467 5.19e-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: 5.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1387 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1466
Cdd:cd06766     1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPDGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                  .
gi 767964245 1467 Q 1467
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 ...
 609-685 4.12e-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: 151.73  E-value: 4.12e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  609 HINLSGQKDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFP 685
Cdd:cd06765     1 HINLSGQKDSGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLMKVFP 77
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 1620-1796 1.97e-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: 1.97e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1620 QKVDCTALRPVLILG---PLLDVVKEMLVNEAPGKFCRcpLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKE 1696
Cdd:smart00072    1 SGVGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNG--VDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQ 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1697 ITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSAKHIKEQRDPiylRDKVTQRHSKEQFEAAQKLEQEYsRYFTGVI 1776
Cdd:smart00072   79 VAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQ---RGTETSERIQKRLAAAQKEAQEY-HLFDYVI 154

                           170       180
                    ....*....|....*....|
gi 767964245   1777 QGGALSSICTQILAMVNQEQ 1796
Cdd:smart00072  155 VNDDLEDAYEELKEILEAEQ 174
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
 1485-1547 1.05e-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: 1.05e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245 1485 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSKYVMDQ 1547
Cdd:cd11860     1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
Takusan pfam04822
Takusan; This domain is named takusan, which is a Japanese word meaning 'many'. Members of ...
 17-101 6.80e-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: 6.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    17 KAPSPPPLLTDQQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDkRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ 96
Cdd:pfam04822    2 ASSSPPTILSKEQRKKELERLKFELQLITNERNELRDILALYTEGDLND-RPYHRLNPEYEILKLQHEKVMSDLQKLENE 80


                   ....*
gi 767964245    97 HTNAL 101
Cdd:pfam04822   81 ISEAL 85
dbPDZ_assoc pfam16610
Unstructured region between two PDZ domains on Dlg5; dbPDZ_assoc is found on higher eukaryote ...
 1315-1387 1.67e-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: 101.52  E-value: 1.67e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1315 YNPHVHQLSSHSRSSSHLDPAGTHSTLQGSGTTTPEHPSVIDPLMEQDEGPSTPPAKQS--------SSRIAGDANKKTL 1386
Cdd:pfam16610    1 YNPHMYQLGNHSRSSSRLEPVSNHSTPQGSGATTPDNHSTIDTLSEQDEGTMTPPSKQTtpatsphnSFRMPGDANKRVP 80


                   .
gi 767964245  1387 E 1387
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 ...
 1235-1317 7.36e-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: 7.36e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1235 EPRHVKVQKGSEPLGISIVSG--EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80


                    ....*
gi 767964245   1313 AQYNP 1317
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) ...
 1235-1317 1.14e-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: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1235 EPRHVKVQKGSEPLGISIVSGEKG-GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
Cdd:cd06795     1 EPRKIVLHKGSTGLGFNIVGGEDGeGIFISFILAGGPADLSGeLRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTII 80


                  ....*
gi 767964245 1313 AQYNP 1317
Cdd:cd06795    81 AQYKP 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-524 9.30e-18

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: 90.12  E-value: 9.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   226 LEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH----HELNKATAQNKDLQWEMELLQSELTELRTtqvk 301
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleERIAQLSKELTELEAEIEELEERLEEAEE---- 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   302 TAKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVEL-------AESKLKSSTSEKKAANEEMEALRQIKDTVTM 374
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   375 DAGRANKEVEILRKQCKALCQELKEALqeadvakcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 454
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL--------------NERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245   455 DTRKQKNDVSRELKELKEQMESQLEK--EARFRQLMAHSSHDSAIDTDSMEWETEVVEFEREtedidLKALG 524
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-----IKELG 985
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1238-1312 7.58e-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: 7.58e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1238 HVKVQKGS-EPLGISIVSGE--KGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
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 ...
 1235-1314 1.83e-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: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1235 EPRHVKVQKGSEPLGISIVSGEKGGIYVSKVTVGSIAHQA-GLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1313
Cdd:cd06766     1 EPRLVFLKKSQVELGIQLCGGNLHGIFVEDVEDDSPAKGPdGLVPGDLILEYNSVDMRNKTAEEAYLEMLKPAETVTLKV 80


                  .
gi 767964245 1314 Q 1314
Cdd:cd06766    81 Q 81
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 590-678 2.69e-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: 2.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  590 INMVVRRRKSLGgkvvtplhINLSGQKDSGIslenGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL 669
Cdd:cd00136     2 VTLEKDPGGGLG--------FSIRGGKDGGG----GIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELL 69


                  ....*....
gi 767964245  670 RSCQDSLTL 678
Cdd:cd00136    70 KSAGGEVTL 78
Guanylate_kin pfam00625
Guanylate kinase;
1628-1795 3.62e-16

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 78.19  E-value: 3.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1628 RPVLILGPLL---DVVKEMLVNEAPGKFCRC---------PLEVMK-----ASQQAIERGVKDCLFVDYKRRSGHFDVTT 1690
Cdd:pfam00625    3 RPVVLSGPSGvgkSHIKKALLSEYPDKFGYSvphttrpprKGEVDGkdyyfVSKEEMERDISANEFLEYAQFSGNMYGTS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1691 VASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIHYKSakhIKEQRDPIYLRDKVTQRHSKEQFEAAQKLEQEYSr 1770
Cdd:pfam00625   83 VETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPS---LKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHYE- 158

                          170       180
                   ....*....|....*....|....*
gi 767964245  1771 yFTGVIQGGALSSICTQILAMVNQE 1795
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) ...
 516-597 8.36e-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: 8.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  516 EDIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGA 589
Cdd:cd06723     2 EEITLergnSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAaaDGRLRVNDIILRVNDVDVRNVTHSVAVEALKEAGSI 81


                  ....*...
gi 767964245  590 INMVVRRR 597
Cdd:cd06723    82 VRLYVKRR 89
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 508-595 6.77e-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: 6.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  508 VVEFERETEdidlKALGFDMAEGVNepcfpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 585
Cdd:cd00136     1 TVTLEKDPG----GGLGFSIRGGKD-----GGGGIFVSRVEPGGPAarDGRLRVGDRILEVNGVSLEGLTHEEAVELLKS 71

                          90
                  ....*....|
gi 767964245  586 GEGAINMVVR 595
Cdd:cd00136    72 AGGEVTLTVR 81
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1244-1311 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 767964245 1244 GSEPLGISIVSG--EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITI 1311
Cdd:cd06738    11 GTRGLGCSISSGptQKPGIFISNVKPGSLAEEVGLEVGDQIVEVNGTSFTNVDHKEAVMAL-KSSRHLTI 79
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 185-486 1.67e-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: 1.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   185 EILNKLYDTA--MDKLEVV----KKDYDALRK------RYSE-KVAIHNADLS----RLEQLGEENQRLLKQTEMLTQQR 247
Cdd:TIGR02168  176 ETERKLERTRenLDRLEDIlnelERQLKSLERqaekaeRYKElKAELRELELAllvlRLEELREELEELQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   248 DTAIQLQHQCALSLRRFEAIHHELNKataqnkdlqwEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSER 327
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEE----------EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   328 DQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKdtvtmdagrankeveilrkqckalcQELKEALQEADV- 406
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL-------------------------EELESRLEELEEq 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   407 ---AKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDdtRKQKNDVSRELKELKEQMESQLEKEAR 483
Cdd:TIGR02168  381 letLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELER 458


                   ...
gi 767964245   484 FRQ 486
Cdd:TIGR02168  459 LEE 461
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 119-483 4.55e-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: 4.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   119 SRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMK-RLHE------EDQKEIGDLRAQQQQVLK-HNGSSEILNKL 190
Cdd:TIGR02169  663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEnRLDElsqelsDASRKIGEIEKEIEQLEQeEEKLKERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   191 yDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLE-QLGEENQRLLKQTEMLTQQRDTAIQLQHQcalSLR-RFEAIH 268
Cdd:TIGR02169  743 -EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEeALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEaRLREIE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   269 HELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKL 348
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   349 KSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKcrrdwafqERDKIVAErdsI 428
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA--------ELQRVEEE---I 967

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245   429 RTLCD-NLrrerdRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEAR 483
Cdd:TIGR02169  968 RALEPvNM-----LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE-EYEKKKR 1017
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 136-485 8.76e-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: 77.02  E-value: 8.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   136 RRENGQLLRERNL--LQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDALRKRyS 213
Cdd:TIGR02168  667 KTNSSILERRREIeeLEEKIEELEEKIAELEKALAELRKELEELEE---ELEQLRKELEELSRQISALRKDLARLEAE-V 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   214 EKVAihnadlSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAihhELNKATAQNKDLQWEMELLQSELT 293
Cdd:TIGR02168  743 EQLE------ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA---QIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   294 ELRTTQvkTAKESEKYREERDAVYSEYKLIMSE------RDQVIS---ELDKLQTEVELAESKLKSSTSEKKAANEEMEA 364
Cdd:TIGR02168  814 LLNEEA--ANLRERLESLERRIAATERRLEDLEeqieelSEDIESlaaEIEELEELIEELESELEALLNERASLEEALAL 891

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   365 LRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDwAFQER----------------DKIVAERDSI 428
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-NLQERlseeysltleeaealeNKIEDDEEEA 970

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245   429 RTLCDNLRRERDR-------AVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEARFR 485
Cdd:TIGR02168  971 RRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE-EIDREARER 1033
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
 1485-1542 9.65e-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: 9.65e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1485 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSK 1542
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 ...
 1387-1470 1.40e-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: 1.40e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   1387 EPRVVFIKKSQLELGVHLCGG--NLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRL 1464
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGGkdEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTL 79


                    ....*.
gi 767964245   1465 KVQYRP 1470
Cdd:smart00228   80 TVLRGG 85
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 128-475 1.82e-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: 1.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   128 LKDDVDMLRRENGQLLRERNLLqqswedmKRLHEEDQ----KEIGDLRAQQQQVLKhngssEIlnklyDTAMDKLEVVKK 203
Cdd:TIGR02169  196 KRQQLERLRREREKAERYQALL-------KEKREYEGyellKEKEALERQKEAIER-----QL-----ASLEEELEKLTE 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   204 DYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLkQTEMLtqqrdtaiQLQHQCALSLRRFEAIHHELNKATAQNKDLQW 283
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIG--------ELEAEIASLERSIAEKERELEDAEERLAKLEA 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   284 EMELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEME 363
Cdd:TIGR02169  330 EIDKLLAEIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   364 ALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAV 443
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482

                          330       340       350
                   ....*....|....*....|....*....|..
gi 767964245   444 SELAEALRSLDDTRKQKNDVSRELKELKEQME 475
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARASEERVRGGRAVEE 514
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 603-681 9.30e-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: 9.30e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245    603 KVVTPLHINLSGQKDSGisleNGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:smart00228    9 KGGGGLGFSLVGGKDEG----GGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 71-438 1.07e-12

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 73.56  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    71 RLNPDYERLKIQCVRAMSDLQSLQNqHTNALKRCEEVAKETdfyhtlHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQ 150
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIEN-RLDELSQELSDASRK------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   151 QSWEDMKRLHEEDQKEIGDLRAQQQQVlkhngsSEILNKLYDT-AMDKLEVVKKDYDALRKRYSEKVAIhnadLSRLEQl 229
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEEDLHKL------EEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEAR----LREIEQ- 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   230 gEENQRLLKQtEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNkatAQNKDLQWEMELLQSELTELRTTQVKTAKEseky 309
Cdd:TIGR02169  820 -KLNRLTLEK-EYLEKEIQELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEAALRDLESRLGDLKKE---- 890

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   310 REERDAVYSEYKlimserdqviSELDKLQTEVELAESKLKSSTSEKKAANEEmeaLRQIKDTVTMDAGRANKE--VEILR 387
Cdd:TIGR02169  891 RDELEAQLRELE----------RKIEELEAQIEKKRKRLSELKAKLEALEEE---LSEIEDPKGEDEEIPEEElsLEDVQ 957

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245   388 KQCKALCQELKE-------ALQEADVAKCRRDWAFQERDKIVAERDSIRTL---CDNLRRE 438
Cdd:TIGR02169  958 AELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERieeYEKKKRE 1018
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 517-585 1.45e-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: 1.45e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245  517 DIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 585
Cdd:cd06724     1 EIKLvkgpKGLGFSIAGGVGNQHIPGDNGIYVTKIIEGGAAqkDGRLQVGDKLLAVNDVSLEEVTHEEAVAALKN 75
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-502 2.21e-12

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 72.38  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   35 ENLSIQLRLMTRERNELRKRLAFATHGTAFDkrpyhrlNPDYERLKIQcvraMSDLQslqnqhtnalKRCEEVAKETDFY 114
Cdd:PRK02224  275 EELAEEVRDLRERLEELEEERDDLLAEAGLD-------DADAEAVEAR----REELE----------DRDEELRDRLEEC 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  115 HTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILnklYDTA 194
Cdd:PRK02224  334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD---LGNA 410

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  195 MDKLEVVKKDYDALRkrysEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAiQLQHQCALSLRRfeaihHELNKA 274
Cdd:PRK02224  411 EDFLEELREERDELR----EREAELEATLRTARERVEEAEALLEAGKCPECGQPVE-GSPHVETIEEDR-----ERVEEL 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  275 TAQNKDLQWEMELLQSELTELrTTQVKTAKESEKYREERDAV---YSEYKLIMSERDQVISEL----DKLQTEVELAESK 347
Cdd:PRK02224  481 EAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLeelIAERRETIEEKRERAEELreraAELEAEAEEKREA 559

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  348 LKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILrkqckALCQELKEALQEadVAKCRRDWAF---QERDKIVAE 424
Cdd:PRK02224  560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL-----AAIADAEDEIER--LREKREALAElndERRERLAEK 632

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  425 RDSIRTLCDNL--------RRERDRAVSELAEALRSLDDTRKQKND-------VSRELKELKEQMESQLEKEARFRQLma 489
Cdd:PRK02224  633 RERKRELEAEFdearieeaREDKERAEEYLEQVEEKLDELREERDDlqaeigaVENELEELEELRERREALENRVEAL-- 710

                         490
                  ....*....|...
gi 767964245  490 HSSHDSAIDTDSM 502
Cdd:PRK02224  711 EALYDEAEELESM 723
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 631-678 3.85e-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: 3.85e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767964245  631 VLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
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 ...
 103-487 6.89e-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: 70.97  E-value: 6.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   103 RCEEVAKETDFYHTLHSRLLSDQTRLKDDVDmlrRENGQLLRERNLLQQSWEDM-KRLHE-EDQKeigdlRAQQQQVLKH 180
Cdd:pfam01576  626 RAEAEAREKETRALSLARALEEALEAKEELE---RTNKQLRAEMEDLVSSKDDVgKNVHElERSK-----RALEQQVEEM 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   181 NGSSEILNKLYDTAMD---KLEVvkkDYDALRkrysekvAIHNADLSRLEQLGEENQR-LLKQT-EMLTQ------QRDT 249
Cdd:pfam01576  698 KTQLEELEDELQATEDaklRLEV---NMQALK-------AQFERDLQARDEQGEEKRRqLVKQVrELEAElederkQRAQ 767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   250 AIQLQHQCALSLRRFEAIHHELNK----ATAQNKDLQWEMELLQSELTELRTTQ---VKTAKESEKYRE--ERDAVYSEY 320
Cdd:pfam01576  768 AVAAKKKLELDLKELEAQIDAANKgreeAVKQLKKLQAQMKDLQRELEEARASRdeiLAQSKESEKKLKnlEAELLQLQE 847

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   321 KLIMSER--DQVISELDKLQTEVELAESKlKSSTSEKKaaneemealRQIKDTVTMdagrankeveilrkqckaLCQELK 398
Cdd:pfam01576  848 DLAASERarRQAQQERDELADEIASGASG-KSALQDEK---------RRLEARIAQ------------------LEEELE 899

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   399 EALQEADVAKCRRDWAFQERDKIVAERDSIRTLC---DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK-EQM 474
Cdd:pfam01576  900 EEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSqksESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKiAQL 979

                          410
                   ....*....|...
gi 767964245   475 ESQLEKEARFRQL 487
Cdd:pfam01576  980 EEQLEQESRERQA 992
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1239-1314 7.01e-12

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


Pssm-ID: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 63.04  E-value: 7.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1239 VKVQKGSEPLGISIVSG----------EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1308
Cdd:cd06702     3 IHLVKAGGPLGLSIVGGsdhsshpfgvDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPGQE 82


                  ....*.
gi 767964245 1309 ITILAQ 1314
Cdd:cd06702    83 IKLLVR 88
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 85-429 8.39e-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: 70.53  E-value: 8.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    85 RAMSDLQ-SLQNQHTNALKRCEEVAKetdfyhtLHSRL---LSDQTRLKDDVDMLRRENGQL------LRERN----LLQ 150
Cdd:pfam15921  496 RTVSDLTaSLQEKERAIEATNAEITK-------LRSRVdlkLQELQHLKNEGDHLRNVQTECealklqMAEKDkvieILR 568

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   151 QSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngssEILNKLYDtaMDKLEVVKKDYDA----LRKRYS----EKVAIHNAD 222
Cdd:pfam15921  569 QQIENMTQLVGQHGRTAGAMQVEKAQLEK-----EINDRRLE--LQEFKILKDKKDAkireLEARVSdlelEKVKLVNAG 641

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   223 LSRL---EQLGEENQRLLKQTEmltQQRDTAIQLQHQCALSLRRFEAIHHELNKATaqNKdLQWEMELLQSELTELRTTq 299
Cdd:pfam15921  642 SERLravKDIKQERDQLLNEVK---TSRNELNSLSEDYEVLKRNFRNKSEEMETTT--NK-LKMQLKSAQSELEQTRNT- 714

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   300 VKTAKESEKYREErdAVYSEYKLIMSERDQViselDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRA 379
Cdd:pfam15921  715 LKSMEGSDGHAMK--VAMGMQKQITAKRGQI----DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM 788

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767964245   380 NKEVEILRKQCKalcqELKEALQEADVAKCRRDWAFQERDKIV--AERDSIR 429
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 ...
 608-680 1.23e-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: 1.23e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245  608 LHINLSGQKDSGISLeNGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 680
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 ...
 1235-1315 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 767964245 1235 EPRHVKVQKGSEpLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIG--QQCDTITIL 1312
Cdd:cd06729     1 DTRLVSFRKGGS-VGLRLAGGNDVGIFVAGVQEGSPAEKQGLQEGDQILKVNGVDFRNLTREEAVLFLLdlPKGEEVTIL 79


                  ...
gi 767964245 1313 AQY 1315
Cdd:cd06729    80 AQS 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 136-473 1.66e-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: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  136 RRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngsseilnklydtamdKLEVVKKDYDALRKRYSEK 215
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-----------------ELEELRLELEELELELEEA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  216 VAIHNADLSRLEQLGEENQRllkQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTEL 295
Cdd:COG1196   287 QAEEYELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  296 RTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMD 375
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  376 AGRANKEVEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIvaerdsirtlcDNLRRERDRAVSELaEALRSLDD 455
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAA----------LLEAAL-----------AELLEELAEAAARL-LLLLEAEA 501

                         330
                  ....*....|....*...
gi 767964245  456 TRKQKNDVSRELKELKEQ 473
Cdd:COG1196   502 DYEGFLEGVKAALLLAGL 519
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 205-522 3.35e-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: 68.56  E-value: 3.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   205 YDALRKRYSEKVAihnaDLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSL-----------RRFEAIHHELNK 273
Cdd:TIGR02169  659 SRAPRGGILFSRS----EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdasrkigeieKEIEQLEQEEEK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   274 ATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREE----RDAVYS-EYKLIMSERDQVISELDKLQTEV------- 341
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDlhklEEALNDlEARLSHSRIPEIQAELSKLEEEVsriearl 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   342 ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEalqeadvakcrrdwafqerdKI 421
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE--------------------LE 874

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   422 VAERDSIRTLCDnLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDS 501
Cdd:TIGR02169  875 AALRDLESRLGD-LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL 953

                          330       340
                   ....*....|....*....|....
gi 767964245   502 MEWETEVVEFERET---EDIDLKA 522
Cdd:TIGR02169  954 EDVQAELQRVEEEIralEPVNMLA 977
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 1389-1467 4.57e-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: 4.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1389 RVVFIKKSQLELGVHLCGGNLH--GVFVAEVEDDSPAKgPDG-LVPGDLILEYGSLDVRNKTVEEVyVEMLK-PRDGVRL 1464
Cdd:cd00136     1 TVTLEKDPGGGLGFSIRGGKDGggGIFVSRVEPGGPAA-RDGrLRVGDRILEVNGVSLEGLTHEEA-VELLKsAGGEVTL 78


                  ...
gi 767964245 1465 KVQ 1467
Cdd:cd00136    79 TVR 81
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 90-507 8.35e-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: 66.46  E-value: 8.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    90 LQSLQNQHTNALKRCE----EVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQK 165
Cdd:pfam07888   36 LEECLQERAELLQAQEaanrQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   166 EIGDLRAQQ----QQVLKHNGSSEILNK---LYDTAMDKL-EVVKKDYDALRKRYSEKVAIHnadlSRLEQLGEENQRLL 237
Cdd:pfam07888  116 EKDALLAQRaaheARIRELEEDIKTLTQrvlERETELERMkERAKKAGAQRKEEEAERKQLQ----AKLQQTEEELRSLS 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   238 KQTEMLTQ---QRDT-AIQLQHQCAlslrrfeAIHHELNkaTAQNKDLqwEMELLQSELTELRTTQVKTAKESEKYREER 313
Cdd:pfam07888  192 KEFQELRNslaQRDTqVLQLQDTIT-------TLTQKLT--TAHRKEA--ENEALLEELRSLQERLNASERKVEGLGEEL 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   314 DAVyseykliMSERDQVISELDKL-----QTEVELAESKLKssTSEKKAA-NEEMEALRQikdtvtmdagRANKEVEILR 387
Cdd:pfam07888  261 SSM-------AAQRDRTQAELHQArlqaaQLTLQLADASLA--LREGRARwAQERETLQQ----------SAEADKDRIE 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   388 KQCKALcQELKEALQEADVakcrrdwafqERDKIVAE----RDSIRTLCDNLRRErdraVSELAEALRSLDDTRKQKNDV 463
Cdd:pfam07888  322 KLSAEL-QRLEERLQEERM----------EREKLEVElgreKDCNRVQLSESRRE----LQELKASLRVAQKEKEQLQAE 386

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 767964245   464 SRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWETE 507
Cdd:pfam07888  387 KQELLEYIRQLEQRLETVADAKWSEAALTSTERPDSPLSDSEDE 430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 194-521 9.87e-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: 67.02  E-value: 9.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   194 AMDKLEVVKKDYDALRKRYSEKvaihnadLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQhqcalsLRRFEAIHHELNK 273
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEK-------RQQLERLRREREKAERYQALLKEKREYEGYEL------LKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   274 ATAQNKDLQWEMELLQSELTELrttqvktAKESEKYREERDAVYSEYKLIMSERD-QVISELDKLQTEVELAESKLKsst 352
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISEL-------EKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIA--- 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   353 sekkaaneemEALRQIKDtvtMDAGRANKEVEILRKQCKAlcQELKEALQEADVakcrrdwafqERDKIVAERDSIRTLC 432
Cdd:TIGR02169  312 ----------EKERELED---AEERLAKLEAEIDKLLAEI--EELEREIEEERK----------RRDKLTEEYAELKEEL 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   433 DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHsshdsaIDTDSMEWETEVVEFE 512
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD------LNAAIAGIEAKINELE 440


                   ....*....
gi 767964245   513 RETEDIDLK 521
Cdd:TIGR02169  441 EEKEDKALE 449
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 24-500 1.09e-10

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 66.67  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    24 LLTDQQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKR 103
Cdd:pfam05483  246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   104 CEEVAKE-------------------TDFYHT---LHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQ---------- 151
Cdd:pfam05483  326 ICQLTEEkeaqmeelnkakaahsfvvTEFEATtcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtkfknnkev 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   152 SWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDT---AMDKLEVVKKDYDALRKRYSEKVA-----IHNADL 223
Cdd:pfam05483  406 ELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArekEIHDLEIQLTAIKTSEEHYLKEVEdlkteLEKEKL 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   224 SRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcalslrrfeaiHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTA 303
Cdd:pfam05483  486 KNIELTAHCDKLLLENKELTQEASDMTLELKKH-----------QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   304 KESEKYREE---------RDAVYSEYKLIMSERDQVISEL--DKLQTEVE---------LAESKL--KSSTSEKKAANE- 360
Cdd:pfam05483  555 EEFIQKGDEvkckldkseENARSIEYEVLKKEKQMKILENkcNNLKKQIEnknknieelHQENKAlkKKGSAENKQLNAy 634

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   361 ---------EMEALRQIKDTVTmdaGRANKEVEILRKQCKALCQELKEALQEADVA---------KCRRDWA----FQER 418
Cdd:pfam05483  635 eikvnklelELASAKQKFEEII---DNYQKEIEDKKISEEKLLEEVEKAKAIADEAvklqkeidkRCQHKIAemvaLMEK 711

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   419 -----DKIVAERDSIRTLCDNLRRERDRAVSELAEALrslddtrkqkNDVSRELKELKEQMEsqLEKEARfRQLMAHSSH 493
Cdd:pfam05483  712 hkhqyDKIIEERDSELGLYKNKEQEQSSAKAALEIEL----------SNIKAELLSLKKQLE--IEKEEK-EKLKMEAKE 778


                   ....*..
gi 767964245   494 DSAIDTD 500
Cdd:pfam05483  779 NTAILKD 785
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 516-585 1.11e-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: 1.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  516 EDIDLK----ALGFDMAEGVNEPCFPGDCGIFVTKV-DKGSIA-DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 585
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 ...
 617-682 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 767964245  617 DSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 682
Cdd:cd06728    13 EYGLRLGSRIFVKEITPDSLAAKDGNLQEGDIILKINGTPVENLSLSEAKKLIEKSKDKLQLVVLR 78
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 615-670 1.14e-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: 1.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  615 QKDSGISLENGVYAAAVL----------PGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLR 670
Cdd:cd06686    17 LKGFGIQLQGGVFATETLsspplisfiePDSPAERCGVLQVGDRVLSINGIPTEDRTLEEANQLLR 82
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 1387-1468 1.37e-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: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1387 EPRVV-FIKKSQLelGVHLCGGNLHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEV--YVEMLKPRDGVR 1463
Cdd:cd06729     1 DTRLVsFRKGGSV--GLRLAGGNDVGIFVAGVQEGSPAEK-QGLQEGDQILKVNGVDFRNLTREEAvlFLLDLPKGEEVT 77


                  ....*
gi 767964245 1464 LKVQY 1468
Cdd:cd06729    78 ILAQS 82
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 1239-1311 1.42e-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: 1.42e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1239 VKVQKGSEPLGISIVSG-----EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1311
Cdd:cd06789     6 VTLKKVGNGMGLSIVAAkgagqDKLGIYIKSVVKGGAADLDGrLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTL 84
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 1237-1302 1.43e-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: 1.43e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1237 RHVKVQKGS--EPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1302
Cdd:cd06755     1 RTVTLTRPSreSPLHFSLLGGsEKGfGIFVSKVEKGSKAAEAGLKRGDQILEVNGQNFENITLKKALEIL 70
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 127-486 1.50e-10

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 66.35  E-value: 1.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   127 RLKDDVDMLRRENGQLLRERNLLQQSWEDMK-RLHEEDQK--EIGDLRAQQQQVLkhngsSEILNKLYDTAMDKLEVVKk 203
Cdd:pfam01576  135 KLEEDILLLEDQNSKLSKERKLLEERISEFTsNLAEEEEKakSLSKLKNKHEAMI-----SDLEERLKKEEKGRQELEK- 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   204 dydALRKRYSEKVAIHN--ADL-SRLEQLG-------EENQRLLKQTEMLTQQRDTAI----QLQHQCALSLRRFEAIHH 269
Cdd:pfam01576  209 ---AKRKLEGESTDLQEqiAELqAQIAELRaqlakkeEELQAALARLEEETAQKNNALkkirELEAQISELQEDLESERA 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   270 ELNKATAQNKDLQWEMELLQselTELRTTQVKTAKESEkYREERDAVYSEYKLIMSER----DQVISELDKLQTEV---- 341
Cdd:pfam01576  286 ARNKAEKQRRDLGEELEALK---TELEDTLDTTAAQQE-LRSKREQEVTELKKALEEEtrshEAQLQEMRQKHTQAleel 361

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   342 --ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRAnkEVEILRKQCKALCQELKEALQEADVAKCRRdwafQER- 418
Cdd:pfam01576  362 teQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ--DSEHKRKKLEGQLQELQARLSESERQRAEL----AEKl 435

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245   419 DKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTR-------KQKNDVSRELKELKEQ---MESQLEKEARFRQ 486
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLSTRLRQLEDErnsLQEQLEEEEEAKR 513
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1244-1314 1.61e-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: 1.61e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  1244 GSEPLGISIVSGEKG---GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1314
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) ...
 523-596 2.60e-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: 2.60e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  523 LGFDMAEGVN---EPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 596
Cdd:cd06749    11 LGFSISGGIGsqgNPFRPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVNIEHGQAVSLLKSFQNTVDLVVER 87
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 28-485 2.66e-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: 65.91  E-value: 2.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    28 QQVNEKVENLSIQLRLMTR---ERNELRKRLAFATHGTAFDkrpyhrLNPDYERLKIQcVRAMSDLQSLQNQHTNALK-R 103
Cdd:pfam15921   74 EHIERVLEEYSHQVKDLQRrlnESNELHEKQKFYLRQSVID------LQTKLQEMQME-RDAMADIRRRESQSQEDLRnQ 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   104 CEEVAKETDFYHTLHSRLLSDQTrlkDDVDMLRRengQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGS 183
Cdd:pfam15921  147 LQNTVHELEAAKCLKEDMLEDSN---TQIEQLRK---MMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGS 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   184 --SEILNKLyDTAMDKLE----VVKKDYDALRKRYSEKVAI---HNADlsRLEQLGEENQ-RLLKQTEMLTQQRDTAIQL 253
Cdd:pfam15921  221 aiSKILREL-DTEISYLKgrifPVEDQLEALKSESQNKIELllqQHQD--RIEQLISEHEvEITGLTEKASSARSQANSI 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   254 QHQcalslrrFEAIHHELNKATA----QNKDLQWEMELLQSELTELRTTQVKTAKESEKY-----------REERDAVYS 318
Cdd:pfam15921  298 QSQ-------LEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanselteaRTERDQFSQ 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   319 EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRankeVEILRKQCKALCQELK 398
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQR----LEALLKAMKSECQGQM 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   399 EalqeadvakcRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQL 478
Cdd:pfam15921  447 E----------RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN 516


                   ....*..
gi 767964245   479 EKEARFR 485
Cdd:pfam15921  517 AEITKLR 523
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 88-523 3.37e-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: 3.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    88 SDLQSLQNQ--HTNALKRCEEVAKETDFYHtLHSRLLSDQTRLKDDVDMLRRE----NGQLLRERNLLQQSWEDMKRLHE 161
Cdd:pfam15921  299 SQLEIIQEQarNQNSMYMRQLSDLESTVSQ-LRSELREAKRMYEDKIEELEKQlvlaNSELTEARTERDQFSQESGNLDD 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   162 EDQKEIGDLRAQQQQVlkhNGSSEILNKLYDTAMDKLEVVkkdyDALRKRYSEKvaihNADLSRLEQLgeenqrllkqte 241
Cdd:pfam15921  378 QLQKLLADLHKREKEL---SLEKEQNKRLWDRDTGNSITI----DHLRRELDDR----NMEVQRLEAL------------ 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   242 MLTQQRDTAIQLQHQCAlslrRFEAIHHELNKATAQNKDLQWEMELLQSELTELrttqvkTAKESEKYREERdaVYSEYK 321
Cdd:pfam15921  435 LKAMKSECQGQMERQMA----AIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL------TAKKMTLESSER--TVSDLT 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   322 LIMSERDQVI----SELDKLQTEVELAESKLKSSTSEK---KAANEEMEALRqikdtvtMDAGRANKEVEILRKQCKALC 394
Cdd:pfam15921  503 ASLQEKERAIeatnAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALK-------LQMAEKDKVIEILRQQIENMT 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   395 Q------------ELKEALQEADVAKCRRDwaFQERDKIVAERDS-IRTL---CDNLRRERDRAVSELAEALRSLDDTRK 458
Cdd:pfam15921  576 QlvgqhgrtagamQVEKAQLEKEINDRRLE--LQEFKILKDKKDAkIRELearVSDLELEKVKLVNAGSERLRAVKDIKQ 653

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245   459 QKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKAL 523
Cdd:pfam15921  654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 239-529 4.57e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 4.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   239 QTEMLTQQRDTAI-QLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVy 317
Cdd:TIGR02168  667 KTNSSILERRREIeELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL- 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   318 seykliMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQikdtvtmDAGRANKEVEILRKQCKALCQEL 397
Cdd:TIGR02168  746 ------EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA-------QIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   398 KEalqeadvakcrrdwafqerdkivaerdsirtlcdnLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESq 477
Cdd:TIGR02168  813 TL-----------------------------------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES- 856

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767964245   478 lekearfrqlMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAE 529
Cdd:TIGR02168  857 ----------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 1237-1315 4.83e-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: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1237 RHVKVQKG-SEPLGISIVSGEKGG--IYVSKVTVGSIAHQ-AGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
Cdd:cd06800     1 RKVLLSKEpHEGLGISITGGKEHGvpILISEIHEGQPADRcGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITLE 80


                  ...
gi 767964245 1313 AQY 1315
Cdd:cd06800    81 VVY 83
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
217-521 5.93e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 64.29  E-value: 5.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  217 AIHNADL-SRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEaihhelnkataqnkDLQWEMELLQSELTEL 295
Cdd:PRK02224  198 EKEEKDLhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE--------------ERREELETLEAEIEDL 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  296 RTTQVKTAKESEKYREErdavyseykliMSERDQVISELDKLQTEVeLAESKLKSSTSEKKAA-----NEEMEALRQIKD 370
Cdd:PRK02224  264 RETIAETEREREELAEE-----------VRDLRERLEELEEERDDL-LAEAGLDDADAEAVEArreelEDRDEELRDRLE 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  371 TVTMDAGRANKEVEILRKQCKALCQELKEALQEA-----DVAKCRRDWAfQERDKIVAERDSIRTL---CDNLRRERDRA 442
Cdd:PRK02224  332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAaelesELEEAREAVE-DRREEIEELEEEIEELrerFGDAPVDLGNA 410

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  443 VSELAEALRSLDDTRKQKNDVSRELKELKEQMEsqlEKEARFR--------QLMAHSSHDSAIDtdsmEWETEVVEFERE 514
Cdd:PRK02224  411 EDFLEELREERDELREREAELEATLRTARERVE---EAEALLEagkcpecgQPVEGSPHVETIE----EDRERVEELEAE 483


                  ....*..
gi 767964245  515 TEDIDLK 521
Cdd:PRK02224  484 LEDLEEE 490
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
210-480 5.95e-10

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 62.62  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  210 KRYSEKVAIHNADLSRLEqlgEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEmelLQ 289
Cdd:COG1340    11 EELEEKIEELREEIEELK---EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE---LN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  290 SELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEV-------ELAEsKLKSSTSEKKAANEEM 362
Cdd:COG1340    85 EKLNELR-------EELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekELVE-KIKELEKELEKAKKAL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  363 EALRQIKDTVTmdagrankEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDS-------IRTLCDNL 435
Cdd:COG1340   157 EKNEKLKELRA--------ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADElhkeiveAQEKADEL 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767964245  436 RRERDRAVSELAEALRSLDDTRKQKNDVSR-----ELKELKEQMESQLEK 480
Cdd:COG1340   229 HEEIIELQKELRELRKELKKLRKKQRALKRekekeELEEKAEEIFEKLKK 278
SH3_ZO-1 cd12026
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ...
 1482-1542 6.11e-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: 56.63  E-value: 6.11e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1482 DSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSK 1542
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 ...
 1239-1312 6.39e-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: 6.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1239 VKVQKGSEPLGISIVSG-----EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
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 ...
 1239-1302 6.83e-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: 6.83e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245 1239 VKVQKGSePLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1302
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 ...
 519-596 7.49e-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: 7.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  519 DLKALGFDMAEGVNEPCF-PGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 595
Cdd:cd06703    10 DGKGLGFSIAGGKGSTPFrDGDEGIFISRITEGGAAdrDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITLVVE 89


                  .
gi 767964245  596 R 596
Cdd:cd06703    90 R 90
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 623-678 8.56e-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: 8.56e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06690    29 SPGIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMDLIRTSGDKLRF 84
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1239-1298 1.06e-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: 1.06e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245 1239 VKVQKGS-EPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd10833     4 VTVEKSPdGSLGFSVRGGsEHGlGIFVSKVEEGSAAERAGLCVGDKITEVNGVSLENITMSSA 66
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1236-1317 1.25e-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: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1236 PRHVKVQKGSEPLGISIVSG--EKGGIYVSKVTVGSIA-HQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
Cdd:cd06796     2 PRVVELPKTEEGLGFNVMGGkeQNSPIYISRIIPGGVAdRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLV 81


                  ....*
gi 767964245 1313 AQYNP 1317
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) ...
 1387-1473 1.37e-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: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1387 EPRVVFIKKSQLELGVHLCGG-NLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLK 1465
Cdd:cd06795     1 EPRKIVLHKGSTGLGFNIVGGeDGEGIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTII 80


                  ....*...
gi 767964245 1466 VQYRPEEF 1473
Cdd:cd06795    81 AQYKPEEY 88
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
106-490 1.39e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.86  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  106 EVAKETdFYHTLHSRLLSdqtRLKDDVDMLRRENGQL----LRERNLLQQSWEDMKRLHEE---DQKEIGDLRAQQQQVl 178
Cdd:COG4717    33 EAGKST-LLAFIRAMLLE---RLEKEADELFKPQGRKpelnLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEEL- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  179 khngssEILNKLYDTAMDKLEVVKKDYDALRKRysEKVAIHNADL-SRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQC 257
Cdd:COG4717   108 ------EAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELpERLEELEERLEELRELEEELEELEAELAELQEEL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  258 ALSLRRF-EAIHHELNKATAQNKDLQWEMELLQSELTELR-------------TTQVKTAKESEKYREER---------- 313
Cdd:COG4717   180 EELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQeeleeleeeleqlENELEAAALEERLKEARlllliaaall 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  314 ------DAVYSEYKLIM---------------------SERDQVISELDKLQTEVELAESKLKS-----STSEKKAANEE 361
Cdd:COG4717   260 allglgGSLLSLILTIAgvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELEEllaalGLPPDLSPEEL 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  362 MEALRQIKDTVTMDAGRANKEVEIlrkQCKALCQELKEALQEADV-------AKCRRdwaFQERDKIVAERDSIRTLCDN 434
Cdd:COG4717   340 LELLDRIEELQELLREAEELEEEL---QLEELEQEIAALLAEAGVedeeelrAALEQ---AEEYQELKEELEELEEQLEE 413

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245  435 LRRERDRAVS---------ELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEARFRQLMAH 490
Cdd:COG4717   414 LLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAELEAELE-QLEEDGELAELLQE 477
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 621-678 1.53e-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: 1.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  621 SLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06694    27 SLDLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 539-597 1.57e-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: 1.57e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  539 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKAL-------LNGEGAINMVVRRR 597
Cdd:cd23059    36 DLGIFIKSIIHGGAAskDGRLRVNDQLIAVNGESLLGLTNSEAMETLrramsteGNIRGMIQLVVARR 103
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 24-483 2.51e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 62.35  E-value: 2.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    24 LLTDQQVNEKVENLSIQLRLMTRERNELRKRLafathgtafdkrpyHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKR 103
Cdd:TIGR04523  203 LSNLKKKIQKNKSLESQISELKKQNNQLKDNI--------------EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   104 CEEVAKETDfyhtLHSRLLSDqtrLKDDVDMLrreNGQLLRERNLLQQSWedMKRLHEEDQKEIGDLRAQQQQVLKHNgs 183
Cdd:TIGR04523  269 LSEKQKELE----QNNKKIKE---LEKQLNQL---KSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNN-- 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   184 sEILNKLydtaMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQ-RDTAIQLQHQcalslr 262
Cdd:TIGR04523  335 -KIISQL----NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQiNDLESKIQNQ------ 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   263 rfeaihHELNKATAQN-KDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEV 341
Cdd:TIGR04523  404 ------EKLNQQKDEQiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   342 ELAESKLKSSTSEKKAANEEMEALrqikdtvtmdagraNKEVEILRKQCKALCQELKEALQEADVAKCRRDwafQERDKI 421
Cdd:TIGR04523  478 NKIKQNLEQKQKELKSKEKELKKL--------------NEEKKELEEKVKDLTKKISSLKEKIEKLESEKK---EKESKI 540

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   422 VAERDSIRTLCDNLRR--------ERDRAVSELAEALRSLDDTRKQKNDV----SRELKELKEQME------SQLEKEAR 483
Cdd:TIGR04523  541 SDLEDELNKDDFELKKenlekeidEKNKEIEELKQTQKSLKKKQEEKQELidqkEKEKKDLIKEIEekekkiSSLEKELE 620
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1482-1544 2.74e-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: 2.74e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245   1482 DSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWMAWQLDENaqkiQRGQIPSKYV 1544
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 ...
 1235-1314 3.17e-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: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1235 EPRHVKVQK-GSEPLGISIVSG-----------EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLI 1301
Cdd:cd06671     1 PPRRVELWRePGKSLGISIVGGrvmgsrlsngeEIRGIFIKHVLEDSPAGRNGtLKTGDRILEVNGVDLRNATHEEAVEA 80

                          90
                  ....*....|...
gi 767964245 1302 IGQQCDTITILAQ 1314
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 ...
 505-598 3.31e-09

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 55.46  E-value: 3.31e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    505 ETEVVEFERETEDidlkaLGFDMAEGVNEpcfpgDCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 583
Cdd:smart00228    1 EPRLVELEKGGGG-----LGFSLVGGKDE-----GGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLL 70

                            90
                    ....*....|....*
gi 767964245    584 LNGEGAINMVVRRRK 598
Cdd:smart00228   71 KKAGGKVTLTVLRGG 85
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1239-1298 6.65e-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: 6.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1239 VKVQKGSEPLGISIV-------SGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06791     5 VELVKDEQGLGITIAgyvgekaSGELSGIFVKSIIPGSAADQDGrIQVNDQIIAVDGVNLQGFTNQEA 72
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-403 7.05e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   28 QQVNEKVENLSIQLRLMTRERNELRKRLAfathgtafDKRPYHRLnpdYERLK--------IQCVRAMSDLQSLQNQHTN 99
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKELEKRLE--------ELEERHEL---YEEAKakkeelerLKKRLTGLTPEKLEKELEE 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  100 ALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRREN------GQLLRE---RNLLQQSWEDMKRLhEEDQKEIG-- 168
Cdd:PRK03918  396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEehrKELLEEYTAELKRI-EKELKEIEek 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  169 --DLRAQQQQVLKHNGSSEILNKLYDTA--------------MDKLEVVKKDYDALRKRYSE---KVAIHNADLSRLEQL 229
Cdd:PRK03918  475 erKLRKELRELEKVLKKESELIKLKELAeqlkeleeklkkynLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEEL 554

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  230 GEENQRLLKQ--------TEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQW---EMELLQSELTELRTT 298
Cdd:PRK03918  555 KKKLAELEKKldeleeelAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEReekELKKLEEELDKAFEE 634

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  299 QVKTAKESEKYREERDAV---YS--EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 373
Cdd:PRK03918  635 LAETEKRLEELRKELEELekkYSeeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714

                         410       420       430
                  ....*....|....*....|....*....|.
gi 767964245  374 mDAGRANKEVEILRKQCKALCQELKE-ALQE 403
Cdd:PRK03918  715 -KLEKALERVEELREKVKKYKALLKErALSK 744
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
 1482-1542 7.69e-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: 7.69e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1482 DSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLDENAQKIQRGQIPSK 1542
Cdd:cd12028     1 DSFYIRTHFDYEPDPPSGLSFTRGEVFHVLDTMHRGKLGSWLAVRMGRDLREMEKGIIPNQ 61
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-373 8.85e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 8.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    10 HPGGTTGKAPSPPPLLTDQQVNEkVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPYHRLNPDYERLKIQCVRAMSD 89
Cdd:TIGR02168  656 RPGGVITGGSAKTNSSILERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    90 LQSLQNQHTNALKRCEEVAKETdfyhtlhSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGD 169
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKEL-------TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   170 LRAQQQQvlkhngsseiLNKLYDTAMDKLEVVKKDYDALRKRY----------SEKVAIHNADLSRLEQLGEEnqrLLKQ 239
Cdd:TIGR02168  808 LRAELTL----------LNEEAANLRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEE---LESE 874

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   240 TEMLTQQRDtaiQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRT----TQVKTAKESEKYREErda 315
Cdd:TIGR02168  875 LEALLNERA---SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELrlegLEVRIDNLQERLSEE--- 948

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245   316 vYS-EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 373
Cdd:TIGR02168  949 -YSlTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 631-678 1.05e-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: 1.05e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767964245  631 VLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06734    33 IIPGSPADRCGQLKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTL 80
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 1237-1302 1.35e-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: 1.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1237 RHV--KVQKGSEPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1302
Cdd:cd06740     2 RQVtlKRSKSHEGLGFSIRGGaEHGvGIYVSLVEPGSLAEKEGLRVGDQILRVNDVSFEKVTHAEAVKIL 71
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 538-597 1.35e-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: 1.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245  538 GDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 597
Cdd:cd06758    27 GDIGIFVAGVEEGGSAdrDGRLKKGDELLMINGQSLIGLSHQEAVAILRSSASPVQLVIASK 88
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 29-367 1.53e-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: 60.08  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    29 QVNEKVENLSI-------QLRLMTRERN------ELRKRLAfathgtafDKRPYHRLNpDYERLKIQCVRAMSDLQSLQN 95
Cdd:TIGR02169  181 EVEENIERLDLiidekrqQLERLRREREkaeryqALLKEKR--------EYEGYELLK-EKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    96 QHTNALKRCEEVAKEtdfYHTLHSRLLSDQTRLKDdvdMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQ 175
Cdd:TIGR02169  252 ELEKLTEEISELEKR---LEEIEQLLEELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   176 QvlkhnGSSEILNKLYD-TAMDK-LEVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLL-------KQTEMLTQQ 246
Cdd:TIGR02169  326 K-----LEAEIDKLLAEiEELEReIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelkdyrEKLEKLKRE 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   247 RDTAIQLQHQCALSLRRFEA----IHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKL 322
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEeladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 767964245   323 IMSERDQVISELDKLQTEVELAESKLKSStsekKAANEEMEALRQ 367
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERVRGG----RAVEEVLKASIQ 521
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1235-1312 1.54e-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: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1235 EPRHVKVQKGS--EPLGISIVSGEK---GGIYVSKV-TVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1308
Cdd:cd06677     2 EITTIEIHRSDpyEELGISIVGGNDtplINIVIQEVyRDGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLRQPCPV 81


                  ....*.
gi 767964245 1309 --ITIL 1312
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) ...
 513-596 1.77e-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: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  513 RETEDIDL-----KALGFDMAeGVNEPCfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDL-INKDKKQAIKALL 584
Cdd:cd06689    13 RQVEYIELekpesGGLGFSVV-GLKSEN-RGELGIFVQEIQPGSVAarDGRLKENDQILAINGQPLdQSISHQQAIAILQ 90

                          90
                  ....*....|..
gi 767964245  585 NGEGAINMVVRR 596
Cdd:cd06689    91 QAKGSVELVVAR 102
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 1244-1302 2.36e-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: 2.36e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1244 GSEPLGISIVSGEKG-GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1302
Cdd:cd23060     8 ANGGLGFSLVGGEGGsGIFVKSISPGGVADRDGrLQVGDRLLQVNGESVIGLSHSKAVNIL 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 30-517 2.48e-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: 59.30  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    30 VNEKVENLSIQLRLMTR------ERNELRKRLAfATHGTAFDKRpYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKR 103
Cdd:TIGR02168  198 LERQLKSLERQAEKAERykelkaELRELELALL-VLRLEELREE-LEELQEELKEAEEELEELTAELQELEEKLEELRLE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   104 CEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhngS 183
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE---E 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   184 SEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLT--QQRDTAIQLQHQCALSL 261
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrRERLQQEIEELLKKLEE 432

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   262 RRFEAIH-------HELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAV---------YSEY-KLIM 324
Cdd:TIGR02168  433 AELKELQaeleeleEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLerlqenlegFSEGvKALL 512

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   325 SERDQ------VISELDKLQTEVELA-ESKLKSS-----TSEKKAANEEMEALRQ------------------------- 367
Cdd:TIGR02168  513 KNQSGlsgilgVLSELISVDEGYEAAiEAALGGRlqavvVENLNAAKKAIAFLKQnelgrvtflpldsikgteiqgndre 592

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   368 IKDTVTMDAGRANKEVEILRKQCKAL---------CQELKEALQEAdvAKCRRDWAF----------------------- 415
Cdd:TIGR02168  593 ILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvVDDLDNALELA--KKLRPGYRIvtldgdlvrpggvitggsaktns 670

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   416 ------QERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMA 489
Cdd:TIGR02168  671 silerrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750

                          570       580
                   ....*....|....*....|....*...
gi 767964245   490 HSSHDSAIDTDSMEWETEVVEFERETED 517
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELA 778
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1237-1311 2.99e-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: 2.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1237 RHVKVQK-GSEPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQcDTITI 1311
Cdd:cd06737     3 RLVRLDRrGPESLGFSVRGGlEHGcGLFVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINLIKTK-KTVSL 79
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 508-596 3.43e-08

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


Pssm-ID: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 52.67  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  508 VVEFERETedidlKALGFDMAEGVNEPCFPG-DCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLN 585
Cdd:cd06704     2 TITIERQT-----GGLGISIAGGKGSTPYKGdDEGIFISRVTEGGPAAkAGVRVGDKLLEVNGVDLVDADHHEAVEALKN 76

                          90
                  ....*....|.
gi 767964245  586 GEGAINMVVRR 596
Cdd:cd06704    77 SGNTVTMVVLR 87
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 26-533 3.73e-08

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 58.90  E-value: 3.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    26 TDQQVNEKVENLSIQLRLMTRERNELRKRLA--------FATHGTAFDKRpYHRLNPDYERLKIQCVRAMSDLQSLQNQ- 96
Cdd:TIGR00606  299 TDEQLNDLYHNHQRTVREKERELVDCQRELEklnkerrlLNQEKTELLVE-QGRLQLQADRHQEHIRARDSLIQSLATRl 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    97 HTNALKRCEEVAKETDFYHTLHSRLLSDQTR--------LKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIG 168
Cdd:TIGR00606  378 ELDGFERGPFSERQIKNFHTLVIERQEDEAKtaaqlcadLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK 457

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   169 DLRAQQQQVlkHNGSSEILNKLYDTAMDKLEVVKKDYDAL---RKRYSEKVAIHNADLSR-LEQLGEENQRL------LK 238
Cdd:TIGR00606  458 FVIKELQQL--EGSSDRILELDQELRKAERELSKAEKNSLtetLKKEVKSLQNEKADLDRkLRKLDQEMEQLnhhtttRT 535

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   239 QTEMLTQQRDTA------IQLQHQCALS--------LRRFEAIHHELNKATAQNKDlqwEMELLQSELTELRTTQVKTAK 304
Cdd:TIGR00606  536 QMEMLTKDKMDKdeqirkIKSRHSDELTsllgyfpnKKQLEDWLHSKSKEINQTRD---RLAKLNKELASLEQNKNHINN 612

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   305 EsEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQ-------IKDTVTMDAG 377
Cdd:TIGR00606  613 E-LESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpVCQRVFQTEA 691

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   378 RANKEVEILRKQCKALCQELKEAlqEADVAKCRRdwafqerdkivaERDSIRTLCDNLRRERDRAVSELAEalrslddTR 457
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKST--ESELKKKEK------------RRDEMLGLAPGRQSIIDLKEKEIPE-------LR 750

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245   458 KQKNDVSRELKELKEQMEsqlEKEARFRQLMA--HSSHDSAIDTDSME-WETEVVEFERETEDIDLKALGFDMAEGVNE 533
Cdd:TIGR00606  751 NKLQKVNRDIQRLKNDIE---EQETLLGTIMPeeESAKVCLTDVTIMErFQMELKDVERKIAQQAAKLQGSDLDRTVQQ 826
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1243-1317 3.80e-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: 3.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245 1243 KGSEPLGISIVSGEKG--GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITILAQYNP 1317
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 ...
 1248-1298 4.09e-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: 4.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1248 LGISIVSGeKG---------GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06704    12 LGISIAGG-KGstpykgddeGIFISRVTEGGPAAKAGVRVGDKLLEVNGVDLVDADHHEA 70
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1235-1312 4.24e-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: 4.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1235 EPRHVKVQKGSEP-------LGISIVSGEKG-----GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLI 1301
Cdd:cd06714     3 LIGRIILQRDPKDgsvsgngLGLKVVGGKMTesgrlGAYVTKVKPGSVADTVGhLREGDEVLEWNGISLQGKTFEEVQDI 82

                          90
                  ....*....|.
gi 767964245 1302 IGQQCDTITIL 1312
Cdd:cd06714    83 ISQSKGEVELV 93
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 75-517 4.50e-08

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: 58.26  E-value: 4.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    75 DYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAketdfyHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWE 154
Cdd:pfam01576  423 ESERQRAELAEKLSKLQSELESVSSLLNEAEGKN------IKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLED 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   155 DMKRLHEEDQKEIGDLRAQQQQVLKHNGS-SEILNKLYDTA--MDKLEVVKK----DYDALRKRYSEKVAIHnadlsrlE 227
Cdd:pfam01576  497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQlSDMKKKLEEDAgtLEALEEGKKrlqrELEALTQQLEEKAAAY-------D 569

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   228 QLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDlqwEMELLQSELTELRTTQVKTAKESE 307
Cdd:pfam01576  570 KLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAE---ERDRAEAEAREKETRALSLARALE 646

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   308 KYREERDAVYSEYKLIMSERDQVISELDKLQTEV-ELAESK--LKSSTSEKKAANEEME-ALRQIKDT-----VTMDAGR 378
Cdd:pfam01576  647 EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVhELERSKraLEQQVEEMKTQLEELEdELQATEDAklrleVNMQALK 726

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   379 ANKEVEILRK------QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSEL------ 446
Cdd:pfam01576  727 AQFERDLQARdeqgeeKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLkklqaq 806

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   447 -AEALRSLDDTRKQKNDV---SRE----LKELKEQM---------------ESQLEKEARFRQLMAHSSHDSAIDTDSME 503
Cdd:pfam01576  807 mKDLQRELEEARASRDEIlaqSKEsekkLKNLEAELlqlqedlaaserarrQAQQERDELADEIASGASGKSALQDEKRR 886

                          490
                   ....*....|....
gi 767964245   504 WETEVVEFERETED 517
Cdd:pfam01576  887 LEARIAQLEEELEE 900
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 607-682 4.82e-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: 4.82e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  607 PLHINLSGQKDsgisLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 682
Cdd:cd06683    14 PLGITISGTEE----PFDPIVISGLTEGGLAERTGAIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTLKISR 85
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 607-681 4.94e-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: 4.94e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245   607 PLHINLSGQKDSGIsleNGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:pfam00595   11 GLGFSLKGGSDQGD---PGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
170-529 5.18e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 5.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  170 LRAQQQQVLKHNGSSEILNKlydTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDT 249
Cdd:COG4717    51 LEKEADELFKPQGRKPELNL---KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  250 AIQLQHQCALS---------LRRFEAIHHELNKATAQNKDLQWEMELLQSELTEL-RTTQVKTAKESEKYREERDAVYSE 319
Cdd:COG4717   128 LPLYQELEALEaelaelperLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQR 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  320 YKLIMSERDQVISELDKLQTEVELAESKLKS------------------------------------------------- 350
Cdd:COG4717   208 LAELEEELEEAQEELEELEEELEQLENELEAaaleerlkearlllliaaallallglggsllsliltiagvlflvlglla 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  351 -----STSEKKAANEEMEA--------------LRQIKDTVTMDAGRANKEVEILRKQCKALCQ---ELKEALQEADVAK 408
Cdd:COG4717   288 llfllLAREKASLGKEAEElqalpaleeleeeeLEELLAALGLPPDLSPEELLELLDRIEELQEllrEAEELEEELQLEE 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  409 CRRDW-------------AFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDT--RKQKNDVSRELKELKEQ 473
Cdd:COG4717   368 LEQEIaallaeagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEE 447

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  474 MESQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAE 529
Cdd:COG4717   448 LEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 187-561 5.25e-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: 58.06  E-value: 5.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   187 LNKLYDTAMDKLEV------VKKDYDALRKRysEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQhqcALS 260
Cdd:pfam02463  175 LKKLIEETENLAELiidleeLKLQELKLKEQ--AKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL---RDE 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   261 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDavysEYKLIMSERDQVISELDKLQTE 340
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL----KLERRKVDDEEKLKESEKEKKK 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   341 VELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVakcRRDWAFQERDK 420
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK---LKEEELELKSE 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   421 IVAERDSI----RTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKEL------KEQMESQLEKEARFRQLMAH 490
Cdd:pfam02463  403 EEKEAQLLlelaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelkllkDELELKKSEDLLKETQLVKL 482

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245   491 SSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAEGVNEPCFP--GDCGIFVTKVD-KGSIADGRLRVND 561
Cdd:pfam02463  483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGrlGDLGVAVENYKvAISTAVIVEVSAT 556
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 1261-1311 5.63e-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: 5.63e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1261 YVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1311
Cdd:cd06746    45 YLESVDPGGVADKAGLKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVL 95
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
286-488 5.99e-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: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  286 ELLQSELTELRTtQVKTA-KESEKYREERDAVYSEyklimSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEA 364
Cdd:COG3206   178 EFLEEQLPELRK-ELEEAeAALEEFRQKNGLVDLS-----EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  365 LRQIKDTVTmdagrANKEVEILRKQCKALCQELKEALQEadvakcrrdwaFQERD-KIVAERDSIRTLCDNLRRERDRAV 443
Cdd:COG3206   252 GPDALPELL-----QSPVIQQLRAQLAELEAELAELSAR-----------YTPNHpDVIALRAQIAALRAQLQQEAQRIL 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767964245  444 SELAEALRSLddtRKQKNDVSRELKELKEQMESQLEKEARFRQLM 488
Cdd:COG3206   316 ASLEAELEAL---QAREASLQAQLAQLEARLAELPELEAELRRLE 357
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 539-596 6.17e-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: 6.17e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  539 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDkkQAIKALLNGEGAINMVVRR 596
Cdd:cd06716    30 DTGIYVSEVDPNSIAakDGRIREGDQILQINGVDVQNRE--EAIALLSEEEKSITLLVAR 87
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1387-1468 6.28e-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: 6.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1387 EPRVVFIKKSQLELGVHLCGGNLHGVFVAEVEDDSPAKgPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1466
Cdd:cd06767     2 EPRHVSIEKGSEPLGISIVSGENGGIFVSSVTEGSLAH-QAGLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80


                  ..
gi 767964245 1467 QY 1468
Cdd:cd06767    81 QY 82
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 612-682 7.32e-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: 7.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245  612 LSGQKDSGISLengvYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 682
Cdd:cd06753    14 LQGGKDFNQPL----TISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLER 79
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
275-482 8.49e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 56.07  E-value: 8.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  275 TAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSE 354
Cdd:COG1340     7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  355 KKAANEEMEALRQIKDTvtmdAGRANKEVEILRKQCKAL-------------------------------------CQEL 397
Cdd:COG1340    87 LNELREELDELRKELAE----LNKAGGSIDKLRKEIERLewrqqtevlspeeekelvekikelekelekakkalekNEKL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  398 KEALQEADVAKCRRDWAFQ-------ERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKEL 470
Cdd:COG1340   163 KELRAELKELRKEAEEIHKkikelaeEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242

                         250
                  ....*....|..
gi 767964245  471 KEQMESQLEKEA 482
Cdd:COG1340   243 RKELKKLRKKQR 254
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 516-596 9.76e-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: 51.10  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  516 EDIDLK----ALGFDMAEGVNEPCFP---GDCGIFVTKVDKGSIAdGR--LRVNDWLLRINDVDLINKDKKQAIKALLNG 586
Cdd:cd06702     1 EEIHLVkaggPLGLSIVGGSDHSSHPfgvDEPGIFISKVIPDGAA-AKsgLRIGDRILSVNGKDLRHATHQEAVSALLSP 79

                          90
                  ....*....|
gi 767964245  587 EGAINMVVRR 596
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 ...
 615-673 9.92e-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: 9.92e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245  615 QKDSGISL------------ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQ 673
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) ...
 1238-1312 1.02e-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: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1238 HVKVQKGSEPLGISIVSGeKG--------GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDT 1308
Cdd:cd06724     1 EIKLVKGPKGLGFSIAGG-VGnqhipgdnGIYVTKIIEGGAAQKDGrLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDV 79


                  ....
gi 767964245 1309 ITIL 1312
Cdd:cd06724    80 VYLK 83
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 616-681 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 767964245  616 KDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:cd23058    24 RDNPTGGSGPIYIKNILPKGAAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKLGGTVSLV 89
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1238-1302 1.09e-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: 50.71  E-value: 1.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1238 HVKVQK-GSEPLGISIVS-GEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1302
Cdd:cd06678     2 HVTLNKrDGEQLGIKLVRkKDEPGVFILDLLEGGLAARDGrLKSDDRVLAINGQDLRHGTPEQAAQII 69
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 630-682 1.12e-07

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


Pssm-ID: 467170 [Multi-domain]  Cd Length: 85  Bit Score: 50.81  E-value: 1.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767964245  630 AVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 682
Cdd:cd06682    33 DVKKGSVAHRTGTLEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIRK 85
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
204-471 1.26e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  204 DYDALRKRYSEKVAIHN-------ADLSRLEQLGEEN-QRLLKQT---------------EMLTQQR--DTAIQLQHQca 258
Cdd:COG4913   156 DIRALKARLKKQGVEFFdsfsaylARLRRRLGIGSEKaLRLLHKTqsfkpigdlddfvreYMLEEPDtfEAADALVEH-- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  259 lsLRRFEAIHHELNKATAQnkdlqweMELLQsELTELRTTQVKTAKESEKYREERDAVysEYKLIMSERDQVISELDKLQ 338
Cdd:COG4913   234 --FDDLERAHEALEDAREQ-------IELLE-PIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELR 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  339 TEVELAESKLKSSTSEKKAANEEMEALRQIKdtvtmdAGRANKEVEILRKQCKALCQELKEALQEAD--VAKCRR-DWAF 415
Cdd:COG4913   302 AELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRArlEALLAAlGLPL 375

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  416 -QERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK 471
Cdd:COG4913   376 pASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 77-489 1.36e-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: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   77 ERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDM 156
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  157 KRLHEEDQKEIGDLRAQQQQVLKHNGSS----EILNKLYDTAMDKLEVVKKDYDALRKR-------------YSEKVAIH 219
Cdd:COG1196   462 LELLAELLEEAALLEAALAELLEELAEAaarlLLLLEAEADYEGFLEGVKAALLLAGLRglagavavligveAAYEAALE 541

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  220 NADLSRLEQLGEEN-QRLLKQTEMLTQQ---RDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSEL--T 293
Cdd:COG1196   542 AALAAALQNIVVEDdEVAAAAIEYLKAAkagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdT 621

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  294 ELRTTQVKTAKESEKYREERDAVyseyklimsERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 373
Cdd:COG1196   622 LLGRTLVAARLEAALRRAVTLAG---------RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  374 MDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRD------------------WAFQERDKIVAERDSIRTLCDNL 435
Cdd:COG1196   693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEaereelleelleeeelleEEALEELPEPPDLEELERELERL 772

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245  436 RRERDR-------AVSELAEALRSLDDTRKQKNDVSRELKELKEQMEsQLEKEARfRQLMA 489
Cdd:COG1196   773 EREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIE-EIDRETR-ERFLE 831
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 608-670 1.49e-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: 1.49e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  608 LHINLSGQ---KDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLR 670
Cdd:cd23059    18 LGVSVKGKtskEDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETLR 83
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-524 1.50e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   24 LLTDQQVNEKVENLSIQLRLMTRERNELRKRLAfathgtafdkrpyhRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKR 103
Cdd:COG1196   231 LLKLRELEAELEELEAELEELEAELEELEAELA--------------ELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  104 CEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKhnGS 183
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--EL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  184 SEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNAdLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRR 263
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  264 FEAihhELNKATAQNKDLQWEMELLQSELTELRTtQVKTAKESEKYREERDAVYSEY---------KLIMSERDQVISEL 334
Cdd:COG1196   454 LEE---EEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEAEADYEGFlegvkaallLAGLRGLAGAVAVL 529

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  335 DKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRAN--------------------------KEVEILRK 388
Cdd:COG1196   530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpldkiraraalaaalargaigaavDLVASDLR 609

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  389 QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAE------------------RDSIRTLCDNLRRERDRAVSELAEAL 450
Cdd:COG1196   610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrevtlegeggsaggsltGGSRRELLAALLEAEAELEELAERLA 689

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  451 RSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAI----------------------DTDSMEWETEV 508
Cdd:COG1196   690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREElleelleeeelleeealeelpePPDLEELEREL 769

                         570
                  ....*....|....*.
gi 767964245  509 VEFEREtedidLKALG 524
Cdd:COG1196   770 ERLERE-----IEALG 780
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
270-586 1.57e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.68  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  270 ELNKATAQNKDLQWEMELLQSELTELrttqvktakesekyREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLK 349
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQA--------------REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  350 SSTSEKKAANEEMEALRQikdtvtmDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDwafQERDKIVAERDSIR 429
Cdd:COG4372    98 QAQEELESLQEEAEELQE-------ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK---ELEEQLESLQEELA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  430 TLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVV 509
Cdd:COG4372   168 ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  510 EFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNG 586
Cdd:COG4372   248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 630-670 1.89e-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: 1.89e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767964245  630 AVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 670
Cdd:cd06782    20 SPIPGGPAEKAG-IKPGDVIVAVDGESVRGMSLDEVVKLLR 59
PDZ_PICK1-like cd06722
PDZ domain of PICK1 (protein interacting with C-kinase 1) and similar domains; PDZ (PSD-95 ...
 615-682 2.33e-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: 2.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  615 QKDS----GISLENG------VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 682
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 ...
 620-681 2.39e-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: 2.39e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245  620 ISLENGVYAAAVLPGSPAakEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:cd06769    16 AGSERPVVVRSVTPGGPS--EGKLLPGDQILKINNEPVEDLPRERVIDLIRECKDSIVLTVL 75
SH3_ZO-2 cd12027
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a ...
 1481-1542 2.42e-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: 2.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1481 GDSFYIRALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWMAWQLdenAQKIQRGQIPSK 1542
Cdd:cd12027     1 GDSFFIRTHFEYEKELPQSLAFTRGEIFRVVDTLYDGKLGNWLAVRI---GNELEKGLIPNK 59
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 327-514 2.59e-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: 55.42  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   327 RDQVISELDKLQTEVelAESKLKSSTSE--KKAANEEMEALRQIKDTVTMDAGRANKEvEILRKQCKALCQ-ELKE---- 399
Cdd:pfam05701   37 RKLVELELEKVQEEI--PEYKKQSEAAEaaKAQVLEELESTKRLIEELKLNLERAQTE-EAQAKQDSELAKlRVEEmeqg 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   400 --------ALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELK 471
Cdd:pfam05701  114 iadeasvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATK 193

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767964245   472 EQMESqlekearfrqlmAHSSHDSA----------IDTDSMEWETEVVEFERE 514
Cdd:pfam05701  194 ESLES------------AHAAHLEAeehrigaalaREQDKLNWEKELKQAEEE 234
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 1237-1311 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 767964245 1237 RHVKVQKG-SEPLGISIvSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1311
Cdd:cd06726     1 RLVEFEKArDEPLGATI-KMEEDSVIVARILHGGMAHRSGlLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTF 76
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 623-681 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 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
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, ...
 626-672 2.99e-07

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


Pssm-ID: 467203 [Multi-domain]  Cd Length: 86  Bit Score: 49.95  E-value: 2.99e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 767964245  626 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 672
Cdd:cd06720    29 VVVANMMPGGPAARSGKLNIGDQIMSINGTSLVGLPLSTCQAIIKNL 75
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 1245-1298 3.30e-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: 3.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1245 SEPLGISIV------SGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06692     7 SKGLGIKIIggyrenTGEEFGIFIKRILPGGLAATDGrLKEGDLILEVNGESLQGVTNERA 67
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 1239-1322 3.42e-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: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1239 VKVQKGSEPLGISIVSGEK---GGIYVSKV-TVGSIAHQAGLEYGDQLLEFNGINLRSATEQQArliigqqcdtITILAQ 1314
Cdd:cd06673     6 IEINKGKKGLGLSIVGGSDtllGAIIIHEVyEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEA----------INVLRQ 75


                  ....*...
gi 767964245 1315 YNPHVHQL 1322
Cdd:cd06673    76 TPQKVRLL 83
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1238-1312 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 767964245 1238 HVKVQKGSEP-LGISIVSGEK----GGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITI 1311
Cdd:cd06682     2 HVKLPKRSGVgLGITISAPKNrkpgDPLIISDVKKGSVAHRTGtLEPGDKLLAIDNIRLDNCSMEDAAQIL-QQAEDIVK 80


                  .
gi 767964245 1312 L 1312
Cdd:cd06682    81 L 81
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
191-483 3.65e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  191 YDTAMDKLEVVKKDYDALRKRYsEKVAIHNADLSrlEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCAL---SLRRFEAI 267
Cdd:PRK03918  160 YENAYKNLGEVIKEIKRRIERL-EKFIKRTENIE--ELIKEKEKELEEVLREINEISSELPELREELEKlekEVKELEEL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  268 HHELNKATAQNKDLQWEMELLQSELTELRT-------------TQVKTAKESEKYREERDAVYSEYKLIMSERDQVISEL 334
Cdd:PRK03918  237 KEEIEELEKELESLEGSKRKLEEKIRELEErieelkkeieeleEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  335 DKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTM---------DAGRANKEVEILRKQCKalCQELKEALQEAD 405
Cdd:PRK03918  317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyeEAKAKKEELERLKKRLT--GLTPEKLEKELE 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  406 VAKCRRDWAFQERDKIVAERDSIRtlcdNLRRERDRAVSELAEAL-------RSLDDTRKQK---------NDVSRELKE 469
Cdd:PRK03918  395 ELEKAKEEIEEEISKITARIGELK----KEIKELKKAIEELKKAKgkcpvcgRELTEEHRKElleeytaelKRIEKELKE 470

                         330
                  ....*....|....
gi 767964245  470 LKEQmESQLEKEAR 483
Cdd:PRK03918  471 IEEK-ERKLRKELR 483
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 610-678 3.81e-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: 3.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245  610 INLSGQKDS--GISLENGVYAAAVLPGSPAakEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06727    15 IAVSGGRDNphFQSGDTSIVISDVLKGGPA--EGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANI 83
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 288-483 4.38e-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: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  288 LQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALR- 366
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKe 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  367 ----QIKDTVTM-------------DAGRANKEVEILR---KQCKALCQELKEALQEADvakcrrdwafQERDKIVAERD 426
Cdd:COG4942   105 elaeLLRALYRLgrqpplalllspeDFLDAVRRLQYLKylaPARREQAEELRADLAELA----------ALRAELEAERA 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  427 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQmESQLEKEAR 483
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIA 230
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 305-489 4.54e-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: 4.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  305 ESEKYREERDAVySEYKLIMSERDQVISELDKLQTEV-----ELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRA 379
Cdd:cd07596     2 EDQEFEEAKDYI-LKLEEQLKKLSKQAQRLVKRRRELgsalgEFGKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  380 NKEVeilRKQCKALCQELKEALQEADVAKCrrdwAFQERDKIVAERDSIRTLCDNLRRERDRAVS-------ELAEALRS 452
Cdd:cd07596    81 EAQA---NQELVKLLEPLKEYLRYCQAVKE----TLDDRADALLTLQSLKKDLASKKAQLEKLKAapgikpaKVEELEEE 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767964245  453 LDDTRKQKNDVSRELKELKEQMESQLE--KEARFRQLMA 489
Cdd:cd07596   154 LEEAESALEEARKRYEEISERLKEELKrfHEERARDLKA 192
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
261-524 4.60e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.14  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  261 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTE 340
Cdd:COG4372    37 LFELDKLQEELEQLREELEQAREELEQLEEELEQAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  341 VELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEAlqEADVAKCRRDWAFQERDK 420
Cdd:COG4372   110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  421 IVAER----DSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSA 496
Cdd:COG4372   188 LLKEAnrnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267

                         250       260
                  ....*....|....*....|....*...
gi 767964245  497 IDTDSMEWETEVVEFERETEDIDLKALG 524
Cdd:COG4372   268 LVEKDTEEEELEIAALELEALEEAALEL 295
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 1238-1311 4.66e-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: 4.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245 1238 HVKVQKGSEPLGISIVSG-EKG-GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA-RLIIGQQCDTITI 1311
Cdd:cd10834     5 HLYTTSDDYCLGFNIRGGsEYGlGIYVSKVDPGGLAEQNGIKVGDQILAVNGVSFEDITHSKAvEVLKSQTHLMLTI 81
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 600-670 4.82e-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: 4.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245  600 LGGKVVTPLHINLSGQKDS-GISL---ENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 670
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 ...
 1242-1313 5.45e-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: 5.45e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1242 QKGsepLGISIVSGEKG-----GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1313
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 ...
 593-674 5.66e-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: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  593 VVRR-RKSLGgkvvtplhINLSGQKDSGISLEN-----GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECE 666
Cdd:cd06671     7 LWREpGKSLG--------ISIVGGRVMGSRLSNgeeirGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEAV 78


                  ....*...
gi 767964245  667 SLLRSCQD 674
Cdd:cd06671    79 EAIRNAGN 86
PDZ5_PTPN13-like cd06697
PDZ domain 5 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 607-678 5.97e-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: 5.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245  607 PLHINLSGQKDSgisLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06697    14 QLGLKLTGGSDS---KYQVIYVLEIVPGSAAAEEGSLQPLDIIHYINGVSTQGMTLEDAVRALEASLPTVVL 82
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 1237-1298 5.98e-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: 5.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1237 RHVKVQKgsEP---LGISIvsgeKGG------IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06801     1 RTVRVVK--QDvggLGISI----KGGaehkmpILISKIFKGQAADQTGqLFVGDAILSVNGENLEDATHDEA 66
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 510-596 6.36e-07

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


Pssm-ID: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 48.75  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  510 EFERETEDIDlKALGFDMAEGVNEPCFPGdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGE 587
Cdd:cd06792     2 VFEVELSKKD-GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAeqDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKNAG 78


                  ....*....
gi 767964245  588 GAINMVVRR 596
Cdd:cd06792    79 QVVTLVLER 87
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1235-1314 6.99e-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: 6.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1235 EPRHVKVQKGSEPLGISIVSGeKG---------GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1304
Cdd:cd06703     1 ETITTTLIRDGKGLGFSIAGG-KGstpfrdgdeGIFISRITEGGAADRDGkLQVGDRVLSINGVDVTEARHDQAVALLTS 79

                          90
                  ....*....|
gi 767964245 1305 QCDTITILAQ 1314
Cdd:cd06703    80 SSPTITLVVE 89
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
136-398 7.80e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.99  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  136 RRE-NGQLLRERNLLQQswedMKRLHEEDQKEIGDLRAQQQQVLkhngssEILNKLYDTA------MDKLEVVKKDYDAL 208
Cdd:COG1340    45 RDElNAQVKELREEAQE----LREKRDELNEKVKELKEERDELN------EKLNELREELdelrkeLAELNKAGGSIDKL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  209 RKRYsekvaihnadlsrlEQLgEENQrllkQTEMLTQQRDTAIQLQhqcalsLRRFEAIHHELNKATAQNKDLQW---EM 285
Cdd:COG1340   115 RKEI--------------ERL-EWRQ----QTEVLSPEEEKELVEK------IKELEKELEKAKKALEKNEKLKElraEL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  286 ELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEAL 365
Cdd:COG1340   170 KELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL 249

                         250       260       270
                  ....*....|....*....|....*....|...
gi 767964245  366 RQIKdtvtmDAGRANKEVEILRKQCKALCQELK 398
Cdd:COG1340   250 RKKQ-----RALKREKEKEELEEKAEEIFEKLK 277
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
 614-678 8.45e-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: 8.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245  614 GQKDSGiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
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 ...
 1387-1467 8.78e-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: 8.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1387 EPRVVFIKK-SQLELGVHLCGGN-----------LHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVyVE 1454
Cdd:cd06671     1 PPRRVELWRePGKSLGISIVGGRvmgsrlsngeeIRGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEA-VE 79

                          90
                  ....*....|....
gi 767964245 1455 MLK-PRDGVRLKVQ 1467
Cdd:cd06671    80 AIRnAGNPVVFLVQ 93
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 522-596 9.08e-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: 9.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  522 ALGFDMA--EGVNEPCFP-GDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 596
Cdd:cd06727    10 GFGFGIAvsGGRDNPHFQsGDTSIVISDVLKGGPAEGKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANITVKR 87
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-336 9.28e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 9.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    28 QQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNaLKrcEEV 107
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LN--EEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   108 AKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEdQKEIGDLRAQQQQVLkhngssEIL 187
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE-LEALLNERASLEEAL------ALL 892

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   188 NKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQLgeeNQRLLKQTEMLT-QQRDTaiqlqhqcalslrrFEA 266
Cdd:TIGR02168  893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSeEYSLT--------------LEE 955

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245   267 IHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSER---DQVISELDK 336
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKetlEEAIEEIDR 1028
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 261-463 9.43e-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: 51.85  E-value: 9.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  261 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMS--ERDQ-----VIS- 332
Cdd:COG1579     9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEeqlgnVRNn 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  333 -ELDKLQTEVELAESKLKSSTSEKKAANEEMEALRqikdtvtmdagranKEVEILRKQCKALCQELKEALQEADvakcrr 411
Cdd:COG1579    89 kEYEALQKEIESLKRRISDLEDEILELMERIEELE--------------EELAELEAELAELEAELEEKKAELD------ 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767964245  412 dwafQERDKIVAERDSirtlcdnLRRERDRAVSELAEALRSL-DDTRKQKNDV 463
Cdd:COG1579   149 ----EELAELEAELEE-------LEAEREELAAKIPPELLALyERIRKRKNGL 190
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
102-487 9.84e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 9.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  102 KRCEEVAKETDFYHTLhSRLLSDqtrLKDDVDMLRRENGQLLRERNLLQQSWEDMkrlhEEDQKEIGDLRAQQQQVLKHN 181
Cdd:PRK03918  283 KELKELKEKAEEYIKL-SEFYEE---YLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEKRL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  182 GSSEILNKLYDTAMDKL---------------EVVKKDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQ 246
Cdd:PRK03918  355 EELEERHELYEEAKAKKeelerlkkrltgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  247 RDTA------IQLQHQCALsLRRFEA----IHHELNKATAQNKDL-----QWEMELL-QSELTELRTT--QVKTAKES-E 307
Cdd:PRK03918  435 KGKCpvcgreLTEEHRKEL-LEEYTAelkrIEKELKEIEEKERKLrkelrELEKVLKkESELIKLKELaeQLKELEEKlK 513

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  308 KYR-EERDAVYSEYKLIMSERDQVISELDKLQTEVE---LAESKLKSSTSEKKAANEEM-EALRQIKDTVTMDAGRANKE 382
Cdd:PRK03918  514 KYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEELaELLKELEELGFESVEELEER 593

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  383 VEILRK------QCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCD------------NLRRERDRAVS 444
Cdd:PRK03918  594 LKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseeeyeELREEYLELSR 673

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 767964245  445 ELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQL 487
Cdd:PRK03918  674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 1238-1312 1.12e-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: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1238 HVKVQKGSEPLGISIVSG------------EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQ 1305
Cdd:cd10822     5 HKLRQGENLILGFSIGGGidqdpsknpfsyTDKGIYVTRVSEGGPAEKAGLQVGDKILQVNGWDMTMVTHKQAVKRLTKK 84


                  ....*..
gi 767964245 1306 CDTITIL 1312
Cdd:cd10822    85 KPVLRML 91
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 119-403 1.20e-06

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: 53.49  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   119 SRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQ---QVLKHNgssEILNKLYDTam 195
Cdd:TIGR04523  338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdleSKIQNQ---EKLNQQKDE-- 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   196 dKLEVVKKDYDALRKRY---SEKVAIHNADLSRLEqlgEENQRLLKQTEMLTQQRDtaiQLQHQCALSLRRFEAIHH--- 269
Cdd:TIGR04523  413 -QIKKLQQEKELLEKEIerlKETIIKNNSEIKDLT---NQDSVKELIIKNLDNTRE---SLETQLKVLSRSINKIKQnle 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   270 -----------ELNKATAQNKDLQWEMELLQSELTELRTTQVK------------TAKESEKYREERDAVYSEYKLIMSE 326
Cdd:TIGR04523  486 qkqkelkskekELKKLNEEKKELEEKVKDLTKKISSLKEKIEKlesekkekeskiSDLEDELNKDDFELKKENLEKEIDE 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   327 RDQVISEL----DKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALcQELKEALQ 402
Cdd:TIGR04523  566 KNKEIEELkqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI-KSKKNKLK 644


                   .
gi 767964245   403 E 403
Cdd:TIGR04523  645 Q 645
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 1248-1298 1.30e-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: 1.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767964245 1248 LGISIVSGEKG-GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06674    16 LGLSIVGKRNDtGVFVSDIVKGGAADADGrLMQGDQILSVNGEDVRNASQEAA 68
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 1237-1298 1.60e-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: 1.60e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1237 RHVKVQKG-SEPLGISIVSGEKGG-----IYVSKV-TVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06679     1 KTVTIKKEpSESLGISVAGGRGSRrgdlpIYVTNVqPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEA 69
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 1239-1310 1.68e-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: 1.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245 1239 VKVQKGSEPLGISIVSGEKGG-IYVSKVTVGSIAHQAGLEY-GDQLLEFNGINLRSATEQQARLIIGQQCDTIT 1310
Cdd:cd06799     3 VRLVKNNEPLGATIKRDEKTGaIVVARIMRGGAADRSGLIHvGDELREVNGISVEGKDPEEVIQILANSQGPIT 76
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 614-681 1.83e-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: 1.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  614 GQKDS-GISLENG---------VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:cd06675     8 GPQDSlGISIAGGvgsplgdvpVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKNASGTIILQVV 85
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 180-491 1.90e-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: 52.80  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   180 HNGSSEILNKLYDTAMDKLEVVKKDYDALrkrYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCal 259
Cdd:pfam05483   55 NSGDCHYQEGLKDSDFENSEGLSRLYSKL---YKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFEN-- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   260 slrrfEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQT 339
Cdd:pfam05483  130 -----EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRV 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   340 EVELA--ESKLKSSTSEKKAANEEMEALRQIKDTvtmdagraNKEVEILRKQCKALCQELKE---ALQEAdvakcrRDWA 414
Cdd:pfam05483  205 QAENArlEMHFKLKEDHEKIQHLEEEYKKEINDK--------EKQVSLLLIQITEKENKMKDltfLLEES------RDKA 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   415 FQERDKIVAERDSIRTLCDnlrrERDRAVSELAEALRSLDDTRKQKNDVSRELK-------ELKEQMESQLEKEARFRQl 487
Cdd:pfam05483  271 NQLEEKTKLQDENLKELIE----KKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKA- 345


                   ....
gi 767964245   488 mAHS 491
Cdd:pfam05483  346 -AHS 348
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 626-681 1.92e-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: 1.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  626 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:cd06676    28 IYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTLTVL 83
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 268-529 2.14e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.05  E-value: 2.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   268 HHELNKATAQNKDLQwemELLQSELTEL----------RTTQVKTAKESEKYREERDAVYSEYKLIMSER----DQVISE 333
Cdd:pfam02463  108 EYYINGKNVTKKEVA---ELLESQGISPeaynflvqggKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEAlkklIEETEN 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   334 LDKLQTEVELAESKLKSstsEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRdw 413
Cdd:pfam02463  185 LAELIIDLEELKLQELK---LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE-- 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   414 aFQERDKIVAERDSIRTLC----DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMA 489
Cdd:pfam02463  260 -IEKEEEKLAQVLKENKEEekekKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 767964245   490 HSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAE 529
Cdd:pfam02463  339 ELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 623-680 2.15e-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: 2.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 680
Cdd:cd10817    21 ENGIVIKSLTEGGPAAKDGRLKVGDQILAVDDESVVGCPYEKAISLLKTAKGTVKLTV 78
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-495 2.17e-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: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   32 EKVENLSiQLRLMTRERNELRKRLAF-----ATHGTAFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEE 106
Cdd:COG4913   249 EQIELLE-PIRELAERYAAARERLAEleylrAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  107 vaketdfyhtLHSRLLSDQTrlkDDVDMLRRENGQLLRERNLLQQSWEDMKRL-------HEEDQKEIGDLRAQ-QQQVL 178
Cdd:COG4913   328 ----------LEAQIRGNGG---DRLEQLEREIERLERELEERERRRARLEALlaalglpLPASAEEFAALRAEaAALLE 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  179 KHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSE----KVAIHNADLSRLEQLGEE---------------------- 232
Cdd:COG4913   395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrKSNIPARLLALRDALAEAlgldeaelpfvgelievrpeee 474

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  233 -----------NQRL------------------LKQTEMLTQQR-------------------------DTAIQ--LQHQ 256
Cdd:COG4913   475 rwrgaiervlgGFALtllvppehyaaalrwvnrLHLRGRLVYERvrtglpdperprldpdslagkldfkPHPFRawLEAE 554

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  257 --------CALS---LRRFE-AI-----------HHELNK-------------ATAQNKDLQWEMELLQSELTELRTTQV 300
Cdd:COG4913   555 lgrrfdyvCVDSpeeLRRHPrAItragqvkgngtRHEKDDrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLE 634

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  301 KTAKESEKYREERDA-----VYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMD 375
Cdd:COG4913   635 ALEAELDALQERREAlqrlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGE 714

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  376 AGRANKEveilRKQCKALCQELKEALQEA-DVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLD 454
Cdd:COG4913   715 IGRLEKE----LEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  455 DTRKQ--------KNDVSREL-------KELKEQMESQL-EKEARFRQLMAHSSHDS 495
Cdd:COG4913   791 RAMRAfnrewpaeTADLDADLeslpeylALLDRLEEDGLpEYEERFKELLNENSIEF 847
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 514-585 2.21e-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: 2.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  514 ETEDIDL----KALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 585
Cdd:cd06791     1 ETFEVELvkdeQGLGITIAGYVGEKASGELSGIFVKSIIPGSAAdqDGRIQVNDQIIAVDGVNLQGFTNQEAVEVLRN 78
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 624-680 2.25e-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: 2.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  624 NGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 680
Cdd:cd23060    23 SGIFVKSISPGGVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 29-482 2.33e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 52.66  E-value: 2.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    29 QVNEKVENLSIQLRLMTRERNELRKRLAFATHgtafdkrpyHRLNPDYERLKIQCVRAMSDLqsLQNQHTNALKRCEEVA 108
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK---------QQSSIEEQRRLLQTLHSQEIH--IRDAHEVATSIREISC 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   109 KETDFYHTLHSrLLSDQTRLKD-------DVDMLRRENGQ---LLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVL 178
Cdd:TIGR00618  373 QQHTLTQHIHT-LQQQKTTLTQklqslckELDILQREQATidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   179 KHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAIHNADLSRLEqlgeENQRLLKQTEMLTQQRDTAI------- 251
Cdd:TIGR00618  452 QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ----EEPCPLCGSCIHPNPARQDIdnpgplt 527

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   252 ----QLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELrTTQVKTAKES-EKYREERDAVYSEYKLIMSE 326
Cdd:TIGR00618  528 rrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL-TQCDNRSKEDiPNLQNITVRLQDLTEKLSEA 606

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   327 RDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADV 406
Cdd:TIGR00618  607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245   407 AKCRRDWAFQErdkIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRE-LKELKEQMESQLEKEA 482
Cdd:TIGR00618  687 SEKEQLTYWKE---MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQsLKELMHQARTVLKART 760
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 598-681 2.47e-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: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  598 KSLGGKVVTPLHinlsgqkdsgislengvYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLT 677
Cdd:cd23070    27 RSINGELYAPLQ-----------------HVSAVLEGGAADKAG-VRKGDRILEVNGVNVEGATHKQVVDLIKSGGDELT 88


                  ....
gi 767964245  678 LSLL 681
Cdd:cd23070    89 LTVI 92
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1485-1543 2.57e-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: 2.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1485 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWMAWQLDENaqkiQRGQIPSKY 1543
Cdd:cd00174     1 YARALYDYEAQDDDELSFKKGDIITVLEKDDDG----WWEGELNGG----REGLFPANY 51
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 1244-1314 3.08e-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: 3.08e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245 1244 GSEPLGISIVSGEKGG--IYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1314
Cdd:cd23068     9 SNTPWGFRLQGGADFGqpLSIQKVNPGSPADKAGLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQ 81
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 608-671 3.27e-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: 3.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  608 LHINLSGQKDSGISlENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 671
Cdd:cd06758    14 LGIQITGGKGSKRG-DIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAILRS 76
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
221-450 3.60e-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: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  221 ADLSRLEQLGEenqRLLKQTEMLTQQRDTAIQLQHQcALSLRRFEAIHHELNKATAQNKDLQWEMEL--LQSELTELRTT 298
Cdd:COG4913   235 DDLERAHEALE---DAREQIELLEPIRELAERYAAA-RERLAELEYLRAALRLWFAQRRLELLEAELeeLRAELARLEAE 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  299 QVKTAKESEKYREERDAVYSEYklimseRDQVISELDKLQTEVELAESKLKSStseKKAANEEMEALRQIKDTVTMDAgr 378
Cdd:COG4913   311 LERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEER---ERRRARLEALLAALGLPLPASA-- 379

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  379 anKEVEILRKQCKALCQELKEALQEADV----AKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEAL 450
Cdd:COG4913   380 --EEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 623-678 3.82e-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: 3.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06724    27 DNGIYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYL 82
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
325-486 4.20e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 4.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  325 SERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEalrqikdtvtmdagRANKEVEILRKQCKALCQELKEALQEA 404
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE--------------QARSELEQLEEELEELNEQLQAAQAEL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  405 DVAKcrrdwafQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARF 484
Cdd:COG4372    97 AQAQ-------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169


                  ..
gi 767964245  485 RQ 486
Cdd:COG4372   170 EQ 171
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 1239-1303 4.26e-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: 4.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1239 VKVQKGSEPLGISIvSGEKG------GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIG 1303
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 ...
 1239-1298 4.40e-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: 4.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1239 VKVQKGSEPLGISIV-------SG-EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06790     5 VELEKGSEGLGISIIgmgvgadAGlEKLGIFVKTVTEGGAAQRDGrIQVNDQIVEVDGISLVGVTQAFA 73
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 590-659 4.61e-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: 4.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  590 INMVVRRRKSL--GGKV------VTPLHINLSGQKDSGISLENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDN 659
Cdd:COG0265   159 INLAKRVVEQLieTGRVrrgwlgVTIQPVTPELAEALGLPEPEGVLVARVEPGSPAAKAG-LRPGDVILAVDGKPVTS 235
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 623-681 4.62e-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: 4.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:cd06692    25 EFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSILRSASASNHMSLL 83
PDZ5_INAD-like cd23066
PDZ domain 5 of inactivation no after potential D (INAD), and related domains; PDZ (PSD-95 ...
 616-682 4.74e-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: 4.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245  616 KDSGISL----ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 682
Cdd:cd23066    10 KELGLSLspneGIGCTIADLLPGGYAEIDGKLQKGDIITKFNGDALSGLPFQVCYALFKGANGKISLEVTR 80
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
224-474 4.83e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  224 SRLEQLGEENQRLLKQTEMLTQQRDTAiqlqhqcalsLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTA 303
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQA----------REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  304 KESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQikdtvTMDAGRANKEV 383
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE-----ELAALEQELQA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  384 EILRKQCKALCQELKEALQEADV--AKCRRDWAFQERDKIVAERDSIRTlcDNLRRERDRAVSELAEALRSLDDTRKQKN 461
Cdd:COG4372   176 LSEAEAEQALDELLKEANRNAEKeeELAEAEKLIESLPRELAEELLEAK--DSLEAKLGLALSALLDALELEEDKEELLE 253

                         250
                  ....*....|...
gi 767964245  462 DVSRELKELKEQM 474
Cdd:COG4372   254 EVILKEIEELELA 266
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1237-1312 4.93e-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: 4.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1237 RHVKVQKG-SEPLGISIVSGEKG-----------GIYVSKVT-VGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIG 1303
Cdd:cd06701     5 QELTIVKEpGEKLGISIRGGAKGhagnpldptdeGIFISKINpDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILR 84


                  ....*....
gi 767964245 1304 QQCDTITIL 1312
Cdd:cd06701    85 SVGDTLTLL 93
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 611-678 5.32e-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: 5.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  611 NLSGQKDsgislENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
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 ...
 1249-1304 5.68e-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: 5.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245 1249 GISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNG--------INLRSATEQQARLIIGQ 1304
Cdd:cd06736    12 QITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGcirgerqsVSLEDCTKEEAHWTLQR 75
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
28-474 5.76e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   28 QQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPyHRLNPDYERLKiQCVRAMSDLQSLQNQHTNALKRCEEv 107
Cdd:COG4717    98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPERLE-ELEERLEELRELEEELEELEAELAE- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  108 aKETDFYHTLHSRLLSDQTRLKDdvdmlrrengqLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEIL 187
Cdd:COG4717   175 -LQEELEELLEQLSLATEEELQD-----------LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  188 NKLYDT-----AMDKLEVVKKDYDALrkrYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLR 262
Cdd:COG4717   243 ERLKEArllllIAAALLALLGLGGSL---LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  263 RFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKES--EKYREERDAVYSEYKliMSERDQVISELDKLQTE 340
Cdd:COG4717   320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAG--VEDEEELRAALEQAEEY 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  341 VELAEsKLKSSTSEKKAANEEMEALRQI--KDTVTMDAGRANKEVEILRKQCKALCQELK----------------EALQ 402
Cdd:COG4717   398 QELKE-ELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAeleaeleqleedgelaELLQ 476

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  403 EADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELA-EALRSLDDTR--------------KQKNDVSREL 467
Cdd:COG4717   477 ELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERAsEYFSRLTDGRyrliridedlslkvDTEDGRTRPV 556

                         490
                  ....*....|.
gi 767964245  468 KEL----KEQM 474
Cdd:COG4717   557 EELsrgtREQL 567
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 ...
 1238-1304 5.88e-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: 5.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245 1238 HVKVQKgsEP---LGISIVS----GEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQ 1304
Cdd:cd06760     6 EVTLNK--EPgvgLGIGLCClpleNDIPGIFIHHLSPGSVAHMDGrLRRGDQILEINGTSLRNVTLNEAYAILSQ 78
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 1389-1467 6.08e-06

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 45.73  E-value: 6.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1389 RVVFIKKSQLELGVHLCGGN---LHGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLK 1465
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSdqgDPGIFVSEVLPGGAAEA-GGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79


                   ..
gi 767964245  1466 VQ 1467
Cdd:pfam00595   80 IL 81
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 621-683 6.13e-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: 6.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245  621 SLENGVYAAAVLPgSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 683
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 ...
 1239-1311 6.15e-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: 6.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1239 VKVQKGSEPLGISIVSGEKGG-----IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1311
Cdd:cd06676     2 ITLERGSDGLGFSIVGGFGSPhgdlpIYVKTVFEKGAAAEDGrLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTL 80
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 1237-1288 6.50e-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: 6.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1237 RHVKVQK-GSEPLGISIVSG---EKG-GIYVSKVTVGSIAHQAGLEY-GDQLLEFNGI 1288
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) ...
 523-597 6.52e-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: 6.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  523 LGFDMAEGVNEPcfpgdcGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 597
Cdd:cd06795    14 LGFNIVGGEDGE------GIFISFILAGGPADlsGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIAQYK 84
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 120-521 7.22e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 51.33  E-value: 7.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   120 RLLSDQTRLKD-DVDMLRRENGQLLRERN--LLQ-----QSWEDMKRLHEEDQKEI-GDLRAQQQQvlkhNGSSEILNKL 190
Cdd:pfam01576  334 KALEEETRSHEaQLQEMRQKHTQALEELTeqLEQakrnkANLEKAKQALESENAELqAELRTLQQA----KQDSEHKRKK 409

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   191 YDTAMDKLEVVKKDYDALRKRYSEKVAIHNADL----SRLEQLGEENQRLLKQTEMLTQQ-RDTAIQLQhqcalslrrfE 265
Cdd:pfam01576  410 LEGQLQELQARLSESERQRAELAEKLSKLQSELesvsSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQ----------E 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   266 AIHHELNKATaQNKDLQWEMELLQSELTElrttQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELD----KLQTEV 341
Cdd:pfam01576  480 ETRQKLNLST-RLRQLEDERNSLQEQLEE----EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEegkkRLQREL 554

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   342 ELAESKLKsstsEKKAANEEMEA----LRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEalQEADVAKcrrdwAFQE 417
Cdd:pfam01576  555 EALTQQLE----EKAAAYDKLEKtknrLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE--EKAISAR-----YAEE 623

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   418 RDKivAERDSirtlcdnlrRERDRAVSELAealRSLDDTRKQKNDVSRELKELKEQMES-------------QLEKEARf 484
Cdd:pfam01576  624 RDR--AEAEA---------REKETRALSLA---RALEEALEAKEELERTNKQLRAEMEDlvsskddvgknvhELERSKR- 688

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 767964245   485 rqlmahsshdsAIDTDSMEWETEVVEFERE---TEDIDLK 521
Cdd:pfam01576  689 -----------ALEQQVEEMKTQLEELEDElqaTEDAKLR 717
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 508-594 9.29e-06

PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight junction (PATJ, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 12 of MUPP1, PDZ domain 10 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like PDZ12 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467163 [Multi-domain]  Cd Length: 86  Bit Score: 45.43  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  508 VVEFERETEDidlkALGFDMAEGVNEPCfpGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 585
Cdd:cd06675     2 TVEIKRGPQD----SLGISIAGGVGSPL--GDVPVFIAMIQPNGVAaqTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKN 75


                  ....*....
gi 767964245  586 GEGAINMVV 594
Cdd:cd06675    76 ASGTIILQV 84
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 616-661 9.48e-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: 9.48e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767964245  616 KDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKS 661
Cdd:cd23063    22 KVSPNTKTTGIFIKGIIPDSPAHKCGRLKVGDRILSVNGNDVRNST 67
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 1390-1467 1.07e-05

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


Pssm-ID: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 45.33  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1390 VVFIKKSQLELGVHLCGGNLH----------GVFVAEVEDDSPAkGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPR 1459
Cdd:cd06702     2 EIHLVKAGGPLGLSIVGGSDHsshpfgvdepGIFISKVIPDGAA-AKSGLRIGDRILSVNGKDLRHATHQEAVSALLSPG 80


                  ....*...
gi 767964245 1460 DGVRLKVQ 1467
Cdd:cd06702    81 QEIKLLVR 88
PDZ1_L-delphilin-like cd06743
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1246-1309 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 767964245 1246 EPLGISIvsGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRS-ATEQQARLiiGQQCDTI 1309
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 ...
 605-671 1.13e-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: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  605 VTPLHINLSGQKDSGIslenGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 671
Cdd:cd06755    11 ESPLHFSLLGGSEKGF----GIFVSKVEKGSKAAEAG-LKRGDQILEVNGQNFENITLKKALEILRN 72
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 1237-1312 1.21e-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: 1.21e-05
                          10        20        30        40        50        60        70
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gi 767964245 1237 RHVKVQKGSEPLGiSIVSGEKGGIYVSKVTVGSIAHQAGLEY-GDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
Cdd:cd06798     1 KIVRIEKTREPLG-ATVRNEGDSVIISRIVKGGAAEKSGLLHeGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFL 76
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 625-678 1.23e-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: 1.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767964245  625 GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06701    39 GIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTL 92
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 1237-1298 1.24e-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: 1.24e-05
                          10        20        30        40        50        60
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gi 767964245 1237 RHVKVQKGSEPLGISIVS-----GEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd23058     6 LHIQLKKGPEGLGFSITSrdnptGGSGPIYIKNILPKGAAIQDGrLKAGDRLLEVNGVDVTGKTQEEV 73
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
277-489 1.25e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.14  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  277 QNKDLQWEMELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQtevelaeSKLKSSTSEKK 356
Cdd:COG1340     2 KTDELSSSLEELEEKIEELR-------EEIEELKEKRDELNEELKELAEKRDELNAQVKELR-------EEAQELREKRD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  357 AANEEMEALRQIKDTVtmdagraNKEVEILRKQCKALCQELKEA-LQEADVAKCRRD-----WAFQERDkivaerdsirt 430
Cdd:COG1340    68 ELNEKVKELKEERDEL-------NEKLNELREELDELRKELAELnKAGGSIDKLRKEierleWRQQTEV----------- 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245  431 lcdnLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMA 489
Cdd:COG1340   130 ----LSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIK 184
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 607-674 1.28e-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: 1.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  607 PLHINLSGQKDsgislENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQD 674
Cdd:cd06678    12 QLGIKLVRKKD-----EPGVFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQASGE 74
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 610-681 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 767964245  610 INLSGQKDSGISLEN------GVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQdSLTLSLL 681
Cdd:cd06738     7 ISLVGTRGLGCSISSgptqkpGIFISNVKPGSLAEEVG-LEVGDQIVEVNGTSFTNVDHKEAVMALKSSR-HLTITVR 82
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-489 1.41e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  109 KETDFYHTLHSRLLSDQTRLK-DDVDMLRRENGQLLRERnLLQQSwedmKRLHEEDqkeiGDLRAQQQQVLkhnGSSeil 187
Cdd:COG4913   543 KPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRAITRAG-QVKGN----GTRHEKD----DRRRIRSRYVL---GFD--- 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  188 nklydtAMDKLEVVKKDYDALRkrysEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQhQCALSLRRFEAi 267
Cdd:COG4913   608 ------NRAKLAALEAELAELE----EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEA- 675

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  268 hhELNKATAQNKDLqwemELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESK 347
Cdd:COG4913   676 --ELERLDASSDDL----AALEEQLEELE-------AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  348 LKSSTS---EKKAANEEMEAL-----RQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERD 419
Cdd:COG4913   743 ARLELRallEERFAAALGDAVerelrENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLD 822

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  420 KIVAER-----------------DSIRTLCDNLRRERDRAVSELAE---ALRSLD---DTRKQ---KNDVSRELKELKEQ 473
Cdd:COG4913   823 RLEEDGlpeyeerfkellnensiEFVADLLSKLRRAIREIKERIDPlndSLKRIPfgpGRYLRleaRPRPDPEVREFRQE 902

                         410       420
                  ....*....|....*....|....*
gi 767964245  474 M---------ESQLEKEARFRQLMA 489
Cdd:COG4913   903 LravtsgaslFDEELSEARFAALKR 927
PDZ3_GRIP1-2-like cd06684
PDZ domain 3 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 619-671 1.57e-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: 1.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  619 GISL-------ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 671
Cdd:cd06684    16 GITLststhrnKQVIVIDSIKPASIADRCGALHVGDHILSIDGTSVEHCSLAEATQLLAS 75
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 523-594 1.60e-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: 1.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  523 LGFDMAEGVNE----PCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 594
Cdd:cd06701    17 LGISIRGGAKGhagnPLDPTDEGIFISKINPDGAAarDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTLLV 94
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1239-1311 1.71e-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: 1.71e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245 1239 VKVQKGSEPLGISIVSGEKGG--IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1311
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 ...
 614-678 1.74e-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: 1.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245  614 GQKDSGISLE----NGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06767    11 GSEPLGISIVsgenGGIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQCGDTITM 78
PDZ_2 pfam13180
PDZ domain;
620-681 1.75e-05

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 44.57  E-value: 1.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245   620 ISLENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALdnKSLNECESLLRSC--QDSLTLSLL 681
Cdd:pfam13180    2 VDLEGGVVVVSVKSSGPAAKAG-LKAGDVILSIDGRKI--NDLTDLESALYGHkpGDTVTLQVY 62
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
279-519 1.75e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  279 KDLQWEMELLQSELTelRTTQVKTA-KESEKYREErdaVYSEYKLIMSERDQVISELDKLQTEV--------ELAESKLK 349
Cdd:PRK03918  172 KEIKRRIERLEKFIK--RTENIEELiKEKEKELEE---VLREINEISSELPELREELEKLEKEVkeleelkeEIEELEKE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  350 SSTSEKKAANEEmEALRQIKDTVTmdagRANKEVEILRKQCKALcQELKEALQEADVAKcrrdwafQERDKIVAERDSIR 429
Cdd:PRK03918  247 LESLEGSKRKLE-EKIRELEERIE----ELKKEIEELEEKVKEL-KELKEKAEEYIKLS-------EFYEEYLDELREIE 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  430 TLCDNLRRER---DRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHDSAIDTDSMEWET 506
Cdd:PRK03918  314 KRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL 393

                         250
                  ....*....|....*
gi 767964245  507 EVVEFERE--TEDID 519
Cdd:PRK03918  394 EELEKAKEeiEEEIS 408
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 233-514 1.78e-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: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   233 NQRLLKQTEMLTQQRDTaiqLQHQCALSLR----RFEAIHHElnkataqnkDLQWEMELLQSELTELRTTQvktakESEK 308
Cdd:pfam17380  261 NGQTMTENEFLNQLLHI---VQHQKAVSERqqqeKFEKMEQE---------RLRQEKEEKAREVERRRKLE-----EAEK 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   309 YR----EERDAVYSEYKLIMSERDQvisELDKLQTEvelaesklksstsEKKaanEEMEALRQIKDTVTMDAGRANKEVE 384
Cdd:pfam17380  324 ARqaemDRQAAIYAEQERMAMERER---ELERIRQE-------------ERK---RELERIRQEEIAMEISRMRELERLQ 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   385 ILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKivaERDSIRTLCDNLRRERDRAVSElaEALRSLDDTRKQKNDVS 464
Cdd:pfam17380  385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKV---EMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQERQ 459

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245   465 RELKELKEQMESQ------LEKEARFRQLmAHSSHDSAIDTDSMEWETEVVEFERE 514
Cdd:pfam17380  460 QQVERLRQQEEERkrkkleLEKEKRDRKR-AEEQRRKILEKELEERKQAMIEEERK 514
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 87-295 2.23e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.06  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   87 MSDLQSLQNQHTNALK-----RCEEVAKE--------TDFYHTL------HSRLLSDQTRLKDDVDMLRRENGQLLRERN 147
Cdd:PRK04778  255 EKEIQDLKEQIDENLAlleelDLDEAEEKneeiqeriDQLYDILerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEID 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  148 LLQQSWEdmkrLHEED-------QKEIGDLRAQQQQVLK--HNGS---SEILNKLyDTAMDKLEVVKKDYD-------AL 208
Cdd:PRK04778  335 RVKQSYT----LNESElesvrqlEKQLESLEKQYDEITEriAEQEiaySELQEEL-EEILKQLEEIEKEQEklsemlqGL 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  209 RKrySEKVAihNADLSRLEQLGEENQRLLKQ----------TEMLTQQRDTAIQLQHQcaLSLRRF--EAIHHELNKATA 276
Cdd:PRK04778  410 RK--DELEA--REKLERYRNKLHEIKRYLEKsnlpglpedyLEMFFEVSDEIEALAEE--LEEKPInmEAVNRLLEEATE 483

                         250       260
                  ....*....|....*....|.
gi 767964245  277 QNKDLQWEMELL--QSELTEL 295
Cdd:PRK04778  484 DVETLEEETEELveNATLTEQ 504
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 1247-1298 2.43e-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: 2.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245 1247 PLGISIVS----GEKGGIYVSKVT-VGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06717    11 FLGISIVGqsneRGDGGIYVGSIMkGGAVAADGRIEPGDMILQVNDISFENMSNDDA 67
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 626-692 2.49e-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: 2.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  626 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLkvfpqssSWSG 692
Cdd:cd06680    30 FFVKSIVPGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTVV-------SWPG 89
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 1239-1302 2.50e-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: 2.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1239 VKVQKGSEPLGISIVSGEK-----GGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1302
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; ...
 626-685 2.60e-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: 2.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  626 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 685
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 ...
 1239-1298 2.66e-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: 44.31  E-value: 2.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1239 VKVQKGSEPLGISIVSG------EKG----GIYVSKVT-VGSIAHQAGLEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06715     5 VVLHRENGSLGFNIIGGrpcennQEGssseGIYVSKIVeNGPAADEGGLQVHDRIIEVNGKDLSKATHEEA 75
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 614-678 2.66e-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: 2.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245  614 GQKDSGiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd23072    21 GGEKSG-RLDLGIFISSITPGGPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTL 84
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 1237-1301 3.09e-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: 3.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245 1237 RHVKVQKGSEPLGISIvSGEKGGIyVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSAT-EQQARLI 1301
Cdd:cd06710     1 RTVEIARGRAGYGFTI-SGQAPCV-LSCVVRGSPADVAGLKAGDQILAVNGINVSKAShEDVVKLI 64
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1238-1311 3.15e-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: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1238 HVKVQKG-SEPLGISIV---SGEKG--GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSA-TEQQARLIIGQQCDTI 1309
Cdd:cd06689    17 YIELEKPeSGGLGFSVVglkSENRGelGIFVQEIQPGSVAARDGrLKENDQILAINGQPLDQSiSHQQAIAILQQAKGSV 96


                  ..
gi 767964245 1310 TI 1311
Cdd:cd06689    97 EL 98
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 523-594 3.16e-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: 3.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  523 LGFDMAEGvnepcfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 594
Cdd:cd23060    12 LGFSLVGG------EGGSGIFVKSISPGGVAdrDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 625-672 3.25e-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: 3.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767964245  625 GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE-CESLLRSC 672
Cdd:cd06714    39 GAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEvQDIISQSK 87
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 325-489 3.37e-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: 48.22  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  325 SERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEAL--------RQIKDT------VTMDAGRANKEVEILRKQC 390
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriaalaRRIRALeqelaaLEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  391 KALCQELKEALQEADVAKCRRDWAF-------------------------QERDKIVAERDSIRTLCDNLRRERDR---A 442
Cdd:COG4942   100 EAQKEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaparrEQAEELRADLAELAALRAELEAERAEleaL 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767964245  443 VSELAEALRSLDDTRKQKNDV----SRELKELKEQMESQLEKEARFRQLMA 489
Cdd:COG4942   180 LAELEEERAALEALKAERQKLlarlEKELAELAAELAELQQEAEELEALIA 230
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 40-364 3.50e-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: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   40 QLRLMTRERNELRKRLAFAthgtAFDKRPYHRL----------------NPDYERLKIQCVRAMSDLQSLQNQHTNALKR 103
Cdd:COG3096   786 RLEELRAERDELAEQYAKA----SFDVQKLQRLhqafsqfvgghlavafAPDPEAELAALRQRRSELERELAQHRAQEQQ 861

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  104 CEEVAKETDFYHTLHSRLLSDQTRLKDD-----VDMLRRENGQLLRERNLLQQSWEDMKRLheEDQKEIgdLRAQQQQVl 178
Cdd:COG3096   862 LRQQLDQLKEQLQLLNKLLPQANLLADEtladrLEELREELDAAQEAQAFIQQHGKALAQL--EPLVAV--LQSDPEQF- 936

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  179 khngssEILNKLYDTAMDKLEVVKKDYDAL---RKR-----YSEKVAIHNADLSRLEQLgeeNQRLLKQTEMLTQQRDTA 250
Cdd:COG3096   937 ------EQLQADYLQAKEQQRRLKQQIFALsevVQRrphfsYEDAVGLLGENSDLNEKL---RARLEQAEEARREAREQL 1007

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  251 IQLQHQCALSLRRFEAIhhelnKATAQNKdlqweMELLQSELTELRTTQVKTAKESE-KYREERDAVYSEYKLIMSERDQ 329
Cdd:COG3096  1008 RQAQAQYSQYNQVLASL-----KSSRDAK-----QQTLQELEQELEELGVQADAEAEeRARIRRDELHEELSQNRSRRSQ 1077

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 767964245  330 VISELDKLQTEVELAESKLKSSTSEKKAANEEMEA 364
Cdd:COG3096  1078 LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
Filament pfam00038
Intermediate filament protein;
276-480 3.65e-05

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 47.99  E-value: 3.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   276 AQNKDLQWEMELLQsELTELRTTQVKTAKESEkYREERDAVYSeyklIMSERDQVISELDKLQTEVELAESKLKSSTSEK 355
Cdd:pfam00038   25 QQNKLLETKISELR-QKKGAEPSRLYSLYEKE-IEDLRRQLDT----LTVERARLQLELDNLRLAAEDFRQKYEDELNLR 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   356 KAANEEMEALRQIKDTVTMdagraNKeVEiLRKQCKALCQELK--EALQEADVAKCRRDWAFQERdkiVAERDSIRTLcd 433
Cdd:pfam00038   99 TSAENDLVGLRKDLDEATL-----AR-VD-LEAKIESLKEELAflKKNHEEEVRELQAQVSDTQV---NVEMDAARKL-- 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 767964245   434 nlrrerdravsELAEALRsldDTRKQKND-VSRELKELKEQMESQLEK 480
Cdd:pfam00038  167 -----------DLTSALA---EIRAQYEEiAAKNREEAEEWYQSKLEE 200
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 619-664 3.75e-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: 3.75e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767964245  619 GISLEN--GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNE 664
Cdd:cd06718    20 GNGVERvpGIFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDD 67
PTZ00121 PTZ00121
MAEBL; Provisional
 154-483 3.77e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  154 EDMKRLHEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEkvAIHNADlsRLEQLGEEN 233
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKK---AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--AKKKAD--AAKKKAEEK 1390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  234 QRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIH--HELNKATAQNKDLQwemELLQSELTELRTTQVKTAKESEKYRE 311
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKkaEEKKKADEAKKKAE---EAKKADEAKKKAEEAKKAEEAKKKAE 1467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  312 ERDAVYSEYKliMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANE--------EMEALRQIKDTVTMDAGRANKEV 383
Cdd:PTZ00121 1468 EAKKADEAKK--KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaeeakKADEAKKAEEAKKADEAKKAEEK 1545

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  384 EILRKQCKAlcQELKEALQEADVAKCRRDwafQERDKIVAERDSIRTLCDNLRRERDRAVSEL-----AEALRSLDDTRK 458
Cdd:PTZ00121 1546 KKADELKKA--EELKKAEEKKKAEEAKKA---EEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmkAEEAKKAEEAKI 1620

                         330       340
                  ....*....|....*....|....*..
gi 767964245  459 QKNDVSRELKELK--EQMESQLEKEAR 483
Cdd:PTZ00121 1621 KAEELKKAEEEKKkvEQLKKKEAEEKK 1647
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 610-681 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 767964245  610 INLSGQKDSGIslengvYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
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 ...
 623-678 4.09e-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: 4.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIalDNKSLNECESLLRSCQDSLTL 678
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 ...
 614-678 4.16e-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: 4.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  614 GQKDSGISL--ENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06744     7 GNGSFGFTLrgHAPVYIESVDPGSAAERAG-LKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMPTL 72
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 110-490 4.20e-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: 48.81  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   110 ETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngSSEILNK 189
Cdd:TIGR00618  174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ------SHAYLTQ 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   190 LYDTAMDKlevvkkdyDALRKRYSEKVAihnadlsRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcalslrrfEAIHH 269
Cdd:TIGR00618  248 KREAQEEQ--------LKKQQLLKQLRA-------RIEELRAQEAVLEETQERINRARKAAPLAAHI--------KAVTQ 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   270 ELNKATAQNKDLQWEMELLQSELTElRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELaESKLK 349
Cdd:TIGR00618  305 IEQQAQRIHTELQSKMRSRAKLLMK-RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIH 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   350 SSTSEKKAANEEMEALRQIKDTVTmdagrankeveilRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIR 429
Cdd:TIGR00618  383 TLQQQKTTLTQKLQSLCKELDILQ-------------REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITC 449

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245   430 TLCDNLRRERdravsELAEALRSLddtrkqkndvsRELKELKEQMESQLEKEARFRQLMAH 490
Cdd:TIGR00618  450 TAQCEKLEKI-----HLQESAQSL-----------KEREQQLQTKEQIHLQETRKKAVVLA 494
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 623-678 4.31e-05

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


Pssm-ID: 467176 [Multi-domain]  Cd Length: 102  Bit Score: 44.16  E-value: 4.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALD-NKSLNECESLLRSCQDSLTL 678
Cdd:cd06689    42 ELGIFVQEIQPGSVAARDGRLKENDQILAINGQPLDqSISHQQAIAILQQAKGSVEL 98
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 523-595 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 767964245   523 LGFDMAEGVNEpcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 595
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 ...
 1261-1312 4.35e-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: 4.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767964245 1261 YVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII--GQQCDTITIL 1312
Cdd:cd23070    39 HVSAVLEGGAADKAGVRKGDRILEVNGVNVEGATHKQVVDLIksGGDELTLTVI 92
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 508-599 4.41e-05

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


Pssm-ID: 467180 [Multi-domain]  Cd Length: 92  Bit Score: 43.92  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  508 VVEFERETEdidlKALGFDMAEGVNEPCFpgDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN 585
Cdd:cd06694     4 IVTLKKDPQ----KGLGFTIVGGENSGSL--DLGIFVKSIIPGGPAdkDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQN 77

                          90
                  ....*....|....
gi 767964245  586 GEGAINMVVRRRKS 599
Cdd:cd06694    78 APDKVELIISQPKS 91
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 125-508 4.48e-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: 48.63  E-value: 4.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   125 QTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQVlkhngsSEILNKLyDTAMDKLEVVKKD 204
Cdd:pfam01576   21 QQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQEL------EEILHEL-ESRLEEEEERSQQ 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   205 YDALRKRYSEkvaiHNADLSrlEQLGEEN---QRLlkQTEMLTqqrdtaiqlqhqCALSLRRFEAihhELNKATAQNKDL 281
Cdd:pfam01576   94 LQNEKKKMQQ----HIQDLE--EQLDEEEaarQKL--QLEKVT------------TEAKIKKLEE---DILLLEDQNSKL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   282 QWEMELLQSELTELRTT---QVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAA 358
Cdd:pfam01576  151 SKERKLLEERISEFTSNlaeEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   359 NEEMEALRQIKDTVTMDA-GRANKEV---EILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRT-LCD 433
Cdd:pfam01576  231 IAELRAQLAKKEEELQAAlARLEEETaqkNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTeLED 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   434 N---------LRRERDRAVSELAEALRslDDTRK---QKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHdsAIDTDS 501
Cdd:pfam01576  311 TldttaaqqeLRSKREQEVTELKKALE--EETRSheaQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ--ALESEN 386


                   ....*..
gi 767964245   502 MEWETEV 508
Cdd:pfam01576  387 AELQAEL 393
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1237-1302 4.64e-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: 43.78  E-value: 4.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1237 RHVKVQKGSEPLGISIVSGEKG-GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1302
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 ...
 541-596 4.75e-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: 4.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  541 GIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKaLLNGEGAINMVVRR 596
Cdd:cd10833    27 GIFVSKVEEGSAAErAGLCVGDKITEVNGVSLENITMSSAVK-VLTGSNRLRMVVRR 82
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 1258-1295 5.16e-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: 5.16e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 767964245 1258 GGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATE 1295
Cdd:cd06785    31 SGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSD 68
PRK01156 PRK01156
chromosome segregation protein; Provisional
 71-475 5.46e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 48.36  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   71 RLNPDYERLK--IQCVRA-MSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERN 147
Cdd:PRK01156  163 SLERNYDKLKdvIDMLRAeISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  148 LLQqSWEDMKRLHEEDQKEI-GDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKR---YSEKVAIHNADL 223
Cdd:PRK01156  243 ELS-SLEDMKNRYESEIKTAeSDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDienKKQILSNIDAEI 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  224 SRLEQlgeenqrLLKQTEMLTQQRDTAIQLQhqcalslRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTA 303
Cdd:PRK01156  322 NKYHA-------IIKKLSVLQKDYNDYIKKK-------SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  304 KESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEAL------------------ 365
Cdd:PRK01156  388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeeks 467

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  366 RQIKDTVTMDAGRANKEVEILRKQCKALCQE------LKEALQEADVAKCRRDWAFQE--RDKIVAERDSIRTLCD---- 433
Cdd:PRK01156  468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKivdlkkRKEYLESEEINKSINEYNKIEsaRADLEDIKIKINELKDkhdk 547

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  434 --------------NLRRERDRAVSELAE-ALRSLDDTRKQKNDVSRELKELKEQME 475
Cdd:PRK01156  548 yeeiknrykslkleDLDSKRTSWLNALAViSLIDIETNRSRSNEIKKQLNDLESRLQ 604
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 508-595 5.83e-05

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


Pssm-ID: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 43.20  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  508 VVEFERETEdidlkALGFDMAEGVNEpcfpgDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLN 585
Cdd:cd06796     4 VVELPKTEE-----GLGFNVMGGKEQ-----NSPIYISRIIPGGVADrhGGLKRGDQLLSVNGVSVEGEHHEKAVELLKA 73

                          90
                  ....*....|
gi 767964245  586 GEGAINMVVR 595
Cdd:cd06796    74 AQGSVKLVVR 83
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 1240-1467 5.90e-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: 5.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1240 KVQKGSepLGISI--VSGEK---------GGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARliigqqcdt 1308
Cdd:TIGR02037  230 KVKRGW--LGVTIqeVTSDLakslglekqRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRA--------- 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1309 itilaqynphVHQLsshsrssshldPAGTHSTLQgsgtttpehpsvidplMEQDEGPSTPPAK-QSSSRIAGDANKKTLE 1387
Cdd:TIGR02037  299 ----------IGTL-----------KPGKKVTLG----------------ILRKGKEKTITVTlGASPEEQASSSNPFLG 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  1388 PRVVFIKKSQLELGVHlcGGNLHGVFVAEVEDDSPAKGPdGLVPGDLILEYGSLDVRNktVEEVY--VEMLKPRDGVRLK 1465
Cdd:TIGR02037  342 LTVANLSPEIRKELRL--KGDVKGVVVTKVVSGSPAARA-GLQPGDVILSVNQQPVSS--VAELRkvLARAKKGGRVALL 416


                   ..
gi 767964245  1466 VQ 1467
Cdd:TIGR02037  417 IL 418
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 270-483 6.21e-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: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  270 ELNKATAQNKDLQWEMELLQSELTELRttqvktaKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLK 349
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQ-------AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  350 ---SSTSEKKAANEEMEALRQIKDTVTMdAGRANKeVEILRKQCKALCQELKEALQEADvakcrrdwafQERDKIVAERD 426
Cdd:COG3883    90 eraRALYRSGGSVSYLDVLLGSESFSDF-LDRLSA-LSKIADADADLLEELKADKAELE----------AKKAELEAKLA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  427 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEAR 483
Cdd:COG3883   158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 1244-1298 6.25e-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: 6.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245 1244 GSEPLGISIVSGE--------KGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd23063     8 EKKSFGICIVRGEvkvspntkTTGIFIKGIIPDSPAHKCGrLKVGDRILSVNGNDVRNSTEQAA 71
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 30-478 6.26e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.89  E-value: 6.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    30 VNEKVENLSIQLRLMTRERNELRKRLAFATHGTAFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQ------HTNALKr 103
Cdd:pfam10174  252 LEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQnsdckqHIEVLK- 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   104 cEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQLLR---ERNLLQQSWEDMKRLHEEDQKEIGDLRAQ---QQQV 177
Cdd:pfam10174  331 -ESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDlteEKSTLAGEIRDLKDMLDVKERKINVLQKKienLQEQ 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   178 LKH-----NGSSEILNKLY------DTAMDKLEVVKKDYDALRKRYSEKVAIHN-ADLSRLEQLGEENQRLLKQTEML-- 243
Cdd:pfam10174  410 LRDkdkqlAGLKERVKSLQtdssntDTALTTLEEALSEKERIIERLKEQREREDrERLEELESLKKENKDLKEKVSALqp 489

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   244 --TQQRDTAIQLQHQcALSLRRfeaihhELNKATAQNKDLQWEMELLQSELTELRTtQVKTAKESEKYREERDAVYSEYK 321
Cdd:pfam10174  490 elTEKESSLIDLKEH-ASSLAS------SGLKKDSKLKSLEIAVEQKKEECSKLEN-QLKKAHNAEEAVRTNPEINDRIR 561

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   322 LIMSERDQVISELDKLQTEVE-----LAESKLKSSTSEKKAANEEMEALRQIKDTVT-----------MDAGRANKEVEI 385
Cdd:pfam10174  562 LLEQEVARYKEESGKAQAEVErllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKkvanikhgqqeMKKKGAQLLEEA 641

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   386 LR-----------KQCKALCQELKEALQEADVAKCRrdwaFQERDKIVAERDSIRTlcdNLRRERDRAVSELAE------ 448
Cdd:pfam10174  642 RRrednladnsqqLQLEELMGALEKTRQELDATKAR----LSSTQQSLAEKDGHLT---NLRAERRKQLEEILEmkqeal 714

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 767964245   449 -----------ALRSLDDTRKQKND-----VSRE----LKELKEQMESQL 478
Cdd:pfam10174  715 laaisekdaniALLELSSSKKKKTQeevmaLKREkdrlVHQLKQQTQNRM 764
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 523-596 6.27e-05

PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of TAX1BP3, and related domains. TAX1BP3 (also known as glutaminase-interacting protein 3, tax interaction protein 1, TIP-1, tax-interacting protein 1) may regulate a number of protein-protein interactions by competing for PDZ domain binding sites. TAX1BP3 binds beta-catenin and may act as an inhibitor of the Wnt signaling pathway. It competes with LIN7A (also known as Lin-7A or LIN-7A) for inward rectifier potassium channel 4 (KCNJ4) binding, and thereby promotes KCNJ4 internalization. It may play a role in the Rho signaling pathway, and in the activation of CDC42 by the viral protein HPV16 E6. Binding partners of the TAX1BP3 PDZ domain include beta-catenin, KCNJ4, glutaminase liver isoform (GLS2), rho guanine nucleotide exchange factor 16 (ARHGEF16), rhotekin, and CDK5 regulatory subunit-associated protein 3 (also known as LAPZ). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This TAX1BP3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467265 [Multi-domain]  Cd Length: 94  Bit Score: 43.48  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  523 LGFDMAEGVNE-----PCFPGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 596
Cdd:cd10822    15 LGFSIGGGIDQdpsknPFSYTDKGIYVTRVSEGGPAEkAGLQVGDKILQVNGWDMTMVTHKQAVKRLTKKKPVLRMLVTR 94
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 605-672 6.54e-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: 6.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  605 VTPLHINLSGQKDSGisLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 672
Cdd:cd06717     9 VNFLGISIVGQSNER--GDGGIYVGSIMKGGAVAADGRIEPGDMILQVNDISFENMSNDDAVRVLREA 74
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 1389-1468 6.55e-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: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1389 RVVFIKKSQLE-LGVHLCGGNLHGV--FVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVyVEMLKPRDG-VRL 1464
Cdd:cd06800     1 RKVLLSKEPHEgLGISITGGKEHGVpiLISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEA-VTILSQQRGeITL 79


                  ....
gi 767964245 1465 KVQY 1468
Cdd:cd06800    80 EVVY 83
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 1390-1457 6.60e-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: 6.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1390 VVFIKKSQLELGVHLCGgnlHG-VFVAEVEDDSPAKGPdGLVPGDLILEYGSLDVRNKTVEEVyVEMLK 1457
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), ...
 542-596 6.98e-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: 6.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  542 IFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 596
Cdd:cd23068    27 LSIQKVNPGSPADKAgLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 56-494 7.14e-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: 48.04  E-value: 7.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    56 AFATHGTAFDKRPYHRLNPDYERLKIQCvRAMSDLQSLQNQhTNALKRCEEVAKETDFYHTLHSRLLSDQtrlkDDVDML 135
Cdd:TIGR00618  185 EFAKKKSLHGKAELLTLRSQLLTLCTPC-MPDTYHERKQVL-EKELKHLREALQQTQQSHAYLTQKREAQ----EEQLKK 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   136 RRENGQLLRErnllQQSWEDMKRLHEEDQKEIgDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVvkkdydalRKRYSEK 215
Cdd:TIGR00618  259 QQLLKQLRAR----IEELRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQIEQQAQRIHTELQS--------KMRSRAK 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   216 VAIHNADLSRLEQLGEENQRLLKQTemltQQRDTAIQLQHQCALSLR-RFEAIHHELNKATAQNKDLQWEMELLQSELTE 294
Cdd:TIGR00618  326 LLMKRAAHVKQQSSIEEQRRLLQTL----HSQEIHIRDAHEVATSIReISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   295 LRTTQVKTAKESEKYREERDAvysEYKLIMSERDQVISELDKLQTEVELAEsKLKSSTSEKKAANEEMEALRQIKDTVtm 374
Cdd:TIGR00618  402 LDILQREQATIDTRTSAFRDL---QGQLAHAKKQQELQQRYAELCAAAITC-TAQCEKLEKIHLQESAQSLKEREQQL-- 475

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   375 dagrANKEVEILR-KQCKALCQELKEALQEADVAKCRrdwafQERDKIVAERDSIRTLCDNLRRERdrAVSELAEALRSL 453
Cdd:TIGR00618  476 ----QTKEQIHLQeTRKKAVVLARLLELQEEPCPLCG-----SCIHPNPARQDIDNPGPLTRRMQR--GEQTYAQLETSE 544

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 767964245   454 DDTRKQKNDVSRELKELKEQMESQLEKEARFRQLMAHSSHD 494
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 1237-1312 7.34e-05

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


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 42.81  E-value: 7.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1237 RHVKVQKGSEPLGISiVSGEKG--GIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
Cdd:cd06768     1 RLCHLVKGPEGYGFN-LHAEKGrpGHFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQVVEKIKASGNQVTLL 77
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 629-678 7.69e-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: 7.69e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767964245   629 AAVLPGSPAAKEGsLAVGDRIVAINGIALdnKSLNECESLLRSCQDSLTL 678
Cdd:pfam17820    3 TAVVPGSPAERAG-LRVGDVILAVNGKPV--RSLEDVARLLQGSAGESVT 49
PDZ_Dishevelled-like cd06717
PDZ domain of segment polarity protein dishevelled homolog DVL1, DVL2, DVL3, and related ...
 538-583 8.18e-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: 8.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767964245  538 GDCGIFVTKVDKGSI--ADGRLRVNDWLLRINDVDLINKDKKQAIKAL 583
Cdd:cd06717    24 GDGGIYVGSIMKGGAvaADGRIEPGDMILQVNDISFENMSNDDAVRVL 71
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 616-681 8.97e-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: 8.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  616 KDSGISLENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKslNECESLLRSCQ--DSLTLSLL 681
Cdd:cd06779    17 KELGLPVNRGVLVAEVIPGSPAAKAG-LKEGDVILSVNGKPVTSF--NDLRAALDTKKpgDSLNLTIL 81
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 1485-1543 8.98e-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: 8.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1485 YIRALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWmaWQ--LDENAQKIQRGQIPSKY 1543
Cdd:cd11883     1 VVVALYDFTPKSKNQLSFKAGDIIYVLNKDPSG----W--WDgvIISSSGKVKRGWFPSNY 55
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 537-596 9.47e-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: 9.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  537 PGDCGIFVTKV-DKG-SIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGE--GAINMVVRR 596
Cdd:cd23058    29 GGSGPIYIKNIlPKGaAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTKlgGTVSLVVSR 92
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 1239-1301 9.69e-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: 9.69e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245 1239 VKVQKGSEPLGISIVSGEKggIYVSKVTVGSIAHQAGLEYGDQLLEFNGINL-RSATEQQARLI 1301
Cdd:cd06711     3 ITIQRGKDGFGFTICDDSP--VRVQAVDPGGPAEQAGLQQGDTVLQINGQPVeRSKCVELAHAI 64
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
629-664 9.87e-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: 9.87e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 767964245  629 AAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNE 664
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) ...
 1235-1298 9.89e-05

PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467157 [Multi-domain]  Cd Length: 98  Bit Score: 42.99  E-value: 9.89e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1235 EPRHVKVQKGSEPLGISI------VSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06669     7 EVTVIELEKGDRGLGFSIldyqdpLDPSETVIVIRSLVPGGVAEQDGrLLPGDRLVFVNDVSLENASLDEA 77
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 1237-1311 1.02e-04

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


Pssm-ID: 467266 [Multi-domain]  Cd Length: 81  Bit Score: 42.54  E-value: 1.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245 1237 RHVKVQKGS-EPLGISIVSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1311
Cdd:cd10830     1 RLVQFEKNTeEPMGITLKLNEKQSCIVARILHGGMIHRQGsLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVSL 77
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 594-680 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 767964245  594 VRRRKSLGGkvvtpLHINLSGQKDSGISLENG--VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 671
Cdd:cd06695     4 VKLTKGSSG-----LGFSFLGGENNSPEDPFSglVRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSLLRG 78


                  ....*....
gi 767964245  672 CQDSLTLSL 680
Cdd:cd06695    79 APPEVTLLL 87
SH3_CAS cd11844
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins ...
 1487-1523 1.32e-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: 41.18  E-value: 1.32e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767964245 1487 RALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWM 1523
Cdd:cd11844     3 RALYDNVAESPDELAFRRGDILTVLEQNTAGLEGWWL 39
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 505-594 1.32e-04

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


Pssm-ID: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 42.31  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  505 ETEVVEFERETEdidlkALGFDMAEGvnepcfpGDCGIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKAL 583
Cdd:cd06767     2 EPRHVSIEKGSE-----PLGISIVSG-------ENGGIFVSSVTEGSLAHqAGLEYGDQLLEVNGINLRNATEQQAALIL 69

                          90
                  ....*....|.
gi 767964245  584 LNGEGAINMVV 594
Cdd:cd06767    70 RQCGDTITMLV 80
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
 1237-1300 1.33e-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: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245 1237 RHVKVQK-GSEPLGIsIVSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARL 1300
Cdd:cd10832     1 RMVGIRKnPGEPLGV-TVRLEEGELVIARILHGGMIDRQGlLHVGDIIKEVNGVPVGSPEQLQEML 65
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 227-483 1.40e-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: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  227 EQLGEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKES 306
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  307 EKYREE-RDAVYSEYKLIMSERDQVISEldklQTEVELAESKLKSSTSEKKAANEEMEALRQIKdtvtmdagranKEVEI 385
Cdd:COG4942   100 EAQKEElAELLRALYRLGRQPPLALLLS----PEDFLDAVRRLQYLKYLAPARREQAEELRADL-----------AELAA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  386 LRKQCKALCQELKEALQEADvakcrrdwafQERDKIVAERDsirtlcdnlrrERDRAVSELAEALRSLDDTRKQKNDVSR 465
Cdd:COG4942   165 LRAELEAERAELEALLAELE----------EERAALEALKA-----------ERQKLLARLEKELAELAAELAELQQEAE 223

                         250
                  ....*....|....*...
gi 767964245  466 ELKELKEQMESQLEKEAR 483
Cdd:COG4942   224 ELEALIARLEAEAAAAAE 241
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 631-682 1.44e-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: 1.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767964245  631 VLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLK 682
Cdd:cd23068    32 VNPGSPADKAG-LRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQR 82
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
360-489 1.56e-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: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  360 EEMEALRQIKDTVT--MDAGRANKEVEILRKQCKAL------CQELKEALQEADVAKCRRDW-----AFQERDKIVAERD 426
Cdd:COG4913   219 EEPDTFEAADALVEhfDDLERAHEALEDAREQIELLepirelAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELE 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245  427 SIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVS--------RELKELKEQMESQLEKEARFRQLMA 489
Cdd:COG4913   299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLA 369
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 220-491 1.56e-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: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   220 NADLSRLEQLGEENQRL------LKQTEMLTQQRDTAIQLQHQCALSLRrfEAIHHELNKATAQNKDLQWEMELLQSELT 293
Cdd:pfam15964  296 NVHMQTIERLTKERDDLmsalvsVRSSLAEAQQRESSAYEQVKQAVQMT--EEANFEKTKALIQCEQLKSELERQKERLE 373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   294 ElrttqvKTAKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVT 373
Cdd:pfam15964  374 K------ELASQQEKRAQEKEALRKEMK---KEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQE 444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   374 MDAGRANKEVEILRKQCKALCQELKEALQEADvAKCRRDWAF--QERDKIVAERDSIRTLCDNLRRERDRAVSE------ 445
Cdd:pfam15964  445 MDVTKVCGEMRYQLNQTKMKKDEAEKEHREYR-TKTGRQLEIkdQEIEKLGLELSESKQRLEQAQQDAARAREEclklte 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245   446 -LAEALRSLDDTRKQKNDVSR------------------ELKELKEQMESQLEKEARFRQLMAHS 491
Cdd:pfam15964  524 lLGESEHQLHLTRLEKESIQQsfsneakaqalqaqqreqELTQKMQQMEAQHDKTVNEQYSLLTS 588
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 1239-1298 1.62e-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: 1.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1239 VKVQKGSEPLGISIVSG-------EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06709     3 ITLKRGPSGLGFNIVGGtdqpyipNDSGIYVAKIKEDGAAAIDGrLQEGDKILEINGQSLENLTHQDA 70
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 1487-1545 1.63e-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: 1.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1487 RALYDRLADVEQELSFKKDDILYVDDTLPQGtfgsWmaWQLDENAQKiqrGQIPSKYVM 1545
Cdd:cd11772     3 RALYDYEAQHPDELSFEEGDLLYISDKSDPN----W--WKATCGGKT---GLIPSNYVE 52
PTZ00121 PTZ00121
MAEBL; Provisional
 154-519 1.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  154 EDMKRLHE----EDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTamdKLEVVKKDYDALRKRYSEKVAIHNADLSRLEQL 229
Cdd:PTZ00121 1549 DELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA---RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  230 GEENQrllkqtemltqQRDTAIQLQHQCALSLRRFEAIH--HELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESE 307
Cdd:PTZ00121 1626 KKAEE-----------EKKKVEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  308 KYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILR 387
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  388 KQCKALcqeLKEALQEADvAKCRRDWAFQERD-----KIVAERDSIRTLCDNLRRERDraVSELAEALrsldDTRKQKND 462
Cdd:PTZ00121 1775 KEKEAV---IEEELDEED-EKRRMEVDKKIKDifdnfANIIEGGKEGNLVINDSKEME--DSAIKEVA----DSKNMQLE 1844

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  463 VSRELKELKEQMESQLEKEarfrqlmAHSSHDSAIDTDSMEWETEVVEFERETEDID 519
Cdd:PTZ00121 1845 EADAFEKHKFNKNNENGED-------GNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 608-678 1.66e-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: 1.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245  608 LHINLSGQKDSGISlengVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06800    13 LGISITGGKEHGVP----ILISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITL 79
PDZ7_GRIP1-2-like cd06685
PDZ domain 7 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 1238-1314 1.68e-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: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1238 HVKVQK--GSEPLGISIVSG--EKGgIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1313
Cdd:cd06685     5 KVTLYKdsDTEDFGFSVSDGlyEKG-VYVNAIRPGGPADLSGLQPYDRILQVNHVRTRDFDCCLVVPLIAESGDKLELVV 83


                  .
gi 767964245 1314 Q 1314
Cdd:cd06685    84 S 84
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 606-678 1.70e-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: 1.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245  606 TPLHINLSGQKDsgislENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06795    12 TGLGFNIVGGED-----GEGIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTI 79
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 631-678 1.76e-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: 1.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767964245  631 VLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06801    32 IFKGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTL 79
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 541-595 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 767964245  541 GIFVTKVDKGSIAD--GrLRVNDWLLRINDVDLINKDKKQAIKALLnGEGAINMVVR 595
Cdd:cd06738    28 GIFISNVKPGSLAEevG-LEVGDQIVEVNGTSFTNVDHKEAVMALK-SSRHLTITVR 82
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 135-533 1.85e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.35  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   135 LRRENGQLLRERNLLQQSWEDMKrLHEEDQKEIgdLRAQQQQVLKhngsseILNKLYDTAMDKleVVKKDYDALRKRyse 214
Cdd:pfam10174  121 LQSEHERQAKELFLLRKTLEEME-LRIETQKQT--LGARDESIKK------LLEMLQSKGLPK--KSGEEDWERTRR--- 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   215 kVAIHNADLSRLEQLgeenqrlLKQTEMLTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTE 294
Cdd:pfam10174  187 -IAEAEMQLGHLEVL-------LDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQM 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   295 LRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALrqiKDTVTM 374
Cdd:pfam10174  259 LKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVL---KESLTA 335

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   375 DAGRAN---KEVEILR-----------KQCKALcQELKE--ALQEADVAKCRRDWAFQERdKIVAERDSIRTLCDNLrRE 438
Cdd:pfam10174  336 KEQRAAilqTEVDALRlrleekesflnKKTKQL-QDLTEekSTLAGEIRDLKDMLDVKER-KINVLQKKIENLQEQL-RD 412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   439 RDRAVSELAEALRSLD------DT-------------------RKQKN-----------DVSRELKELKEQMESQ----L 478
Cdd:pfam10174  413 KDKQLAGLKERVKSLQtdssntDTalttleealsekeriierlKEQREredrerleeleSLKKENKDLKEKVSALqpelT 492

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245   479 EKEARFRQLMAHSS--------HDSAIDTDSMEWETEVVEFEReTEDIDLKALGFDMAEGVNE 533
Cdd:pfam10174  493 EKESSLIDLKEHASslassglkKDSKLKSLEIAVEQKKEECSK-LENQLKKAHNAEEAVRTNP 554
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1487-1543 2.09e-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: 2.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245 1487 RALYDRLADVEQELSFKKDDILYVDDTlpqgTFGSWmaWqLDENAQKIQRGQIPSKY 1543
Cdd:cd11845     3 VALYDYEARTDDDLSFKKGDRLQILDD----SDGDW--W-LARHLSTGKEGYIPSNY 52
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 197-475 2.17e-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: 46.37  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   197 KLEVVKKDYDALR---KRYSEKVAIHNADLSRLeQLGEENQRllkqtEMLTQQRDTAIQL--QHQcALSLRRFEAIHHEL 271
Cdd:pfam12128  605 RLDKAEEALQSARekqAAAEEQLVQANGELEKA-SREETFAR-----TALKNARLDLRRLfdEKQ-SEKDKKNKALAERK 677

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   272 NKATAQNKDLQWEMELLQSELtelrttQVKTAKESEKYREERDAVYSEYKLIMSERDqviSELDKLQTEVELAESKLKSs 351
Cdd:pfam12128  678 DSANERLNSLEAQLKQLDKKH------QAWLEEQKEQKREARTEKQAYWQVVEGALD---AQLALLKAAIAARRSGAKA- 747

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   352 tsekkaaneEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWA----FQERDKIVAE--- 424
Cdd:pfam12128  748 ---------ELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYqetwLQRRPRLATQlsn 818

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767964245   425 -RDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQME 475
Cdd:pfam12128  819 iERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 625-680 2.23e-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: 2.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  625 GVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQdSLTLSL 680
Cdd:cd06740    28 GIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKILRVSK-KLVLSV 81
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 593-678 2.32e-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: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  593 VVRRRKSLGgkvvtPLHINLSGQKDS-----GISlENGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECES 667
Cdd:cd06702     2 EIHLVKAGG-----PLGLSIVGGSDHsshpfGVD-EPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVS 74

                          90
                  ....*....|.
gi 767964245  668 LLRSCQDSLTL 678
Cdd:cd06702    75 ALLSPGQEIKL 85
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 ...
 606-661 2.38e-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: 2.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  606 TPLHINLSGQKD-SGISlengVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKS 661
Cdd:cd06672    11 SGLGLSLAGNKDrSRMS----VFVVGIDPDGAAGKDGRIQVGDELLEINGQVLYGRS 63
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 77-487 2.40e-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: 45.89  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    77 ERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDdvdmlrrengqlLRERNLLQQSWEDM 156
Cdd:pfam05557  121 QRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE------------LEFEIQSQEQDSEI 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   157 KRLHEEDQKEIGDLRAQQQQVLKHN-------GSSEILN--------KLY--DTAMDKLEVVKKDYDALRKRYSEKVAI- 218
Cdd:pfam05557  189 VKNSKSELARIPELEKELERLREHNkhlneniENKLLLKeevedlkrKLEreEKYREEAATLELEKEKLEQELQSWVKLa 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   219 --HNADL-------SRLEQLGEENQRLLKQTEMLTQQ----RDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEM 285
Cdd:pfam05557  269 qdTGLNLrspedlsRRIEQLQQREIVLKEENSSLTSSarqlEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   286 ELL--------------QSELTELRTTQVKTA--KESEKYREERDAVYSEYKLIMSE-RDQVISELDKLQT-EVELAESK 347
Cdd:pfam05557  349 LLLtkerdgyrailesyDKELTMSNYSPQLLEriEEAEDMTQKMQAHNEEMEAQLSVaEEELGGYKQQAQTlERELQALR 428

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   348 LKSSTSEKKAANEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDS 427
Cdd:pfam05557  429 QQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEK 508

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   428 IRTLCDNLRReRDRAVSELAEALRSLDDTRKQKNDvsRELKELKEQMESqleKEARFRQL 487
Cdd:pfam05557  509 LQAEIERLKR-LLKKLEDDLEQVLRLPETTSTMNF--KEVLDLRKELES---AELKNQRL 562
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 1389-1460 2.43e-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: 2.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245 1389 RVVFIKKSQLELGVHLCGGN----LHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRD 1460
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 ...
 1239-1302 2.43e-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: 2.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245 1239 VKVQKGSEPLGISIvSGEKGG----IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1302
Cdd:cd06672     4 IELEKGSSGLGLSL-AGNKDRsrmsVFVVGIDPDGAAGKDGrIQVGDELLEINGQVLYGRSHLNASAII 71
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 541-596 2.48e-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: 2.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  541 GIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKaLLNGEGAINMVVRR 596
Cdd:cd06741    27 GIYVTGVDPGSVAENAgLKVGDQILEVNGRSFLDITHDEAVK-ILKSSKHLIMTVKD 82
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 1261-1312 2.53e-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: 2.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767964245  1261 YVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSaTEQQARLIIGQQCDTITIL 1312
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRS-LEDVARLLQGSAGESVTLT 51
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 71-373 2.72e-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: 45.78  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    71 RLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTRLKDDVDMLRRENGQL-------L 143
Cdd:TIGR04523  339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdeqikklQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   144 RERNLLQQSWEDMKRLHEEDQKEIGDLRAQ----QQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVaih 219
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE--- 495

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   220 nadlSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHQcaLSLR------------------------------------R 263
Cdd:TIGR04523  496 ----KELKKLNEEKKELEEKVKDLTKKISSLKEKIEK--LESEkkekeskisdledelnkddfelkkenlekeideknkE 569

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   264 FEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVEL 343
Cdd:TIGR04523  570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649

                          330       340       350
                   ....*....|....*....|....*....|
gi 767964245   344 AESKLksstseKKAANEEMEALRQIKDTVT 373
Cdd:TIGR04523  650 IKETI------KEIRNKWPEIIKKIKESKT 673
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 606-686 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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  606 TPLHINLSGQKDSGISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLsLLKVFP 685
Cdd:cd06691    15 GPLGIHVVPFSSSLSGRTLGLLIRGIEEGSRAERDGRFQENDCIVEINGVDLIDKSFEQAQDIFRQAMRSPEV-KLHVVP 93


                  .
gi 767964245  686 Q 686
Cdd:cd06691    94 A 94
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 325-489 3.01e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  325 SERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALR-QIKDTVTmDAGRANKEVEILRKQCKALCQELKEALQE 403
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQaELEALQA-EIDKLQAEIAEAEAEIEERREELGERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  404 ADVAKCRRDW-----------AFQER----DKIV-AERDSIRTLcdnlrrERDRAvsELAEALRSLDDTRKQKNDVSREL 467
Cdd:COG3883    95 LYRSGGSVSYldvllgsesfsDFLDRlsalSKIAdADADLLEEL------KADKA--ELEAKKAELEAKLAELEALKAEL 166

                         170       180
                  ....*....|....*....|...
gi 767964245  468 KELKEQMESQL-EKEARFRQLMA 489
Cdd:COG3883   167 EAAKAELEAQQaEQEALLAQLSA 189
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 608-671 3.02e-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: 3.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  608 LHINLSGQKDSGIslenGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRS 671
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 ...
 596-657 3.05e-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: 3.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245  596 RRKSLGGKVVtplhinlsGQKDSgISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIAL 657
Cdd:cd06759    10 GGKGLGFSIV--------GGRDS-PRGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESL 62
fliJ PRK07720
flagellar biosynthesis chaperone FliJ;
198-337 3.14e-04

flagellar biosynthesis chaperone FliJ;


Pssm-ID: 181091 [Multi-domain]  Cd Length: 146  Bit Score: 42.75  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  198 LEVVKKDYDALRKRYSEKVaihnadlSRLEQLGEENQRLLKQTEMLTQQRDTAIQ-------LQHQCALSLRRFEAIHHe 270
Cdd:PRK07720   11 LELKENEKEKALGEYEEAV-------SRFEQVAEKLYELLKQKEDLEQAKEEKLQsglsiqeIRHYQQFVTNLERTIDH- 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  271 LNKATAQNKDlqwEMELLQSELTELRTtqvktakESEKYREERDAVYSEYKLIMSERDQviSELDKL 337
Cdd:PRK07720   83 YQLLVMQARE---QMNRKQQDLTEKNI-------EVKKYEKMKEKKQEMFALEEKAAEM--KEMDEI 137
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 ...
 534-596 3.26e-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: 3.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  534 PCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN-GEGAINMVVRR 596
Cdd:cd06760    25 PLENDIPGIFIHHLSPGSVAhmDGRLRRGDQILEINGTSLRNVTLNEAYAILSQcKPGPVTLIISR 90
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 629-659 3.31e-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: 3.31e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767964245  629 AAVLPGSPAAKEGsLAVGDRIVAINGIALDN 659
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 ...
 619-671 3.51e-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: 3.51e-04
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                  ....*....|....*....|....*....|....*....|....*....|....
gi 767964245  619 GISLEN-GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 671
Cdd:cd06762    21 GSDLENkSITVHRVFPSGLAAQEGTIQKGDRILSINGKSLKGVTHGDALSVLKQ 74
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 1257-1311 3.78e-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: 3.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767964245 1257 KGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITI 1311
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 ...
 521-596 3.83e-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: 3.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  521 KALGFDMAEGVNEPcfpgdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 596
Cdd:cd06678    11 EQLGIKLVRKKDEP------GVFILDLLEGGLAarDGRLKSDDRVLAINGQDLRHGTPEQAAQIIQASGERVHFVVSR 82
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 1254-1314 4.15e-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: 4.15e-04
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                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1254 SGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQ 1314
Cdd:cd10820    18 SEQKKPLQVAKIRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 607-673 4.19e-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: 4.19e-04
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  607 PLHINLSGQKDSgisleNGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQ 673
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 ...
 1239-1294 4.34e-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: 4.34e-04
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                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245 1239 VKVQKGSEPLGISIVSgeKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSAT 1294
Cdd:cd06744     2 VRVYRGNGSFGFTLRG--HAPVYIESVDPGSAAERAGLKPGDRILFLNGLDVRNCS 55
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 591-685 4.51e-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: 4.51e-04
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gi 767964245  591 NMVVRRRKSlggkvVTPLHINLSGQKDSGIslenGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLR 670
Cdd:cd06752     1 RTVVLKRPP-----GEQLGFNIRGGKASGL----GIFISKVIPDSDAHRLG-LKEGDQILSVNGVDFEDIEHSEAVKVLK 70

                          90
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gi 767964245  671 ScqdSLTLSL-LKVFP 685
Cdd:cd06752    71 T---AREIQMrVRYFP 83
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 516-596 4.53e-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: 4.53e-04
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gi 767964245  516 EDIDL----KALGFDMAEGVNEpcfpgdcGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGA 589
Cdd:cd06667     1 EVIELvndgSGLGFGIVGGKST-------GVVVKTILPGGVAdrDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSH 73


                  ....*..
gi 767964245  590 INMVVRR 596
Cdd:cd06667    74 VRLVVAR 80
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 613-657 4.60e-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: 4.60e-04
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gi 767964245  613 SGQKDSGIslengvYAAAVLPGSPAAKEGSLAVGDRIVAINGIAL 657
Cdd:cd06789    25 AGQDKLGI------YIKSVVKGGAADLDGRLQAGDQLLSVDGHSL 63
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 144-407 4.88e-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: 45.11  E-value: 4.88e-04
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gi 767964245   144 RERNLLQQSWEDMKRLHEedqkeigdlRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKrysekvaihnadl 223
Cdd:pfam17380  346 RERELERIRQEERKRELE---------RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARK------------- 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   224 srLEQLGEENQRLLKQT----EMLTQQRDTAIQLQhqcalsLRRFEAIH-HELNKATAQNKDLQWEMELLQSELTELRTT 298
Cdd:pfam17380  404 --VKILEEERQRKIQQQkvemEQIRAEQEEARQRE------VRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRK 475

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   299 QVKTAKESEKYRE---------ERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIK 369
Cdd:pfam17380  476 KLELEKEKRDRKRaeeqrrkilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555

                          250       260       270       280
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gi 767964245   370 DTVtMDAGRANKEVEILRKQCKALCQ--ELKEALQEADVA 407
Cdd:pfam17380  556 EQM-RKATEERSRLEAMEREREMMRQivESEKARAEYEAT 594
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 607-680 4.98e-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: 4.98e-04
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gi 767964245  607 PLHINLS-GQKDSGISLENG--VYAAAVLPGSPAAKEGsLAVGDRIVAINGiaLDNK--SLNECESLLRSC-QDSLTLSL 680
Cdd:cd06712     1 PRTVHLTkEEGGFGFTLRGDspVQVASVDPGSCAAEAG-LKEGDYIVSVGG--VDCKwsKHSEVVKLLKSAgEEGLELQV 77
PDZ3_harmonin cd06739
PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic ...
 607-675 5.02e-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: 5.02e-04
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gi 767964245  607 PLHINLSGQKDSgiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDS 675
Cdd:cd06739    13 PLDLALEGGIDS--PLGGKIVVSAVYEGGAADKHGGIVKGDQIMMVNGKSLTDVTLAEAEAALQRAMNS 79
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
1248-1313 5.16e-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: 5.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1248 LGISiVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSAT--EQQARLIIGqqcDTITILA 1313
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) ...
 594-682 5.27e-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: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  594 VRRRKSLGgkvvtplhINLSGQKDSGISLE-NGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSC 672
Cdd:cd06791     8 VKDEQGLG--------ITIAGYVGEKASGElSGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEAVEVLRNT 79

                          90
                  ....*....|
gi 767964245  673 QDSLTLSLLK 682
Cdd:cd06791    80 GQVVHLTLAR 89
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1410-1466 6.03e-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: 6.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1410 HGVFVAEVEDDSPA-KGpdGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKV 1466
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 ...
 608-680 6.09e-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: 6.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245  608 LHINLSGQKDSGISLENG------VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALdNKSLNECESLLRSCQDSLTLSL 680
Cdd:cd06750     3 IEVQLQGGAPWGFTLKGGlehgepLVISKIEEGGKAASVGKLQVGDEVVNINGVPL-SGSRQEAIQLVKGSHKTLKLVV 80
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 601-682 6.27e-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: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  601 GGKVVTPLHINlsgqkDSGIslengvYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 680
Cdd:cd06704    18 GGKGSTPYKGD-----DEGI------FISRVTEGGPAAKAG-VRVGDKLLEVNGVDLVDADHHEAVEALKNSGNTVTMVV 85


                  ..
gi 767964245  681 LK 682
Cdd:cd06704    86 LR 87
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 1248-1306 6.45e-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: 6.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1248 LGISIVSGEKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIgQQC 1306
Cdd:cd06667    12 LGFGIVGGKSTGVVVKTILPGGVADRDGrLRSGDHILQIGDTNLRGMGSEQVAQVL-RQC 70
mukB PRK04863
chromosome partition protein MukB;
35-496 6.50e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 6.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   35 ENLSIQLRlmtRERNELRKRLAFAthgtAFDKRPYHRLNPDYERLKIQCVR---------AMSDLQSLQNQHTNALKRCE 105
Cdd:PRK04863  785 EKRIEQLR---AEREELAERYATL----SFDVQKLQRLHQAFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHE 857

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  106 EvaketdfyHTLHSRLLSDQtrLKDDVDMLRRENGQL-LRERNLLQQswedmkRLhEEDQKEIGDLRAQQQQVLKHNGSS 184
Cdd:PRK04863  858 S--------QEQQQRSQLEQ--AKEGLSALNRLLPRLnLLADETLAD------RV-EEIREQLDEAEEAKRFVQQHGNAL 920

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  185 EILNKLYDTAM---DKLEVVKKDYDALRKR----------------------YSEKVAIHNADLSRLEQLgeeNQRLLKQ 239
Cdd:PRK04863  921 AQLEPIVSVLQsdpEQFEQLKQDYQQAQQTqrdakqqafaltevvqrrahfsYEDAAEMLAKNSDLNEKL---RQRLEQA 997

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  240 TEMLTQQRDTAIQLQHQcalsLRRFEAIHHELNKA-TAQNKDLQwemELLQsELTELrTTQVkTAKESEKYREERDAVYS 318
Cdd:PRK04863  998 EQERTRAREQLRQAQAQ----LAQYNQVLASLKSSyDAKRQMLQ---ELKQ-ELQDL-GVPA-DSGAEERARARRDELHA 1067

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  319 EYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDTVtMDAGRANKEVEILRKqckalcQELk 398
Cdd:PRK04863 1068 RLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHR------REL- 1139

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  399 eALQEADVAKCRRDWAFQERDKIVAE----RDSIRTLCDNLRRERD-----RAVSELAEALRslddtrkqkNDVSR--EL 467
Cdd:PRK04863 1140 -AYLSADELRSMSDKALGALRLAVADnehlRDVLRLSEDPKRPERKvqfyiAVYQHLRERIR---------QDIIRtdDP 1209

                         490       500       510
                  ....*....|....*....|....*....|....
gi 767964245  468 KELKEQMESQL-----EKEARFRQLmAHSSHDSA 496
Cdd:PRK04863 1210 VEAIEQMEIELsrlteELTSREQKL-AISSESVA 1242
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 1411-1466 6.57e-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: 6.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1411 GVFVAEVEDDSPAKgPDGLVPGDLILEY------GSLDVRNKtveevyVEMLKPRDGVRLKV 1466
Cdd:cd10839    26 GALVAQVLPDSPAA-KAGLKAGDVILSLngkpitSSADLRNR------VATTKPGTKVELKI 80
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 1248-1300 6.59e-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: 6.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245 1248 LGISIVS-----------GEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1300
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 ...
 1487-1544 6.59e-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: 6.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1487 RALYDRLADVEQELSFKKDDILYVDDTLPQGTfgsWMAWQLDENAQkiqrGQIPSKYV 1544
Cdd:cd11858     3 KALYDFAGSVANELSLKKDDIVYIVQKEDNGW---WLAKKLDESKE----GWVPAAYL 53
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 540-595 6.74e-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: 6.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  540 CGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLNGEgAINMVVR 595
Cdd:cd06752    25 LGIFISKVIPDSDAHRLgLKEGDQILSVNGVDFEDIEHSEAVKVLKTAR-EIQMRVR 80
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 326-480 6.94e-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: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  326 ERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQ-I-KDTVTMDAGRANKEVEILRKQCkalcqelkealqe 403
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArIkKYEEQLGNVRNNKEYEALQKEI------------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  404 advakcrrdwAFQERDKIVAErDSIRTL---CDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEK 480
Cdd:COG1579    99 ----------ESLKRRISDLE-DEILELmerIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 1400-1467 7.00e-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: 7.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1400 LGVHLCGGNLHGVFVAEVEDDSPA-KGpdGLVPGDLILEYGSLDVRNKTVEEVyVEMLKPRDG--VRLKVQ 1467
Cdd:cd06782     4 IGIEIGKDDDGYLVVVSPIPGGPAeKA--GIKPGDVIVAVDGESVRGMSLDEV-VKLLRGPKGtkVKLTIR 71
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 541-579 7.01e-04

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


Pssm-ID: 467178 [Multi-domain]  Cd Length: 98  Bit Score: 40.68  E-value: 7.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767964245  541 GIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQA 579
Cdd:cd06691    34 GLLIRGIEEGSRAerDGRFQENDCIVEINGVDLIDKSFEQA 74
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
128-389 7.28e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 7.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  128 LKDDVDMLRRENGQLLRERNL----LQQSWEDMKRLHEEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKK 203
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQlreeLEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  204 DYDALRKRYSEkvaiHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAI-QLQHQCALSLRRFEAIHHELNKATAQNKDLQ 282
Cdd:COG4372   109 EAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELkELEEQLESLQEELAALEQELQALSEAEAEQA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  283 WEMELLQSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEM 362
Cdd:COG4372   185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264

                         250       260
                  ....*....|....*....|....*..
gi 767964245  363 EALRQIKDTVTMDAGRANKEVEILRKQ 389
Cdd:COG4372   265 LAILVEKDTEEEELEIAALELEALEEA 291
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 623-678 7.60e-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: 7.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06703    31 DEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITL 86
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 615-685 8.10e-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: 39.78  E-value: 8.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245  615 QKDS----GISL----ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 685
Cdd:cd10831     6 QKNTdepmGITLkmneDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSIT---FKIVP 81
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
 521-575 8.26e-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: 8.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  521 KALGFDMAEGVNEPCFPGdcgIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKD 575
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 ...
 593-680 8.41e-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: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  593 VVRRRKSLGgkvvtplhINLSGQKDSGISlengvyaaAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSC 672
Cdd:cd06710     5 IARGRAGYG--------FTISGQAPCVLS--------CVVRGSPADVAG-LKAGDQILAVNGINVSKASHEDVVKLIGKC 67


                  ....*...
gi 767964245  673 QDSLTLSL 680
Cdd:cd06710    68 TGVLRLVI 75
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
223-485 8.94e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  223 LSRLEQLGE---------ENQRLLK---QTEMLtqqrDT---AIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMEL 287
Cdd:COG0497   115 LSQLRELGEllvdihgqhEHQSLLDpdaQRELL----DAfagLEELLEEYREAYRAWRALKKELEELRADEAERARELDL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  288 LQSELTELRTTQVKtAKESEKYREER----------DAVYSEYKLIMSERDQVISELDKLQTEVE-LAE--SKLKSSTSE 354
Cdd:COG0497   191 LRFQLEELEAAALQ-PGEEEELEEERrrlsnaeklrEALQEALEALSGGEGGALDLLGQALRALErLAEydPSLAELAER 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  355 KKAANEEME----ALRQIKDTVTMDAGRANkEVE----ILRKQCK----------ALCQELKEALQEADvakcRRDWAFQ 416
Cdd:COG0497   270 LESALIELEeaasELRRYLDSLEFDPERLE-EVEerlaLLRRLARkygvtveellAYAEELRAELAELE----NSDERLE 344

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  417 ERDKIVAE-RDSIRTLCDNLRRERDRAVSELAEAlrslddtrkqkndVSRELKELKeqMESqlekeARFR 485
Cdd:COG0497   345 ELEAELAEaEAELLEAAEKLSAARKKAAKKLEKA-------------VTAELADLG--MPN-----ARFE 394
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 590-671 9.05e-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: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  590 INMVVRRRKSLGgkvvtplhINLSGQKDSGIslenGVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLL 669
Cdd:cd06741     4 VNLVVEDGQSLG--------LMIRGGAEYGL----GIYVTGVDPGSVAENAG-LKVGDQILEVNGRSFLDITHDEAVKIL 70


                  ..
gi 767964245  670 RS 671
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 ...
 1390-1467 9.13e-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: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1390 VVFIKKSQLE-LGVHLCGGNLHG--VFVAEVEDDSPAKgPDGLVPGDLILEYGSLDVRNKTVEEVyVEMLKPRDGVRLKV 1466
Cdd:cd10833     3 TVTVEKSPDGsLGFSVRGGSEHGlgIFVSKVEEGSAAE-RAGLCVGDKITEVNGVSLENITMSSA-VKVLTGSNRLRMVV 80


                  .
gi 767964245 1467 Q 1467
Cdd:cd10833    81 R 81
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 626-678 9.70e-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: 9.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  626 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL----RSCQDSLTL 678
Cdd:cd06733    27 VSIGAIVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKVVDLMgnaaRNGQVNLTV 83
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 528-597 9.87e-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: 9.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245  528 AEGVNEPcfpgDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRR 597
Cdd:cd06789    22 AKGAGQD----KLGIYIKSVVKGGAAdlDGRLQAGDQLLSVDGHSLVGLSQERAAELMTKTGSVVTLEVAKQ 89
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 261-348 1.03e-03

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: 40.67  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   261 LRRFEAIHHELNKataQNKDLQWEMELLQS-------ELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISE 333
Cdd:pfam20492   29 LEESEETAEELEE---ERRQAEEEAERLEQkrqeaeeEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEE 105

                           90
                   ....*....|....*
gi 767964245   334 LDKLQTEVELAESKL 348
Cdd:pfam20492  106 ARRLQEELEEAREEE 120
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 627-683 1.04e-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: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  627 YAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKV 683
Cdd:cd06746    45 YLESVDPGGVADKAG-LKKGDFLLEINGEDVVKASHEQVVNLIRQSGNTLVLKVVTV 100
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 515-681 1.05e-03

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: 43.75  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   515 TEDIdLKALGFDMAEGVnepcfpgdcgiFVTKVDKGSIAD-GRLRVNDWLLRINDVDLIN-KDKKQAIKALLNGEGAINM 592
Cdd:TIGR02037  244 TSDL-AKSLGLEKQRGA-----------LVAQVLPGSPAEkAGLKAGDVITSVNGKPISSfADLRRAIGTLKPGKKVTLG 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   593 VVRRRKSLGGKVV--TPLHINLSGQKDS-GISLEN----------------GVYAAAVLPGSPAAKEGsLAVGDRIVAIN 653
Cdd:TIGR02037  312 ILRKGKEKTITVTlgASPEEQASSSNPFlGLTVANlspeirkelrlkgdvkGVVVTKVVSGSPAARAG-LQPGDVILSVN 390

                          170       180
                   ....*....|....*....|....*...
gi 767964245   654 GIALdnKSLNECESLLRSCQDSLTLSLL 681
Cdd:TIGR02037  391 QQPV--SSVAELRKVLARAKKGGRVALL 416
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 606-678 1.08e-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: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  606 TPLHINLSGQKDSG-ISLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06709    10 SGLGFNIVGGTDQPyIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDAVELFRNAGEDVKL 83
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 1238-1314 1.15e-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: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1238 HVKVQKGSEPLGISIVSGE---KGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILA 1313
Cdd:cd06735     3 SVELERGPKGFGFSIRGGReynNMPLYVLRLAEDGPAQRDGrLRVGDQILEINGESTQGMTHAQAIELIRSGGSVVRLLL 82


                  .
gi 767964245 1314 Q 1314
Cdd:cd06735    83 R 83
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
 629-685 1.16e-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: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  629 AAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTlslLKVFP 685
Cdd:cd10830    28 ARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVS---LKVIP 81
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 1411-1467 1.20e-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: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245 1411 GVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKVQ 1467
Cdd:cd06714    39 GAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEVQDIISQSKGEVELVVS 95
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 128-357 1.23e-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: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   128 LKDDVDMLRRENGQLLrernllQQSWEDMKRLHEEDQKEigDLRAQQQQVLKHngSSEILNKLYDTAMDKLEVVKKDYDA 207
Cdd:pfam17078    8 LHDQIDALTKTNLQLT------VQSQNLLSKLEIAQQKE--SKFLENLASLKH--ENDNLSSMLNRKERRLKDLEDQLSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   208 LRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTAIQLQHqcalslRRFEAIHHELNKATAQNKDLQWEMEl 287
Cdd:pfam17078   78 LKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQN------EYKDHYQQEINTLQESLEDLKLENE- 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245   288 lqSELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQ-VISELDKLQTEVELAESKLKSSTSEKKA 357
Cdd:pfam17078  151 --KQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKI 219
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 624-681 1.23e-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: 1.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  624 NGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLL 681
Cdd:cd06798    21 DSVIISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFLLI 78
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 ...
 506-595 1.27e-03

PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 39.52  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  506 TEVVEFERetediDLKALGFDMAEGVNEPCfpGDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQA---I 580
Cdd:cd06763     1 AVTVELEK-----GSAGLGFSLEGGKGSPL--GDRPLTIKRIFKGGAAEqsGVLQVGDEILQINGTSLQGLTRFEAwniI 73

                          90
                  ....*....|....*
gi 767964245  581 KALlnGEGAINMVVR 595
Cdd:cd06763    74 KSL--PEGPVTLLIR 86
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1388-1466 1.37e-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: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1388 PRVVFIKKSQLELGVHLCGGNlhGVFVAEVEDDSPAKGpDGLVPGDLILEYGSLDVRNKTVEEVyVEMLK--PRDGVRLK 1465
Cdd:cd06712     1 PRTVHLTKEEGGFGFTLRGDS--PVQVASVDPGSCAAE-AGLKEGDYIVSVGGVDCKWSKHSEV-VKLLKsaGEEGLELQ 76


                  .
gi 767964245 1466 V 1466
Cdd:cd06712    77 V 77
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1244-1302 1.42e-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: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245 1244 GSEPLGISIVsgekGG------IYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLII 1302
Cdd:cd06753     6 GPAPWGFRLQ----GGkdfnqpLTISRVTPGGKAAQANLRPGDVILAINGESTEGMTHLEAQNKI 66
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
 1237-1302 1.51e-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: 1.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767964245 1237 RHVKVQKGSEpLGISIVSG----EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLII 1302
Cdd:cd06698     3 QLITVAKSTG-LGLSIVGGinrpEGPMVFIQEVIPGGDCYKDGrLRPGDQLVSINKESLIGVTLEEAKSIL 72
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 1235-1312 1.51e-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: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1235 EPRHVKVQKGSEP-LGISIVSGEKG-----GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQARLIIGQQCD 1307
Cdd:cd23072     1 EITLVNLKKDAKYgLGFQIVGGEKSgrldlGIFISSITPGGPADLDGrLKPGDRLISVNDVSLEGLSHDAAVEILQNAPE 80


                  ....*
gi 767964245 1308 TITIL 1312
Cdd:cd23072    81 DVTLV 85
PLN02939 PLN02939
transferase, transferring glycosyl groups
 56-425 1.63e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 43.35  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   56 AFATHGTAFDKRPYHRLNPDYERLKIQCV---RAMSDLQSLQNQHTNALKRCEEVAK---ETDFYHTLHSRLL------- 122
Cdd:PLN02939    8 ALLSHGCGPIRSRAPFYLPSRRRLAVSCRarrRGFSSQQKKKRGKNIAPKQRSSNSKlqsNTDENGQLENTSLrtvmelp 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  123 SDQTRLKDDVDMLRRENGQLLRERNLLQQswEDMKRLHEEDQKEIGDLRAQQQQVLKhngSSEILNKLYDTAMDKLEVVK 202
Cdd:PLN02939   88 QKSTSSDDDHNRASMQRDEAIAAIDNEQQ--TNSKDGEQLSDFQLEDLVGMIQNAEK---NILLLNQARLQALEDLEKIL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  203 KDYDALRKryseKVAIHNADLS----RLEQLGEENQRLLKQTEMLTQQRDtaiQLQHQCALSLRRFEAIHHELNKATAQN 278
Cdd:PLN02939  163 TEKEALQG----KINILEMRLSetdaRIKLAAQEKIHVEILEEQLEKLRN---ELLIRGATEGLCVHSLSKELDVLKEEN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  279 KDLQWEMELLQSELTELRTTQVKTAKeSEKYREERDAVYS--EYKLIMSERDqvISELDKLQTE-----VELAESKLKSS 351
Cdd:PLN02939  236 MLLKDDIQFLKAELIEVAETEERVFK-LEKERSLLDASLRelESKFIVAQED--VSKLSPLQYDcwwekVENLQDLLDRA 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  352 TSEKKAANEEMEALRQIKDTVtmdagrankeveilrkqckalcQELKEALQEADVAK--CRRDWAFQERDKIVAER 425
Cdd:PLN02939  313 TNQVEKAALVLDQNQDLRDKV----------------------DKLEASLKEANVSKfsSYKVELLQQKLKLLEER 366
PDZ0_GgPro-IL-16-like cd23062
PDZ domain 0 of Gallus gallus interleukin-16, and related domains; N-terminal PDZ (PSD-95 ...
 608-671 1.66e-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: 1.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  608 LHINLSGQKDSGiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRS 671
Cdd:cd23062    11 SGIKLSRNPNCA-SLWKGFTGCHVPAGGTANRDGCLSPRDELLTLNGQSLKDLSSKEAESLIQS 73
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
 1237-1294 1.67e-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: 1.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1237 RHVKVQKGS-EPLGISIVSGEKGGIYVSKVTVGSIAH-QAGLEYGDQLLEFNGINLRSAT 1294
Cdd:cd10831     1 RLVQFQKNTdEPMGITLKMNEDGRCIVARIMHGGMIHrQGTLHVGDEIREINGISVANQT 60
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 607-680 1.71e-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: 1.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  607 PLHINLSGQKDSGiSLENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSL 680
Cdd:cd06679    12 SLGISVAGGRGSR-RGDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSIVL 84
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 625-678 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 767964245  625 GVYAAAVLPGSPAAKEGsLAVGDRIVAINGIALDNKSLNECESLLRScQDSLTL 678
Cdd:cd06737    28 GLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLIKT-KKTVSL 79
PDZ_LIMK-like cd06754
PDZ domain of LIM Kinase (LIMK) family, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 642-671 1.80e-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: 1.80e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 767964245  642 SLAVGDRIVAINGIALDNKSLNECESLLRS 671
Cdd:cd06754    50 SLHVGDRILEVNGTPVRDLSLEEIDDLIQS 79
PDZ_ARHGAP21_23-like cd06756
PDZ domain of ARHGAP21 and ARHGAP23, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1260-1313 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 767964245 1260 IYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIgQQCDTITILA 1313
Cdd:cd06756    55 IFVKQVKEGGPAHQAGLCTGDRIVKVNGESVIGKTYSQVIALI-QNSDSTLELS 107
PDZ5_MUPP1-like cd06669
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ...
 504-583 1.82e-03

PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467157 [Multi-domain]  Cd Length: 98  Bit Score: 39.52  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  504 WETEVVEFERETEDidlKALGFDMAEgVNEPCFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIK 581
Cdd:cd06669     4 WSDEVTVIELEKGD---RGLGFSILD-YQDPLDPSETVIVIRSLVPGGVAeqDGRLLPGDRLVFVNDVSLENASLDEAVQ 79


                  ..
gi 767964245  582 AL 583
Cdd:cd06669    80 AL 81
SH3_DLG-like cd11861
Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding ...
 1485-1542 1.84e-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: 1.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245 1485 YIRALYDRLADVE-----QELSFKKDDILYV----DDTLpqgtfgsWMAWQLDENAQKIQRGQIPSK 1542
Cdd:cd11861     1 YVRALFDYDPSRDsglpsQGLSFKFGDILHVtnasDDEW-------WQARRVTPNGEEEEVGVIPSK 60
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 619-654 1.87e-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: 1.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 767964245  619 GISLENGVYAAAVLPGSPAAKEGsLAVGDRIVAING 654
Cdd:cd10839    20 GLKEPKGALVAQVLPDSPAAKAG-LKAGDVILSLNG 54
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 762-1191 1.88e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  762 GGPLQVCPQACPSASERSLSSFRSDASGDRGFGLVD---VRGRRPLLPFETEVGPCGVGEAsldKADSEGSNSGGTWPka 838
Cdd:PHA03307   17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAvtvVAGAAACDRFEPPTGPPPGPGT---EAPANESRSTPTWS-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  839 mlSSTAVPEKlsvykkPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGPAHSPQPSKRAGPLTPPKPPRRSDSIKFQHR--- 915
Cdd:PHA03307   92 --LSTLAPAS------PAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAava 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  916 ------------LETSSESEATLVGSSPSTSppsalpPDVDPGEPMHASPPRKARVRIASSYYPEGDGDSSHLPAKKSCD 983
Cdd:PHA03307  164 sdaassrqaalpLSSPEETARAPSSPPAEPP------PSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  984 EDLTSQKVD-ELGQKRRRPKSAPSFRPKLAPVVIPAQFLEEQKCVPASGELSPELQEWAPYSPGHSSRHSNPPLYPSRPS 1062
Cdd:PHA03307  238 DSSSSESSGcGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1063 VGTVPRSLTPSTTVSSILRNPIYTVRS---HRVGPCSSPPAARDAGPQGLHPSVQHQGRLSldlshrtcsdysemRATHG 1139
Cdd:PHA03307  318 SSSSRESSSSSTSSSSESSRGAAVSPGpspSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP--------------AASAG 383

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1140 SNSLPSSARLGSSSNLQfkaeRIKIPSTPRYPRSVVGSERGSVSHSECSTPP 1191
Cdd:PHA03307  384 RPTRRRARAAVAGRARR----RDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 523-594 1.91e-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: 1.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  523 LGFDMAEGVNEpcFPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVV 594
Cdd:cd06680    13 LGFSIVGGYEE--SHGNQPFFVKSIVPGTPAynDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTV 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 ...
 1239-1298 1.95e-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: 1.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245 1239 VKVQKGSEPLGISIvSGEKGG------IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06763     4 VELEKGSAGLGFSL-EGGKGSplgdrpLTIKRIFKGGAAEQSGvLQVGDEILQINGTSLQGLTRFEA 69
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 281-487 2.12e-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: 42.21  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   281 LQWEMELLQSELTE-LRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKLQTEV--ELAESKLKSSTSEKKA 357
Cdd:pfam13868   67 RKEERKRYRQELEEqIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKELE 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   358 ANEEMEALRQIKDTVTMDAGR-ANKEVEILRKQCK--ALCQELKEALQEADVAKcrrdwafQERDKIVAERdsirTLCDN 434
Cdd:pfam13868  147 KEEEREEDERILEYLKEKAEReEEREAEREEIEEEkeREIARLRAQQEKAQDEK-------AERDELRAKL----YQEEQ 215

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767964245   435 LRRERDRAVSELAEALRSLDDTRKQkNDVSRELKELKEQMESQLEKEARFRQL 487
Cdd:pfam13868  216 ERKERQKEREEAEKKARQRQELQQA-REEQIELKERRLAEEAEREEEEFERML 267
PHA03247 PHA03247
large tegument protein UL36; Provisional
 863-1236 2.16e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  863 DPNTFKRPQTPPKIDYLLPGPGPAHSPQPSKRAGPLTPPKPPRRSDSI-----KFQHRLETSSESEATLVGSSPSTSPPS 937
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDdpapgRVSRPRRARRLGRAAQASSPPQRPRRR 2686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  938 ALPPDV---------DPGEPMHASPPRKARVRIASSYYPEGDGDSSHLPAKKSCDEDLTSQKVDELGQKRRRPKSAPSFR 1008
Cdd:PHA03247 2687 AARPTVgsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP 2766

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1009 PKLAPVVIPAQFLEEQKCVPASGELSPELQE----WAPYSPGHSSRHSNPPLYPSRPSVGTVPRSLTPSTTVSSILRNPI 1084
Cdd:PHA03247 2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESlpspWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1085 YTVRS-----------HRVGPCSSPPAARDAGPqglHPSVQHQGRLSLDLSHRtcsdysemrathgSNSLPssarlgsss 1153
Cdd:PHA03247 2847 PPSLPlggsvapggdvRRRPPSRSPAAKPAAPA---RPPVRRLARPAVSRSTE-------------SFALP--------- 2901

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1154 nlQFKAERIKIPSTPRYPRSVVGSERGSVSHSECSTP--PQSPLNIDTLSSCSQSQTSASTLPRI-AVNPASLGERR--- 1227
Cdd:PHA03247 2902 --PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPprPQPPLAPTTDPAGAGEPSGAVPQPWLgALVPGRVAVPRfrv 2979

                         410
                  ....*....|
gi 767964245 1228 -KDRPYVEEP 1236
Cdd:PHA03247 2980 pQPAPSREAP 2989
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 615-678 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 767964245  615 QKDSGISL---------ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
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 ...
 1243-1298 2.22e-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: 2.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1243 KGSEPLGISIVSGE---KG--GIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06759     9 AGGKGLGFSIVGGRdspRGpmGIYVKTIFPGGAAAEDGrLKEGDEILEVNGESLQGLTHQEA 70
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
370-521 2.26e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  370 DTVTMDAGRANKEVEILRKQCKALCQELKEALQEAdvakcrRDWAfQERDKIVAERDSIRTLCDNLRRERDRAVSELAEA 449
Cdd:COG1340     4 DELSSSLEELEEKIEELREEIEELKEKRDELNEEL------KELA-EKRDELNAQVKELREEAQELREKRDELNEKVKEL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245  450 lrslddtRKQKNDVSRELKELKEQMESQLEKEARFRQlmahsshdSAIDTDSMEWETEVVEFERETEDIDLK 521
Cdd:COG1340    77 -------KEERDELNEKLNELREELDELRKELAELNK--------AGGSIDKLRKEIERLEWRQQTEVLSPE 133
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 126-311 2.28e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 41.04  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   126 TRLKDDVDMLRRENGQLLRERNLLQQswedMKRLHEEDQKEIGDLRAQQQQVL-KHNGSSEILNKLYDTAMDKLEVVKKd 204
Cdd:pfam15619   14 KELQNELAELQSKLEELRKENRLLKR----LQKRQEKALGKYEGTESELPQLIaRHNEEVRVLRERLRRLQEKERDLER- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   205 ydALRKRYSEkvaIH--NADLSRLEQLG--------EENQRLLKQTEMLTQQRDTAIQ-LQHQCALSLRRFeaiHHELNK 273
Cdd:pfam15619   89 --KLKEKEAE---LLrlRDQLKRLEKLSedknlaerEELQKKLEQLEAKLEDKDEKIQdLERKLELENKSF---RRQLAA 160

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 767964245   274 ATAQNKDLQWEMELLQSELTELRTtqvktaKESEKYRE 311
Cdd:pfam15619  161 EKKKHKEAQEEVKILQEEIERLQQ------KLKEKERE 192
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 123-360 2.34e-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: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  123 SDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngsseilnklydtAMDKLEVVK 202
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-----------------LQAEIAEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  203 KDYDALRKRYSEKVA---IHNADLSRLEQL--GEENQRLLKQTEMLTQ--QRDTAIqlqhqcalsLRRFEAIHHELNKAT 275
Cdd:COG3883    79 AEIEERREELGERARalyRSGGSVSYLDVLlgSESFSDFLDRLSALSKiaDADADL---------LEELKADKAELEAKK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  276 AQNKDLQWEMELLQSELTELRttqvktaKESEKYREERDAVYSEYKlimSERDQVISELDKLQTEVELAESKLKSSTSEK 355
Cdd:COG3883   150 AELEAKLAELEALKAELEAAK-------AELEAQQAEQEALLAQLS---AEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219


                  ....*
gi 767964245  356 KAANE 360
Cdd:COG3883   220 AAAAA 224
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 631-655 2.34e-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: 2.34e-03
                          10        20
                  ....*....|....*....|....*
gi 767964245  631 VLPGSPAAKEGSLAVGDRIVAINGI 655
Cdd:cd06731    32 VVPDGPAALDGKLRTGDVLVSVNDT 56
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 1256-1299 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 767964245 1256 EKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQAR 1299
Cdd:cd10838    31 EVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRI 74
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 292-510 2.63e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 42.30  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   292 LTELRTTQVKTAKESEKYREERDavyseyklimserdqviSELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQIKDT 371
Cdd:pfam05262  169 VSDVDTDSISDKKVVEALREDNE-----------------KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   372 VTMDAGRANKEVEILRKqckalcqELKEALQE-------ADVAKCRRDWAFQERDKIVAERDSIRT--LCDNLRRERDRA 442
Cdd:pfam05262  232 AQQKADFAQDNADKQRD-------EVRQKQQEaknlpkpADTSSPKEDKQVAENQKREIEKAQIEIkkNDEEALKAKDHK 304

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   443 VSELAEALRSLDDTRKQKN-DVSRELKELKEQMESQL-EKEARfrqlmAHSSHDSAIDTDSMEWETEVVE 510
Cdd:pfam05262  305 AFDLKQESKASEKEAEDKElEAQKKREPVAEDLQKTKpQVEAQ-----PTSLNEDAIDSSNPVYGLKVVD 369
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 1258-1295 2.65e-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: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 767964245 1258 GGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATE 1295
Cdd:cd06777    25 QGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLE 62
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 1261-1312 2.71e-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: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1261 YVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITIL 1312
Cdd:cd06713    38 YVCRVHEDSPAYLAGLTAGDVILSVNGVSVEGASHQEIVELIRSSGNTLRLE 89
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 1245-1300 2.82e-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: 2.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245 1245 SEPLGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQARL 1300
Cdd:cd06779    12 SPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAAL 67
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 243-408 2.98e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  243 LTQQRDTAIQLQHQCALSLRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRtTQVKTAKESEKYREER--DAVYSEY 320
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-AEIAEAEAEIEERREElgERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  321 K----------------------------LIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAANEEMEALRQikdtv 372
Cdd:COG3883    97 RsggsvsyldvllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA----- 171

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767964245  373 TMDAGRANKEVEI--LRKQCKALCQELKEALQEADVAK 408
Cdd:COG3883   172 ELEAQQAEQEALLaqLSAEEAAAEAQLAELEAELAAAE 209
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 625-678 3.13e-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: 3.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767964245  625 GVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06667    23 GVVVKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRL 76
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 209-522 3.15e-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: 42.63  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  209 RKRYSEKVAIHNADL-SRLEQLGEENQRLLKQTEMLTQQ--RDTAIQLQHQCALS-LRRFeaihheLNKATAQNKDLQWE 284
Cdd:COG3096   280 RRELSERALELRRELfGARRQLAEEQYRLVEMARELEELsaRESDLEQDYQAASDhLNLV------QTALRQQEKIERYQ 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  285 MELlqSELT---ELRTTQVKTAKES-EKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKsstsekkaANE 360
Cdd:COG3096   354 EDL--EELTerlEEQEEVVEEAAEQlAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ--------ALE 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  361 EMEALRQIKDtvtMDAGRANKEVEILRKQCKALCQELKEA---LQEADVAKCRRDWAFQERDKIVAErdsirtlcdnlrR 437
Cdd:COG3096   424 KARALCGLPD---LTPENAEDYLAAFRAKEQQATEEVLELeqkLSVADAARRQFEKAYELVCKIAGE------------V 488

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  438 ERDRAVSELAEALRSLDDTRKQKNDVS---RELKELKEQMESQleKEARfRQLMAHSSHDSAIDTDSMEWETEVVEFERE 514
Cdd:COG3096   489 ERSQAWQTARELLRRYRSQQALAQRLQqlrAQLAELEQRLRQQ--QNAE-RLLEEFCQRIGQQLDAAEELEELLAELEAQ 565


                  ....*...
gi 767964245  515 TEDIDLKA 522
Cdd:COG3096   566 LEELEEQA 573
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 523-596 3.18e-03

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


Pssm-ID: 467199 [Multi-domain]  Cd Length: 92  Bit Score: 38.53  E-value: 3.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767964245  523 LGFDMAEG---VNEPCFPGDCGIFVTKV-DKGSIAD-GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 596
Cdd:cd06715    14 LGFNIIGGrpcENNQEGSSSEGIYVSKIvENGPAADeGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKEPIVVQVLR 92
46 PHA02562
endonuclease subunit; Provisional
 153-470 3.25e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  153 WEDMKRLHEEdqKEIGDLRAQQQQVLKHN----------GSS--------------EILNKLYD----TAMDKLEVVK-- 202
Cdd:PHA02562  100 YCNGKLLDES--ASSKDFQKYFEQMLGMNyksfkqivvlGTAgyvpfmqlsaparrKLVEDLLDisvlSEMDKLNKDKir 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  203 ------KDYDALRKRYSEKVAIHNADLSRLEQLGEENQRLLKqtEMLTQQRDTAiqlqhqcalslrrfEAIHHELNKATA 276
Cdd:PHA02562  178 elnqqiQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQ--NKYDELVEEA--------------KTIKAEIEELTD 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  277 QNKDLQWEMELLQSELTELRTTQVKTAKESEKYreERDAVYSEYKLIMSERDQVISELDKLQTEVElaeSKLKSSTSEKK 356
Cdd:PHA02562  242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF--QKVIKMYEKGGVCPTCTQQISEGPDRITKIK---DKLKELQHSLE 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  357 AANEEMEALRQIKDtvtmdagrankevEILRKQCKAlcQELKealqeADVAKCRRDWAfqerdKIVAERDSIRTLCDNLR 436
Cdd:PHA02562  317 KLDTAIDELEEIMD-------------EFNEQSKKL--LELK-----NKISTNKQSLI-----TLVDKAKKVKAAIEELQ 371

                         330       340       350
                  ....*....|....*....|....*....|....
gi 767964245  437 RERDRAVSELAEALRSLDDTRKQKNDVSRELKEL 470
Cdd:PHA02562  372 AEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
SH3_NEDD9 cd12002
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, ...
 1487-1523 3.61e-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: 3.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767964245 1487 RALYDRLADVEQELSFKKDDILYVDDTLPQGTFGSWM 1523
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 ...
 1245-1312 3.64e-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: 3.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245 1245 SEPLGISIVSG----EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSatEQQARLIIGQQCDTITIL 1312
Cdd:cd06716    14 QEKLGLTLCYRtddeEDTGIYVSEVDPNSIAAKDGrIREGDQILQINGVDVQN--REEAIALLSEEEKSITLL 84
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 541-605 3.92e-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: 3.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245  541 GIFVTKVDKGSIAD-GRLRVNDWLLRINDVDLINKDKKQaikallngegainmVVRRRKSLGGKVV 605
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 ...
 1410-1474 3.97e-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: 3.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245 1410 HGVFVAEVEDDSPAKGPdGLVPGDLILEYGSLDVRNKT-VEEVYVEMlKPRDGVRLKVQYRPEEFT 1474
Cdd:cd06779    25 RGVLVAEVIPGSPAAKA-GLKEGDVILSVNGKPVTSFNdLRAALDTK-KPGDSLNLTILRDGKTLT 88
SH3_CRK_N cd11758
N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ...
 1485-1544 4.02e-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: 36.96  E-value: 4.02e-03
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gi 767964245 1485 YIRALYDRLADVEQELSFKKDDILYVDDTlPQGTFgsWMAwqldENAQKiQRGQIPSKYV 1544
Cdd:cd11758     2 YVRALFDFPGNDDEDLPFKKGEILTVIRK-PEEQW--WNA----RNSEG-KTGMIPVPYV 53
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 1249-1314 4.15e-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: 4.15e-03
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gi 767964245 1249 GISIvsgeKGGIYVSKVTVGS-IAHQAGLEYGDQLLEFNGINL--RSATEQQARLIIGQQCDTITILAQ 1314
Cdd:cd06765    11 GISL----ENGVFISRIVPGSpAAKEGSLTVGDRIIAINGIALdnKSLSECEALLRSCRDSLSLSLMKV 75
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 607-654 4.30e-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: 4.30e-03
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gi 767964245  607 PLHINLSGQKDSgisLENGVYAAAVLPGSPAAKEGSLAVGDRIVAING 654
Cdd:cd23065    10 PLGVSVVGGKNH---VTTGCIITHIYPNSIVAADKRLKVFDQILDING 54
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 541-595 4.36e-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: 4.36e-03
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gi 767964245  541 GIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVR 595
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), ...
 626-678 4.40e-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: 4.40e-03
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gi 767964245  626 VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTL 678
Cdd:cd06796    28 IYISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKL 80
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 595-682 4.66e-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: 4.66e-03
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gi 767964245  595 RRRKSLGGKVVTPlhiNLSGQKDSGISLEnGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQD 674
Cdd:cd06715     9 RENGSLGFNIIGG---RPCENNQEGSSSE-GIYVSKIVENGPAADEGGLQVHDRIIEVNGKDLSKATHEEAVEAFRTAKE 84


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gi 767964245  675 SLTLSLLK 682
Cdd:cd06715    85 PIVVQVLR 92
PDZ9_MUPP1-like cd10817
PDZ domain 9 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 1238-1286 4.66e-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: 4.66e-03
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gi 767964245 1238 HVKVQKGSEPLGISIVSGEK-GGIYVSKVTVGSIAHQAG-LEYGDQLLEFN 1286
Cdd:cd10817     1 HVELPKDQGGLGIAISEEDTeNGIVIKSLTEGGPAAKDGrLKVGDQILAVD 51
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 138-368 4.86e-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: 4.86e-03
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gi 767964245   138 ENGQLLRERNLLQQSWEDMKRLhEEDQKEIGDLRAQQQQVLK------HNGSSEILNKLYDTAMDKLEVVKKDYDALRKR 211
Cdd:pfam06160  170 ESGDYLEAREVLEKLEEETDAL-EELMEDIPPLYEELKTELPdqleelKEGYREMEEEGYALEHLNVDKEIQQLEEQLEE 248

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gi 767964245   212 YSEkvAIHNADLSRLEqlgEENQRLLKQTEMLTQQRDTAIQLQHQCALSLRRFEAihhELNKATAQNKDLQWEMELLQ-- 289
Cdd:pfam06160  249 NLA--LLENLELDEAE---EALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIED---YLEHAEEQNKELKEELERVQqs 320

                          170       180       190       200       210       220       230       240
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gi 767964245   290 -----SELTELR--TTQVKTAK----ESEKYREERDAVYSEyklIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAA 358
Cdd:pfam06160  321 ytlneNELERVRglEKQLEELEkrydEIVERLEEKEVAYSE---LQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEA 397

                          250
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gi 767964245   359 NEEMEALRQI 368
Cdd:pfam06160  398 REKLDEFKLE 407
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 625-654 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 767964245  625 GVYAAAVLPGSPAAkeGSLAVGDRIVAING 654
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, ...
 1238-1298 4.94e-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: 4.94e-03
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gi 767964245 1238 HVKVQKGSEPLGISIVSGEKGG--IYVSKVTVGSIAHQAG-LEYGDQLLEFNGINLRSATEQQA 1298
Cdd:cd06731     3 RTSLKKSARGFGFTIIGGDEPDefLQIKSVVPDGPAALDGkLRTGDVLVSVNDTCVLGYTHADV 66
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 1234-1311 5.01e-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: 5.01e-03
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gi 767964245 1234 EEPRHVKVQKGSEPLGISI-VSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLRSATEQQA-RLIIGQQCDTITI 1311
Cdd:COG0793    46 EEYEDFQESTSGEFGGLGAeLGEEDGKVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAGLTLDDAvKLLRGKAGTKVTL 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 538-574 5.04e-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: 5.04e-03
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gi 767964245  538 GDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINK 574
Cdd:cd06714    36 GRLGAYVTKVKPGSVADtvGHLREGDEVLEWNGISLQGK 74
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 505-585 5.26e-03

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


Pssm-ID: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 38.07  E-value: 5.26e-03
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gi 767964245  505 ETEVVEFERETEdidlKALGFDMAEGVNEPCFPGD----CGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQ 578
Cdd:cd06671     1 PPRRVELWREPG----KSLGISIVGGRVMGSRLSNgeeiRGIFIKHVLEDSPAGrnGTLKTGDRILEVNGVDLRNATHEE 76


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gi 767964245  579 AIKALLN 585
Cdd:cd06671    77 AVEAIRN 83
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 539-598 5.38e-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: 5.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245  539 DCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK 598
Cdd:cd06674    26 DTGVFVSDIVKGGAAdaDGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGKVRLEVGRLK 87
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 184-483 5.43e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 41.74  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  184 SEILNKLYDTAMDKLEVVKKDYD----ALRKRYSEKVAIHNADLSRLEQLGEENQRLLKQTEMLTQQRDTA-----IQLQ 254
Cdd:PTZ00440 1086 VEALLKKIDENKNKLIEIKNKSHehvvNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLnevneIEIE 1165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  255 HQCALslrrfeaIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESE------KYREERDAVYSEYKLIM---- 324
Cdd:PTZ00440 1166 YERIL-------IDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNdhlttfEYNAYYDKATASYENIEeltt 1238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  325 --------SERDQVISELDKLQTEVelaESKLKSSTSEkkaaNEEME-ALRQIKDT----VTMDAGRANKEVEILRKQCK 391
Cdd:PTZ00440 1239 eakglkgeANRSTNVDELKEIKLQV---FSYLQQVIKE----NNKMEnALHEIKNMyeflISIDSEKILKEILNSTKKAE 1311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  392 ALCQELKEALQEADvakcrrDWAFQERDKIVAERDSIRTLCDNLRRER-DRAVSELAEALRSLDDTRKQKNDVSRELKEL 470
Cdd:PTZ00440 1312 EFSNDAKKELEKTD------NLIKQVEAKIEQAKEHKNKIYGSLEDKQiDDEIKKIEQIKEEISNKRKEINKYLSNIKSN 1385

                         330
                  ....*....|...
gi 767964245  471 KEQMESQLEKEAR 483
Cdd:PTZ00440 1386 KEKCDLHVRNASR 1398
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 27-446 5.50e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.73  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    27 DQQVN---EKVENLSIQLRLMTRERNELRKRL------------AFATHGTAFDKRpyHRLnpdYERLKIQcvRAMSDLQ 91
Cdd:pfam10174  393 ERKINvlqKKIENLQEQLRDKDKQLAGLKERVkslqtdssntdtALTTLEEALSEK--ERI---IERLKEQ--REREDRE 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    92 SLQNQHTnaLKRCEEVAKETdfYHTLHSRLLSDQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLR 171
Cdd:pfam10174  466 RLEELES--LKKENKDLKEK--VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK 541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   172 AQQQQVLKHNGSSEILnklydtamDKLEVVKKDYdalrKRYSEKVAIHNADLSRLeqLGeenqrLLKQTEMLTQQRDTAI 251
Cdd:pfam10174  542 KAHNAEEAVRTNPEIN--------DRIRLLEQEV----ARYKEESGKAQAEVERL--LG-----ILREVENEKNDKDKKI 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   252 QLQHQCALSLrrfeaiHHELNKATAQNKDLQWEMELLQSELTElrttqvktakesEKYREERDAVYSEYKLIMSErdqVI 331
Cdd:pfam10174  603 AELESLTLRQ------MKEQNKKVANIKHGQQEMKKKGAQLLE------------EARRREDNLADNSQQLQLEE---LM 661

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   332 SELDKlqTEVELAESKLKSSTSEKKAANEE--MEALRQIKdtvtmdagrankeveilRKQCkalcQELKEALQEADVAkc 409
Cdd:pfam10174  662 GALEK--TRQELDATKARLSSTQQSLAEKDghLTNLRAER-----------------RKQL----EEILEMKQEALLA-- 716

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 767964245   410 rrdwAFQERDKIVA-------ERDSIRTLCDNLRRERDRAVSEL 446
Cdd:pfam10174  717 ----AISEKDANIAllelsssKKKKTQEEVMALKREKDRLVHQL 756
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 543-596 6.01e-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: 6.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767964245   543 FVTKVDKGSIAD-GRLRVNDWLLRINDVDLinKDKKQAIKALLNGEGA-INMVVRR 596
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 ...
 1393-1469 6.54e-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: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1393 IKKSQLELGVHLCGGN---LHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDVRNKTVEEVYVEMLKPRDGVRLKVqYR 1469
Cdd:cd06673     8 INKGKKGLGLSIVGGSdtlLGAIIIHEVYEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEAINVLRQTPQKVRLLV-YR 86
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 523-598 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 767964245  523 LGFDMAEGvnEPCFPGDCGIFVTKVDKGSIAD--GRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK 598
Cdd:cd23072    15 LGFQIVGG--EKSGRLDLGIFISSITPGGPADldGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVSQPK 90
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 133-298 6.63e-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: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  133 DMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQqvlKHNGSSEILNKLYDTAMDKLEVVK--KDYDALRK 210
Cdd:COG1579    20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYEEQLGNVRnnKEYEALQK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  211 ryseKVAIHNADLSRLEqlgEENQRLLKQTEMLTQQRDtaiQLQHQCALSLRRFEAIHHELNKATAqnkDLQWEMELLQS 290
Cdd:COG1579    97 ----EIESLKRRISDLE---DEILELMERIEELEEELA---ELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163


                  ....*...
gi 767964245  291 ELTELRTT 298
Cdd:COG1579   164 EREELAAK 171
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 261-489 6.80e-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: 40.67  E-value: 6.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   261 LRRFEAIHHELNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDAVY-SEYKLIMSERDQVISELDKLQT 339
Cdd:pfam13868   33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRqEEYEEKLQEREQMDEIVERIQE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   340 EvELAESKLKSStsEKKAANEEM-EALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQE- 417
Cdd:pfam13868  113 E-DQAEAEEKLE--KQRQLREEIdEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARl 189

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245   418 RDKIVAERDSIRTLcDNLRRERDRAVSELAEALRSLDDTRKQKndvsRELKELKEQMESQLEKEARFRQLMA 489
Cdd:pfam13868  190 RAQQEKAQDEKAER-DELRAKLYQEEQERKERQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEA 256
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 416-488 6.94e-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: 6.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767964245  416 QERDKivaERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMESQLEKEARFRQLM 488
Cdd:COG1579    13 QELDS---ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 523-596 7.03e-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: 7.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767964245  523 LGFDMAEGVNepcfpgDCGIFVTK-VDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRR 596
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 ...
 522-583 7.18e-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: 7.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964245  522 ALGFDMAEGVNEPcfPGDCGIFVTKVD-KGSIA-DGRLRVNDWLLRINDVDLINKDKKQAIKAL 583
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 ...
 541-583 7.57e-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: 7.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767964245  541 GIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKAL 583
Cdd:cd06740    28 GIYVSLVEPGSLAEKEgLRVGDQILRVNDVSFEKVTHAEAVKIL 71
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 7-514 7.75e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.19  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245     7 KQSHPGGTTGKAPSPP--PLLTD---------QQVNEKVENLSIQLRLMTRERNELRKRLAFATHGTA------FDKRPY 69
Cdd:TIGR00606  555 KSRHSDELTSLLGYFPnkKQLEDwlhskskeiNQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklFDVCGS 634

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245    70 HRLNPDYERLKIQCVRAMSDL--------------QSLQNQHTNALKRCEEV----AKETDFYHTLHSRLLSDQTRLKDd 131
Cdd:TIGR00606  635 QDEESDLERLKEEIEKSSKQRamlagatavysqfiTQLTDENQSCCPVCQRVfqteAELQEFISDLQSKLRLAPDKLKS- 713

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   132 vdmLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQV------LKHNGSSEilNKLYDTAMDKLEVVKkdy 205
Cdd:TIGR00606  714 ---TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVnrdiqrLKNDIEEQ--ETLLGTIMPEEESAK--- 785

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   206 dalrkrysekvaIHNADLSRLEQLGEENQRLLKQTEMLTQQRD------TAIQLQHQCALSLRRFEAIHHELNKATAQNK 279
Cdd:TIGR00606  786 ------------VCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   280 DLQWEMELLQSELTELRTTQVKTAKE-------SEKYREERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSST 352
Cdd:TIGR00606  854 DQQEQIQHLKSKTNELKSEKLQIGTNlqrrqqfEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE 933

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   353 SEKKAANEEMEALRQIKDTVTM-------------DAGRANKEVEILRKQCK-ALCQELKEALQEaDVAKCRRDWAFQER 418
Cdd:TIGR00606  934 TSNKKAQDKVNDIKEKVKNIHGymkdienkiqdgkDDYLKQKETELNTVNAQlEECEKHQEKINE-DMRLMRQDIDTQKI 1012

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   419 DKivaerdsiRTLCDNL-RRERDRAVSELAEALRSLDDTRKQknDVSRELKELKEQMESQLEKEARfrqlmahssHDSAI 497
Cdd:TIGR00606 1013 QE--------RWLQDNLtLRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKR---------NHVLA 1073

                          570
                   ....*....|....*..
gi 767964245   498 DTDSMEWETEVVEFERE 514
Cdd:TIGR00606 1074 LGRQKGYEKEIKHFKKE 1090
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 1248-1291 7.84e-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: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767964245 1248 LGISIVSGEKGGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINLR 1291
Cdd:cd06782     4 IGIEIGKDDDGYLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVR 47
Cep57_CLD_2 pfam14197
Centrosome localization domain of PPC89; The N-terminal region of the fission yeast spindle ...
 433-473 8.16e-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: 36.49  E-value: 8.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767964245   433 DNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQ 473
Cdd:pfam14197   27 KRLRRERDSAVRQLGVAYLEIQELKAENEALRKELKEQRAQ 67
COG5022 COG5022
Myosin heavy chain [General function prediction only];
209-472 8.20e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 8.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  209 RKRYSEKVAIhNADLsrleQLGEENQRLLKQTEmltqqrdtAIQLQHQCALSLRRFEAIHHELNKATAQNKDL-----QW 283
Cdd:COG5022   809 RKEYRSYLAC-IIKL----QKTIKREKKLRETE--------EVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETiylqsAQ 875

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  284 EMELLQSELTELRTTqvktakesekyREERDAVYseykLIMSERDQVISELDKLQTEVELAESKLKS--STSEKKAANEe 361
Cdd:COG5022   876 RVELAERQLQELKID-----------VKSISSLK----LVNLELESEIIELKKSLSSDLIENLEFKTelIARLKKLLNN- 939

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  362 mealRQIKDTVTMDAGRaNKEVEILRKQCKalcqELKEALQEadvakcrrdwafqerdkivaeRDSIRTLCDNLRRERDR 441
Cdd:COG5022   940 ----IDLEEGPSIEYVK-LPELNKLHEVES----KLKETSEE---------------------YEDLLKKSTILVREGNK 989

                         250       260       270
                  ....*....|....*....|....*....|.
gi 767964245  442 AVSELAEALRSLDDTRKQKNDVSRELKELKE 472
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 ...
 1258-1290 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 767964245 1258 GGIYVSKVTVGSIAHQAGLEYGDQLLEFNGINL 1290
Cdd:cd06721    22 KGVFVQLVQANSPAALAGLRFGDQILQINGENV 54
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 ...
 521-595 8.32e-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: 8.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245  521 KALGFDMAEGVNEPcfPGDCGIFVTKVDKGSIA--DGRLRVNDWLLRINDVDLINKDKKQAIKALLN-GEGAINMVVR 595
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 ...
 1239-1302 8.37e-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: 8.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245 1239 VKVQK--GSEpLGISIVSG---EKGGIYVSKVTVGSIAHQAG-LEYGDQLLEFNGIN------------LRSATEQQARL 1300
Cdd:cd06684     5 VEIEKtpGSS-LGITLSTSthrNKQVIVIDSIKPASIADRCGaLHVGDHILSIDGTSvehcslaeatqlLASNSGDQVKL 83


                  ..
gi 767964245 1301 II 1302
Cdd:cd06684    84 EI 85
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 135-480 8.45e-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: 40.83  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   135 LRRENGQLLRERNLLQQSWEDMKRLHEEDQKEIGDLRAQQQQvlkhngsseiLNKLYDTAmdklEVVKKDYDALRKRySE 214
Cdd:pfam05622   64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE----------LTSLAEEA----QALKDEMDILRES-SD 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   215 KVAIHNADLS----RLEQLGEenqrLLKQTEMLtqQRDTAIQLQHQCALslrrfeaiHHELNKATAqnkdLQWEMELLQS 290
Cdd:pfam05622  129 KVKKLEATVEtykkKLEDLGD----LRRQVKLL--EERNAEYMQRTLQL--------EEELKKANA----LRGQLETYKR 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   291 ELTELRTTQVKTAKESEKYREERDAVYSEYKLIMSERDQVISELDKL-------------QTEVELAESKLKSSTSEKKA 357
Cdd:pfam05622  191 QVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLretneelrcaqlqQAELSQADALLSPSSDPGDN 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   358 ANEEMEALrQIKDTVTmdagRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSirtlcdnlrr 437
Cdd:pfam05622  271 LAAEIMPA-EIREKLI----RLQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRIL---------- 335

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 767964245   438 ERDRAVSELAEALRSL----DDTRKQKNDVSRELKELKEqMESQLEK 480
Cdd:pfam05622  336 ELQQQVEELQKALQEQgskaEDSSLLKQKLEEHLEKLHE-AQSELQK 381
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
 623-681 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 767964245  623 ENGVYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDN-KSLNEcesLLRSCQDSLTLSLL 681
Cdd:cd10832    21 EGELVIARILHGGMIDRQGLLHVGDIIKEVNGVPVGSpEQLQE---MLKNASGSVTLKIL 77
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 539-585 9.02e-03

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


Pssm-ID: 467211 [Multi-domain]  Cd Length: 82  Bit Score: 36.78  E-value: 9.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767964245  539 DCGIFVTKVDKGSIADGR-LRVNDWLLRINDVDLINKDKKQAIKALLN 585
Cdd:cd06729    22 DVGIFVAGVQEGSPAEKQgLQEGDQILKVNGVDFRNLTREEAVLFLLD 69
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 88-315 9.15e-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: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245   88 SDLQSLQNQHTNALKRCEEVAKEtdfyhtlhsrllsdQTRLKDDVDMLRRENGQLLRERNLLQQSWEDMKRLHEEDQKEI 167
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  168 GDLRAQ---QQQVLkhngsSEILNKLYDTA-MDKLEVVKKDYDAL----RKRYSEKVAihNADLSRLEQLGEENQRLLKQ 239
Cdd:COG4942    93 AELRAEleaQKEEL-----AELLRALYRLGrQPPLALLLSPEDFLdavrRLQYLKYLA--PARREQAEELRADLAELAAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964245  240 TEMLTQQRDTAIQLQHQCALSLRRFEAIHHE----LNKATAQNKDLQWEMELLQSELTELRTTQVKTAKESEKYREERDA 315
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
PDZ3_harmonin cd06739
PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic ...
 1237-1299 9.65e-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: 9.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964245 1237 RHVKVQKgSEPLGISIVSGE----KGGIYVSKVTVGSIAH-QAGLEYGDQLLEFNGINLRSATEQQAR 1299
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 ...
 605-669 9.79e-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: 9.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964245  605 VTPLHINLSGqkdsGISLENG--VYAAAVLPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLL 669
Cdd:cd06698    10 STGLGLSIVG----GINRPEGpmVFIQEVIPGGDCYKDGRLRPGDQLVSINKESLIGVTLEEAKSIL 72
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 1487-1544 9.85e-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: 9.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767964245 1487 RALYDRLADVEQELSFKKDDILY----VDDtlpqgtfgswmAWQLDENAQKiQRGQIPSKYV 1544
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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