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Conserved domains on  [gi|124487143|ref|NP_001074656|]
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serine protease HTRA4 precursor [Mus musculus]

Protein Classification

Kazal-type serine protease inhibitor family protein( domain architecture ID 13622476)

Kazal-type serine protease inhibitor family protein may function as a serine protease inhibitor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 206-480 1.04e-96

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: 292.82  E-value: 1.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 206 SSGSGFIVSEDGLIVTNAHVLTNQQKIQVELQSGARYEATVKDIDHKLDLALIKIEPDtELPVLLLGRSSDLRAGEFVVA 285
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAK-DLPAAPLGDSDKLRVGDWVLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 286 LGSPFSLQNTVTAGIVSTTqrgGRELGLKNSDI--DYIQTDAIINHGNSGGPLVNLDGDVIGINTLKVT-----AGISFA 358
Cdd:COG0265   80 IGNPFGLGQTVTAGIVSAL---GRSIGSSGGGTydDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 359 IPSDRIRQFLEdyherQLKGKAPLQKKYLGLRMLPLTLNLLQEMKRQDPEfpdvssGVFVYEVIQGSAAASSGLRDHDVI 438
Cdd:COG0265  157 IPINLAKRVVE-----QLIETGRVRRGWLGVTIQPVTPELAEALGLPEPE------GVLVARVEPGSPAAKAGLRPGDVI 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 124487143 439 VSINGQPVTTTTDVIEAVKD---NDFLSIIVLRGSQTLFLTVTPE 480
Cdd:COG0265  226 LAVDGKPVTSARDLQRLLASlkpGDTVTLTVLRGGKELTVTVTLG 270
IGFBP pfam00219
Insulin-like growth factor binding protein;
39-93 8.01e-18

Insulin-like growth factor binding protein;


:

Pssm-ID: 459717  Cd Length: 53  Bit Score: 76.98  E-value: 8.01e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124487143   39 CPDACDPTRCP-TLPTCSAGLapVPDRCGCCRVCAAAEGQECGGARGrPCAPRLRC 93
Cdd:pfam00219   1 CPPPCDPERCPpPPPGCPAGV--VLDGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 110-158 5.07e-07

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


:

Pssm-ID: 400135  Cd Length: 50  Bit Score: 46.33  E-value: 5.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 124487143  110 CGCAEgAEDAVVCGSDGRTYPSLCALRKENRAARQRGALPAVpVQKGAC 158
Cdd:pfam07648   4 CQCPK-TEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 206-480 1.04e-96

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: 292.82  E-value: 1.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 206 SSGSGFIVSEDGLIVTNAHVLTNQQKIQVELQSGARYEATVKDIDHKLDLALIKIEPDtELPVLLLGRSSDLRAGEFVVA 285
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAK-DLPAAPLGDSDKLRVGDWVLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 286 LGSPFSLQNTVTAGIVSTTqrgGRELGLKNSDI--DYIQTDAIINHGNSGGPLVNLDGDVIGINTLKVT-----AGISFA 358
Cdd:COG0265   80 IGNPFGLGQTVTAGIVSAL---GRSIGSSGGGTydDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 359 IPSDRIRQFLEdyherQLKGKAPLQKKYLGLRMLPLTLNLLQEMKRQDPEfpdvssGVFVYEVIQGSAAASSGLRDHDVI 438
Cdd:COG0265  157 IPINLAKRVVE-----QLIETGRVRRGWLGVTIQPVTPELAEALGLPEPE------GVLVARVEPGSPAAKAGLRPGDVI 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 124487143 439 VSINGQPVTTTTDVIEAVKD---NDFLSIIVLRGSQTLFLTVTPE 480
Cdd:COG0265  226 LAVDGKPVTSARDLQRLLASlkpGDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 176-478 7.09e-84

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: 265.24  E-value: 7.09e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  176 IAAVVEKVAPSVVHL--------------------QLFRRS----PLTNQEIPSSS-GSGFIVSEDGLIVTNAHVLTNQQ 230
Cdd:TIGR02037   3 FAPLVEKVAPAVVNIsvegtvkrrnrppalppffrQFFGDDmpdfPRQQREQKVRGlGSGVIISADGYVLTNNHVVDGAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  231 KIQVELQSGARYEATVKDIDHKLDLALIKIEPDTELPVLLLGRSSDLRAGEFVVALGSPFSLQNTVTAGIVSTTQRGGre 310
Cdd:TIGR02037  83 EITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG-- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  311 LGLKNSDiDYIQTDAIINHGNSGGPLVNLDGDVIGINTLKVT-----AGISFAIPSDRIRQFLEdyherQLKGKAPLQKK 385
Cdd:TIGR02037 161 LGIGDYE-NFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNMAKNVVD-----QLIEGGKVKRG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  386 YLGLRMLPLTLNLLQEMKRQDPEfpdvssGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAV---KDNDFL 462
Cdd:TIGR02037 235 WLGVTIQEVTSDLAKSLGLEKQR------GALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIgtlKPGKKV 308

                         330
                  ....*....|....*.
gi 124487143  463 SIIVLRGSQTLFLTVT 478
Cdd:TIGR02037 309 TLGILRKGKEKTITVT 324
PRK10942 PRK10942
serine endoprotease DegP;
152-448 1.10e-52

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 184.58  E-value: 1.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 152 PVQKGACEEAGTTRAGRLRRkynfIAAVVEKVAPSVVHLQL-------------------------------FRRSPLTN 200
Cdd:PRK10942  20 PLSATAAETSSATTAQQMPS----LAPMLEKVMPSVVSINVegsttvntprmprqfqqffgdnspfcqegspFQSSPFCQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 201 QEIPSSS----------GSGFIV-SEDGLIVTNAHVLTNQQKIQVELQSGARYEATVKDIDHKLDLALIKIEPDTELPVL 269
Cdd:PRK10942  96 GGQGGNGggqqqkfmalGSGVIIdADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAI 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 270 LLGRSSDLRAGEFVVALGSPFSLQNTVTAGIVSTTQRGGreLGLKNSDiDYIQTDAIINHGNSGGPLVNLDGDVIGINTL 349
Cdd:PRK10942 176 KMADSDALRVGDYTVAIGNPYGLGETVTSGIVSALGRSG--LNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTA 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 350 KVTA-----GISFAIPSDRIRQFLEdyherQLKGKAPLQKKYLGLRMLPLTLNLLQEMKrqdpefPDVSSGVFVYEVIQG 424
Cdd:PRK10942 253 ILAPdggniGIGFAIPSNMVKNLTS-----QMVEYGQVKRGELGIMGTELNSELAKAMK------VDAQRGAFVSQVLPN 321

                        330       340
                 ....*....|....*....|....
gi 124487143 425 SAAASSGLRDHDVIVSINGQPVTT 448
Cdd:PRK10942 322 SSAAKAGIKAGDVITSLNGKPISS 345
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 384-481 3.52e-51

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: 168.83  E-value: 3.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 384 KKYLGLRMLPLTLNLLQEMKRQDPEFPDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKDNDFLS 463
Cdd:cd06785    1 KRYIGIRMLTLTPSLLEELKQRNPDFPDVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSSLL 80

                         90
                 ....*....|....*...
gi 124487143 464 IIVLRGSQTLFLTVTPEI 481
Cdd:cd06785   81 VVVRRGNEDLLLTVTPEE 98
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 208-346 9.56e-33

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 121.37  E-value: 9.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  208 GSGFIVSEDGLIVTNAHVLTNQQKIQVE-----LQSGARYEATVKDIDHKLDLALIKI-EPDTELPVLLLGRSSDLRAGE 281
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVElvsvvLADGREYPATVVARDPDLDLALLRVsGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487143  282 FVVALGSPFSLQ-NTVTAGIVSTTQRGGRELGlknsDIDYIQTDAIINHGNSGGPLVNLDGDVIGI 346
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDGGD----DGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
IGFBP pfam00219
Insulin-like growth factor binding protein;
39-93 8.01e-18

Insulin-like growth factor binding protein;


Pssm-ID: 459717  Cd Length: 53  Bit Score: 76.98  E-value: 8.01e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124487143   39 CPDACDPTRCP-TLPTCSAGLapVPDRCGCCRVCAAAEGQECGGARGrPCAPRLRC 93
Cdd:pfam00219   1 CPPPCDPERCPpPPPGCPAGV--VLDGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 177-346 1.72e-16

MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens.


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 81.00  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 177 AAVVEKVAPSVVHLQlfRRSPLTNQeipSSSGSGFIVSeDGLIVTNAHVLTNQQKIQVELQSGARYEATVKDIDHKLDLA 256
Cdd:NF033740 187 SPAVRRARPSVVKVR--GTAPSCGR---ALEGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 257 LIKIePDTELPVLLLGrSSDLRAGEFVVALGSPFSLQNTVTAGIVSTTQRggrelgLKNSDI--------DYIQTDAIIN 328
Cdd:NF033740 261 VLAV-PGLGLPPLPFA-DEPAETGDDAIVLGYPEGGPFTATPARVRERIA------LSGPDIygsgtvtrEVYTLRGTVR 332

                        170
                 ....*....|....*...
gi 124487143 329 HGNSGGPLVNLDGDVIGI 346
Cdd:NF033740 333 PGNSGGPLLDPDGRVLGV 350
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
 38-110 1.16e-12

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


Pssm-ID: 197525  Cd Length: 75  Bit Score: 63.25  E-value: 1.16e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487143    38 PCPdACDPTRCPTLP-TCSAGLapVPDRCGCCRVCAAAEGQECgGARGRPCAPRLRCGAPFSRDPSGGAWL---GTC 110
Cdd:smart00121   2 RCP-PCDPARCPPCPpGCAELV--RLDGCGCCPVCARQEGEPC-GVYTPRCAPGLRCQPPPGEERPLRALLhgqGVC 74
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 410-470 4.15e-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: 53.54  E-value: 4.15e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487143   410 PDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTD--VIEAVKDN-DFLSIIVLRGS 470
Cdd:smart00228  22 KDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKAgGKVTLTVLRGG 85
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 110-158 5.07e-07

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 46.33  E-value: 5.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 124487143  110 CGCAEgAEDAVVCGSDGRTYPSLCALRKENRAARQRGALPAVpVQKGAC 158
Cdd:pfam07648   4 CQCPK-TEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 121-140 2.08e-05

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 41.51  E-value: 2.08e-05
                           10        20
                   ....*....|....*....|
gi 124487143   121 VCGSDGRTYPSLCALRKENR 140
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAAC 32
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 121-145 1.87e-04

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 38.79  E-value: 1.87e-04
                         10        20
                 ....*....|....*....|....*
gi 124487143 121 VCGSDGRTYPSLCALRKENRAARQR 145
Cdd:cd00104    8 VCGSDGKTYSNECHLGCAACRSGRS 32
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 206-480 1.04e-96

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: 292.82  E-value: 1.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 206 SSGSGFIVSEDGLIVTNAHVLTNQQKIQVELQSGARYEATVKDIDHKLDLALIKIEPDtELPVLLLGRSSDLRAGEFVVA 285
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAK-DLPAAPLGDSDKLRVGDWVLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 286 LGSPFSLQNTVTAGIVSTTqrgGRELGLKNSDI--DYIQTDAIINHGNSGGPLVNLDGDVIGINTLKVT-----AGISFA 358
Cdd:COG0265   80 IGNPFGLGQTVTAGIVSAL---GRSIGSSGGGTydDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 359 IPSDRIRQFLEdyherQLKGKAPLQKKYLGLRMLPLTLNLLQEMKRQDPEfpdvssGVFVYEVIQGSAAASSGLRDHDVI 438
Cdd:COG0265  157 IPINLAKRVVE-----QLIETGRVRRGWLGVTIQPVTPELAEALGLPEPE------GVLVARVEPGSPAAKAGLRPGDVI 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 124487143 439 VSINGQPVTTTTDVIEAVKD---NDFLSIIVLRGSQTLFLTVTPE 480
Cdd:COG0265  226 LAVDGKPVTSARDLQRLLASlkpGDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 176-478 7.09e-84

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: 265.24  E-value: 7.09e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  176 IAAVVEKVAPSVVHL--------------------QLFRRS----PLTNQEIPSSS-GSGFIVSEDGLIVTNAHVLTNQQ 230
Cdd:TIGR02037   3 FAPLVEKVAPAVVNIsvegtvkrrnrppalppffrQFFGDDmpdfPRQQREQKVRGlGSGVIISADGYVLTNNHVVDGAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  231 KIQVELQSGARYEATVKDIDHKLDLALIKIEPDTELPVLLLGRSSDLRAGEFVVALGSPFSLQNTVTAGIVSTTQRGGre 310
Cdd:TIGR02037  83 EITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG-- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  311 LGLKNSDiDYIQTDAIINHGNSGGPLVNLDGDVIGINTLKVT-----AGISFAIPSDRIRQFLEdyherQLKGKAPLQKK 385
Cdd:TIGR02037 161 LGIGDYE-NFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNMAKNVVD-----QLIEGGKVKRG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  386 YLGLRMLPLTLNLLQEMKRQDPEfpdvssGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAV---KDNDFL 462
Cdd:TIGR02037 235 WLGVTIQEVTSDLAKSLGLEKQR------GALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIgtlKPGKKV 308

                         330
                  ....*....|....*.
gi 124487143  463 SIIVLRGSQTLFLTVT 478
Cdd:TIGR02037 309 TLGILRKGKEKTITVT 324
PRK10942 PRK10942
serine endoprotease DegP;
152-448 1.10e-52

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 184.58  E-value: 1.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 152 PVQKGACEEAGTTRAGRLRRkynfIAAVVEKVAPSVVHLQL-------------------------------FRRSPLTN 200
Cdd:PRK10942  20 PLSATAAETSSATTAQQMPS----LAPMLEKVMPSVVSINVegsttvntprmprqfqqffgdnspfcqegspFQSSPFCQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 201 QEIPSSS----------GSGFIV-SEDGLIVTNAHVLTNQQKIQVELQSGARYEATVKDIDHKLDLALIKIEPDTELPVL 269
Cdd:PRK10942  96 GGQGGNGggqqqkfmalGSGVIIdADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAI 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 270 LLGRSSDLRAGEFVVALGSPFSLQNTVTAGIVSTTQRGGreLGLKNSDiDYIQTDAIINHGNSGGPLVNLDGDVIGINTL 349
Cdd:PRK10942 176 KMADSDALRVGDYTVAIGNPYGLGETVTSGIVSALGRSG--LNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTA 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 350 KVTA-----GISFAIPSDRIRQFLEdyherQLKGKAPLQKKYLGLRMLPLTLNLLQEMKrqdpefPDVSSGVFVYEVIQG 424
Cdd:PRK10942 253 ILAPdggniGIGFAIPSNMVKNLTS-----QMVEYGQVKRGELGIMGTELNSELAKAMK------VDAQRGAFVSQVLPN 321

                        330       340
                 ....*....|....*....|....
gi 124487143 425 SAAASSGLRDHDVIVSINGQPVTT 448
Cdd:PRK10942 322 SSAAKAGIKAGDVITSLNGKPISS 345
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 384-481 3.52e-51

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: 168.83  E-value: 3.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 384 KKYLGLRMLPLTLNLLQEMKRQDPEFPDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKDNDFLS 463
Cdd:cd06785    1 KRYIGIRMLTLTPSLLEELKQRNPDFPDVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSSLL 80

                         90
                 ....*....|....*...
gi 124487143 464 IIVLRGSQTLFLTVTPEI 481
Cdd:cd06785   81 VVVRRGNEDLLLTVTPEE 98
PRK10139 PRK10139
serine endoprotease DegQ;
176-448 1.64e-48

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 173.21  E-value: 1.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 176 IAAVVEKVAPSVVHLQLfRRSPLTNQEIPSSS-------------------GSGFIV-SEDGLIVTNAHVLTNQQKIQVE 235
Cdd:PRK10139  42 LAPMLEKVLPAVVSVRV-EGTASQGQKIPEEFkkffgddlpdqpaqpfeglGSGVIIdAAKGYVLTNNHVINQAQKISIQ 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 236 LQSGARYEATVKDIDHKLDLALIKIEPDTELPVLLLGRSSDLRAGEFVVALGSPFSLQNTVTAGIVSTTQRGGREL-GLK 314
Cdd:PRK10139 121 LNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGRSGLNLeGLE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 315 NsdidYIQTDAIINHGNSGGPLVNLDGDVIGINTLKV-----TAGISFAIPSDRIRQFledyhERQLKGKAPLQKKYLGL 389
Cdd:PRK10139 201 N----FIQTDASINRGNSGGALLNLNGELIGINTAILapgggSVGIGFAIPSNMARTL-----AQQLIDFGEIKRGLLGI 271

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124487143 390 RMLPLTLNLLQEMKRqdpefpDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTT 448
Cdd:PRK10139 272 KGTEMSADIAKAFNL------DVQRGAFVSEVLPNSGSAKAGVKAGDIITSLNGKPLNS 324
PRK10898 PRK10898
serine endoprotease DegS;
180-478 3.36e-45

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 161.32  E-value: 3.36e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 180 VEKVAPSVVHL--QLFRRSPLTNQEIpSSSGSGFIVSEDGLIVTNAHVLTNQQKIQVELQSGARYEATVKDIDHKLDLAL 257
Cdd:PRK10898  51 VRRAAPAVVNVynRSLNSTSHNQLEI-RTLGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 258 IKIEPdTELPVLLLGRSSDLRAGEFVVALGSPFSLQNTVTAGIVSTTQRggreLGLKNSD-IDYIQTDAIINHGNSGGPL 336
Cdd:PRK10898 130 LKINA-TNLPVIPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGR----IGLSPTGrQNFLQTDASINHGNSGGAL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 337 VNLDGDVIGINTL--------KVTAGISFAIPSD---RIRQFL-EDyhERQLKGkaplqkkYLGlrmlpLTLNLLQEMKR 404
Cdd:PRK10898 205 VNSLGELMGINTLsfdksndgETPEGIGFAIPTQlatKIMDKLiRD--GRVIRG-------YIG-----IGGREIAPLHA 270

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487143 405 QDPEFpDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQP---VTTTTDVIEAVKDNDFLSIIVLRGSQTLFLTVT 478
Cdd:PRK10898 271 QGGGI-DQLQGIVVNEVSPDGPAAKAGIQVNDLIISVNNKPaisALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVT 346
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 208-346 9.56e-33

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 121.37  E-value: 9.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  208 GSGFIVSEDGLIVTNAHVLTNQQKIQVE-----LQSGARYEATVKDIDHKLDLALIKI-EPDTELPVLLLGRSSDLRAGE 281
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVElvsvvLADGREYPATVVARDPDLDLALLRVsGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487143  282 FVVALGSPFSLQ-NTVTAGIVSTTQRGGRELGlknsDIDYIQTDAIINHGNSGGPLVNLDGDVIGI 346
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDGGD----DGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 386-480 1.05e-20

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: 86.99  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 386 YLGLRMLPLTLNLLQEMkRQDPEFPDV---SSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDV---IEAVKDN 459
Cdd:cd10838    3 YLGIQMTTLTPELAQQN-NRNPNSPVRipeVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVqriVEQAGVG 81

                         90       100
                 ....*....|....*....|.
gi 124487143 460 DFLSIIVLRGSQTLFLTVTPE 480
Cdd:cd10838   82 EELELTVLRGDRRQTLAVKPG 102
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 386-480 9.74e-20

circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana putative protease DEGP14 and related domains. DEGP14 is a putative protease belonging to the HtrA family of housekeeping proteases. 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 AtDEGP14-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: 467632 [Multi-domain]  Cd Length: 101  Bit Score: 84.05  E-value: 9.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 386 YLGLRMLPLTLNLLQEMKRQDPEFPDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKDNDFLSII 465
Cdd:cd23085    3 WLGMKMLELNEHIIAQLKERDPMFPDVKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQIIDALGDKVGKPFK 82

                         90
                 ....*....|....*...
gi 124487143 466 VL---RGSQTLFLTVTPE 480
Cdd:cd23085   83 VVvkrANKVQVTLTVTPE 100
IGFBP pfam00219
Insulin-like growth factor binding protein;
39-93 8.01e-18

Insulin-like growth factor binding protein;


Pssm-ID: 459717  Cd Length: 53  Bit Score: 76.98  E-value: 8.01e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124487143   39 CPDACDPTRCP-TLPTCSAGLapVPDRCGCCRVCAAAEGQECGGARGrPCAPRLRC 93
Cdd:pfam00219   1 CPPPCDPERCPpPPPGCPAGV--VLDGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 177-346 1.72e-16

MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens.


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 81.00  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 177 AAVVEKVAPSVVHLQlfRRSPLTNQeipSSSGSGFIVSeDGLIVTNAHVLTNQQKIQVELQSGARYEATVKDIDHKLDLA 256
Cdd:NF033740 187 SPAVRRARPSVVKVR--GTAPSCGR---ALEGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 257 LIKIePDTELPVLLLGrSSDLRAGEFVVALGSPFSLQNTVTAGIVSTTQRggrelgLKNSDI--------DYIQTDAIIN 328
Cdd:NF033740 261 VLAV-PGLGLPPLPFA-DEPAETGDDAIVLGYPEGGPFTATPARVRERIA------LSGPDIygsgtvtrEVYTLRGTVR 332

                        170
                 ....*....|....*...
gi 124487143 329 HGNSGGPLVNLDGDVIGI 346
Cdd:NF033740 333 PGNSGGPLLDPDGRVLGV 350
Trypsin pfam00089
Trypsin;
210-368 3.10e-15

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 74.79  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  210 GFIVSEDGlIVTNAHVLTNQQKIQVEL-------QSGARYEATVKDI---------DHKLDLALIKIEPDTEL-----PV 268
Cdd:pfam00089  29 GSLISENW-VLTAAHCVSGASDVKVVLgahnivlREGGEQKFDVEKIivhpnynpdTLDNDIALLKLESPVTLgdtvrPI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143  269 LLLGRSSDLRAGEFVVA--------LGSPFSLQnTVTAGIVSTtQRGGRELGLKNSDiDYIQTDAI---INHGNSGGPLV 337
Cdd:pfam00089 108 CLPDASSDLPVGTTCTVsgwgntktLGPSDTLQ-EVTVPVVSR-ETCRSAYGGTVTD-TMICAGAGgkdACQGDSGGPLV 184

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 124487143  338 NLDGDVIGINTLK----VTAGISFAIPSDRIRQFL 368
Cdd:pfam00089 185 CSDGELIGIVSWGygcaSGNYPGVYTPVSSYLDWI 219
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 386-477 4.37e-14

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: 67.70  E-value: 4.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 386 YLGLRMLPLTLNLLQEMkrqdpeFPDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAV---KDNDFL 462
Cdd:cd06779    3 YLGIEMENISPLLAKEL------GLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALdtkKPGDSL 76

                         90
                 ....*....|....*
gi 124487143 463 SIIVLRGSQTLFLTV 477
Cdd:cd06779   77 NLTILRDGKTLTVTV 91
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 418-481 1.03e-13

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 72.04  E-value: 1.03e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487143 418 VYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKDN--DFLSIIVLRGSQTLFLTVTPEI 481
Cdd:COG0750  132 VGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRASpgKPLTLTVERDGEELTLTVTPRL 197
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
 38-110 1.16e-12

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


Pssm-ID: 197525  Cd Length: 75  Bit Score: 63.25  E-value: 1.16e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487143    38 PCPdACDPTRCPTLP-TCSAGLapVPDRCGCCRVCAAAEGQECgGARGRPCAPRLRCGAPFSRDPSGGAWL---GTC 110
Cdd:smart00121   2 RCP-PCDPARCPPCPpGCAELV--RLDGCGCCPVCARQEGEPC-GVYTPRCAPGLRCQPPPGEERPLRALLhgqGVC 74
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 420-481 1.67e-12

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with its associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467638 [Multi-domain]  Cd Length: 83  Bit Score: 62.98  E-value: 1.67e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487143 420 EVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKDN--DFLSIIVLRGSQTLFLTVTPEI 481
Cdd:cd23081    5 EVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIVRIVRENpgKPLTLKIERDGKILTVTVTPEL 68
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 386-478 1.51e-11

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: 60.73  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 386 YLGLRMLPLTLnlLQEMKRQDPEFPD-VSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTD---VIEAVKDNDF 461
Cdd:cd06781    3 SLGISMVDLSD--VPEYEQQSLKLPSnVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDlrqILYSHKVGDT 80

                         90
                 ....*....|....*..
gi 124487143 462 LSIIVLRGSQTLFLTVT 478
Cdd:cd06781   81 VKVTIYRDGKEKTLNIK 97
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 387-477 2.43e-10

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


Pssm-ID: 467631 [Multi-domain]  Cd Length: 83  Bit Score: 56.87  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 387 LGLRMLPLTLNLLQemkrqdpefpdvsSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKD-NDFLSII 465
Cdd:cd23084    4 EGATVSNVTDEDGG-------------KGVVVTEVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRKVLKSkPSAVLLQ 70

                         90
                 ....*....|..
gi 124487143 466 VLRGSQTLFLTV 477
Cdd:cd23084   71 IKRGDSSRYLAL 82
PDZ_2 pfam13180
PDZ domain;
409-478 8.50e-10

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 54.97  E-value: 8.50e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487143  409 FPDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAV---KDNDFLSIIVLRGSQTLFLTVT 478
Cdd:pfam13180   1 FVDLEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALyghKPGDTVTLQVYRDGKLLTVEVK 73
Peptidase_M50 pfam02163
Peptidase family M50;
412-480 1.32e-09

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 59.04  E-value: 1.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487143  412 VSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKDNDF--LSIIVLRGSQTLFLTVTPE 480
Cdd:pfam02163  91 PPAPPVIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEALAKSPGkpITLTVERGGQTLTVTITPK 161
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 386-477 3.06e-09

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: 54.02  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 386 YLGLRMLPLTLNLLQEMKRQDPEfpdvssGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTD---VIEAVKDNDFL 462
Cdd:cd10839    3 WLGVQIQELTPDLAESFGLKEPK------GALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADlrnRVATTKPGTKV 76

                         90
                 ....*....|....*
gi 124487143 463 SIIVLRGSQTLFLTV 477
Cdd:cd10839   77 ELKILRDGKEKTLTV 91
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 410-470 4.15e-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: 53.54  E-value: 4.15e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487143   410 PDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTD--VIEAVKDN-DFLSIIVLRGS 470
Cdd:smart00228  22 KDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKAgGKVTLTVLRGG 85
cpPDZ2_EcRseP-like cd23083
circularly permuted PDZ domain 2 (PDZ-C) of Escherichia coli Regulator of sigma-E protease ...
 420-480 8.86e-09

circularly permuted PDZ domain 2 (PDZ-C) of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL) and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmaE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with it associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467640 [Multi-domain]  Cd Length: 85  Bit Score: 52.51  E-value: 8.86e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487143 420 EVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKDN--DFLSIIVLRGSQTLFLTVTPE 480
Cdd:cd23083    5 NVQPNSAAEKAGLQAGDRIVKVDGQPLTQWQTFVMAVRDNpgKPLALEIERQGSPLSLTLIPD 67
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 205-370 2.07e-07

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.22  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 205 SSSGSGFIVSEDgLIVTNAHVLTNQ------QKIQVEL-QSGARYEAT-----------VKDIDHKLDLALIKIEPDTEL 266
Cdd:COG3591   11 GGVCTGTLIGPN-LVLTAGHCVYDGagggwaTNIVFVPgYNGGPYGTAtatrfrvppgwVASGDAGYDYALLRLDEPLGD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 267 PV--LLLGRSSDLRAGEFVVALGSPFSLQNTVTAgivsttQRGGRELGLKNSDIDYiqtDAIINHGNSGGPLVNLDGD-- 342
Cdd:COG3591   90 TTgwLGLAFNDAPLAGEPVTIIGYPGDRPKDLSL------DCSGRVTGVQGNRLSY---DCDTTGGSSGSPVLDDSDGgg 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 124487143 343 -VIGINTLKVTAGISFAIP-SDRIRQFLED 370
Cdd:COG3591  161 rVVGVHSAGGADRANTGVRlTSAIVAALRA 190
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 412-478 3.81e-07

circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana DEGP1 (also known as protease Do-like 1, chloroplastic, protein DEGRADATION OF PERIPLASMIC PROTEINS 1, DEGP PROTEASE 1 and DEG1), and related domains. DEGP1 is a serine protease that is required at high temperature and may be involved in the degradation of damaged proteins. This family also includes Arabidopsis protease DEGP8/Do-like 8 (chloroplastic), a probable serine protease. 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 AtDEGP-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: 467618 [Multi-domain]  Cd Length: 102  Bit Score: 48.34  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 412 VSSGVFVYEVIQGSAAASSGL----RDH-------DVIVSINGQPVTTTTD---VIEAVKDNDFLSIIVLRGSQTLFLTV 477
Cdd:cd00990   21 VRSGVLVLDVPPGGPAAKAGLrgtkRDEfgrivlgDVIVAVDGKPVKNESDlyrALDEYKVGDVVTLKVLRGGTKVDLKV 100


                 .
gi 124487143 478 T 478
Cdd:cd00990  101 T 101
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 417-468 3.87e-07

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 46.75  E-value: 3.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124487143  417 FVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVK--DNDFLSIIVLR 468
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLLQgsAGESVTLTVRR 54
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 110-158 5.07e-07

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 46.33  E-value: 5.07e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 124487143  110 CGCAEgAEDAVVCGSDGRTYPSLCALRKENRAARQRGALPAVpVQKGAC 158
Cdd:pfam07648   4 CQCPK-TEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 415-457 6.60e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 46.89  E-value: 6.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 124487143  415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTT--DVIEAVK 457
Cdd:pfam00595  26 GIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTheEAVLALK 70
PRK10779 PRK10779
sigma E protease regulator RseP;
395-480 1.61e-06

sigma E protease regulator RseP;


Pssm-ID: 182723 [Multi-domain]  Cd Length: 449  Bit Score: 50.45  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487143 395 TLNLLQ---EMKRQDPEfpdVSSGV---------FVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVKDN--D 460
Cdd:PRK10779 193 TLDLRHwafEPDKQDPV---SSLGIrprgpqiepVLAEVQPNSAASKAGLQAGDRIVKVDGQPLTQWQTFVTLVRDNpgK 269

                         90       100
                 ....*....|....*....|
gi 124487143 461 FLSIIVLRGSQTLFLTVTPE 480
Cdd:PRK10779 270 PLALEIERQGSPLSLTLTPD 289
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 415-477 3.64e-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: 44.74  E-value: 3.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTT--DVIEAVKDNdflsiivlrGSQTLFLTV 477
Cdd:cd06768   24 GHFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESheQVVEKIKAS---------GNQVTLLVV 79
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 413-466 5.21e-06

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: 44.50  E-value: 5.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124487143 413 SSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPV--TTTTDVIEAVKD--NDFLSIIV 466
Cdd:cd06712   20 DSPVQVASVDPGSCAAEAGLKEGDYIVSVGGVDCkwSKHSEVVKLLKSagEEGLELQV 77
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 418-478 1.45e-05

Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 46.13  E-value: 1.45e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487143 418 VYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEA---VKDNDFLSIIVLRGSQTLFLTVT 478
Cdd:COG3031  155 VNPGRPGSLFSKLGLQPGDVITSINGQDLTDPAQALELlqqLRDASEVTLTVERNGQPVTLTYN 218
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 415-482 1.79e-05

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: 46.79  E-value: 1.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVT--TTTDVIEAV--KDNDFLSIIVLRG--SQTLFLTVTPEII 482
Cdd:COG0793   72 KVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAglTLDDAVKLLrgKAGTKVTLTIKRPgeGEPITVTLTRAEI 145
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 121-140 2.08e-05

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 41.51  E-value: 2.08e-05
                           10        20
                   ....*....|....*....|
gi 124487143   121 VCGSDGRTYPSLCALRKENR 140
Cdd:smart00280  13 VCGSDGVTYSNECHLCKAAC 32
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 411-467 2.91e-05

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: 42.14  E-value: 2.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487143 411 DVSSGVFVYEVIQGSAAASSG-LRDHDVIVSINGQPVTTTT--DVIEAVKDN-DFLSIIVL 467
Cdd:cd00136   21 DGGGGIFVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTheEAVELLKSAgGEVTLTVR 81
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 415-466 3.29e-05

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


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 42.25  E-value: 3.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTT--DVIEAVKDNDFLSIIV 466
Cdd:cd06737   28 GLFVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTheEVINLIKTKKTVSLKV 81
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 415-466 8.99e-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: 41.10  E-value: 8.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVT--TTTDVIEAVKDNDFLSIIV 466
Cdd:cd06755   27 GIFVSKVEKGSKAAEAGLKRGDQILEVNGQNFEniTLKKALEILRNNTHLSITV 80
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
415-480 1.30e-04

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 44.43  E-value: 1.30e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTT--DVIEAVKDNDFLSIIVLRGSQTLFLTVTPE 480
Cdd:COG3975  495 GLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTADNldDALAAYKPGDPIELLVFRRDELRTVTVTLA 562
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 405-450 1.38e-04

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: 40.78  E-value: 1.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124487143 405 QDPE-----FPDvsSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTT 450
Cdd:cd10822   25 QDPSknpfsYTD--KGIYVTRVSEGGPAEKAGLQVGDKILQVNGWDMTMVT 73
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 413-457 1.75e-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: 1.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 124487143 413 SSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVT--TTTDVIEAVK 457
Cdd:cd06782   13 DGYLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVRgmSLDEVVKLLR 59
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 121-145 1.87e-04

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 38.79  E-value: 1.87e-04
                         10        20
                 ....*....|....*....|....*
gi 124487143 121 VCGSDGRTYPSLCALRKENRAARQR 145
Cdd:cd00104    8 VCGSDGKTYSNECHLGCAACRSGRS 32
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 413-457 3.20e-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: 39.52  E-value: 3.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 124487143 413 SSGVFVYEVIQGSAAASSG-LRDHDVIVSINGQPVT--TTTDVIEAVK 457
Cdd:cd06791   30 LSGIFVKSIIPGSAADQDGrIQVNDQIIAVDGVNLQgfTNQEAVEVLR 77
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 415-449 1.03e-03

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: 38.38  E-value: 1.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 124487143 415 GVFVYEVIQGSAAASSG-LRDHDVIVSINGQPVTTT 449
Cdd:cd06689   44 GIFVQEIQPGSVAARDGrLKENDQILAINGQPLDQS 79
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 418-455 1.05e-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: 37.89  E-value: 1.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 124487143 418 VYEVIQGSAAASSGLRDHDVIVSINGQPvTTTTDVIEA 455
Cdd:cd06753   26 ISRVTPGGKAAQANLRPGDVILAINGES-TEGMTHLEA 62
PDZ2_ZO1-like_ds cd06728
PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and ZO-3, and related domains; form ...
 416-468 1.32e-03

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: 37.59  E-value: 1.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124487143 416 VFVYEVIQGS-AAASSGLRDHDVIVSINGQPV-----TTTTDVIEAVKDNdfLSIIVLR 468
Cdd:cd06728   22 IFVKEITPDSlAAKDGNLQEGDIILKINGTPVenlslSEAKKLIEKSKDK--LQLVVLR 78
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 410-477 1.42e-03

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: 37.68  E-value: 1.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124487143 410 PDVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVtTTTDVIEAVkdndflsiIVLRGSQTLFLTV 477
Cdd:cd06738   23 PTQKPGIFISNVKPGSLAEEVGLEVGDQIVEVNGTSF-TNVDHKEAV--------MALKSSRHLTITV 81
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 415-457 1.71e-03

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: 37.62  E-value: 1.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDViEAVK 457
Cdd:cd06702   33 GIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATHQ-EAVS 74
cpPDZ2_MamE-like cd23086
circularly permuted PDZ domain 2 of Magnetospirillum magneticum magnetosome formation protease ...
 415-457 2.08e-03

circularly permuted PDZ domain 2 of Magnetospirillum magneticum magnetosome formation protease MamE, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Magnetospirillum magneticum MamE (also known as magnetochrome MamE and magnetosome serine protease MamE), and related domains. MamE is a serine protease required to produce magnetite crystals in the magnetotactic bacterium M. magneticum. It is involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome, and likely cleaves at least itself, MamO and MamP. Its autoproteolysis is stimulated by exogenous substrates or peptides that bind to its PDZ domains. Peptide binding to either the first or the second PDZ domain of MamE can activate proteolysis; activation through PDZ2 is much weaker. 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 MamE-like PDZ domain 2 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467633 [Multi-domain]  Cd Length: 96  Bit Score: 37.62  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDVIEAVK 457
Cdd:cd23086   31 GAQVAEVLAGSRAAVAGLQANDLILEVNNRPVTSPARLDAAIK 73
cpPDZ_RseP_YlbL-like cd10824
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), ...
 416-480 3.05e-03

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), Bacillus subtilis YlbL protease, and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), Bacillus subtilis YlbL, and related domains, including archaeal and chloroplast PDZ domains. RseP participates in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmaE) protein RseA. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. 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 beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP-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: 467636 [Multi-domain]  Cd Length: 82  Bit Score: 36.78  E-value: 3.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124487143 416 VFVYEVIQGSAAASSgLRDHDVIVSINGQPVTTTTDVIEAVKDN---DFLSIIVLRGSQTLFLTVTPE 480
Cdd:cd10824    1 VVVLSVKPNSPAAKA-LHAGDLITEIDGQPTKSWQTFIDYIHDKkvgESVKITYKHGNKNEEASLKLT 67
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 415-477 3.20e-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: 36.57  E-value: 3.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDViEAVKdndflsiiVLRGSQTLFLTV 477
Cdd:cd06740   28 GIYVSLVEPGSLAEKEGLRVGDQILRVNDVSFEKVTHA-EAVK--------ILRVSKKLVLSV 81
PDZ1_syntenin-like cd06721
PDZ domain 1 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 411-447 3.27e-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: 36.44  E-value: 3.27e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 124487143 411 DVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVT 447
Cdd:cd06721   19 SIDKGVFVQLVQANSPAALAGLRFGDQILQINGENVA 55
PDZ_ARHGEF11-12-like cd23069
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 416-467 3.59e-03

PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGEF11, ARHGEF12, and related domains. This subfamily includes the GEFs (guanine exchange factors) ARHGEF11 (Rho guanine nucleotide exchange factor 11, known as PDZ-RhoGEF) and ARHGEF12 (Rho guanine nucleotide exchange factor 12, also known as leukemia-associated RhoGEF). GEFs activate Rho GTPases by promoting GTP binding. ARHGEF11/12 are regulators of G protein signaling (RGS) domain-containing GEFs; the RGS domain mediates their binding to and activation of Galpha (and Gq also in the case of ARHGEF12), in response to G-protein coupled receptor activation. ARHGEF11 and 12 are involved in serum-signaling, and regulate Yes-Associated Protein (YAP1)-dependent transcription. The ARHGEF12 PDZ domain binds plexin-B1 and the receptor tyrosine kinase insulin-like growth factor receptor (IGF-R1) beta-subunit. ARHGEF12 also interacts with glutamate receptor delta-1(GluD1), a postsynaptic organizer of inhibitory synapses in cortical pyramidal neurons. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGEF11-12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467282 [Multi-domain]  Cd Length: 76  Bit Score: 36.22  E-value: 3.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124487143 416 VFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTT--DVIEAVKDNDFLSIIVL 467
Cdd:cd23069   23 VFVQSVKEGGAAYRAGVQEGDRIIKVNGTLVTHSNhlEVVKLIKSGSYVALTLL 76
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 418-467 4.23e-03

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: 36.13  E-value: 4.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 124487143 418 VYEVIQGSAAASSGLRDHDVIVSINGQPVT--TTTDVIEAV-KDNDFLSIIVL 467
Cdd:cd10820   26 VAKIRKKSKAALAGLCEGDELLSINGKPCAdlSHSEAMDLIdSSGDTLQLLIK 78
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 415-477 4.32e-03

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


Pssm-ID: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 36.09  E-value: 4.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDViEAVKdndflsiiVLRGSQTLFLTV 477
Cdd:cd06741   27 GIYVTGVDPGSVAENAGLKVGDQILEVNGRSFLDITHD-EAVK--------ILKSSKHLIMTV 80
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 414-444 6.19e-03

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: 35.68  E-value: 6.19e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 124487143 414 SGVFVYEVIQGSAAASSG-LRDHDVIVSINGQ 444
Cdd:cd06678   24 PGVFILDLLEGGLAARDGrLKSDDRVLAINGQ 55
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 402-447 7.86e-03

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: 35.58  E-value: 7.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 124487143 402 MKRQDPEFP---------DVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVT 447
Cdd:cd23068    4 LRRDDSNTPwgfrlqggaDFGQPLSIQKVNPGSPADKAGLRRGDVILRINGTDTS 58
cpPDZ1_MamE-like cd23087
circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease ...
 391-452 7.95e-03

circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease MamE and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Magnetospirillum magneticum MamE (also known as magnetochrome MamE and magnetosome serine protease MamE), and related domains. MamE is a serine protease required to produce magnetite crystals in the magnetotactic bacterium M. magneticum. It is involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome, and likely cleaves at least itself, MamO and MamP. MamE-PDZ1 may bind MamB. Its autoproteolysis is stimulated by exogenous substrates or peptides that bind to its PDZ domains. Peptide binding to either the first or the second PDZ domain of MamE can activate proteolysis; activation through PDZ2 is much weaker. 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 MamE-like 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: 467634 [Multi-domain]  Cd Length: 91  Bit Score: 35.62  E-value: 7.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487143 391 MLPLTLNLLQEMKRQDPEFPdVSSGVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTTTTDV 452
Cdd:cd23087    3 LLGAALTPMQQRLGQQTNLP-AGRGVFVSGVTPNTPAAAAGLRPGDVILKVDGRPVHQPEEV 63
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 415-478 9.09e-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: 35.45  E-value: 9.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487143 415 GVFVYEVIQGSAAASSGLRDHDVIVSINGQPVTT---TTDVIEAVKDNDFLSIIVLRGSQTLFLTVT 478
Cdd:cd06777   26 GALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISvleLMDLVAEIRPGTVIPVVVLRDGKQLTLEVT 92
PDZ_MAST4 cd23076
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ ...
 418-479 9.51e-03

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST4, and related domains. MAST4 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain. MAST4 is a component of the AICD-MAST4-FOXO1-RTKN2 neuroprotective pathway; MAST4 phosphorylation of forkhead box protein O1 (FOXO1) regulates rhotekin 2 (RTKN2) expression. As this pathway is repressed in Alzheimer's Disease (AD), MAST4 may play a role in preventing AD pathogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST4 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467289 [Multi-domain]  Cd Length: 95  Bit Score: 35.78  E-value: 9.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487143 418 VYEVIQGSAAASSGLRDHDVIVSINGQPV--TTTTDVIEavkdndflsiIVLRGSQTLFLTVTP 479
Cdd:cd23076   37 VWNVEEGSPACQAGLKAGDLITHINGEPVhgLVHTEVIE----------LLLKSGNKVSITTTP 90
 
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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