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Conserved domains on  [gi|194740868|ref|XP_001952912|]
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serine protease HTRA2, mitochondrial [Drosophila ananassae]

Protein Classification

S1C family serine protease( domain architecture ID 11415729)

S1C family serine protease contains the catalytic triad His, Asp and Ser, similar to Bacillus subtilis serine protease Do-like HtrB that degrades abnormal exported proteins

CATH:  2.30.42.10
EC:  3.4.21.-
Gene Ontology:  GO:0004252
MEROPS:  S1C
PubMed:  9383148|12408815|30712672|11158544|11283303

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 ...
 145-425 4.09e-90

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: 273.95  E-value: 4.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 145 GSGFIIEQNGLILTNAHVVinKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVSNLSVMRLGKSSTLRSGEWVVAL 224
Cdd:COG0265    3 GSGVIISPDGYILTNNHVV--EGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 225 GSPLALSNTVTAGVISSTQRASQELGLRNRDiNYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVT-----AGISFAIPI 299
Cdd:COG0265   81 GNPFGLGQTVTAGIVSALGRSIGSSGGGTYD-DFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 300 DYVKVFLEraaerrkkgAAYKTGYPVKRYMGITMLTLTPDIlfelkSRSQNMPSnlTHGVLVWKVIVGSPAHSGGLQPGD 379
Cdd:COG0265  160 NLAKRVVE---------QLIETGRVRRGWLGVTIQPVTPEL-----AEALGLPE--PEGVLVARVEPGSPAAKAGLRPGD 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 194740868 380 IVTHINKKEIKNSSDVYDALADNS--KHLDIVILRGVKQMHVTITPED 425
Cdd:COG0265  224 VILAVDGKPVTSARDLQRLLASLKpgDTVTLTVLRGGKELTVTVTLGE 271
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 145-425 4.09e-90

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: 273.95  E-value: 4.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 145 GSGFIIEQNGLILTNAHVVinKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVSNLSVMRLGKSSTLRSGEWVVAL 224
Cdd:COG0265    3 GSGVIISPDGYILTNNHVV--EGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 225 GSPLALSNTVTAGVISSTQRASQELGLRNRDiNYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVT-----AGISFAIPI 299
Cdd:COG0265   81 GNPFGLGQTVTAGIVSALGRSIGSSGGGTYD-DFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 300 DYVKVFLEraaerrkkgAAYKTGYPVKRYMGITMLTLTPDIlfelkSRSQNMPSnlTHGVLVWKVIVGSPAHSGGLQPGD 379
Cdd:COG0265  160 NLAKRVVE---------QLIETGRVRRGWLGVTIQPVTPEL-----AEALGLPE--PEGVLVARVEPGSPAAKAGLRPGD 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 194740868 380 IVTHINKKEIKNSSDVYDALADNS--KHLDIVILRGVKQMHVTITPED 425
Cdd:COG0265  224 VILAVDGKPVTSARDLQRLLASLKpgDTVTLTVLRGGKELTVTVTLGE 271
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 110-422 3.89e-73

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: 235.58  E-value: 3.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  110 IADVVAGCADSVVYIEIKDTR-----------HFDYFSGQP-----------ITASNGSGFIIEQNGLILTNAHVVINKp 167
Cdd:TIGR02037   3 FAPLVEKVAPAVVNISVEGTVkrrnrppalppFFRQFFGDDmpdfprqqreqKVRGLGSGVIISADGYVLTNNHVVDGA- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  168 hTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQV-SNLSVMRLGKSSTLRSGEWVVALGSPLALSNTVTAGVISSTQRAS 246
Cdd:TIGR02037  82 -DEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAkKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  247 QELGLRNrdiNYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVT-----AGISFAIPIDYVKVFLERAAERRKkgaaykt 321
Cdd:TIGR02037 161 LGIGDYE---NFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNMAKNVVDQLIEGGK------- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  322 gypVKR-YMGITMLTLTPDILFELKSRSQnmpsnltHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALA 400
Cdd:TIGR02037 231 ---VKRgWLGVTIQEVTSDLAKSLGLEKQ-------RGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIG 300

                         330       340
                  ....*....|....*....|....
gi 194740868  401 DN--SKHLDIVILRGVKQMHVTIT 422
Cdd:TIGR02037 301 TLkpGKKVTLGILRKGKEKTITVT 324
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 326-425 2.00e-45

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: 152.27  E-value: 2.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 326 KRYMGITMLTLTPDILFELKSRSQNMPsNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADNSKh 405
Cdd:cd06785    1 KRYIGIRMLTLTPSLLEELKQRNPDFP-DVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSS- 78

                         90       100
                 ....*....|....*....|
gi 194740868 406 LDIVILRGVKQMHVTITPED 425
Cdd:cd06785   79 LLVVVRRGNEDLLLTVTPEE 98
PRK10942 PRK10942
serine endoprotease DegP;
145-389 6.89e-43

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 156.85  E-value: 6.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 145 GSGFIIE-QNGLILTNAHVVINKphTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQ-VSNLSVMRLGKSSTLRSGEWVV 222
Cdd:PRK10942 113 GSGVIIDaDKGYVVTNNHVVDNA--TKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQnPKNLTAIKMADSDALRVGDYTV 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 223 ALGSPLALSNTVTAGVISSTQRASqeLGLRNRDiNYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVTA-----GISFAI 297
Cdd:PRK10942 191 AIGNPYGLGETVTSGIVSALGRSG--LNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTAILAPdggniGIGFAI 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 298 PIDYVKVFLERAAERRKkgaayktgypVKR-YMGITMLTLTPDIlfelksrSQNMPSNLTHGVLVWKVIVGSPAHSGGLQ 376
Cdd:PRK10942 268 PSNMVKNLTSQMVEYGQ----------VKRgELGIMGTELNSEL-------AKAMKVDAQRGAFVSQVLPNSSAAKAGIK 330

                        250
                 ....*....|...
gi 194740868 377 PGDIVTHINKKEI 389
Cdd:PRK10942 331 AGDVITSLNGKPI 343
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 145-284 1.11e-30

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 114.83  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  145 GSGFIIEQNGLILTNAHVV---INKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVS--NLSVMRLGKSSTLRSGE 219
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVddaEEAAVELVSVVLADGREYPATVVARDPDLDLALLRVSGDgrGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194740868  220 WVVALGSPLALS-NTVTAGVISSTQRASQElglrNRDINYLQTDAAITFGNSGGPLVNLDGEAIGV 284
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDG----GDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 111-284 9.54e-12

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: 65.98  E-value: 9.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 111 ADVVAGCADSVVYIEikdtrhFDYFSGQpiTASNGSGFIIEQnGLILTNAHVV--INKPhtmvQVRLSDGRTFPATIEDV 188
Cdd:NF033740 187 SPAVRRARPSVVKVR------GTAPSCG--RALEGSGFVVAP-DRVMTNAHVVagTDEV----TVETVGGGTLDARVVYY 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 189 DQTSDLATLRIQVSNLSVMRLGkSSTLRSGEWVVALGSPLALSNTVTAGVISSTQRAS----QELGLRNRDInYlQTDAA 264
Cdd:NF033740 254 DPDRDIAVLAVPGLGLPPLPFA-DEPAETGDDAIVLGYPEGGPFTATPARVRERIALSgpdiYGSGTVTREV-Y-TLRGT 330

                        170       180
                 ....*....|....*....|
gi 194740868 265 ITFGNSGGPLVNLDGEAIGV 284
Cdd:NF033740 331 VRPGNSGGPLLDPDGRVLGV 350
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 357-413 1.76e-08

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: 51.23  E-value: 1.76e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 194740868   357 HGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSD--VYDALADNSKHLDIVILRG 413
Cdd:smart00228  26 GGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKAGGKVTLTVLRG 84
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 145-425 4.09e-90

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: 273.95  E-value: 4.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 145 GSGFIIEQNGLILTNAHVVinKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVSNLSVMRLGKSSTLRSGEWVVAL 224
Cdd:COG0265    3 GSGVIISPDGYILTNNHVV--EGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 225 GSPLALSNTVTAGVISSTQRASQELGLRNRDiNYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVT-----AGISFAIPI 299
Cdd:COG0265   81 GNPFGLGQTVTAGIVSALGRSIGSSGGGTYD-DFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 300 DYVKVFLEraaerrkkgAAYKTGYPVKRYMGITMLTLTPDIlfelkSRSQNMPSnlTHGVLVWKVIVGSPAHSGGLQPGD 379
Cdd:COG0265  160 NLAKRVVE---------QLIETGRVRRGWLGVTIQPVTPEL-----AEALGLPE--PEGVLVARVEPGSPAAKAGLRPGD 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 194740868 380 IVTHINKKEIKNSSDVYDALADNS--KHLDIVILRGVKQMHVTITPED 425
Cdd:COG0265  224 VILAVDGKPVTSARDLQRLLASLKpgDTVTLTVLRGGKELTVTVTLGE 271
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 110-422 3.89e-73

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: 235.58  E-value: 3.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  110 IADVVAGCADSVVYIEIKDTR-----------HFDYFSGQP-----------ITASNGSGFIIEQNGLILTNAHVVINKp 167
Cdd:TIGR02037   3 FAPLVEKVAPAVVNISVEGTVkrrnrppalppFFRQFFGDDmpdfprqqreqKVRGLGSGVIISADGYVLTNNHVVDGA- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  168 hTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQV-SNLSVMRLGKSSTLRSGEWVVALGSPLALSNTVTAGVISSTQRAS 246
Cdd:TIGR02037  82 -DEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAkKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  247 QELGLRNrdiNYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVT-----AGISFAIPIDYVKVFLERAAERRKkgaaykt 321
Cdd:TIGR02037 161 LGIGDYE---NFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNMAKNVVDQLIEGGK------- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  322 gypVKR-YMGITMLTLTPDILFELKSRSQnmpsnltHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALA 400
Cdd:TIGR02037 231 ---VKRgWLGVTIQEVTSDLAKSLGLEKQ-------RGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIG 300

                         330       340
                  ....*....|....*....|....
gi 194740868  401 DN--SKHLDIVILRGVKQMHVTIT 422
Cdd:TIGR02037 301 TLkpGKKVTLGILRKGKEKTITVT 324
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 326-425 2.00e-45

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: 152.27  E-value: 2.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 326 KRYMGITMLTLTPDILFELKSRSQNMPsNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADNSKh 405
Cdd:cd06785    1 KRYIGIRMLTLTPSLLEELKQRNPDFP-DVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSS- 78

                         90       100
                 ....*....|....*....|
gi 194740868 406 LDIVILRGVKQMHVTITPED 425
Cdd:cd06785   79 LLVVVRRGNEDLLLTVTPEE 98
PRK10942 PRK10942
serine endoprotease DegP;
145-389 6.89e-43

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 156.85  E-value: 6.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 145 GSGFIIE-QNGLILTNAHVVINKphTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQ-VSNLSVMRLGKSSTLRSGEWVV 222
Cdd:PRK10942 113 GSGVIIDaDKGYVVTNNHVVDNA--TKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQnPKNLTAIKMADSDALRVGDYTV 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 223 ALGSPLALSNTVTAGVISSTQRASqeLGLRNRDiNYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVTA-----GISFAI 297
Cdd:PRK10942 191 AIGNPYGLGETVTSGIVSALGRSG--LNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTAILAPdggniGIGFAI 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 298 PIDYVKVFLERAAERRKkgaayktgypVKR-YMGITMLTLTPDIlfelksrSQNMPSNLTHGVLVWKVIVGSPAHSGGLQ 376
Cdd:PRK10942 268 PSNMVKNLTSQMVEYGQ----------VKRgELGIMGTELNSEL-------AKAMKVDAQRGAFVSQVLPNSSAAKAGIK 330

                        250
                 ....*....|...
gi 194740868 377 PGDIVTHINKKEI 389
Cdd:PRK10942 331 AGDVITSLNGKPI 343
PRK10898 PRK10898
serine endoprotease DegS;
145-422 8.30e-40

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 145.53  E-value: 8.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 145 GSGFIIEQNGLILTNAHVvINKPHTMVqVRLSDGRTFPATIEDVDQTSDLATLRIQVSNLSVMRLGKSSTLRSGEWVVAL 224
Cdd:PRK10898  80 GSGVIMDQRGYILTNKHV-INDADQII-VALQDGRVFEALLVGSDSLTDLAVLKINATNLPVIPINPKRVPHIGDVVLAI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 225 GSPLALSNTVTAGVISSTQRasqeLGLR-NRDINYLQTDAAITFGNSGGPLVNLDGEAIGVNSM--------KVTAGISF 295
Cdd:PRK10898 158 GNPYNLGQTITQGIISATGR----IGLSpTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLsfdksndgETPEGIGF 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 296 AIPIDYVKVFLERAAerrkkgaayKTGYPVKRYMGITMLTLTPdilfelkSRSQNMPSNLTHGVLVWKVIVGSPAHSGGL 375
Cdd:PRK10898 234 AIPTQLATKIMDKLI---------RDGRVIRGYIGIGGREIAP-------LHAQGGGIDQLQGIVVNEVSPDGPAAKAGI 297

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 194740868 376 QPGDIVTHINKKEIKNSSDVYDALADNS--KHLDIVILRGVKQMHVTIT 422
Cdd:PRK10898 298 QVNDLIISVNNKPAISALETMDQVAEIRpgSVIPVVVMRDDKQLTLQVT 346
PRK10139 PRK10139
serine endoprotease DegQ;
145-422 1.82e-36

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 138.93  E-value: 1.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 145 GSGFIIEQN-GLILTNAHVvINKPHTmVQVRLSDGRTFPATIEDVDQTSDLATLRIQ-VSNLSVMRLGKSSTLRSGEWVV 222
Cdd:PRK10139  92 GSGVIIDAAkGYVLTNNHV-INQAQK-ISIQLNDGREFDAKLIGSDDQSDIALLQIQnPSKLTQIAIADSDKLRVGDFAV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 223 ALGSPLALSNTVTAGVISSTQRASQEL-GLRNrdinYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKV-----TAGISFA 296
Cdd:PRK10139 170 AVGNPFGLGQTATSGIISALGRSGLNLeGLEN----FIQTDASINRGNSGGALLNLNGELIGINTAILapgggSVGIGFA 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 297 IPIDYVKVFLERAAERRKkgaayktgypVKR-YMGITMLTLTPDIlfelksrSQNMPSNLTHGVLVWKVIVGSPAHSGGL 375
Cdd:PRK10139 246 IPSNMARTLAQQLIDFGE----------IKRgLLGIKGTEMSADI-------AKAFNLDVQRGAFVSEVLPNSGSAKAGV 308

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 194740868 376 QPGDIVTHINKKEIKNSSDVYDALA--DNSKHLDIVILRGVKQMHVTIT 422
Cdd:PRK10139 309 KAGDIITSLNGKPLNSFAELRSRIAttEPGTKVKLGLLRNGKPLEVEVT 357
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 145-284 1.11e-30

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 114.83  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  145 GSGFIIEQNGLILTNAHVV---INKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVS--NLSVMRLGKSSTLRSGE 219
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVddaEEAAVELVSVVLADGREYPATVVARDPDLDLALLRVSGDgrGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194740868  220 WVVALGSPLALS-NTVTAGVISSTQRASQElglrNRDINYLQTDAAITFGNSGGPLVNLDGEAIGV 284
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDG----GDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 328-425 3.62e-17

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: 76.59  E-value: 3.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 328 YMGITMLTLTPDILFELKsRSQNMPSNL--THGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVyDALADNSK- 404
Cdd:cd10838    3 YLGIQMTTLTPELAQQNN-RNPNSPVRIpeVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDV-QRIVEQAGv 80

                         90       100
                 ....*....|....*....|...
gi 194740868 405 --HLDIVILRGVKQMHVTITPED 425
Cdd:cd10838   81 geELELTVLRGDRRQTLAVKPGD 103
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 326-421 5.71e-17

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: 75.79  E-value: 5.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 326 KRYMGITMLTLTPDILFELKSRSQNmpsnlthGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDAL--ADNS 403
Cdd:cd06779    1 RPYLGIEMENISPLLAKELGLPVNR-------GVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALdtKKPG 73

                         90
                 ....*....|....*...
gi 194740868 404 KHLDIVILRGVKQMHVTI 421
Cdd:cd06779   74 DSLNLTILRDGKTLTVTV 91
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 328-425 1.43e-15

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: 72.11  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 328 YMGITMLTLTPDILFELKSRSQNMPsNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADN-SKHL 406
Cdd:cd23085    3 WLGMKMLELNEHIIAQLKERDPMFP-DVKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQIIDALGDKvGKPF 81

                         90       100
                 ....*....|....*....|
gi 194740868 407 DIVILRGVK-QMHVTITPED 425
Cdd:cd23085   82 KVVVKRANKvQVTLTVTPEE 101
Trypsin pfam00089
Trypsin;
147-303 1.83e-12

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 66.31  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  147 GFIIEQNGlILTNAHVVINKPHTMV-----QVRLSDGRTFPATIEDV---------DQTSDLATLRIQ---VSNLSVM-- 207
Cdd:pfam00089  29 GSLISENW-VLTAAHCVSGASDVKVvlgahNIVLREGGEQKFDVEKIivhpnynpdTLDNDIALLKLEspvTLGDTVRpi 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868  208 ---RLGKSSTLRSGEWVVALGSP--LALSNTVTAGVIS--STQRASQELGLRNRDiNYLQTDA---AITFGNSGGPLVNL 277
Cdd:pfam00089 108 clpDASSDLPVGTTCTVSGWGNTktLGPSDTLQEVTVPvvSRETCRSAYGGTVTD-TMICAGAggkDACQGDSGGPLVCS 186

                         170       180       190
                  ....*....|....*....|....*....|
gi 194740868  278 DGEAIGVNSMK----VTAGISFAIPIDYVK 303
Cdd:pfam00089 187 DGELIGIVSWGygcaSGNYPGVYTPVSSYL 216
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 328-422 4.40e-12

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: 61.88  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 328 YMGITMLTLtpDILFELKSRSQNMPSNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALadnSKHLD 407
Cdd:cd06781    3 SLGISMVDL--SDVPEYEQQSLKLPSNVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQIL---YSHKV 77

                         90       100
                 ....*....|....*....|
gi 194740868 408 -----IVILRGVKQMHVTIT 422
Cdd:cd06781   78 gdtvkVTIYRDGKEKTLNIK 97
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 111-284 9.54e-12

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: 65.98  E-value: 9.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 111 ADVVAGCADSVVYIEikdtrhFDYFSGQpiTASNGSGFIIEQnGLILTNAHVV--INKPhtmvQVRLSDGRTFPATIEDV 188
Cdd:NF033740 187 SPAVRRARPSVVKVR------GTAPSCG--RALEGSGFVVAP-DRVMTNAHVVagTDEV----TVETVGGGTLDARVVYY 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 189 DQTSDLATLRIQVSNLSVMRLGkSSTLRSGEWVVALGSPLALSNTVTAGVISSTQRAS----QELGLRNRDInYlQTDAA 264
Cdd:NF033740 254 DPDRDIAVLAVPGLGLPPLPFA-DEPAETGDDAIVLGYPEGGPFTATPARVRERIALSgpdiYGSGTVTREV-Y-TLRGT 330

                        170       180
                 ....*....|....*....|
gi 194740868 265 ITFGNSGGPLVNLDGEAIGV 284
Cdd:NF033740 331 VRPGNSGGPLLDPDGRVLGV 350
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 363-424 1.36e-11

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: 60.28  E-value: 1.36e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194740868 363 KVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADN-SKHLDIVILRGVKQMHVTITPE 424
Cdd:cd23081    5 EVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIVRIVRENpGKPLTLKIERDGKILTVTVTPE 67
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 328-421 1.99e-11

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: 59.80  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 328 YMGITMLTLTPDIL--FELKSrsqnmpsnlTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADNS-- 403
Cdd:cd10839    3 WLGVQIQELTPDLAesFGLKE---------PKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADLRNRVATTKpg 73

                         90
                 ....*....|....*...
gi 194740868 404 KHLDIVILRGVKQMHVTI 421
Cdd:cd10839   74 TKVELKILRDGKEKTLTV 91
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 363-424 1.72e-09

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 58.94  E-value: 1.72e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194740868 363 KVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADNS-KHLDIVILRGVKQMHVTITPE 424
Cdd:COG0750  134 EVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRASPgKPLTLTVERDGEELTLTVTPR 196
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 354-422 6.28e-09

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: 53.35  E-value: 6.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 354 NLTHGVLVWKVIVGSPAHSGGLQP-----------GDIVTHINKKEIKNSSDVYDALaDNSK---HLDIVILRGVKQMHV 419
Cdd:cd00990   20 GVRSGVLVLDVPPGGPAAKAGLRGtkrdefgrivlGDVIVAVDGKPVKNESDLYRAL-DEYKvgdVVTLKVLRGGTKVDL 98


                 ...
gi 194740868 420 TIT 422
Cdd:cd00990   99 KVT 101
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 357-413 1.76e-08

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: 51.23  E-value: 1.76e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 194740868   357 HGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSD--VYDALADNSKHLDIVILRG 413
Cdd:smart00228  26 GGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKAGGKVTLTVLRG 84
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 120-312 2.73e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 53.53  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 120 SVVYIEIKDTRHFdyfsgqpitasnGSGFIIEQNgLILTNAHVVIN----KPHTMVQV------------RLSDGRTFPA 183
Cdd:COG3591    1 AVGRLETDGGGGV------------CTGTLIGPN-LVLTAGHCVYDgaggGWATNIVFvpgynggpygtaTATRFRVPPG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 184 TIEDVDQTSDLATLRIQ---VSNLSVMRLGKSSTLRSGEWVVALGSPLALSNTVTAGvisstqrasQELGLRNRDINYLQ 260
Cdd:COG3591   68 WVASGDAGYDYALLRLDeplGDTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSLD---------CSGRVTGVQGNRLS 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 194740868 261 TDAAITFGNSGGPLVNLD---GEAIGVNSMKVTAGISFAIPIDYVKV-FLERAAER 312
Cdd:COG3591  139 YDCDTTGGSSGSPVLDDSdggGRVVGVHSAGGADRANTGVRLTSAIVaALRAWASA 194
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 352-413 4.31e-08

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: 50.32  E-value: 4.31e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194740868 352 PSNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADNSKHLDIVILRG 413
Cdd:cd23084   13 DEDGGKGVVVTEVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRKVLKSKPSAVLLQIKRG 74
Peptidase_M50 pfam02163
Peptidase family M50;
355-425 5.15e-08

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 54.04  E-value: 5.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194740868  355 LTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADN-SKHLDIVILRGVKQMHVTITPED 425
Cdd:pfam02163  91 PPAPPVIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEALAKSpGKPITLTVERGGQTLTVTITPKS 162
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 364-412 1.03e-06

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 45.60  E-value: 1.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 194740868  364 VIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALA-DNSKHLDIVILR 412
Cdd:pfam17820   5 VVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLLQgSAGESVTLTVRR 54
PDZ_MAST3 cd23075
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 3 (MAST3); PDZ ...
 360-389 2.05e-05

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 3 (MAST3); PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST3, and related domains. MAST3 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. MAST3 plays a critical role in regulating the immune response of inflammatory bowel disease (IBD), and is involved in the process of cytoskeleton organization, intracellular signal transduction and peptidyl-serine phosphorylation. MAST3 also promotes the proliferation and inflammation of fibroblast-like synoviocytes in rheumatoid arthritis. Binding partners of MAST3 include cAMP-regulated phosphoprotein (ARPP-16) and the tumor suppressor PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST3 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467288 [Multi-domain]  Cd Length: 94  Bit Score: 43.09  E-value: 2.05e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 194740868 360 LVWKVIVGSPAHSGGLQPGDIVTHINKKEI 389
Cdd:cd23075   36 MVWSVEDGSPAQEAGLRAGDLITHINGESV 65
PDZ_MAST cd06705
PDZ domain of the microtubule-associated serine-threonine (MAST) protein kinase family; PDZ ...
 360-423 3.20e-05

PDZ domain of the microtubule-associated serine-threonine (MAST) protein kinase family; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinases, including MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain; MAST family member MASTL is a shorter protein lacking the PDZ domain. The PDZ domain gives the MAST family the capacity to scaffold its own kinase activity. These kinases are implicated in the inhibition of neurite outgrowth and regeneration in cultured cells. Their binding partners include microtubules, beta2-syntrophin, TNF receptor-associated factor 6 (TRAF6), cAMP-regulated phosphoprotein (ARPP-16), and PTEN. This family also includes Caenorhabditis elegans KIN-4 MAST kinase, a key longevity factor acting through binding PTEN phosphatase, and Drosophila Drop out which regulates dynein-dependent transport during embryonic development. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467189 [Multi-domain]  Cd Length: 93  Bit Score: 42.23  E-value: 3.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194740868 360 LVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSdvydaladnskHLDIV--ILRGVKQMHVTITP 423
Cdd:cd06705   36 LVTAVEEGSPAYEAGLRPGDLITHVNGEPVQGLL-----------HTQVVqlILKGGNKVSIRATP 90
PDZ_2 pfam13180
PDZ domain;
353-422 4.01e-05

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 41.49  E-value: 4.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194740868  353 SNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADNSKHLDIV--ILRGVKQMHVTIT 422
Cdd:pfam13180   2 VDLEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALYGHKPGDTVTlqVYRDGKLLTVEVK 73
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 361-412 4.37e-05

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


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 41.74  E-value: 4.37e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194740868 361 VWKVIVGSPAHSGGLQPGDIVTHINKKEIKN--SSDVYDALADNSKHLDIVILR 412
Cdd:cd23068   29 IQKVNPGSPADKAGLRRGDVILRINGTDTSNltHKQAQDLIKRAGNDLQLTVQR 82
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 356-422 1.13e-04

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: 40.84  E-value: 1.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194740868 356 THGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALAD--NSKHLDIVILRGVKQMHVTIT 422
Cdd:cd06777   24 LQGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLELMDLVAEirPGTVIPVVVLRDGKQLTLEVT 92
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 358-422 1.25e-04

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: 43.71  E-value: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194740868 358 GVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIK--NSSDVYDAL--ADNSKhLDIVILRGVKQMHVTIT 422
Cdd:COG0793   72 KVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAglTLDDAVKLLrgKAGTK-VTLTIKRPGEGEPITVT 139
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 353-411 3.12e-04

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: 39.06  E-value: 3.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194740868 353 SNLTHGVLVWKVIVGSPAH-SGGLQPGDIVTHINKKEIKNSS--DVYDALADNSKHLDIVIL 411
Cdd:cd00136   20 KDGGGGIFVSRVEPGGPAArDGRLRVGDRILEVNGVSLEGLTheEAVELLKSAGGEVTLTVR 81
cpPDZ_MBTPS2-like cd06775
circularly permuted PDZ domain of membrane-bound transcription factor site-2 protease (MBTPS2, ...
 357-394 7.99e-04

circularly permuted PDZ domain of membrane-bound transcription factor site-2 protease (MBTPS2, also known as S2P) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MBTPS2, also known as sterol regulatory element-binding protein (SREBP) Site-2 protease (S2P), and related domains. MBTPS2 is a zinc metalloprotease (MEROPS family M50A). In the Golgi, it catalyzes the second step in the proteolytic activation of sterol regulatory element-binding proteins (SREBPs), releasing the transcriptionally active N-terminal domain of SREBP, which then enters the nucleus and activates genes encoding the low density lipoprotein (LDL) receptor and enzymes for cholesterol and fatty acid biosynthesis. MBTPS2 also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF6. ATF6 is a membrane-bound transcription factor that activates genes in the endoplasmic reticulum (ER) stress response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. One permutation places beta-strand A on the C-terminus, another permutation places both beta-strands A and B on the C-terminus.


Pssm-ID: 467619 [Multi-domain]  Cd Length: 107  Bit Score: 38.76  E-value: 7.99e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 194740868 357 HGVLVWKVIVGSPAhSG--GLQPGDIVTHINKKEIKNSSD 394
Cdd:cd06775   35 SGVVVTEVVENSPV-SGprGLFVGDVITSINDCPVTSVED 73
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 351-411 9.10e-04

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 38.03  E-value: 9.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194740868  351 MPSNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSS--DVYDALADNSKHLDIVIL 411
Cdd:pfam00595  19 GSDQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTheEAVLALKGSGGKVTLTIL 81
PDZ_MAST1 cd23073
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 ...
 360-423 9.63e-04

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinase MAST1, and related domains. MAST1 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; MAST family member MASTL is a shorter protein lacking the PDZ domain. MAST1 functions as a scaffold protein to link the dystrophin/utrophin network with microfilaments via syntrophin, and it has been identified as a main driver of cisplatin resistance in human cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST1 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467286 [Multi-domain]  Cd Length: 95  Bit Score: 38.47  E-value: 9.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194740868 360 LVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSdvydaladnskHLDIV--ILRGVKQMHVTITP 423
Cdd:cd23073   36 IVWHVEEGGPAQEAGLCAGDLITHVNGEPVHGMV-----------HPEVVelILKSGNKVAVTTTP 90
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 358-422 1.62e-03

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


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 37.46  E-value: 1.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194740868 358 GVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSdVYDALAdnskhldivILRGVKQMHVTIT 422
Cdd:cd06782   15 YLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVRGMS-LDEVVK---------LLRGPKGTKVKLT 69
cpPDZ_RseP_YlbL-like cd10824
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), ...
 359-424 2.64e-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: 2.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194740868 359 VLVWKVIVGSPAhSGGLQPGDIVTHINKKEIKNSSDVYDALADNS--KHLDIVILRGVKQMHVTITPE 424
Cdd:cd10824    1 VVVLSVKPNSPA-AKALHAGDLITEIDGQPTKSWQTFIDYIHDKKvgESVKITYKHGNKNEEASLKLT 67
cpPDZ2_EcRseP-like cd23083
circularly permuted PDZ domain 2 (PDZ-C) of Escherichia coli Regulator of sigma-E protease ...
 364-424 2.84e-03

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: 36.72  E-value: 2.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194740868 364 VIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADN-SKHLDIVILRGVKQMHVTITPE 424
Cdd:cd23083    6 VQPNSAAEKAGLQAGDRIVKVDGQPLTQWQTFVMAVRDNpGKPLALEIERQGSPLSLTLIPD 67
cpPDZ1_ScNma111-like cd06786
circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine ...
 334-423 3.47e-03

circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine protease Nma111p and related domains; First PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the HtrA-type protease Saccharomyces cerevisiae Nma111p (also known as Ynm3p), and related domains. Nma111p is a nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor Bir1p. Nma111p is composed of 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. 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 ScNma111-like PDZ1 domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation places both beta-strands A and B on the C-terminus.


Pssm-ID: 467625 [Multi-domain]  Cd Length: 89  Bit Score: 36.40  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194740868 334 LTLTPDilFELKSRSQNmPSNLthGVLVWKVIV-GSPAHsGGLQPGDIVTHINKKEIKNSSDVYDALADN-SKHLDIVIL 411
Cdd:cd06786    4 LGLTPE--TEAAVRKAF-PSET--GMLVAETVLpEGPAD-GKLEEGDVLISVNGELITQFIRLEEILDENvGKTVELVVQ 77

                         90
                 ....*....|..
gi 194740868 412 RGVKQMHVTITP 423
Cdd:cd06786   78 RGGEEITVTITV 89
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 374-422 3.57e-03

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 38.81  E-value: 3.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194740868 374 GLQPGDIVTHINKKEIKNSSD---VYDALADNSKhLDIVILRGVKQMHVTIT 422
Cdd:COG3031  168 GLQPGDVITSINGQDLTDPAQaleLLQQLRDASE-VTLTVERNGQPVTLTYN 218
TIGR00054 TIGR00054
RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are ...
 363-425 3.99e-03

RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 272878 [Multi-domain]  Cd Length: 419  Bit Score: 39.42  E-value: 3.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194740868  363 KVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADN-SKHLDIVILRGVKQMHVTITPED 425
Cdd:TIGR00054 208 DVTPNSPAEKAGLKEGDYIQSINGEKLRSWTDFVSAVKENpGKSMDIKVERNGETLSISLTPEA 271
PDZ_MAST4 cd23076
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ ...
 360-389 4.61e-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: 36.55  E-value: 4.61e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 194740868 360 LVWKVIVGSPAHSGGLQPGDIVTHINKKEI 389
Cdd:cd23076   36 IVWNVEEGSPACQAGLKAGDLITHINGEPV 65
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 361-393 6.95e-03

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 35.68  E-value: 6.95e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 194740868 361 VWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSS 393
Cdd:cd06713   39 VCRVHEDSPAYLAGLTAGDVILSVNGVSVEGAS 71
PDZ_MAST2 cd23074
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 2; PDZ (PSD-95 ...
 360-389 9.70e-03

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 2; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST2 (also known as microtubule-associated serine/threonine kinase-205 kD, MAST205) , and related domains. MAST2 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. MAST2 may function to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Binding partners of MAST2 include beta2-syntrophin, TNF receptor-associated factor 6 (TRAF6), cAMP-regulated phosphoprotein (ARPP-16), Na+/H+ exchanger NHE3 (SLC9A3) and PTEN. MAST2 is also associated with microtubules of the spermatid manchette. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST2 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467287 [Multi-domain]  Cd Length: 93  Bit Score: 35.37  E-value: 9.70e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 194740868 360 LVWKVIVGSPAHSGGLQPGDIVTHINKKEI 389
Cdd:cd23074   36 MVWHVEDGGPASEAGLRQGDLITHVNGEPV 65
 
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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