NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|548923719|ref|NP_001271389|]
View 

serine protease HTRA2, mitochondrial [Canis lupus familiaris]

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
SCOP:  4001790

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 182-455 3.22e-77

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: 241.98  E-value: 3.22e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 182 GSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKePLPTLPLGRSADVRQGEFVVAMG 261
Cdd:COG0265    3 GSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAK-DLPAAPLGDSDKLRVGDWVLAIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 262 SPFALQNTITSGIVSSAQRPARDLGlPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSD 336
Cdd:COG0265   82 NPFGLGQTVTAGIVSALGRSIGSSG-GGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPIN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 337 RLREFLHRGEKKnswfgisGSQRR-YIGVMMLTLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPGDVILA 415
Cdd:COG0265  161 LAKRVVEQLIET-------GRVRRgWLGVTIQPVTPELAEALGL------PEPEGVLVARVEPGSPAAKAGLRPGDVILA 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 548923719 416 IGEQLVQNAEDIYEAVRTQ---SQLAVRIRRGPETLTLYVTPE 455
Cdd:COG0265  228 VDGKPVTSARDLQRLLASLkpgDTVTLTVLRGGKELTVTVTLG 270
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 182-455 3.22e-77

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: 241.98  E-value: 3.22e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 182 GSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKePLPTLPLGRSADVRQGEFVVAMG 261
Cdd:COG0265    3 GSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAK-DLPAAPLGDSDKLRVGDWVLAIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 262 SPFALQNTITSGIVSSAQRPARDLGlPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSD 336
Cdd:COG0265   82 NPFGLGQTVTAGIVSALGRSIGSSG-GGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPIN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 337 RLREFLHRGEKKnswfgisGSQRR-YIGVMMLTLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPGDVILA 415
Cdd:COG0265  161 LAKRVVEQLIET-------GRVRRgWLGVTIQPVTPELAEALGL------PEPEGVLVARVEPGSPAAKAGLRPGDVILA 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 548923719 416 IGEQLVQNAEDIYEAVRTQ---SQLAVRIRRGPETLTLYVTPE 455
Cdd:COG0265  228 VDGKPVTSARDLQRLLASLkpgDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 150-453 4.62e-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: 236.35  E-value: 4.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  150 IADVVEKTAPAVVYIEILG---------------RHPFsGREVPISN-----------GSGFVVAADGLIVTNAHVVADR 203
Cdd:TIGR02037   3 FAPLVEKVAPAVVNISVEGtvkrrnrppalppffRQFF-GDDMPDFPrqqreqkvrglGSGVIISADGYVLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  204 RRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRpaR 283
Cdd:TIGR02037  82 DEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGR--S 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  284 DLGLpQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSD---RLREFLHRGEKknswfgis 355
Cdd:TIGR02037 160 GLGI-GDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNmakNVVDQLIEGGK-------- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  356 gSQRRYIGVMMLTLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQ- 434
Cdd:TIGR02037 231 -VKRGWLGVTIQEVTSDLAKSLGL------EKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLk 303

                         330       340
                  ....*....|....*....|.
gi 548923719  435 --SQLAVRIRRGPETLTLYVT 453
Cdd:TIGR02037 304 pgKKVTLGILRKGKEKTITVT 324
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 359-456 7.24e-50

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: 164.59  E-value: 7.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 359 RRYIGVMMLTLTPSILAELQLREPSFPDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQSQLA 438
Cdd:cd06785    1 KRYIGIRMLTLTPSLLEELKQRNPDFPDVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSSLL 80

                         90
                 ....*....|....*...
gi 548923719 439 VRIRRGPETLTLYVTPEV 456
Cdd:cd06785   81 VVVRRGNEDLLLTVTPEE 98
PRK10942 PRK10942
serine endoprotease DegP;
182-416 4.72e-38

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 144.14  E-value: 4.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 182 GSGFVV-AADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAM 260
Cdd:PRK10942 113 GSGVIIdADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDALRVGDYTVAI 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 261 GSPFALQNTITSGIVSSAQRPardlGLPQTNVE-YIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTA-----GISFAIP 334
Cdd:PRK10942 193 GNPYGLGETVTSGIVSALGRS----GLNVENYEnFIQTDAAINRGNSGGALVNLNGELIGINTAILAPdggniGIGFAIP 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 335 SDRLR----EFLHRGEKKNSWFGISGSQrryigvmmltLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPG 410
Cdd:PRK10942 269 SNMVKnltsQMVEYGQVKRGELGIMGTE----------LNSELAKAMKV------DAQRGAFVSQVLPNSSAAKAGIKAG 332


                 ....*.
gi 548923719 411 DVILAI 416
Cdd:PRK10942 333 DVITSL 338
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 182-320 2.41e-28

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 109.05  E-value: 2.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  182 GSGFVVAADGLIVTNAH-----VVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRI-QTKEPLPTLPLGRSADVRQGE 255
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHvvddaEEAAVELVSVVLADGREYPATVVARDPDLDLALLRVsGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923719  256 FVVAMGSPFALQ-NTITSGIVSSAQRPARdlglPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGV 320
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRD----GGDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 151-320 6.81e-14

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: 72.91  E-value: 6.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 151 ADVVEKTAPAVVYIeiLGRHPFSGRevpISNGSGFVVAaDGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIA 230
Cdd:NF033740 187 SPAVRRARPSVVKV--RGTAPSCGR---ALEGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 231 TLRIqtkePLPTLPLGRSAD--VRQGEFVVAMGSPFALQNTITSGIVSSAQ-RPARDL-GLPQTNVEYIQTDAAIDFGNS 306
Cdd:NF033740 261 VLAV----PGLGLPPLPFADepAETGDDAIVLGYPEGGPFTATPARVRERIaLSGPDIyGSGTVTREVYTLRGTVRPGNS 336

                        170
                 ....*....|....
gi 548923719 307 GGPLVNLDGEVIGV 320
Cdd:NF033740 337 GGPLLDPDGRVLGV 350
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 385-452 2.57e-10

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: 56.62  E-value: 2.57e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923719   385 PDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAediyeavrTQSQLAVRIRRGPETLTLYV 452
Cdd:smart00228  22 KDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGL--------THLEAVDLLKKAGGKVTLTV 81
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 182-455 3.22e-77

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: 241.98  E-value: 3.22e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 182 GSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKePLPTLPLGRSADVRQGEFVVAMG 261
Cdd:COG0265    3 GSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAK-DLPAAPLGDSDKLRVGDWVLAIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 262 SPFALQNTITSGIVSSAQRPARDLGlPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSD 336
Cdd:COG0265   82 NPFGLGQTVTAGIVSALGRSIGSSG-GGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPIN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 337 RLREFLHRGEKKnswfgisGSQRR-YIGVMMLTLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPGDVILA 415
Cdd:COG0265  161 LAKRVVEQLIET-------GRVRRgWLGVTIQPVTPELAEALGL------PEPEGVLVARVEPGSPAAKAGLRPGDVILA 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 548923719 416 IGEQLVQNAEDIYEAVRTQ---SQLAVRIRRGPETLTLYVTPE 455
Cdd:COG0265  228 VDGKPVTSARDLQRLLASLkpgDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 150-453 4.62e-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: 236.35  E-value: 4.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  150 IADVVEKTAPAVVYIEILG---------------RHPFsGREVPISN-----------GSGFVVAADGLIVTNAHVVADR 203
Cdd:TIGR02037   3 FAPLVEKVAPAVVNISVEGtvkrrnrppalppffRQFF-GDDMPDFPrqqreqkvrglGSGVIISADGYVLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  204 RRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRpaR 283
Cdd:TIGR02037  82 DEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGR--S 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  284 DLGLpQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSD---RLREFLHRGEKknswfgis 355
Cdd:TIGR02037 160 GLGI-GDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNmakNVVDQLIEGGK-------- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  356 gSQRRYIGVMMLTLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQ- 434
Cdd:TIGR02037 231 -VKRGWLGVTIQEVTSDLAKSLGL------EKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLk 303

                         330       340
                  ....*....|....*....|.
gi 548923719  435 --SQLAVRIRRGPETLTLYVT 453
Cdd:TIGR02037 304 pgKKVTLGILRKGKEKTITVT 324
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 359-456 7.24e-50

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: 164.59  E-value: 7.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 359 RRYIGVMMLTLTPSILAELQLREPSFPDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQSQLA 438
Cdd:cd06785    1 KRYIGIRMLTLTPSLLEELKQRNPDFPDVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSSLL 80

                         90
                 ....*....|....*...
gi 548923719 439 VRIRRGPETLTLYVTPEV 456
Cdd:cd06785   81 VVVRRGNEDLLLTVTPEE 98
PRK10942 PRK10942
serine endoprotease DegP;
182-416 4.72e-38

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 144.14  E-value: 4.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 182 GSGFVV-AADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAM 260
Cdd:PRK10942 113 GSGVIIdADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDALRVGDYTVAI 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 261 GSPFALQNTITSGIVSSAQRPardlGLPQTNVE-YIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTA-----GISFAIP 334
Cdd:PRK10942 193 GNPYGLGETVTSGIVSALGRS----GLNVENYEnFIQTDAAINRGNSGGALVNLNGELIGINTAILAPdggniGIGFAIP 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 335 SDRLR----EFLHRGEKKNSWFGISGSQrryigvmmltLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPG 410
Cdd:PRK10942 269 SNMVKnltsQMVEYGQVKRGELGIMGTE----------LNSELAKAMKV------DAQRGAFVSQVLPNSSAAKAGIKAG 332


                 ....*.
gi 548923719 411 DVILAI 416
Cdd:PRK10942 333 DVITSL 338
PRK10139 PRK10139
serine endoprotease DegQ;
128-425 1.35e-37

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 142.78  E-value: 1.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 128 PPAVLASVLGSPPSSPrsQYNFIADVVEKTAPAVVYIEILG------RHP-----FSGREVPISN-------GSGFVV-A 188
Cdd:PRK10139  22 SFQAVASIPGQVAGQA--PLPSLAPMLEKVLPAVVSVRVEGtasqgqKIPeefkkFFGDDLPDQPaqpfeglGSGVIIdA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 189 ADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQN 268
Cdd:PRK10139 100 AKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQ 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 269 TITSGIVSSAQRPARDL-GLPQtnveYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKV-----TAGISFAIPSDRLR--- 339
Cdd:PRK10139 180 TATSGIISALGRSGLNLeGLEN----FIQTDASINRGNSGGALLNLNGELIGINTAILapgggSVGIGFAIPSNMARtla 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 340 -EFLHRGEKKNSWFGISGSQrryigvmmltLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPGDVILAI-G 417
Cdd:PRK10139 256 qQLIDFGEIKRGLLGIKGTE----------MSADIAKAFNL------DVQRGAFVSEVLPNSGSAKAGVKAGDIITSLnG 319


                 ....*...
gi 548923719 418 EQLVQNAE 425
Cdd:PRK10139 320 KPLNSFAE 327
PRK10898 PRK10898
serine endoprotease DegS;
154-453 3.61e-35

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 133.97  E-value: 3.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 154 VEKTAPAVVYIEILGRHPFSGREVPISN-GSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATL 232
Cdd:PRK10898  51 VRRAAPAVVNVYNRSLNSTSHNQLEIRTlGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 233 RIQTKEpLPTLPLG--RSADVrqGEFVVAMGSPFALQNTITSGIVSSAQRpardLGL-PQTNVEYIQTDAAIDFGNSGGP 309
Cdd:PRK10898 131 KINATN-LPVIPINpkRVPHI--GDVVLAIGNPYNLGQTITQGIISATGR----IGLsPTGRQNFLQTDASINHGNSGGA 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 310 LVNLDGEVIGVNTM--------KVTAGISFAIPSD---RLREFLHR-GEKKNSWFGISGSQRRYIGVmmltlTPSILAEL 377
Cdd:PRK10898 204 LVNSLGELMGINTLsfdksndgETPEGIGFAIPTQlatKIMDKLIRdGRVIRGYIGIGGREIAPLHA-----QGGGIDQL 278

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923719 378 QlrepsfpdvqhGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAV---RTQSQLAVRIRRGPETLTLYVT 453
Cdd:PRK10898 279 Q-----------GIVVNEVSPDGPAAKAGIQVNDLIISVNNKPAISALETMDQVaeiRPGSVIPVVVMRDDKQLTLQVT 346
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 182-320 2.41e-28

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 109.05  E-value: 2.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  182 GSGFVVAADGLIVTNAH-----VVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRI-QTKEPLPTLPLGRSADVRQGE 255
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHvvddaEEAAVELVSVVLADGREYPATVVARDPDLDLALLRVsGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923719  256 FVVAMGSPFALQ-NTITSGIVSSAQRPARdlglPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGV 320
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRD----GGDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 359-452 4.88e-23

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: 92.74  E-value: 4.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 359 RRYIGVMMLTLTPSILAELqlrepsFPDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQ---S 435
Cdd:cd06779    1 RPYLGIEMENISPLLAKEL------GLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTKkpgD 74

                         90
                 ....*....|....*..
gi 548923719 436 QLAVRIRRGPETLTLYV 452
Cdd:cd06779   75 SLNLTILRDGKTLTVTV 91
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 359-455 6.97e-21

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: 87.13  E-value: 6.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 359 RRYIGVMMLTLTPSILAELQLREPSFPDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEA----VRTQ 434
Cdd:cd23085    1 RPWLGMKMLELNEHIIAQLKERDPMFPDVKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQIIDAlgdkVGKP 80

                         90       100
                 ....*....|....*....|.
gi 548923719 435 SQLAVRiRRGPETLTLYVTPE 455
Cdd:cd23085   81 FKVVVK-RANKVQVTLTVTPE 100
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 361-455 6.33e-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: 76.20  E-value: 6.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 361 YIGVMMLTLTPSiLAELQLREPSFPDV---QHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAV-RTQ-- 434
Cdd:cd10838    3 YLGIQMTTLTPE-LAQQNNRNPNSPVRipeVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRIVeQAGvg 81

                         90       100
                 ....*....|....*....|.
gi 548923719 435 SQLAVRIRRGPETLTLYVTPE 455
Cdd:cd10838   82 EELELTVLRGDRRQTLAVKPG 102
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 151-320 6.81e-14

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: 72.91  E-value: 6.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 151 ADVVEKTAPAVVYIeiLGRHPFSGRevpISNGSGFVVAaDGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIA 230
Cdd:NF033740 187 SPAVRRARPSVVKV--RGTAPSCGR---ALEGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 231 TLRIqtkePLPTLPLGRSAD--VRQGEFVVAMGSPFALQNTITSGIVSSAQ-RPARDL-GLPQTNVEYIQTDAAIDFGNS 306
Cdd:NF033740 261 VLAV----PGLGLPPLPFADepAETGDDAIVLGYPEGGPFTATPARVRERIaLSGPDIyGSGTVTREVYTLRGTVRPGNS 336

                        170
                 ....*....|....
gi 548923719 307 GGPLVNLDGEVIGV 320
Cdd:NF033740 337 GGPLLDPDGRVLGV 350
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 393-458 1.07e-11

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 65.88  E-value: 1.07e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923719 393 IHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRT--QSQLAVRIRRGPETLTLYVTPEVTE 458
Cdd:COG0750  132 VGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRAspGKPLTLTVERDGEELTLTVTPRLVE 199
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 395-458 1.36e-10

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: 57.59  E-value: 1.36e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548923719 395 KVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVR--TQSQLAVRIRRGPETLTLYVTPEVTE 458
Cdd:cd23081    5 EVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIVRIVRenPGKPLTLKIERDGKILTVTVTPELVE 70
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 385-452 2.57e-10

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: 56.62  E-value: 2.57e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923719   385 PDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAediyeavrTQSQLAVRIRRGPETLTLYV 452
Cdd:smart00228  22 KDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGL--------THLEAVDLLKKAGGKVTLTV 81
Trypsin pfam00089
Trypsin;
228-342 9.93e-10

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 58.61  E-value: 9.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  228 DIATLRIQTK-------EPLPTLPLGRSADVRQGEFVVAMGSPFALQ-----NTITSGIVSSAQRPARDLGlpQTNVEYI 295
Cdd:pfam00089  88 DIALLKLESPvtlgdtvRPICLPDASSDLPVGTTCTVSGWGNTKTLGpsdtlQEVTVPVVSRETCRSAYGG--TVTDTMI 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 548923719  296 QTDA---AIDFGNSGGPLVNLDGEVIGVNTMK----VTAGISFAIPSDRLREFL 342
Cdd:pfam00089 166 CAGAggkDACQGDSGGPLVCSDGELIGIVSWGygcaSGNYPGVYTPVSSYLDWI 219
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 359-452 1.23e-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: 54.80  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 359 RRYIGVMMLTLTPSILAELQLrepsfpDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQ---S 435
Cdd:cd10839    1 RGWLGVQIQELTPDLAESFGL------KEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADLRNRVATTkpgT 74

                         90
                 ....*....|....*..
gi 548923719 436 QLAVRIRRGPETLTLYV 452
Cdd:cd10839   75 KVELKILRDGKEKTLTV 91
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 362-450 3.68e-09

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: 53.40  E-value: 3.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 362 IGVMMLTLTPSilaelqlrepsfpDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQ-SQLAVR 440
Cdd:cd23084    4 EGATVSNVTDE-------------DGGKGVVVTEVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRKVLKSKpSAVLLQ 70

                         90
                 ....*....|
gi 548923719 441 IRRGPETLTL 450
Cdd:cd23084   71 IKRGDSSRYL 80
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 387-453 8.65e-08

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: 49.88  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 387 VQHGVLIHKVILDSPAHRAGLRP-----------GDVILAIGEQLVQNAEDIYEAVRTQS---QLAVRIRRGPETLTLYV 452
Cdd:cd00990   21 VRSGVLVLDVPPGGPAAKAGLRGtkrdefgrivlGDVIVAVDGKPVKNESDLYRALDEYKvgdVVTLKVLRGGTKVDLKV 100


                 .
gi 548923719 453 T 453
Cdd:cd00990  101 T 101
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 386-453 9.89e-08

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: 49.08  E-value: 9.89e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923719 386 DVQHGVLIHKVILDSPAHRAG-LRPGDVILAIGEQLVQNAediyeavrTQSQLAVRIRRGPETLTLYVT 453
Cdd:cd00136   21 DGGGGIFVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGL--------THEEAVELLKSAGGEVTLTVR 81
Peptidase_M50 pfam02163
Peptidase family M50;
387-458 2.23e-07

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 52.11  E-value: 2.23e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548923719  387 VQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQ--SQLAVRIRRGPETLTLYVTPEVTE 458
Cdd:pfam02163  91 PPAPPVIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEALAKSpgKPITLTVERGGQTLTVTITPKSSE 164
PDZ_2 pfam13180
PDZ domain;
390-453 2.76e-07

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 47.65  E-value: 2.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923719  390 GVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRT---QSQLAVRIRRGPETLTLYVT 453
Cdd:pfam13180   7 GVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALYGhkpGDTVTLQVYRDGKLLTVEVK 73
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 396-443 4.05e-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: 4.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 548923719  396 VILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQ--SQLAVRIRR 443
Cdd:pfam17820   5 VVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLLQGSagESVTLTVRR 54
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 390-453 7.19e-07

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 51.02  E-value: 7.19e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923719 390 GVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQ--NAEDIYEAVRTQ--SQLAVRIRRGPETLTLYVT 453
Cdd:COG0793   72 KVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAglTLDDAVKLLRGKagTKVTLTIKRPGEGEPITVT 139
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 390-452 8.57e-07

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


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 46.66  E-value: 8.57e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548923719 390 GVLIHKVILDSPAHRAGLRPGDVILAIgeqlvqNAEDIYEAvrTQSQLAVRIRRGPETLTLYV 452
Cdd:cd06768   24 GHFIREVDPGSPAERAGLKDGDRLVEV------NGENVEGE--SHEQVVEKIKASGNQVTLLV 78
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 359-427 9.71e-07

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: 46.86  E-value: 9.71e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 359 RRYIGVMMLTLtpSILAELQLREPSFPD-VQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDI 427
Cdd:cd06781    1 RPSLGISMVDL--SDVPEYEQQSLKLPSnVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDL 68
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 390-450 1.56e-06

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: 45.94  E-value: 1.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 390 GVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNaEDIYEAV-----RTQSQLAVRIRRG----PETLTL 450
Cdd:cd06782   15 YLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVRG-MSLDEVVkllrgPKGTKVKLTIRRGgegePRDVTL 83
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
390-455 4.89e-06

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 49.05  E-value: 4.89e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923719 390 GVLIHKVILDSPAHRAGLRPGDVILAIGEQLV--QNAEDIYEAVRTQSQLAVRIRRGPETLTLYVTPE 455
Cdd:COG3975  495 GLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVtaDNLDDALAAYKPGDPIELLVFRRDELRTVTVTLA 562
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 393-423 6.17e-06

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


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 44.06  E-value: 6.17e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 548923719 393 IHKVILDSPAHRAGLRPGDVILAIGEQLVQN 423
Cdd:cd23068   29 IQKVNPGSPADKAGLRRGDVILRINGTDTSN 59
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 395-432 1.43e-05

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: 43.38  E-value: 1.43e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 548923719 395 KVILDSPAHRAGLRPGDVILAIGEQLVQNA--EDIYEAVR 432
Cdd:cd06713   41 RVHEDSPAYLAGLTAGDVILSVNGVSVEGAshQEIVELIR 80
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
 400-455 2.07e-05

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 46.65  E-value: 2.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923719 400 SPAHRAGLRPGDVILAIGEQLVQNAeDIYEAVR-----TQSQLAVRIRRGPETLTLYVTPE 455
Cdd:PLN00049 113 GPAARAGIRPGDVILAIDGTSTEGL-SLYEAADrlqgpEGSSVELTLRRGPETRLVTLTRE 172
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
 386-432 2.39e-05

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


Pssm-ID: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 42.69  E-value: 2.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548923719 386 DVQHGVLIHKVILDSPAHRAGLRPGDVILAIGE------------QLVQNAEDIYEAVR 432
Cdd:cd06752   22 ASGLGIFISKVIPDSDAHRLGLKEGDQILSVNGvdfediehseavKVLKTAREIQMRVR 80
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 385-452 3.62e-05

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 41.88  E-value: 3.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923719  385 PDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAediyeavrTQSQLAVRIRRGPETLTLYV 452
Cdd:pfam00595  21 DQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENM--------THEEAVLALKGSGGKVTLTI 80
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 404-453 7.33e-05

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 43.82  E-value: 7.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 548923719 404 RAGLRPGDVILAI-GEQL--VQNAEDIYEAVRTQSQLAVRIRRGPETLTLYVT 453
Cdd:COG3031  166 KLGLQPGDVITSInGQDLtdPAQALELLQQLRDASEVTLTVERNGQPVTLTYN 218
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 382-452 2.19e-04

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 40.27  E-value: 2.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548923719 382 PSFPDVQHgvlIHKVILDSPAHRAGLRPGDVILAIgeqlvqNAEDIyeaVRTQSQLAVR-IRRGPETLTLYV 452
Cdd:cd06746   38 PAFPALQY---LESVDPGGVADKAGLKKGDFLLEI------NGEDV---VKASHEQVVNlIRQSGNTLVLKV 97
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 393-450 2.46e-04

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 39.44  E-value: 2.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548923719 393 IHKVILDSPAHRAGLRPGDVILAIgeqlvqNAEDIYEAVRTQSQLAVRIRRGPETLTL 450
Cdd:cd06753   26 ISRVTPGGKAAQANLRPGDVILAI------NGESTEGMTHLEAQNKIKAATGSLSLTL 77
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 160-334 3.13e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 41.59  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 160 AVVYIEILGRHPFsgrevpisnGSGFVVAADgLIVTNAH----VVADRRRVRVRLLSGD------TYEAVVTAVDPV--- 226
Cdd:COG3591    1 AVGRLETDGGGGV---------CTGTLIGPN-LVLTAGHcvydGAGGGWATNIVFVPGYnggpygTATATRFRVPPGwva 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 227 -----ADIATLRIQTKEPLPT--LPLGRSADVRQGEFVVAMGSPFALQNTIT---SGIVSSAQRpardlglpqtnvEYIQ 296
Cdd:COG3591   71 sgdagYDYALLRLDEPLGDTTgwLGLAFNDAPLAGEPVTIIGYPGDRPKDLSldcSGRVTGVQG------------NRLS 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 548923719 297 TDAAIDFGNSGGPLVNLD---GEVIGVNTMKVTAGISFAIP 334
Cdd:COG3591  139 YDCDTTGGSSGSPVLDDSdggGRVVGVHSAGGADRANTGVR 179
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
 388-424 3.16e-04

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467194 [Multi-domain]  Cd Length: 76  Bit Score: 39.15  E-value: 3.16e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 548923719 388 QHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNA 424
Cdd:cd06710   19 QAPCVLSCVVRGSPADVAGLKAGDQILAVNGINVSKA 55
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 389-452 5.07e-04

PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467247 [Multi-domain]  Cd Length: 81  Bit Score: 38.91  E-value: 5.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923719 389 HGVLIHKVILDSPAHRA-GLRPGDVILAIGEQLVQNaediyeavRTQSQLAVRIRRGPETLTLYV 452
Cdd:cd06766   24 HGIFVEDVEDDSPAKGPdGLVPGDLILEYNSVDMRN--------KTAEEAYLEMLKPAETVTLKV 80
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 390-431 6.60e-04

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


Pssm-ID: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 38.41  E-value: 6.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 548923719 390 GVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDiYEAV 431
Cdd:cd06704   31 GIFISRVTEGGPAAKAGVRVGDKLLEVNGVDLVDADH-HEAV 71
PDZ1_INAD-like cd23063
PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 383-424 6.95e-04

PDZ domain 1 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This INAD-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467276 [Multi-domain]  Cd Length: 87  Bit Score: 38.65  E-value: 6.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 548923719 383 SFPDVQHGVLIHKVILDSPAHRAG-LRPGDVILAIGEQLVQNA 424
Cdd:cd23063   24 SPNTKTTGIFIKGIIPDSPAHKCGrLKVGDRILSVNGNDVRNS 66
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
 388-453 9.38e-04

C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]


Pssm-ID: 272970 [Multi-domain]  Cd Length: 334  Bit Score: 41.19  E-value: 9.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719  388 QHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQ--NAEDIYEAVRTQ--SQLAVRIRRGPETLTLYVT 453
Cdd:TIGR00225  61 DGKIVIVSPFEGSPAEKAGIKPGDKIIKINGKSVAgmSLDDAVALIRGKkgTKVSLEILRAGKSKPLSFT 130
TIGR00054 TIGR00054
RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are ...
 393-455 1.24e-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: 40.96  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548923719  393 IHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVR--TQSQLAVRIRRGPETLTLYVTPE 455
Cdd:TIGR00054 206 LSDVTPNSPAEKAGLKEGDYIQSINGEKLRSWTDFVSAVKenPGKSMDIKVERNGETLSISLTPE 270
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 384-454 1.71e-03

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


Pssm-ID: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 37.77  E-value: 1.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548923719 384 FPDVQHgvlIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAediyeavrTQSQLAVRIRRGPETLTLYVTP 454
Cdd:cd23070   34 YAPLQH---VSAVLEGGAADKAGVRKGDRILEVNGVNVEGA--------THKQVVDLIKSGGDELTLTVIS 93
PDZ_MAST cd06705
PDZ domain of the microtubule-associated serine-threonine (MAST) protein kinase family; PDZ ...
 386-454 2.47e-03

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: 37.22  E-value: 2.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548923719 386 DVQHgvLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAediyeavrTQSQLAVRIRRGPETLTLYVTP 454
Cdd:cd06705   32 TVHH--LVTAVEEGSPAYEAGLRPGDLITHVNGEPVQGL--------LHTQVVQLILKGGNKVSIRATP 90
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 389-453 2.79e-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: 36.99  E-value: 2.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548923719 389 HGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAE---DIYEAVRTQSQLAVRIRRGPETLTLYVT 453
Cdd:cd06777   25 QGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLelmDLVAEIRPGTVIPVVVLRDGKQLTLEVT 92
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 390-443 2.80e-03

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


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 36.85  E-value: 2.80e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 548923719 390 GVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNA--EDIYEAVRTQSQLAVRIRR 443
Cdd:cd06737   28 GLFVSHVSPGSQADNKGLRVGDEIVRINGYSISQCthEEVINLIKTKKTVSLKVRH 83
GRASP55_65 pfam04495
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ...
 387-452 2.82e-03

GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain.


Pssm-ID: 427981 [Multi-domain]  Cd Length: 138  Bit Score: 38.02  E-value: 2.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548923719  387 VQHGVLIHKVILDSPAHRAGLRP-GDVILAIGEQLVQNAEDIYEAVRTQSQlavrirrgpETLTLYV 452
Cdd:pfam04495  41 LENVWHVLDVHENSPAAKAGLQPySDYIIGTPKGLLKGEDDLYTLVEDHED---------RPLRLYV 98
cpPDZ1_MamE-like cd23087
circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease ...
 390-427 4.05e-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: 36.39  E-value: 4.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 548923719 390 GVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDI 427
Cdd:cd23087   26 GVFVSGVTPNTPAAAAGLRPGDVILKVDGRPVHQPEEV 63
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 390-443 4.49e-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: 36.08  E-value: 4.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 548923719 390 GVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNA---EDIYEAVRTQSQLAVRIRR 443
Cdd:cd06702   33 GIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHAthqEAVSALLSPGQEIKLLVRH 89
PRK10779 PRK10779
sigma E protease regulator RseP;
377-456 5.35e-03

sigma E protease regulator RseP;


Pssm-ID: 182723 [Multi-domain]  Cd Length: 449  Bit Score: 38.89  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548923719 377 LQLREPSF-PDVQHGVL--------------IHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQ--SQLAV 439
Cdd:PRK10779 194 LDLRHWAFePDKQDPVSslgirprgpqiepvLAEVQPNSAASKAGLQAGDRIVKVDGQPLTQWQTFVTLVRDNpgKPLAL 273

                         90
                 ....*....|....*..
gi 548923719 440 RIRRGPETLTLYVTPEV 456
Cdd:PRK10779 274 EIERQGSPLSLTLTPDS 290
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH