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Conserved domains on  [gi|506372187|ref|WP_015891906|]
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SepM family pheromone-processing serine protease [Brevibacillus brevis]

Protein Classification

PDZ domain-containing protein( domain architecture ID 11466013)

PDZ domain-containing protein similar to Bacillus subtilis YlbL, which belongs to the peptidase S16 family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
10-355 4.22e-136

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


:

Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 391.10  E-value: 4.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  10 RRRssgTRGFSWILALVFVLLGISFFVPTNYYVSRPGSAIEL------GPMIQVEGGKKDET-GSFMLTTVRM-GEANLP 81
Cdd:COG3480    4 RRR---SWTLLVALLLLVVLLLLLALLPVPYVIESPGPTYDTlgevdgKPVISVEGAETYPTsGSLRLTTVSVtGGATLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  82 WYWYAKMAQDVELLPKELVVSKGEDSEDFIRREQAVMDNSQKIAEAVAFRLAGFEVKiekQGVWVMGTLEGFPAHKTLRI 161
Cdd:COG3480   81 EALYAWLDPDYAVVPREEVYPPGESDEEYNQQNAAQMESSQENAIAAALRAAGYPVT---EGVYVASVLEGSPADGVLQP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 162 GDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKS-VGIGVRPDnkQEIIIPKEVTIAS 240
Cdd:COG3480  158 GDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVTLVKLPDDDGrAGIGISLV--TKVDFPFDVDIDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 241 QGIGGPSAGLMMTLEIYDQLnTETDLTKGYKIAGTGTISLDGKVGRIGGINLKVIAADKAGAEIFFAPQDtpdtssNYEE 320
Cdd:COG3480  236 GDIGGPSAGLMFALGIYDQL-TPGDLTGGKKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPAS------NCAE 308

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 506372187 321 ALATakrIGTSMKVVPIKTVEEAITYLNAQKPKST 355
Cdd:COG3480  309 AVGT---IPTGLKVVPVDTLDDALDALEALRAGGD 340
 
Name Accession Description Interval E-value
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
10-355 4.22e-136

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 391.10  E-value: 4.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  10 RRRssgTRGFSWILALVFVLLGISFFVPTNYYVSRPGSAIEL------GPMIQVEGGKKDET-GSFMLTTVRM-GEANLP 81
Cdd:COG3480    4 RRR---SWTLLVALLLLVVLLLLLALLPVPYVIESPGPTYDTlgevdgKPVISVEGAETYPTsGSLRLTTVSVtGGATLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  82 WYWYAKMAQDVELLPKELVVSKGEDSEDFIRREQAVMDNSQKIAEAVAFRLAGFEVKiekQGVWVMGTLEGFPAHKTLRI 161
Cdd:COG3480   81 EALYAWLDPDYAVVPREEVYPPGESDEEYNQQNAAQMESSQENAIAAALRAAGYPVT---EGVYVASVLEGSPADGVLQP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 162 GDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKS-VGIGVRPDnkQEIIIPKEVTIAS 240
Cdd:COG3480  158 GDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVTLVKLPDDDGrAGIGISLV--TKVDFPFDVDIDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 241 QGIGGPSAGLMMTLEIYDQLnTETDLTKGYKIAGTGTISLDGKVGRIGGINLKVIAADKAGAEIFFAPQDtpdtssNYEE 320
Cdd:COG3480  236 GDIGGPSAGLMFALGIYDQL-TPGDLTGGKKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPAS------NCAE 308

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 506372187 321 ALATakrIGTSMKVVPIKTVEEAITYLNAQKPKST 355
Cdd:COG3480  309 AVGT---IPTGLKVVPVDTLDDALDALEALRAGGD 340
SepM_fam_S16 NF041438
SepM family pheromone-processing serine protease; This HMM describes a peptide ...
 21-347 4.55e-88

SepM family pheromone-processing serine protease; This HMM describes a peptide pheromone-processing S16-type serine protease found broadly in Gram-positive bacteria, and named for the founding member from Streptococcus mutans (see BlastRule NBR014542). The Lon-like catalytic domain is located toward the C-terminus, and has a Ser-Lys active site dyad rather than the more common Ser-His-Asp triad found in large numbers of serine proteases. Members of this family also have a PDZ domain.


Pssm-ID: 469329 [Multi-domain]  Cd Length: 340  Bit Score: 268.43  E-value: 4.55e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  21 WILALV-FVLLGISFFVPTNYYVSRPGSAIELGPMIQVEGGKKDETGSFMLTTVRMGEANLPWYWYAKMAQDVELLPKEl 99
Cdd:NF041438   5 WLLGILaLLLLLFALFFPLPYYIEMPGGAYDIRSVLTVNGKEDKEKGSYNFVAVSLSRATLAQLLYAWLTPFTEISSAE- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 100 VVSKGEDSEDFIRREQAVMDNSQKIAEAVAFRLAGFEVKIEKQGVWVM-----GTLEGfpahkTLRIGDVITYVDGVRTS 174
Cdd:NF041438  84 ETTGGYSDADYMRINQFYMETSQNGAIYQALKLAGKKVSLDYKGVYVLdvskdSTFKG-----VLNIADTVTGVNGKTFK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 175 EAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKSvGIGVRPDNKQEIIIPKEVTIASQGIGGPSAGLMMTL 254
Cdd:NF041438 159 SSKELIKYVSGLKLGSKVTVQYTSNGKKKSAKGKIIKLKNGKN-GIGIGLTDHTEVSSDDKVKFSTEGVGGPSAGLMFTL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 255 EIYDQLNTEtDLTKGYKIAGTGTISLDGKVGRIGGINLKVIAADKAGAEIFFAP---------QDTPDTSSNYEEALATA 325
Cdd:NF041438 238 DIYDQLNKE-DLRKGRKIAGTGTIEQDGSVGDIGGAGLKVVAAAKIGADIFFVPnnpvdkalkKANPDAKTNYQEAKEAA 316

                        330       340
                 ....*....|....*....|..
gi 506372187 326 KRIGTSMKVVPIKTVEEAITYL 347
Cdd:NF041438 317 KKLKTKMKIVPVKTVQEAIDYL 338
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 143-222 3.49e-15

circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis YlbL and related domains. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. Deletion of both proteases leads to accumulation of the cell division inhibitor YneA. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This YlbL family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467637 [Multi-domain]  Cd Length: 83  Bit Score: 69.83  E-value: 3.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 143 GVWVMGTLEGFPAHKTLRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKS-VGIG 221
Cdd:cd23080    1 GVYVLSVVENMPAKGILEAGDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKLKQFPDEKNrIGIG 80


                 .
gi 506372187 222 V 222
Cdd:cd23080   81 V 81
PDZ_2 pfam13180
PDZ domain;
137-200 1.02e-08

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 51.50  E-value: 1.02e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506372187  137 VKIEKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDG 200
Cdd:pfam13180   1 FVDLEGGVVVVSVKSSGPAAKAgLKAGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDG 65
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 138-219 3.20e-07

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: 51.84  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  138 KIEKQ-GVWVMGTLEGFPAHK-TLRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPES 215
Cdd:TIGR02037 252 GLEKQrGALVAQVLPGSPAEKaGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKEKTITVTLGASPEE 331


                  ....
gi 506372187  216 KSVG 219
Cdd:TIGR02037 332 QASS 335
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 134-200 5.16e-05

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: 41.21  E-value: 5.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506372187   134 GFEV---KIEKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDG 200
Cdd:smart00228  15 GFSLvggKDEGGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85
 
Name Accession Description Interval E-value
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
10-355 4.22e-136

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 391.10  E-value: 4.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  10 RRRssgTRGFSWILALVFVLLGISFFVPTNYYVSRPGSAIEL------GPMIQVEGGKKDET-GSFMLTTVRM-GEANLP 81
Cdd:COG3480    4 RRR---SWTLLVALLLLVVLLLLLALLPVPYVIESPGPTYDTlgevdgKPVISVEGAETYPTsGSLRLTTVSVtGGATLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  82 WYWYAKMAQDVELLPKELVVSKGEDSEDFIRREQAVMDNSQKIAEAVAFRLAGFEVKiekQGVWVMGTLEGFPAHKTLRI 161
Cdd:COG3480   81 EALYAWLDPDYAVVPREEVYPPGESDEEYNQQNAAQMESSQENAIAAALRAAGYPVT---EGVYVASVLEGSPADGVLQP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 162 GDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKS-VGIGVRPDnkQEIIIPKEVTIAS 240
Cdd:COG3480  158 GDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVTLVKLPDDDGrAGIGISLV--TKVDFPFDVDIDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 241 QGIGGPSAGLMMTLEIYDQLnTETDLTKGYKIAGTGTISLDGKVGRIGGINLKVIAADKAGAEIFFAPQDtpdtssNYEE 320
Cdd:COG3480  236 GDIGGPSAGLMFALGIYDQL-TPGDLTGGKKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPAS------NCAE 308

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 506372187 321 ALATakrIGTSMKVVPIKTVEEAITYLNAQKPKST 355
Cdd:COG3480  309 AVGT---IPTGLKVVPVDTLDDALDALEALRAGGD 340
SepM_fam_S16 NF041438
SepM family pheromone-processing serine protease; This HMM describes a peptide ...
 21-347 4.55e-88

SepM family pheromone-processing serine protease; This HMM describes a peptide pheromone-processing S16-type serine protease found broadly in Gram-positive bacteria, and named for the founding member from Streptococcus mutans (see BlastRule NBR014542). The Lon-like catalytic domain is located toward the C-terminus, and has a Ser-Lys active site dyad rather than the more common Ser-His-Asp triad found in large numbers of serine proteases. Members of this family also have a PDZ domain.


Pssm-ID: 469329 [Multi-domain]  Cd Length: 340  Bit Score: 268.43  E-value: 4.55e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  21 WILALV-FVLLGISFFVPTNYYVSRPGSAIELGPMIQVEGGKKDETGSFMLTTVRMGEANLPWYWYAKMAQDVELLPKEl 99
Cdd:NF041438   5 WLLGILaLLLLLFALFFPLPYYIEMPGGAYDIRSVLTVNGKEDKEKGSYNFVAVSLSRATLAQLLYAWLTPFTEISSAE- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 100 VVSKGEDSEDFIRREQAVMDNSQKIAEAVAFRLAGFEVKIEKQGVWVM-----GTLEGfpahkTLRIGDVITYVDGVRTS 174
Cdd:NF041438  84 ETTGGYSDADYMRINQFYMETSQNGAIYQALKLAGKKVSLDYKGVYVLdvskdSTFKG-----VLNIADTVTGVNGKTFK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 175 EAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKSvGIGVRPDNKQEIIIPKEVTIASQGIGGPSAGLMMTL 254
Cdd:NF041438 159 SSKELIKYVSGLKLGSKVTVQYTSNGKKKSAKGKIIKLKNGKN-GIGIGLTDHTEVSSDDKVKFSTEGVGGPSAGLMFTL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 255 EIYDQLNTEtDLTKGYKIAGTGTISLDGKVGRIGGINLKVIAADKAGAEIFFAP---------QDTPDTSSNYEEALATA 325
Cdd:NF041438 238 DIYDQLNKE-DLRKGRKIAGTGTIEQDGSVGDIGGAGLKVVAAAKIGADIFFVPnnpvdkalkKANPDAKTNYQEAKEAA 316

                        330       340
                 ....*....|....*....|..
gi 506372187 326 KRIGTSMKVVPIKTVEEAITYL 347
Cdd:NF041438 317 KKLKTKMKIVPVKTVQEAIDYL 338
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 143-222 3.49e-15

circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis YlbL and related domains. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. Deletion of both proteases leads to accumulation of the cell division inhibitor YneA. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This YlbL family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467637 [Multi-domain]  Cd Length: 83  Bit Score: 69.83  E-value: 3.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 143 GVWVMGTLEGFPAHKTLRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKS-VGIG 221
Cdd:cd23080    1 GVYVLSVVENMPAKGILEAGDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKLKQFPDEKNrIGIG 80


                 .
gi 506372187 222 V 222
Cdd:cd23080   81 V 81
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 140-214 2.45e-14

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: 72.10  E-value: 2.45e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506372187 140 EKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPE 214
Cdd:COG0265  199 EPEGVLVARVEPGSPAAKAgLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
243-347 1.10e-13

Predicted archaeal serine protease, S18 family [General function prediction only];


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 69.24  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 243 IGGPSAGLMMTLEIYDQLnteTDLTKGYKIAGTGTISLDGKVGRIGGINLKVIAADKAGAEIFFAPQD-TPDTSSNYEEA 321
Cdd:COG1750  107 VGGPSAGGAMTVATYAAL---LGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGqAILTGYNTQVG 183

                         90       100       110
                 ....*....|....*....|....*....|.
gi 506372187 322 -----LATAKRIGTsmKVVPIKTVEEAITYL 347
Cdd:COG1750  184 etvdlVEYGKELGV--KVIEVSTIADALQYF 212
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 141-209 9.50e-11

circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This BsHtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 58.03  E-value: 9.50e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 141 KQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTL 209
Cdd:cd06781   29 NKGVYVAQVQSNSPAEKAgLKKGDVITKLDGKKVESSSDLRQILYSHKVGDTVKVTIYRDGKEKTLNIKL 98
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 140-212 8.63e-09

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: 52.71  E-value: 8.63e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506372187 140 EKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPL 212
Cdd:cd10838   31 EVDGVLIMQVLPNSPAARAgLRRGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGDRRQTLAVKPGDL 104
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 140-207 8.89e-09

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: 52.30  E-value: 8.89e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506372187 140 EKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTML 207
Cdd:cd06779   23 VNRGVLVAEVIPGSPAAKAgLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDSLNLTILRDGKTLTVTV 91
PDZ_2 pfam13180
PDZ domain;
137-200 1.02e-08

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 51.50  E-value: 1.02e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506372187  137 VKIEKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDG 200
Cdd:pfam13180   1 FVDLEGGVVVVSVKSSGPAAKAgLKAGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDG 65
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
134-216 1.35e-08

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 56.37  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 134 GFEVKIEKQGVWVMGTLEGFPAHK-TLRIGDVITYVDGVRTSeAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPL 212
Cdd:COG3975  486 GLRVSADGGGLVVTSVLWGSPAYKaGLSAGDELLAIDGLRVT-ADNLDDALAAYKPGDPIELLVFRRDELRTVTVTLAAA 564


                 ....
gi 506372187 213 PESK 216
Cdd:COG3975  565 PADT 568
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 141-209 1.55e-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: 51.81  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 141 KQGVWVMGTLEGFPAHK-----TLR-------IGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLT 208
Cdd:cd00990   22 RSGVLVLDVPPGGPAAKaglrgTKRdefgrivLGDVIVAVDGKPVKNESDLYRALDEYKVGDVVTLKVLRGGTKVDLKVT 101


                 .
gi 506372187 209 L 209
Cdd:cd00990  102 L 102
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 138-219 3.20e-07

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: 51.84  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  138 KIEKQ-GVWVMGTLEGFPAHK-TLRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPES 215
Cdd:TIGR02037 252 GLEKQrGALVAQVLPGSPAEKaGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKEKTITVTLGASPEE 331


                  ....
gi 506372187  216 KSVG 219
Cdd:TIGR02037 332 QASS 335
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 150-231 4.52e-07

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 50.86  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 150 LEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSaKKAGDQVEITYTRDGQEAKTMLTLEPLPESKSVGIGVRPDNKQ 228
Cdd:COG0750  136 VPGSPAAKAgLQPGDRIVAINGQPVTSWDDLVDIIR-ASPGKPLTLTVERDGEELTLTVTPRLVEEDGVGRIGVSPSGEV 214


                 ...
gi 506372187 229 EII 231
Cdd:COG0750  215 VTV 217
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 116-202 4.94e-07

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: 47.09  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 116 AVMDNSQKIAEAvafrlagFEVKiEKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEI 194
Cdd:cd10839    7 QIQELTPDLAES-------FGLK-EPKGALVAQVLPDSPAAKAgLKAGDVILSLNGKPITSSADLRNRVATTKPGTKVEL 78


                 ....*...
gi 506372187 195 TYTRDGQE 202
Cdd:cd10839   79 KILRDGKE 86
cpPDZ_RseP_YlbL-like cd10824
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), ...
 144-224 1.76e-06

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), Bacillus subtilis YlbL protease, and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), Bacillus subtilis YlbL, and related domains, including archaeal and chloroplast PDZ domains. RseP participates in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmaE) protein RseA. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP-YlbL family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467636 [Multi-domain]  Cd Length: 82  Bit Score: 45.26  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 144 VWVMGTLEGFPAHKTLRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKSVG-IGV 222
Cdd:cd10824    1 VVVLSVKPNSPAAKALHAGDLITEIDGQPTKSWQTFIDYIHDKKVGESVKITYKHGNKNEEASLKLTAIPKEKGTPgIGI 80


                 ..
gi 506372187 223 RP 224
Cdd:cd10824   81 RP 82
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 245-342 7.08e-06

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 46.46  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  245 GPSAGLMMTLEIYDQLnteTDLTKGYKIAGTGTISLDGKVGRIGGINLKVIAADKAGAEIFFAPQDtpdtssNYEEALAT 324
Cdd:pfam05362 109 GPSAGVTMATALVSAL---TGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKE------NEKDLEDI 179

                          90
                  ....*....|....*...
gi 506372187  325 AKRIGTSMKVVPIKTVEE 342
Cdd:pfam05362 180 PENVREGLEIIPVEHVDE 197
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 134-209 7.36e-06

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: 47.17  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 134 GFEVKIEKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKdlLTALSAK---KAGDQVEITYTRDGQEAKTMLTL 209
Cdd:COG0793   63 GAELGEEDGKVVVVSVIPGSPAEKAgIKPGDIILAIDGKSVAGLT--LDDAVKLlrgKAGTKVTLTIKRPGEGEPITVTL 140
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 134-200 5.16e-05

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: 41.21  E-value: 5.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506372187   134 GFEV---KIEKQGVWVMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDG 200
Cdd:smart00228  15 GFSLvggKDEGGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 245-344 6.61e-04

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 41.54  E-value: 6.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187 245 GPSAGLMMTLEIYDQLnTETDLTKgyKIAGTGTISLDGKVGRIGGINLKVIAADKAGAEIFFAPQD-TPDtssnYEEALA 323
Cdd:COG0466  680 GPSAGITMATALVSAL-TGRPVRS--DVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKEnEKD----LEEIPE 752

                         90       100
                 ....*....|....*....|.
gi 506372187 324 TAKRigtSMKVVPIKTVEEAI 344
Cdd:COG0466  753 EVKK---GLEFHPVEHIDEVL 770
Tricorn_PDZ pfam14685
Tricorn protease PDZ domain; This domain is the PDZ domain of tricorn protease.
 159-205 2.11e-03

Tricorn protease PDZ domain; This domain is the PDZ domain of tricorn protease.


Pssm-ID: 405386 [Multi-domain]  Cd Length: 88  Bit Score: 36.79  E-value: 2.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 506372187  159 LRIGDVITYVDGVRTSEAKDLLTALsAKKAGDQVEITYTRDGQEAKT 205
Cdd:pfam14685  40 VRVGDCILAVDGRPVGPVTGPYSLL-VGKAGQEVELTVRRKDGDARR 85
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 159-224 3.90e-03

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: 36.02  E-value: 3.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506372187 159 LRIGDVITYVDGVRTSEAKDLLTALSAKKaGDQVEITYTRDGQEAKTMLTLEpLPESKSVG---IGVRP 224
Cdd:cd23081   17 LKPGDRILKIDGQKVRTWEDIVRIVRENP-GKPLTLKIERDGKILTVTVTPE-LVEVEGKGvgrIGVQP 83
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 146-210 5.81e-03

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


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 35.54  E-value: 5.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506372187 146 VMGTLEGFPAHKT-LRIGDVITYVDGVRTS-----EAKDLLTAlsakKAGDQVEITYTRDGQEAKTMLTLE 210
Cdd:cd06782   18 VVSPIPGGPAEKAgIKPGDVIVAVDGESVRgmsldEVVKLLRG----PKGTKVKLTIRRGGEGEPRDVTLT 84
Peptidase_M50 pfam02163
Peptidase family M50;
146-297 5.99e-03

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 37.86  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506372187  146 VMGTLEGFPAHKT-LRIGDVITYVDGVRTSEAKDLLTALsAKKAGDQVEITYTRDGQEAKTMLTLEPLPESKSVGIGvrp 224
Cdd:pfam02163  97 IGGVAPGSPAAKAgLKPGDVILSINGKKITSWQDLVEAL-AKSPGKPITLTVERGGQTLTVTITPKSSEESKFIGIG--- 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506372187  225 dnkqeiIIPKEVTIASQGIGGPSAGLMMTLEIYDQLNTETDLTKGYKIAgtGTISLDGKVGRIGGINLKVIAA 297
Cdd:pfam02163 173 ------PVYVKYGLLEALGFALEKTVNLVTLTLKALGKLITGVSLKNLG--GPIGIAGQAAEAGLIAFLYFLA 237
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 159-201 9.83e-03

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 36.88  E-value: 9.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 506372187 159 LRIGDVITYVDGVRTSEAKDLLTALSAKKAGDQVEITYTRDGQ 201
Cdd:COG3031  169 LQPGDVITSINGQDLTDPAQALELLQQLRDASEVTLTVERNGQ 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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