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Conserved domains on  [gi|659497588|gb|KEJ88652|]
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serine protease [Sulfitobacter donghicola DSW-25 = KCTC 12864 = JCM 14565]

Protein Classification

Do family serine endopeptidase( domain architecture ID 1000019)

Do/DeqQ family serine endopeptidase belonging to the peptidase S1C family, contains a PDZ-domain, similar to Lactococcus lactis Do-like HtrA (High-temperature requirement A), which is a surface protease responsible for the housekeeping of exported proteins and plays a role in stress resistance during active exponential growth

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
degP_htrA_DO super family cl37035
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 29-452 2.40e-137

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]


The actual alignment was detected with superfamily member TIGR02037:

Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 401.21  E-value: 2.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   29 LSFVPVVKQAAPAVVNIYAKVVREVRRTPLQSDPFFERFFRDP----QEGRKPRVQNSLGSGVILSADGLVVSNYHVVGM 104
Cdd:TIGR02037   1 PSFAPLVEKVAPAVVNISVEGTVKRRNRPPALPPFFRQFFGDDmpdfPRQQREQKVRGLGSGVIISADGYVLTNNHVVDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  105 ATDIRVVLNDRREFTAKVLLGDEASDLAILKIDAPDPLPFLELRQSDSVEVGELALAIGNPFGVGQTVSSGIVSGLARSG 184
Cdd:TIGR02037  81 ADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  185 GSGGQGHGyFIQTDAPINPGNSGGALVDMAGRLIGVNTSILTRSGGSNGIGFAIPADLVAEFVSQSeMGHSDFGRPWAGI 264
Cdd:TIGR02037 161 LGIGDYEN-FIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQL-IEGGKVKRGWLGV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  265 SGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVFSRQGEE 344
Cdd:TIGR02037 239 TIQEVTSDLAKSLGLEKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  345 AHTQVDLIAAPEEPARdqyelpERSLFPGLILTRINPAVLSELNLPLEAKGVAV--VQTGPYAARAGLRAGDVLSSINDE 422
Cdd:TIGR02037 319 KTITVTLGASPEEQAS------SSNPFLGLTVANLSPEIRKELRLKGDVKGVVVtkVVSGSPAARAGLQPGDVILSVNQQ 392

                         410       420       430
                  ....*....|....*....|....*....|..
gi 659497588  423 VLDHPEAAAELL--SGKQRSISMVVQRGDRRI 452
Cdd:TIGR02037 393 PVSSVAELRKVLarAKKGGRVALLILRGGATI 424
 
Name Accession Description Interval E-value
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 29-452 2.40e-137

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: 401.21  E-value: 2.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   29 LSFVPVVKQAAPAVVNIYAKVVREVRRTPLQSDPFFERFFRDP----QEGRKPRVQNSLGSGVILSADGLVVSNYHVVGM 104
Cdd:TIGR02037   1 PSFAPLVEKVAPAVVNISVEGTVKRRNRPPALPPFFRQFFGDDmpdfPRQQREQKVRGLGSGVIISADGYVLTNNHVVDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  105 ATDIRVVLNDRREFTAKVLLGDEASDLAILKIDAPDPLPFLELRQSDSVEVGELALAIGNPFGVGQTVSSGIVSGLARSG 184
Cdd:TIGR02037  81 ADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  185 GSGGQGHGyFIQTDAPINPGNSGGALVDMAGRLIGVNTSILTRSGGSNGIGFAIPADLVAEFVSQSeMGHSDFGRPWAGI 264
Cdd:TIGR02037 161 LGIGDYEN-FIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQL-IEGGKVKRGWLGV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  265 SGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVFSRQGEE 344
Cdd:TIGR02037 239 TIQEVTSDLAKSLGLEKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  345 AHTQVDLIAAPEEPARdqyelpERSLFPGLILTRINPAVLSELNLPLEAKGVAV--VQTGPYAARAGLRAGDVLSSINDE 422
Cdd:TIGR02037 319 KTITVTLGASPEEQAS------SSNPFLGLTVANLSPEIRKELRLKGDVKGVVVtkVVSGSPAARAGLQPGDVILSVNQQ 392

                         410       420       430
                  ....*....|....*....|....*....|..
gi 659497588  423 VLDHPEAAAELL--SGKQRSISMVVQRGDRRI 452
Cdd:TIGR02037 393 PVSSVAELRKVLarAKKGGRVALLILRGGATI 424
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 82-356 3.50e-108

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: 321.33  E-value: 3.50e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  82 SLGSGVILSADGLVVSNYHVVGMATDIRVVLNDRREFTAKVLLGDEASDLAILKIDAPDpLPFLELRQSDSVEVGELALA 161
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKD-LPAAPLGDSDKLRVGDWVLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 162 IGNPFGVGQTVSSGIVSGLARSGGSGGQGHGY-FIQTDAPINPGNSGGALVDMAGRLIGVNTSILTRSGGSNGIGFAIPA 240
Cdd:COG0265   80 IGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDdFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAIPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 241 DLVAEFVSQ-SEMGHSDfgRPWAGISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPS 319
Cdd:COG0265  160 NLAKRVVEQlIETGRVR--RGWLGVTIQPVTPELAEALGLPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSAR 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 659497588 320 EMIYRMSVAGLEAKADVVFSRQGEEAHTQVDLIAAPE 356
Cdd:COG0265  238 DLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
PRK10942 PRK10942
serine endoprotease DegP;
1-452 7.17e-74

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 239.67  E-value: 7.17e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   1 MKYIVLILTLLAAPLS---AQQVPQSSAEMQLSFVPVVKQAAPAVVNIYAK--VVREVRRTPLQSDPFF----------E 65
Cdd:PRK10942   7 LSALALSLGLALSPLSataAETSSATTAQQMPSLAPMLEKVMPSVVSINVEgsTTVNTPRMPRQFQQFFgdnspfcqegS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  66 RFFRDP--------QEGRKPRVQNSLGSGVILSAD-GLVVSNYHVVGMATDIRVVLNDRREFTAKVLLGDEASDLAILKI 136
Cdd:PRK10942  87 PFQSSPfcqggqggNGGGQQQKFMALGSGVIIDADkGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 137 DAPDPLPFLELRQSDSVEVGELALAIGNPFGVGQTVSSGIVSGLARSGGSGGQGHGyFIQTDAPINPGNSGGALVDMAGR 216
Cdd:PRK10942 167 QNPKNLTAIKMADSDALRVGDYTVAIGNPYGLGETVTSGIVSALGRSGLNVENYEN-FIQTDAAINRGNSGGALVNLNGE 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 217 LIGVNTSILTRSGGSNGIGFAIPADLVAEFVSQ-SEMGHSDFGRpwAGISGQSLDADMAATLGFDRSGGIIISGLHPVSP 295
Cdd:PRK10942 246 LIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQmVEYGQVKRGE--LGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 296 FRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVFSRQGEEAHTQVDLiaapEEPARDQYELperslfpGLI 375
Cdd:PRK10942 324 AAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVEL----QQSSQNQVDS-------SNI 392

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 659497588 376 LTRINPAVLSELNlplEAKGVAV--VQTGPYAARAGLRAGDVLSSINDEVLDHPEAAAELLSGKQRSISMVVQRGDRRI 452
Cdd:PRK10942 393 FNGIEGAELSNKG---GDKGVVVdnVKPGTPAAQIGLKKGDVIIGANQQPVKNIAELRKILDSKPSVLALNIQRGDSSI 468
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 30-321 8.46e-70

HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous serine proteases HhoA, HhoB, and HtrA of the model cyanobacterial isolate Synechocystis sp. PCC 6803. They resemble the paralogous trio of serine proteases DegQ, DegP, and DegS of Escherichia coli.


Pssm-ID: 469406 [Multi-domain]  Cd Length: 334  Bit Score: 224.66  E-value: 8.46e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  30 SFVP-VVKQAAPAVVNIYAKVVREVRRTPLQSDPFFERFFRDPQEGRKP--RVQNSLGSGVILSADGLVVSNYHVVGMAT 106
Cdd:NF041521   1 NFVAaAVEKVGPAVVRIDAERTVVTQVPPFFNDPFFRRFFGSDIPPPPPqeRVERGTGSGFIISSDGIILTNAHVVDGAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 107 DIRVVLNDRREFTAKVLLGDEASDLAILKIDAPDpLPFLELRQSDSVEVGELALAIGNPFGVGQTVSSGIVSGLARSGGS 186
Cdd:NF041521  81 TVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKN-LPTVPLGNSDQLQPGEWAIAIGNPLGLDNTVTLGIISATGRSSSQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 187 GGQGH--GYFIQTDAPINPGNSGGALVDMAGRLIGVNTSILtrsGGSNGIGFAIPADLVAEFVSQ-SEMGHSDfgRPWAG 263
Cdd:NF041521 160 VGVPDkrVDFIQTDAAINPGNSGGPLLNARGEVIGINTAIR---AGAQGLGFAIPINTAQRIADQlIAGGKVE--HPYLG 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659497588 264 IS--------GQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEM 321
Cdd:NF041521 235 IQmvtltpelKQEINSDPNSGFTVPEDEGVLIVRVVPNSPAARAGLRAGDVIQKINGQPVTTAEQV 300
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 84-220 1.30e-32

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 120.60  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   84 GSGVILSADGLVVSNYHVVGMATDIRV-----VLNDRREFTAKVLLGDEASDLAILKIDAP-DPLPFLELRQSDSVEVGE 157
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVelvsvVLADGREYPATVVARDPDLDLALLRVSGDgRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 659497588  158 LALAIGNPFGVG-QTVSSGIVSGLARSGGSGGQGhgYFIQTDAPINPGNSGGALVDMAGRLIGV 220
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDGGDDG--RVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 259-344 4.94e-14

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: 67.51  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 259 RPWAGISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMiyRMSVAGLEA--KADV 336
Cdd:cd10839    1 RGWLGVQIQELTPDLAESFGLKEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADL--RNRVATTKPgtKVEL 78


                 ....*...
gi 659497588 337 VFSRQGEE 344
Cdd:cd10839   79 KILRDGKE 86
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 396-449 1.60e-04

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: 40.44  E-value: 1.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 659497588   396 VAVVQTGPYAARAGLRAGDVLSSINDEVLDH--PEAAAELLSGKQRSISMVVQRGD 449
Cdd:smart00228  30 VSSVVPGSPAAKAGLRVGDVILEVNGTSVEGltHLEAVDLLKKAGGKVTLTVLRGG 85
 
Name Accession Description Interval E-value
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 29-452 2.40e-137

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: 401.21  E-value: 2.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   29 LSFVPVVKQAAPAVVNIYAKVVREVRRTPLQSDPFFERFFRDP----QEGRKPRVQNSLGSGVILSADGLVVSNYHVVGM 104
Cdd:TIGR02037   1 PSFAPLVEKVAPAVVNISVEGTVKRRNRPPALPPFFRQFFGDDmpdfPRQQREQKVRGLGSGVIISADGYVLTNNHVVDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  105 ATDIRVVLNDRREFTAKVLLGDEASDLAILKIDAPDPLPFLELRQSDSVEVGELALAIGNPFGVGQTVSSGIVSGLARSG 184
Cdd:TIGR02037  81 ADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  185 GSGGQGHGyFIQTDAPINPGNSGGALVDMAGRLIGVNTSILTRSGGSNGIGFAIPADLVAEFVSQSeMGHSDFGRPWAGI 264
Cdd:TIGR02037 161 LGIGDYEN-FIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQL-IEGGKVKRGWLGV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  265 SGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVFSRQGEE 344
Cdd:TIGR02037 239 TIQEVTSDLAKSLGLEKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  345 AHTQVDLIAAPEEPARdqyelpERSLFPGLILTRINPAVLSELNLPLEAKGVAV--VQTGPYAARAGLRAGDVLSSINDE 422
Cdd:TIGR02037 319 KTITVTLGASPEEQAS------SSNPFLGLTVANLSPEIRKELRLKGDVKGVVVtkVVSGSPAARAGLQPGDVILSVNQQ 392

                         410       420       430
                  ....*....|....*....|....*....|..
gi 659497588  423 VLDHPEAAAELL--SGKQRSISMVVQRGDRRI 452
Cdd:TIGR02037 393 PVSSVAELRKVLarAKKGGRVALLILRGGATI 424
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 82-356 3.50e-108

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: 321.33  E-value: 3.50e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  82 SLGSGVILSADGLVVSNYHVVGMATDIRVVLNDRREFTAKVLLGDEASDLAILKIDAPDpLPFLELRQSDSVEVGELALA 161
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKD-LPAAPLGDSDKLRVGDWVLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 162 IGNPFGVGQTVSSGIVSGLARSGGSGGQGHGY-FIQTDAPINPGNSGGALVDMAGRLIGVNTSILTRSGGSNGIGFAIPA 240
Cdd:COG0265   80 IGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDdFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAIPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 241 DLVAEFVSQ-SEMGHSDfgRPWAGISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPS 319
Cdd:COG0265  160 NLAKRVVEQlIETGRVR--RGWLGVTIQPVTPELAEALGLPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSAR 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 659497588 320 EMIYRMSVAGLEAKADVVFSRQGEEAHTQVDLIAAPE 356
Cdd:COG0265  238 DLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
PRK10942 PRK10942
serine endoprotease DegP;
1-452 7.17e-74

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 239.67  E-value: 7.17e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   1 MKYIVLILTLLAAPLS---AQQVPQSSAEMQLSFVPVVKQAAPAVVNIYAK--VVREVRRTPLQSDPFF----------E 65
Cdd:PRK10942   7 LSALALSLGLALSPLSataAETSSATTAQQMPSLAPMLEKVMPSVVSINVEgsTTVNTPRMPRQFQQFFgdnspfcqegS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  66 RFFRDP--------QEGRKPRVQNSLGSGVILSAD-GLVVSNYHVVGMATDIRVVLNDRREFTAKVLLGDEASDLAILKI 136
Cdd:PRK10942  87 PFQSSPfcqggqggNGGGQQQKFMALGSGVIIDADkGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 137 DAPDPLPFLELRQSDSVEVGELALAIGNPFGVGQTVSSGIVSGLARSGGSGGQGHGyFIQTDAPINPGNSGGALVDMAGR 216
Cdd:PRK10942 167 QNPKNLTAIKMADSDALRVGDYTVAIGNPYGLGETVTSGIVSALGRSGLNVENYEN-FIQTDAAINRGNSGGALVNLNGE 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 217 LIGVNTSILTRSGGSNGIGFAIPADLVAEFVSQ-SEMGHSDFGRpwAGISGQSLDADMAATLGFDRSGGIIISGLHPVSP 295
Cdd:PRK10942 246 LIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQmVEYGQVKRGE--LGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 296 FRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVFSRQGEEAHTQVDLiaapEEPARDQYELperslfpGLI 375
Cdd:PRK10942 324 AAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVEL----QQSSQNQVDS-------SNI 392

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 659497588 376 LTRINPAVLSELNlplEAKGVAV--VQTGPYAARAGLRAGDVLSSINDEVLDHPEAAAELLSGKQRSISMVVQRGDRRI 452
Cdd:PRK10942 393 FNGIEGAELSNKG---GDKGVVVdnVKPGTPAAQIGLKKGDVIIGANQQPVKNIAELRKILDSKPSVLALNIQRGDSSI 468
PRK10139 PRK10139
serine endoprotease DegQ;
8-457 2.17e-71

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 232.91  E-value: 2.17e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   8 LTLLAAPLSAQQVP-QSSAEMQL-SFVPVVKQAAPAVVNIyakvvrEVRRTPLQSDPF---FERFFRD--PQEGRKPRvq 80
Cdd:PRK10139  17 LTLSASFQAVASIPgQVAGQAPLpSLAPMLEKVLPAVVSV------RVEGTASQGQKIpeeFKKFFGDdlPDQPAQPF-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  81 NSLGSGVIL-SADGLVVSNYHVVGMATDIRVVLNDRREFTAKVLLGDEASDLAILKIDAPDPLPFLELRQSDSVEVGELA 159
Cdd:PRK10139  89 EGLGSGVIIdAAKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 160 LAIGNPFGVGQTVSSGIVSGLARSGGSGGQGHGyFIQTDAPINPGNSGGALVDMAGRLIGVNTSILTRSGGSNGIGFAIP 239
Cdd:PRK10139 169 VAVGNPFGLGQTATSGIISALGRSGLNLEGLEN-FIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIP 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 240 ADLvAEFVSQSEMGHSDFGRPWAGISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPS 319
Cdd:PRK10139 248 SNM-ARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFNLDVQRGAFVSEVLPNSGSAKAGVKAGDIITSLNGKPLNSFA 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 320 EMIYRMSVAGLEAKADVVFSRQGEEAHTQVDLIAAPEEPARDQyelperslfpgLILTRINPAVLSELNLPLEAKGVAV- 398
Cdd:PRK10139 327 ELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDTSTSSSASAE-----------MITPALQGATLSDGQLKDGTKGIKId 395

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 399 -VQTGPYAARAGLRAGDVLSSINDEVLDHPEAAAELLSGKQRSISMVVQRGDRRISMRFR 457
Cdd:PRK10139 396 eVVKGSPAAQAGLQKDDVIIGVNRDRVNSIAEMRKVLAAKPAIIALQIVRGNESIYLLLR 455
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 30-321 8.46e-70

HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous serine proteases HhoA, HhoB, and HtrA of the model cyanobacterial isolate Synechocystis sp. PCC 6803. They resemble the paralogous trio of serine proteases DegQ, DegP, and DegS of Escherichia coli.


Pssm-ID: 469406 [Multi-domain]  Cd Length: 334  Bit Score: 224.66  E-value: 8.46e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  30 SFVP-VVKQAAPAVVNIYAKVVREVRRTPLQSDPFFERFFRDPQEGRKP--RVQNSLGSGVILSADGLVVSNYHVVGMAT 106
Cdd:NF041521   1 NFVAaAVEKVGPAVVRIDAERTVVTQVPPFFNDPFFRRFFGSDIPPPPPqeRVERGTGSGFIISSDGIILTNAHVVDGAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 107 DIRVVLNDRREFTAKVLLGDEASDLAILKIDAPDpLPFLELRQSDSVEVGELALAIGNPFGVGQTVSSGIVSGLARSGGS 186
Cdd:NF041521  81 TVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKN-LPTVPLGNSDQLQPGEWAIAIGNPLGLDNTVTLGIISATGRSSSQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 187 GGQGH--GYFIQTDAPINPGNSGGALVDMAGRLIGVNTSILtrsGGSNGIGFAIPADLVAEFVSQ-SEMGHSDfgRPWAG 263
Cdd:NF041521 160 VGVPDkrVDFIQTDAAINPGNSGGPLLNARGEVIGINTAIR---AGAQGLGFAIPINTAQRIADQlIAGGKVE--HPYLG 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659497588 264 IS--------GQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEM 321
Cdd:NF041521 235 IQmvtltpelKQEINSDPNSGFTVPEDEGVLIVRVVPNSPAARAGLRAGDVIQKINGQPVTTAEQV 300
PRK10898 PRK10898
serine endoprotease DegS;
4-321 1.95e-50

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 174.80  E-value: 1.95e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   4 IVLILTLLAAP------LSAQQVPQSSAEMQLSFVPVVKQAAPAVVNIYAKVVrevrrtplqsDPFferffrdPQEGRKP 77
Cdd:PRK10898  14 IVAAILLVAMPslrslnPLSTPQFDSTDETPASYNQAVRRAAPAVVNVYNRSL----------NST-------SHNQLEI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  78 RvqnSLGSGVILSADGLVVSNYHVVGMATDIRVVLNDRREFTAKVLLGDEASDLAILKIDApDPLPFLELRQSDSVEVGE 157
Cdd:PRK10898  77 R---TLGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINA-TNLPVIPINPKRVPHIGD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 158 LALAIGNPFGVGQTVSSGIVSGLARsGGSGGQGHGYFIQTDAPINPGNSGGALVDMAGRLIGVNTsiLTRSGGSN----- 232
Cdd:PRK10898 153 VVLAIGNPYNLGQTITQGIISATGR-IGLSPTGRQNFLQTDASINHGNSGGALVNSLGELMGINT--LSFDKSNDgetpe 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 233 GIGFAIPADLvAEFVSQSEMGHSDFGRPWAGISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGG 312
Cdd:PRK10898 230 GIGFAIPTQL-ATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAAKAGIQVNDLIISVNN 308


                 ....*....
gi 659497588 313 QTVNTPSEM 321
Cdd:PRK10898 309 KPAISALET 317
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 84-220 1.30e-32

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 120.60  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   84 GSGVILSADGLVVSNYHVVGMATDIRV-----VLNDRREFTAKVLLGDEASDLAILKIDAP-DPLPFLELRQSDSVEVGE 157
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVelvsvVLADGREYPATVVARDPDLDLALLRVSGDgRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 659497588  158 LALAIGNPFGVG-QTVSSGIVSGLARSGGSGGQGhgYFIQTDAPINPGNSGGALVDMAGRLIGV 220
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDGGDDG--RVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 259-344 4.94e-14

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: 67.51  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 259 RPWAGISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMiyRMSVAGLEA--KADV 336
Cdd:cd10839    1 RGWLGVQIQELTPDLAESFGLKEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADL--RNRVATTKPgtKVEL 78


                 ....*...
gi 659497588 337 VFSRQGEE 344
Cdd:cd10839   79 KILRDGKE 86
Trypsin pfam00089
Trypsin;
86-247 3.73e-13

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 68.62  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588   86 GVILSADGlVVSNYHVVGMATDIRVVL-------NDRREFTAKVL---------LGDEASDLAILKIDAPD-------PL 142
Cdd:pfam00089  29 GSLISENW-VLTAAHCVSGASDVKVVLgahnivlREGGEQKFDVEkiivhpnynPDTLDNDIALLKLESPVtlgdtvrPI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  143 PFLELRQSDSVEVGELALAIGNPF--GVGQTVSSGIVSGLARSGGSGGQGHGY---FIQTDAP---INPGNSGGALVDMA 214
Cdd:pfam00089 108 CLPDASSDLPVGTTCTVSGWGNTKtlGPSDTLQEVTVPVVSRETCRSAYGGTVtdtMICAGAGgkdACQGDSGGPLVCSD 187

                         170       180       190
                  ....*....|....*....|....*....|...
gi 659497588  215 GRLIGVNTSILTRSGGsNGIGFAIPADLVAEFV 247
Cdd:pfam00089 188 GELIGIVSWGYGCASG-NYPGVYTPVSSYLDWI 219
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 259-344 1.69e-10

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: 57.30  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 259 RPWAGISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVF 338
Cdd:cd06779    1 RPYLGIEMENISPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDSLNLTI 80


                 ....*.
gi 659497588 339 SRQGEE 344
Cdd:cd06779   81 LRDGKT 86
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 259-351 8.53e-09

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: 52.78  E-value: 8.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 259 RPWAGISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVF 338
Cdd:cd06777    1 RGYLGITLSEIPPAMARGGGIDQLQGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLELMDLVAEIRPGTVIPVVV 80

                         90
                 ....*....|...
gi 659497588 339 SRQGEEAHTQVDL 351
Cdd:cd06777   81 LRDGKQLTLEVTI 93
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 395-447 5.81e-08

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 49.06  E-value: 5.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 659497588  395 GVAVVQTGPYAARAGLRAGDVLSSINDEVLDHPEAAAELLSGKQ-RSISMVVQR 447
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLLQGSAgESVTLTVRR 54
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 373-455 1.52e-07

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: 48.83  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 373 GLILTRINPAVLSELNLPlEAKGVAV--VQTGPYAARAGLRAGDVLSSINDEVLDHPEAAAELLSGKQ--RSISMVVQRG 448
Cdd:cd06779    5 GIEMENISPLLAKELGLP-VNRGVLVaeVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTKKpgDSLNLTILRD 83


                 ....*..
gi 659497588 449 DRRISMR 455
Cdd:cd06779   84 GKTLTVT 90
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 80-244 5.38e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.06  E-value: 5.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588  80 QNSLGSGVILSADgLVVSNYHVV------GMATDIRVVLNDRRE----FTAKVLL--------GDEASDLAILKIDAP-- 139
Cdd:COG3591   10 GGGVCTGTLIGPN-LVLTAGHCVydgaggGWATNIVFVPGYNGGpygtATATRFRvppgwvasGDAGYDYALLRLDEPlg 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 140 DPLPFLELRQSDSVEVGELALAIGNPFGVGQTVS---SGIVSGLArsggsggqghGYFIQTDAPINPGNSGGALVDM--- 213
Cdd:COG3591   89 DTTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSldcSGRVTGVQ----------GNRLSYDCDTTGGSSGSPVLDDsdg 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 659497588 214 AGRLIGVNTSiltRSGGSNGIGFAIPADLVA 244
Cdd:COG3591  159 GGRVVGVHSA---GGADRANTGVRLTSAIVA 186
PDZ_2 pfam13180
PDZ domain;
280-351 8.60e-07

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 46.50  E-value: 8.60e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 659497588  280 DRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSvaGLEAKADVVFS--RQGEEAHTQVDL 351
Cdd:pfam13180   3 DLEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALY--GHKPGDTVTLQvyRDGKLLTVEVKL 74
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 259-357 1.44e-06

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: 46.69  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 259 RPWAGISGQSLDADMAATL-----GF-DRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMS-VAGLE 331
Cdd:cd23085    1 RPWLGMKMLELNEHIIAQLkerdpMFpDVKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQIIDALGdKVGKP 80

                         90       100
                 ....*....|....*....|....*.
gi 659497588 332 AKadVVFSRQGEEahtQVDLIAAPEE 357
Cdd:cd23085   81 FK--VVVKRANKV---QVTLTVTPEE 101
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 406-457 2.32e-06

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 48.44  E-value: 2.32e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 659497588 406 ARAGLRAGDVLSSINDEVLDHPEAAAELLS--GKQRSISMVVQRGDRRISMRFR 457
Cdd:COG3031  165 SKLGLQPGDVITSINGQDLTDPAQALELLQqlRDASEVTLTVERNGQPVTLTYN 218
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 373-457 3.56e-06

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: 45.39  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 373 GLILTRINPAVLSELN--------LPlEAKGVAVVQTGPY--AARAGLRAGDVLSSINDEVLDHPEAAAEL--LSGKQRS 440
Cdd:cd10838    5 GIQMTTLTPELAQQNNrnpnspvrIP-EVDGVLIMQVLPNspAARAGLRRGDVIQAVDGQPVTTADDVQRIveQAGVGEE 83

                         90
                 ....*....|....*..
gi 659497588 441 ISMVVQRGDRRISMRFR 457
Cdd:cd10838   84 LELTVLRGDRRQTLAVK 100
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
272-365 3.64e-06

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 49.43  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 272 DMAATLGF---DRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVnTPSEMIYRMSVAGLEAKADVVFSRQGEEAHTQ 348
Cdd:COG3975  480 SLKPSLGLrvsADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRV-TADNLDDALAAYKPGDPIELLVFRRDELRTVT 558

                         90
                 ....*....|....*..
gi 659497588 349 VDLIAAPeepaRDQYEL 365
Cdd:COG3975  559 VTLAAAP----ADTYKL 571
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 273-357 5.50e-06

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 48.16  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 273 MAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGlEAKADVVFSRQGEEAHTQVDLI 352
Cdd:COG0750  118 LFMTVGVPVLTPPVVGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRASP-GKPLTLTVERDGEELTLTVTPR 196


                 ....*
gi 659497588 353 AAPEE 357
Cdd:COG0750  197 LVEED 201
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 382-450 1.30e-05

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: 43.39  E-value: 1.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659497588 382 AVLSELNLPLEAKGVAV--VQTGPYAARAGLRAGDVLSSINDEVLDHPEAAAELLSGKQRSISMVVQRGDR 450
Cdd:cd23084    6 ATVSNVTDEDGGKGVVVteVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRKVLKSKPSAVLLQIKRGDS 76
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 284-349 7.40e-05

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: 41.92  E-value: 7.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659497588 284 GIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVFSRQGEEAHTQV 349
Cdd:cd10838   34 GVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGDRRQTLAV 99
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 396-449 1.16e-04

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


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 40.54  E-value: 1.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 659497588 396 VAVVQTGPyAARAGLRAGDVLSSINDEVLD--HPEAAAELLSGKQRS-ISMVVQRGD 449
Cdd:cd06782   19 VSPIPGGP-AEKAGIKPGDVIVAVDGESVRgmSLDEVVKLLRGPKGTkVKLTIRRGG 74
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 259-320 1.39e-04

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


Pssm-ID: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 40.70  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659497588 259 RPWAGISGQSLDADMAAT-----LGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSE 320
Cdd:cd06781    1 RPSLGISMVDLSDVPEYEqqslkLPSNVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSD 67
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 396-449 1.60e-04

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: 40.44  E-value: 1.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 659497588   396 VAVVQTGPYAARAGLRAGDVLSSINDEVLDH--PEAAAELLSGKQRSISMVVQRGD 449
Cdd:smart00228  30 VSSVVPGSPAAKAGLRVGDVILEVNGTSVEGltHLEAVDLLKKAGGKVTLTVLRGG 85
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 278-342 1.96e-04

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: 40.05  E-value: 1.96e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 659497588   278 GFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVFSRQG 342
Cdd:smart00228  21 GKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 286-320 9.42e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 37.12  E-value: 9.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 659497588  286 IISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSE 320
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSLED 35
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 286-364 1.03e-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: 37.94  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659497588 286 IISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMiyRMSVAGLEAKA-DVVFSRQGEEahtqVDLIAAPEEPARDQYE 364
Cdd:cd23081    2 VVGEVVANSPAAEAGLKPGDRILKIDGQKVRTWEDI--VRIVRENPGKPlTLKIERDGKI----LTVTVTPELVEVEGKG 75
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 398-447 1.05e-03

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: 38.03  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 659497588 398 VVQTGPyAARAGLRAGDVLSSINDEVL---DHPEaAAELLSGKQRSISMVVQR 447
Cdd:cd06704   37 VTEGGP-AAKAGVRVGDKLLEVNGVDLvdaDHHE-AVEALKNSGNTVTMVVLR 87
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 396-453 1.51e-03

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 40.46  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 659497588 396 VAVVQTGPYAARAGLRAGDVLSSINDEVLDHPEAAAELLSG-KQRSISMVVQRGDRRIS 453
Cdd:COG0750  132 VGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRAsPGKPLTLTVERDGEELT 190
cpPDZ1_MamE-like cd23087
circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease ...
 263-326 2.94e-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: 36.78  E-value: 2.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 659497588 263 GISGQSLDADMAATLGFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEMIYRMS 326
Cdd:cd23087    5 GAALTPMQQRLGQQTNLPAGRGVFVSGVTPNTPAAAAGLRPGDVILKVDGRPVHQPEEVSAIMA 68
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 284-360 3.30e-03

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


Pssm-ID: 467637 [Multi-domain]  Cd Length: 83  Bit Score: 36.70  E-value: 3.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 659497588 284 GIIISGLHPVSPFrqAG-LTVGDVILSVGGQTVNTPSEMIYRMSVAGLEAKADVVFSRQGEEAHTQVDLIAAPEEPAR 360
Cdd:cd23080    1 GVYVLSVVENMPA--KGiLEAGDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKLKQFPDEKNR 76
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
 399-447 3.52e-03

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


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 36.35  E-value: 3.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 659497588 399 VQTGPYAARAGLRAGDVLSSINDE---VLDHPEAAAELL-SGKQrsISMVVQR 447
Cdd:cd23068   32 VNPGSPADKAGLRRGDVILRINGTdtsNLTHKQAQDLIKrAGND--LQLTVQR 82
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 281-316 3.91e-03

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


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 39.08  E-value: 3.91e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 659497588 281 RSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVN 316
Cdd:COG0793   69 EDGKVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVA 104
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 280-320 5.45e-03

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: 36.32  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 659497588 280 DRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSE 320
Cdd:cd06785   28 DVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSD 68
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 280-321 7.20e-03

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 35.33  E-value: 7.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 659497588  280 DRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQTVNTPSEM 321
Cdd:pfam00595  22 QGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHE 63
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 278-313 7.92e-03

PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RapGEF2 and RapGEF6 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467237 [Multi-domain]  Cd Length: 83  Bit Score: 35.32  E-value: 7.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 659497588 278 GFDRSGGIIISGLHPVSPFRQAGLTVGDVILSVGGQ 313
Cdd:cd06755   21 GSEKGFGIFVSKVEKGSKAAEAGLKRGDQILEVNGQ 56
 
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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