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Conserved domains on  [gi|492529449|ref|WP_005874875|]
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DegQ family serine endoprotease [Porphyromonas gingivalis]

Protein Classification

DegQ family serine endoprotease( domain architecture ID 11493471)

DegQ family serine endoprotease 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 TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 64-486 0e+00

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: 533.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449   64 PNLVGAAEASVHAVVHIKVESEQRMDSQQYFDP--FEFFFGGESRNFQRPQ-TRQVVGYGSGVIISTDGYIITNNHVVKG 140
Cdd:TIGR02037   1 PSFAPLVEKVAPAVVNISVEGTVKRRNRPPALPpfFRQFFGDDMPDFPRQQrEQKVRGLGSGVIISADGYVLTNNHVVDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  141 AKEMTVTLNDNRTFKAKLIGSDATTDIALLKVDAKG-LPTIPFGDSDKLRVGEWVLAVGNPFNLTSTVTAGIVSAKGRST 219
Cdd:TIGR02037  81 ADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKnLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  220 QqvargGSLQIESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYAGYSFAVPISIAAKVVADIKQYGTVQRAV 299
Cdd:TIGR02037 161 L-----GIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGW 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  300 LGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRK 379
Cdd:TIGR02037 236 LGVTIQEVTSDLAKSLGLEKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRK 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  380 GATKELTVTLKNNEGstsvITGESTGNVLGASFKDLSAEQ---MRSYGVSYGVEVTSVSSGKF-KDAGIKKGFIILSINR 455
Cdd:TIGR02037 316 GKEKTITVTLGASPE----EQASSSNPFLGLTVANLSPEIrkeLRLKGDVKGVVVTKVVSGSPaARAGLQPGDVILSVNQ 391

                         410       420       430
                  ....*....|....*....|....*....|.
gi 492529449  456 QPVSSGADVSDIVREAGQSRSGRLIIVRGFY 486
Cdd:TIGR02037 392 QPVSSVAELRKVLARAKKGGRVALLILRGGA 422
 
Name Accession Description Interval E-value
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 64-486 0e+00

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: 533.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449   64 PNLVGAAEASVHAVVHIKVESEQRMDSQQYFDP--FEFFFGGESRNFQRPQ-TRQVVGYGSGVIISTDGYIITNNHVVKG 140
Cdd:TIGR02037   1 PSFAPLVEKVAPAVVNISVEGTVKRRNRPPALPpfFRQFFGDDMPDFPRQQrEQKVRGLGSGVIISADGYVLTNNHVVDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  141 AKEMTVTLNDNRTFKAKLIGSDATTDIALLKVDAKG-LPTIPFGDSDKLRVGEWVLAVGNPFNLTSTVTAGIVSAKGRST 219
Cdd:TIGR02037  81 ADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKnLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  220 QqvargGSLQIESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYAGYSFAVPISIAAKVVADIKQYGTVQRAV 299
Cdd:TIGR02037 161 L-----GIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGW 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  300 LGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRK 379
Cdd:TIGR02037 236 LGVTIQEVTSDLAKSLGLEKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRK 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  380 GATKELTVTLKNNEGstsvITGESTGNVLGASFKDLSAEQ---MRSYGVSYGVEVTSVSSGKF-KDAGIKKGFIILSINR 455
Cdd:TIGR02037 316 GKEKTITVTLGASPE----EQASSSNPFLGLTVANLSPEIrkeLRLKGDVKGVVVTKVVSGSPaARAGLQPGDVILSVNQ 391

                         410       420       430
                  ....*....|....*....|....*....|.
gi 492529449  456 QPVSSGADVSDIVREAGQSRSGRLIIVRGFY 486
Cdd:TIGR02037 392 QPVSSVAELRKVLARAKKGGRVALLILRGGA 422
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 118-389 1.64e-136

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: 394.90  E-value: 1.64e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 118 GYGSGVIISTDGYIITNNHVVKGAKEMTVTLNDNRTFKAKLIGSDATTDIALLKVDAKGLPTIPFGDSDKLRVGEWVLAV 197
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 198 GNPFNLTSTVTAGIVSAKGRSTQQVARGGslqIESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYAGYSFAV 277
Cdd:COG0265   81 GNPFGLGQTVTAGIVSALGRSIGSSGGGT---YDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 278 PISIAAKVVADIKQYGTVQRAVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFP 357
Cdd:COG0265  158 PINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALGLPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSAR 237

                        250       260       270
                 ....*....|....*....|....*....|..
gi 492529449 358 QLQEAISRYRPGDKVKLTINRKGATKELTVTL 389
Cdd:COG0265  238 DLQRLLASLKPGDTVTLTVLRGGKELTVTVTL 269
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 76-388 1.87e-92

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: 284.37  E-value: 1.87e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  76 AVVHIKVESE-QRMDSQQYFDPF--EFFfgGESRNFQRPQTRQVVGYGSGVIISTDGYIITNNHVVKGAKEMTVTLNDNR 152
Cdd:NF041521  13 AVVRIDAERTvVTQVPPFFNDPFfrRFF--GSDIPPPPPQERVERGTGSGFIISSDGIILTNAHVVDGADTVTVTLKDGR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 153 TFKAKLIGSDATTDIALLKVDAKGLPTIPFGDSDKLRVGEWVLAVGNPFNLTSTVTAGIVSAKGRSTQQVarGGSLQIES 232
Cdd:NF041521  91 TFEGKVLGTDPVTDVAVVKIEAKNLPTVPLGNSDQLQPGEWAIAIGNPLGLDNTVTLGIISATGRSSSQV--GVPDKRVD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 233 FIQTDAAVNSGNSGGALVNDRGELIGINTMIysqTGNYAGYSFAVPISIAAKVVADIKQYGTVQRAVLGIAGGDISDEAV 312
Cdd:NF041521 169 FIQTDAAINPGNSGGPLLNARGEVIGINTAI---RAGAQGLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVTLTPELK 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 313 KE------YDLKVRE--GALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKGATKE 384
Cdd:NF041521 246 QEinsdpnSGFTVPEdeGVLIVRVVPNSPAARAGLRAGDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQT 325


                 ....
gi 492529449 385 LTVT 388
Cdd:NF041521 326 LTVR 329
PRK10139 PRK10139
serine endoprotease DegQ;
61-484 4.53e-88

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 277.60  E-value: 4.53e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  61 AALPNLVGAAEASVHAVVHIKVESEQrMDSQQYFDPFEFFFGGESRNfqrPQTRQVVGYGSGVII-STDGYIITNNHVVK 139
Cdd:PRK10139  37 APLPSLAPMLEKVLPAVVSVRVEGTA-SQGQKIPEEFKKFFGDDLPD---QPAQPFEGLGSGVIIdAAKGYVLTNNHVIN 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 140 GAKEMTVTLNDNRTFKAKLIGSDATTDIALLKV-DAKGLPTIPFGDSDKLRVGEWVLAVGNPFNLTSTVTAGIVSAKGRS 218
Cdd:PRK10139 113 QAQKISIQLNDGREFDAKLIGSDDQSDIALLQIqNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGRS 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 219 tqqvarGGSLQ-IESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYAGYSFAVPISIAAKVVADIKQYGTVQR 297
Cdd:PRK10139 193 ------GLNLEgLENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKR 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 298 AVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTIN 377
Cdd:PRK10139 267 GLLGIKGTEMSADIAKAFNLDVQRGAFVSEVLPNSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLL 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 378 RKGATKELTVTLKNNEGSTSviTGESTGNVL-GASFKDlsaEQMRSYgvSYGVEVTSVSSGK-FKDAGIKKGFIILSINR 455
Cdd:PRK10139 347 RNGKPLEVEVTLDTSTSSSA--SAEMITPALqGATLSD---GQLKDG--TKGIKIDEVVKGSpAAQAGLQKDDVIIGVNR 419

                        410       420
                 ....*....|....*....|....*....
gi 492529449 456 QPVSSGADVSDIVreAGQSRSGRLIIVRG 484
Cdd:PRK10139 420 DRVNSIAEMRKVL--AAKPAIIALQIVRG 446
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 120-259 4.41e-34

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 125.23  E-value: 4.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  120 GSGVIISTDGYIITNNHVVKGAKE-----MTVTLNDNRTFKAKLIGSDATTDIALLKV--DAKGLPTIPFGDSDKLRVGE 192
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEaavelVSVVLADGREYPATVVARDPDLDLALLRVsgDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492529449  193 WVLAVGNPFNLT-STVTAGIVSAKGRSTQQvarggsLQIESFIQTDAAVNSGNSGGALVNDRGELIGI 259
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDG------GDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 297-387 2.27e-26

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: 102.37  E-value: 2.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 297 RAVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTI 376
Cdd:cd06779    1 RPYLGIEMENISPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDSLNLTI 80

                         90
                 ....*....|.
gi 492529449 377 NRKGATKELTV 387
Cdd:cd06779   81 LRDGKTLTVTV 91
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 321-380 3.66e-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: 42.37  E-value: 3.66e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449   321 EGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKG 380
Cdd:smart00228  26 GGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 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 ...
 64-486 0e+00

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: 533.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449   64 PNLVGAAEASVHAVVHIKVESEQRMDSQQYFDP--FEFFFGGESRNFQRPQ-TRQVVGYGSGVIISTDGYIITNNHVVKG 140
Cdd:TIGR02037   1 PSFAPLVEKVAPAVVNISVEGTVKRRNRPPALPpfFRQFFGDDMPDFPRQQrEQKVRGLGSGVIISADGYVLTNNHVVDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  141 AKEMTVTLNDNRTFKAKLIGSDATTDIALLKVDAKG-LPTIPFGDSDKLRVGEWVLAVGNPFNLTSTVTAGIVSAKGRST 219
Cdd:TIGR02037  81 ADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKnLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  220 QqvargGSLQIESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYAGYSFAVPISIAAKVVADIKQYGTVQRAV 299
Cdd:TIGR02037 161 L-----GIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGW 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  300 LGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRK 379
Cdd:TIGR02037 236 LGVTIQEVTSDLAKSLGLEKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRK 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  380 GATKELTVTLKNNEGstsvITGESTGNVLGASFKDLSAEQ---MRSYGVSYGVEVTSVSSGKF-KDAGIKKGFIILSINR 455
Cdd:TIGR02037 316 GKEKTITVTLGASPE----EQASSSNPFLGLTVANLSPEIrkeLRLKGDVKGVVVTKVVSGSPaARAGLQPGDVILSVNQ 391

                         410       420       430
                  ....*....|....*....|....*....|.
gi 492529449  456 QPVSSGADVSDIVREAGQSRSGRLIIVRGFY 486
Cdd:TIGR02037 392 QPVSSVAELRKVLARAKKGGRVALLILRGGA 422
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 118-389 1.64e-136

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: 394.90  E-value: 1.64e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 118 GYGSGVIISTDGYIITNNHVVKGAKEMTVTLNDNRTFKAKLIGSDATTDIALLKVDAKGLPTIPFGDSDKLRVGEWVLAV 197
Cdd:COG0265    1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 198 GNPFNLTSTVTAGIVSAKGRSTQQVARGGslqIESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYAGYSFAV 277
Cdd:COG0265   81 GNPFGLGQTVTAGIVSALGRSIGSSGGGT---YDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 278 PISIAAKVVADIKQYGTVQRAVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFP 357
Cdd:COG0265  158 PINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALGLPEPEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTSAR 237

                        250       260       270
                 ....*....|....*....|....*....|..
gi 492529449 358 QLQEAISRYRPGDKVKLTINRKGATKELTVTL 389
Cdd:COG0265  238 DLQRLLASLKPGDTVTLTVLRGGKELTVTVTL 269
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 76-388 1.87e-92

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: 284.37  E-value: 1.87e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  76 AVVHIKVESE-QRMDSQQYFDPF--EFFfgGESRNFQRPQTRQVVGYGSGVIISTDGYIITNNHVVKGAKEMTVTLNDNR 152
Cdd:NF041521  13 AVVRIDAERTvVTQVPPFFNDPFfrRFF--GSDIPPPPPQERVERGTGSGFIISSDGIILTNAHVVDGADTVTVTLKDGR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 153 TFKAKLIGSDATTDIALLKVDAKGLPTIPFGDSDKLRVGEWVLAVGNPFNLTSTVTAGIVSAKGRSTQQVarGGSLQIES 232
Cdd:NF041521  91 TFEGKVLGTDPVTDVAVVKIEAKNLPTVPLGNSDQLQPGEWAIAIGNPLGLDNTVTLGIISATGRSSSQV--GVPDKRVD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 233 FIQTDAAVNSGNSGGALVNDRGELIGINTMIysqTGNYAGYSFAVPISIAAKVVADIKQYGTVQRAVLGIAGGDISDEAV 312
Cdd:NF041521 169 FIQTDAAINPGNSGGPLLNARGEVIGINTAI---RAGAQGLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVTLTPELK 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 313 KE------YDLKVRE--GALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKGATKE 384
Cdd:NF041521 246 QEinsdpnSGFTVPEdeGVLIVRVVPNSPAARAGLRAGDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQT 325


                 ....
gi 492529449 385 LTVT 388
Cdd:NF041521 326 LTVR 329
PRK10139 PRK10139
serine endoprotease DegQ;
61-484 4.53e-88

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 277.60  E-value: 4.53e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  61 AALPNLVGAAEASVHAVVHIKVESEQrMDSQQYFDPFEFFFGGESRNfqrPQTRQVVGYGSGVII-STDGYIITNNHVVK 139
Cdd:PRK10139  37 APLPSLAPMLEKVLPAVVSVRVEGTA-SQGQKIPEEFKKFFGDDLPD---QPAQPFEGLGSGVIIdAAKGYVLTNNHVIN 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 140 GAKEMTVTLNDNRTFKAKLIGSDATTDIALLKV-DAKGLPTIPFGDSDKLRVGEWVLAVGNPFNLTSTVTAGIVSAKGRS 218
Cdd:PRK10139 113 QAQKISIQLNDGREFDAKLIGSDDQSDIALLQIqNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGRS 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 219 tqqvarGGSLQ-IESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYAGYSFAVPISIAAKVVADIKQYGTVQR 297
Cdd:PRK10139 193 ------GLNLEgLENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKR 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 298 AVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTIN 377
Cdd:PRK10139 267 GLLGIKGTEMSADIAKAFNLDVQRGAFVSEVLPNSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLL 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 378 RKGATKELTVTLKNNEGSTSviTGESTGNVL-GASFKDlsaEQMRSYgvSYGVEVTSVSSGK-FKDAGIKKGFIILSINR 455
Cdd:PRK10139 347 RNGKPLEVEVTLDTSTSSSA--SAEMITPALqGATLSD---GQLKDG--TKGIKIDEVVKGSpAAQAGLQKDDVIIGVNR 419

                        410       420
                 ....*....|....*....|....*....
gi 492529449 456 QPVSSGADVSDIVreAGQSRSGRLIIVRG 484
Cdd:PRK10139 420 DRVNSIAEMRKVL--AAKPAIIALQIVRG 446
PRK10942 PRK10942
serine endoprotease DegP;
54-468 2.21e-87

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 276.26  E-value: 2.21e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  54 TTTSGASAALPNLVGAAEASVHAVVHIKVESEQRMDSQQYFDPFEFFFGGES------RNFQ-------------RPQTR 114
Cdd:PRK10942  28 TSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRQFQQFFGDNSpfcqegSPFQsspfcqggqggngGGQQQ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 115 QVVGYGSGVIISTD-GYIITNNHVVKGAKEMTVTLNDNRTFKAKLIGSDATTDIALLKV-DAKGLPTIPFGDSDKLRVGE 192
Cdd:PRK10942 108 KFMALGSGVIIDADkGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLqNPKNLTAIKMADSDALRVGD 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 193 WVLAVGNPFNLTSTVTAGIVSAKGRSTQQVArggslQIESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYAG 272
Cdd:PRK10942 188 YTVAIGNPYGLGETVTSGIVSALGRSGLNVE-----NYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIG 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 273 YSFAVPISIAAKVVADIKQYGTVQRAVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQ 352
Cdd:PRK10942 263 IGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKP 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 353 IKSFPQLQEAISRYRPGDKVKLTINRKGATKELTVTLKNnegstSVITGESTGNVlgasFKDLSAEQMRSYGVSYGVEVT 432
Cdd:PRK10942 343 ISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVELQQ-----SSQNQVDSSNI----FNGIEGAELSNKGGDKGVVVD 413

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 492529449 433 SVSSGK-FKDAGIKKGFIILSINRQPVSSGADVSDIV 468
Cdd:PRK10942 414 NVKPGTpAAQIGLKKGDVIIGANQQPVKNIAELRKIL 450
PRK10898 PRK10898
serine endoprotease DegS;
120-387 1.46e-65

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 215.64  E-value: 1.46e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 120 GSGVIISTDGYIITNNHVVKGAKEMTVTLNDNRTFKAKLIGSDATTDIALLKVDAKGLPTIPFGDSDKLRVGEWVLAVGN 199
Cdd:PRK10898  80 GSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATNLPVIPINPKRVPHIGDVVLAIGN 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 200 PFNLTSTVTAGIVSAKGR-STQQVARggslqiESFIQTDAAVNSGNSGGALVNDRGELIGINTMIYSQTGNYA---GYSF 275
Cdd:PRK10898 160 PYNLGQTITQGIISATGRiGLSPTGR------QNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGEtpeGIGF 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 276 AVPISIAAKVVADIKQYGTVQRAVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKS 355
Cdd:PRK10898 234 AIPTQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAAKAGIQVNDLIISVNNKPAIS 313

                        250       260       270
                 ....*....|....*....|....*....|..
gi 492529449 356 FPQLQEAISRYRPGDKVKLTINRKGatKELTV 387
Cdd:PRK10898 314 ALETMDQVAEIRPGSVIPVVVMRDD--KQLTL 343
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 120-259 4.41e-34

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 125.23  E-value: 4.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  120 GSGVIISTDGYIITNNHVVKGAKE-----MTVTLNDNRTFKAKLIGSDATTDIALLKV--DAKGLPTIPFGDSDKLRVGE 192
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEaavelVSVVLADGREYPATVVARDPDLDLALLRVsgDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492529449  193 WVLAVGNPFNLT-STVTAGIVSAKGRSTQQvarggsLQIESFIQTDAAVNSGNSGGALVNDRGELIGI 259
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGRDG------GDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 297-387 2.27e-26

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: 102.37  E-value: 2.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 297 RAVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTI 376
Cdd:cd06779    1 RPYLGIEMENISPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDSLNLTI 80

                         90
                 ....*....|.
gi 492529449 377 NRKGATKELTV 387
Cdd:cd06779   81 LRDGKTLTVTV 91
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 297-387 6.52e-21

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: 87.15  E-value: 6.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 297 RAVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTI 376
Cdd:cd10839    1 RGWLGVQIQELTPDLAESFGLKEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADLRNRVATTKPGTKVELKI 80

                         90
                 ....*....|.
gi 492529449 377 NRKGATKELTV 387
Cdd:cd10839   81 LRDGKEKTLTV 91
PDZ2-4_Nma111p-like cd06719
second and fourth PDZ domains (PDZ2 and 4) of Saccharomyces cerevisiae pro-apoptotic serine ...
 403-480 1.11e-18

second and fourth PDZ domains (PDZ2 and 4) of Saccharomyces cerevisiae pro-apoptotic serine protease Nma111p and related domains; Second and fourth PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens 1)) domains of the HtrA-type protease Saccharomyces cerevisiae Nma11p (also known as Ynm3p), and related domains. Nma111p is a nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor Bir1p. Nma111p is composed of two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminus 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 beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. One permutation places beta-strand A at the C-terminus, another permutation places both beta-strands A and B at the C-terminus. This Nma111p-like family PDZ2 and PDZ4 domains show similarity to permuted PDZ domains.


Pssm-ID: 467617 [Multi-domain]  Cd Length: 79  Bit Score: 80.36  E-value: 1.11e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492529449 403 STGNVLGASFKDLSAEQMRSYGVSYGVEVTSVSSGKFKDA-GIKKGFIILSINRQPVSSGADVSDIVREAGQSRSGRLI 480
Cdd:cd06719    1 RFVEVAGATFHDLSYQQARSYAIPVRGVYVSEASGSFKLAgGISKGWIITSVNNQPTPNLDTFIEVMKTIPDNSRVRVR 79
PDZ_1 pfam12812
PDZ-like domain; PDZ domains are found in diverse signalling proteins in bacteria, yeasts, ...
 399-470 1.55e-18

PDZ-like domain; PDZ domains are found in diverse signalling proteins in bacteria, yeasts, plants, insects and vertebrates. this is a family of PDZ-like domains from bacteria, plants and fungi.


Pssm-ID: 372324 [Multi-domain]  Cd Length: 78  Bit Score: 80.02  E-value: 1.55e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492529449  399 ITGESTGNVLGASFKDLSAEQMRSYGVSYGVEVTSVSSGKFKDA-GIKKGFIILSINRQPVSSGADVSDIVRE 470
Cdd:pfam12812   2 ITPSRFVEVAGATFHDLSYQQARSYAIPIRGVYVSEASGSFKLSgGESKGWIITSVNNQPTPNLDTFIEVMKK 74
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 297-389 5.87e-18

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: 78.83  E-value: 5.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 297 RAVLGIAGGDISDEAVKEYDL-----KVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDK 371
Cdd:cd06781    1 RPSLGISMVDLSDVPEYEQQSlklpsNVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDT 80

                         90
                 ....*....|....*...
gi 492529449 372 VKLTINRKGATKELTVTL 389
Cdd:cd06781   81 VKVTIYRDGKEKTLNIKL 98
Trypsin pfam00089
Trypsin;
122-286 1.09e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 79.02  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  122 GVIISTDgYIITNNHVVKGAKEMTVTLNDN---------------RTFKAKLIGSDATT-DIALLKVDAK---GLPTIPF 182
Cdd:pfam00089  29 GSLISEN-WVLTAAHCVSGASDVKVVLGAHnivlreggeqkfdveKIIVHPNYNPDTLDnDIALLKLESPvtlGDTVRPI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449  183 -----GDSDKLRVGEWVLAVGNPFNLTSTVTAGIVSAKGRSTQQVARGGSLQI-ESFIQTDA---AVNSGNSGGALVNDR 253
Cdd:pfam00089 108 clpdaSSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVtDTMICAGAggkDACQGDSGGPLVCSD 187

                         170       180       190
                  ....*....|....*....|....*....|....
gi 492529449  254 GELIGINTMIYS-QTGNYagYSFAVPISIAAKVV 286
Cdd:pfam00089 188 GELIGIVSWGYGcASGNY--PGVYTPVSSYLDWI 219
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
311-397 1.51e-15

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 77.93  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 311 AVKEYDLKVREGALVADFAEVSAAisAG-MQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKGATKELTVTL 389
Cdd:COG3480  128 ALRAAGYPVTEGVYVASVLEGSPA--DGvLQPGDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVTL 205


                 ....*...
gi 492529449 390 KNNEGSTS 397
Cdd:COG3480  206 VKLPDDDG 213
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 295-389 3.66e-14

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: 68.37  E-value: 3.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 295 VQRAVLGIAGGdiSDEAVKEydLKVREGALVADFAEVSAAISAGMQK-----------GDVITAVEGKQIKSFPQLQEAI 363
Cdd:cd00990    1 VVRPGLGISFA--PDQVARQ--LGVRSGVLVLDVPPGGPAAKAGLRGtkrdefgrivlGDVIVAVDGKPVKNESDLYRAL 76

                         90       100
                 ....*....|....*....|....*.
gi 492529449 364 SRYRPGDKVKLTINRKGATKELTVTL 389
Cdd:cd00990   77 DEYKVGDVVTLKVLRGGTKVDLKVTL 102
PDZ_2 pfam13180
PDZ domain;
319-389 4.10e-14

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 67.30  E-value: 4.10e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492529449  319 VREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKGATKELTVTL 389
Cdd:pfam13180   4 LEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDGKLLTVEVKL 74
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 323-396 2.54e-13

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 71.27  E-value: 2.54e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492529449 323 ALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYrPGDKVKLTINRKGATKELTVTLKNNEGST 396
Cdd:COG0750  130 PVVGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRAS-PGKPLTLTVERDGEELTLTVTPRLVEEDG 202
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 325-395 4.85e-12

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


Pssm-ID: 467638 [Multi-domain]  Cd Length: 83  Bit Score: 61.44  E-value: 4.85e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492529449 325 VADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRyRPGDKVKLTINRKGATKELTVTLKNNEGS 395
Cdd:cd23081    3 VGEVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIVRIVRE-NPGKPLTLKIERDGKILTVTVTPELVEVE 72
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
317-400 1.19e-09

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 60.61  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 317 LKVRE---GALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFpQLQEAISRYRPGDKVKLTINRKGATKELTVTLKNNE 393
Cdd:COG3975  487 LRVSAdggGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTAD-NLDDALAAYKPGDPIELLVFRRDELRTVTVTLAAAP 565


                 ....*..
gi 492529449 394 GSTSVIT 400
Cdd:COG3975  566 ADTYKLE 572
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 332-390 9.53e-09

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: 52.49  E-value: 9.53e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492529449 332 SAAISAGMQKGDVITAVEGKQIKSFPqLQEAISRYR--PGDKVKLTINRKGATKELTVTLK 390
Cdd:cd06782   25 GPAEKAGIKPGDVIVAVDGESVRGMS-LDEVVKLLRgpKGTKVKLTIRRGGEGEPRDVTLT 84
Peptidase_M50 pfam02163
Peptidase family M50;
324-398 1.05e-08

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 56.35  E-value: 1.05e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492529449  324 LVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRyRPGDKVKLTINRKGATKELTVTLKNNEGSTSV 398
Cdd:pfam02163  96 VIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEALAK-SPGKPITLTVERGGQTLTVTITPKSSEESKFI 169
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 408-484 2.14e-08

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: 51.52  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 408 LGASFKDLSAEQMRSYGVS--YGVEVTSVSSG-KFKDAGIKKGFIILSINRQPVSSGADVSDIVREAGQSRSGRLIIVRG 484
Cdd:cd06779    4 LGIEMENISPLLAKELGLPvnRGVLVAEVIPGsPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDSLNLTILRD 83
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 321-390 2.20e-08

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: 51.94  E-value: 2.20e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 321 EGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKGatKELTVTLK 390
Cdd:cd10838   33 DGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGD--RRQTLAVK 100
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 319-388 3.31e-08

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: 51.35  E-value: 3.31e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 319 VREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRyrpGDKVKLTINRKGATKELTVT 388
Cdd:cd06785   29 VSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVKS---GSSLLVVVRRGNEDLLLTVT 95
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 332-390 1.05e-07

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


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 53.72  E-value: 1.05e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492529449 332 SAAISAGMQKGDVITAVEGKQIKSFpQLQEAISRYR--PGDKVKLTINRKGATKELTVTLK 390
Cdd:COG0793   82 SPAEKAGIKPGDIILAIDGKSVAGL-TLDDAVKLLRgkAGTKVTLTIKRPGEGEPITVTLT 141
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 118-291 1.79e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.60  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 118 GYGSGVIISTDgYIITNNHVVKG------AKEMTVTLNDN------------RTFKAKLIGSDATTDIALLKVDAK-GLP 178
Cdd:COG3591   12 GVCTGTLIGPN-LVLTAGHCVYDgagggwATNIVFVPGYNggpygtatatrfRVPPGWVASGDAGYDYALLRLDEPlGDT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 179 TIPFG--DSDKLRVGEWVLAVG----NPFNLTSTVTAGIVSAKGRstqqvarggslqiesFIQTDAAVNSGNSGGALVND 252
Cdd:COG3591   91 TGWLGlaFNDAPLAGEPVTIIGypgdRPKDLSLDCSGRVTGVQGN---------------RLSYDCDTTGGSSGSPVLDD 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 492529449 253 ---RGELIGINTMIYSQTGNYAgysfavpISIAAKVVADIKQ 291
Cdd:COG3591  156 sdgGGRVVGVHSAGGADRANTG-------VRLTSAIVAALRA 190
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 337-389 1.30e-06

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 49.21  E-value: 1.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492529449 337 AGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKGATKELTVTL 389
Cdd:COG3031  167 LGLQPGDVITSINGQDLTDPAQALELLQQLRDASEVTLTVERNGQPVTLTYNL 219
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 297-389 3.13e-06

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: 45.46  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 297 RAVLGIAGGDISDEAVKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTI 376
Cdd:cd06777    1 RGYLGITLSEIPPAMARGGGIDQLQGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLELMDLVAEIRPGTVIPVVV 80

                         90
                 ....*....|...
gi 492529449 377 NRKGATKELTVTL 389
Cdd:cd06777   81 LRDGKQLTLEVTI 93
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 342-390 3.42e-06

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: 45.18  E-value: 3.42e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 492529449 342 GDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKGATKELTVTLK 390
Cdd:cd23080   20 GDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKLK 68
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 425-484 1.66e-05

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: 43.64  E-value: 1.66e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492529449 425 VSYGVEVTSVSSGKFKD-AGIKKGFIILSINRQPVSSGADVSDIVReagQSRSGRLIIVRG 484
Cdd:cd06785   29 VSSGVYVHKVIPGSPAQrAGLKDGDVIISINGKPVKSSSDVYEAVK---SGSSLLVVVRRG 86
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 408-496 2.51e-05

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: 42.85  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 408 LGASFKDLSAEQMRSYGVS--YGVEVTSVSS-GKFKDAGIKKGFIILSINRQPVSSGADVSDIVREAGQSRSGRLIIVRg 484
Cdd:cd10839    4 LGVQIQELTPDLAESFGLKepKGALVAQVLPdSPAAKAGLKAGDVILSLNGKPITSSADLRNRVATTKPGTKVELKILR- 82

                         90
                 ....*....|..
gi 492529449 485 fypDGNIRTFEV 496
Cdd:cd10839   83 ---DGKEKTLTV 91
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 405-463 2.89e-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: 42.23  E-value: 2.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 405 GNVLGASFKDLSAEQMRSygvsyGVEVTSVSSGKFK-DAGIKKGFIILSINRQPVSSGAD 463
Cdd:cd23084    1 LALEGATVSNVTDEDGGK-----GVVVTEVDPGSPAaQSGLKKGDVIIGVNRQPVKSIAE 55
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 321-380 3.66e-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: 42.37  E-value: 3.66e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449   321 EGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKG 380
Cdd:smart00228  26 GGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 332-378 6.21e-05

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 40.59  E-value: 6.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 492529449  332 SAAISAGMQKGDVITAVEGKQIKSFPQLQEAIsRYRPGDKVKLTINR 378
Cdd:pfam17820   9 SPAERAGLRVGDVILAVNGKPVRSLEDVARLL-QGSAGESVTLTVRR 54
cpPDZ2_EcRseP-like cd23083
circularly permuted PDZ domain 2 (PDZ-C) of Escherichia coli Regulator of sigma-E protease ...
 325-405 1.85e-04

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


Pssm-ID: 467640 [Multi-domain]  Cd Length: 85  Bit Score: 40.19  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492529449 325 VADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAIsRYRPGDKVKLTINRKGATKELTVTlknnEGSTSVITGEST 404
Cdd:cd23083    3 LANVQPNSAAEKAGLQAGDRIVKVDGQPLTQWQTFVMAV-RDNPGKPLALEIERQGSPLSLTLI----PDSKELNQGKAI 77


                 .
gi 492529449 405 G 405
Cdd:cd23083   78 G 78
PDZ_2 pfam13180
PDZ domain;
425-498 2.12e-04

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 39.56  E-value: 2.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492529449  425 VSYGVEVTSV-SSGKFKDAGIKKGFIILSINRQPVSSGADVsdiVREAGQSRSGRLIIVRgFYPDGNIRTFEVEL 498
Cdd:pfam13180   4 LEGGVVVVSVkSSGPAAKAGLKAGDVILSIDGRKINDLTDL---ESALYGHKPGDTVTLQ-VYRDGKLLTVEVKL 74
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 312-376 1.16e-03

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 37.65  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492529449  312 VKEYDLKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTI 376
Cdd:pfam00595  16 LKGGSDQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTI 80
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 298-363 2.08e-03

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: 37.22  E-value: 2.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492529449 298 AVLGIAGGDISDEavkeydlKVREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAI 363
Cdd:cd23084    2 ALEGATVSNVTDE-------DGGKGVVVTEVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRKVL 60
cpPDZ1_EcRseP-like cd23082
circularly permuted PDZ domain 1 (PDZ-N) of Escherichia coli Regulator of sigma-E protease ...
 325-389 2.33e-03

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


Pssm-ID: 467639 [Multi-domain]  Cd Length: 89  Bit Score: 37.35  E-value: 2.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492529449 325 VADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISRYRPGDKVKLTINRKGATKELTVTL 389
Cdd:cd23082    3 IGEIAPNSIAAQAGIEPGDEIKAVDGIEVPDWDSVRLQLVDKLGAGSVQITVQPFGSGAEREVTL 67
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 430-475 2.78e-03

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 35.97  E-value: 2.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 492529449  430 EVTSVSSG-KFKDAGIKKGFIILSINRQPVSSGADVSDIVREAGQSR 475
Cdd:pfam17820   1 VVTAVVPGsPAERAGLRVGDVILAVNGKPVRSLEDVARLLQGSAGES 47
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 442-484 2.91e-03

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: 37.30  E-value: 2.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 492529449 442 AGIKKGFIILSINRQPVSSGADVSDIVREAGQSRSGRLIIVRG 484
Cdd:cd10838   49 AGLRRGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRG 91
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 442-498 5.39e-03

circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Escherichia coli DegS and related domains. DegS (also known as Site-1 protease DegS, S1P protease DegS, and Site-1-type intramembrane protease) participates in the activation of the sigma(E) extracytoplasmic stress response. Initially, there is an accumulation of misfolded membrane proteins (OMPs) in the periplasm which bind by their YXF motif to the DegS PDZ domain, activating DegS-catalyzed cleavage of the RseA periplasmic domain and making RseA a substrate for cleavage by another membrane protease RseP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegS family PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467620 [Multi-domain]  Cd Length: 93  Bit Score: 36.22  E-value: 5.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492529449 442 AGIKKGFIILSINRQPVSSGADVSDIVREAGQSRSGRLIIVRgfypDGNIRTFEVEL 498
Cdd:cd06777   41 AGIQVGDIILQFDNKPVISVLELMDLVAEIRPGTVIPVVVLR----DGKQLTLEVTI 93
PRK10779 PRK10779
sigma E protease regulator RseP;
332-388 6.91e-03

sigma E protease regulator RseP;


Pssm-ID: 182723 [Multi-domain]  Cd Length: 449  Bit Score: 38.89  E-value: 6.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492529449 332 SAAISAGMQKGDVITAVEGKQIKSFPQLQEAIsRYRPGDKVKLTINRKGATKELTVT 388
Cdd:PRK10779 232 SAASKAGLQAGDRIVKVDGQPLTQWQTFVTLV-RDNPGKPLALEIERQGSPLSLTLT 287
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 319-388 8.13e-03

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: 35.90  E-value: 8.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492529449 319 VREGALVADFAEVSAAISAGMQKGDVITAVEGKQIKSFPQLQEAISrYRPGDKVKLTINRKGATKE-LTVT 388
Cdd:cd23085   29 VKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQIIDALG-DKVGKPFKVVVKRANKVQVtLTVT 98
 
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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