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Conserved domains on  [gi|1308502472|gb|PKL26787|]
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peptidase S1 [Spirochaetae bacterium HGW-Spirochaetae-3]

Protein Classification

S1C family serine protease( domain architecture ID 11415729)

S1C family serine protease containing a C-terminal PDZ domain, similar to the Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins

CATH:  2.40.10.10|2.30.42.10
EC:  3.4.21.-
Gene Ontology:  GO:0006508|GO:0004252|GO:0005515
MEROPS:  S1C
PubMed:  12408815|30712672|11158544|11283303|9383148

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 171-467 6.97e-113

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: 333.65  E-value: 6.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 171 GSGSGSIIDRRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKdmtLTVVPYGDSSNLKVGQKV 250
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKD---LPAAPLGDSDKLRVGDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 251 LAIGNPFGLERTLTTGIVSGLGRPVQQDSKTIIRDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYSPSGGSVGVGFAV 330
Cdd:COG0265    78 LAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 331 PVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRggttpvryyqsv 410
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALG-----LPEPEGVLVARVEPGSPAAKAGLR------------ 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1308502472 411 fnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVLSDRAE 467
Cdd:COG0265   221 ---PGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 171-467 6.97e-113

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: 333.65  E-value: 6.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 171 GSGSGSIIDRRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKdmtLTVVPYGDSSNLKVGQKV 250
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKD---LPAAPLGDSDKLRVGDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 251 LAIGNPFGLERTLTTGIVSGLGRPVQQDSKTIIRDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYSPSGGSVGVGFAV 330
Cdd:COG0265    78 LAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 331 PVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRggttpvryyqsv 410
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALG-----LPEPEGVLVARVEPGSPAAKAGLR------------ 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1308502472 411 fnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVLSDRAE 467
Cdd:COG0265   221 ---PGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 168-462 1.14e-91

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: 284.88  E-value: 1.14e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 168 KEGGSGSGSIIDRRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKDmtLTVVPYGDSSNLKVG 247
Cdd:TIGR02037  55 KVRGLGSGVIISADGYVLTNNHVVDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKN--LPVIKLGDSDKLRVG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 248 QKVLAIGNPFGLERTLTTGIVSGLGRpVQQDSKTIiRDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYSPSGGSVGVG 327
Cdd:TIGR02037 133 DWVLAIGNPFGLGQTVTSGIVSALGR-SGLGIGDY-ENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIG 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 328 FAVPVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRggttpvryy 407
Cdd:TIGR02037 211 FAIPSNMAKNVVDQLIEGGKVKRGWLGVTIQEVTSDLAKSLG-----LEKQRGALVAQVLPGSPAEKAGLK--------- 276

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308502472 408 qsvfnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVL 462
Cdd:TIGR02037 277 ------AGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKEKTITVTL 325
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 169-460 1.23e-74

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: 237.76  E-value: 1.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 169 EGGSGSGSIIDRRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKdmtLTVVPYGDSSNLKVGQ 248
Cdd:NF041521   54 ERGTGSGFIISSDGIILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKN---LPTVPLGNSDQLQPGE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 249 KVLAIGNPFGLERTLTTGIVSGLGRPVQQ----DsKTIirDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYspsGGSV 324
Cdd:NF041521  131 WAIAIGNPLGLDNTVTLGIISATGRSSSQvgvpD-KRV--DFIQTDAAINPGNSGGPLLNARGEVIGINTAIR---AGAQ 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 325 GVGFAVPVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPAL---IEYMKDKGGSLPVDKGLLVSTARKGGNADRSGVRggt 401
Cdd:NF041521  205 GLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVTLTPELkqeINSDPNSGFTVPEDEGVLIVRVVPNSPAARAGLR--- 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1308502472 402 tpvryyqsvfnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDV 460
Cdd:NF041521  282 ------------AGDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQTLTV 328
PRK10139 PRK10139
serine endoprotease DegQ;
171-462 6.99e-62

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 208.26  E-value: 6.99e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 171 GSGSGSIID-RRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKDMTLTVVpyGDSSNLKVGQK 249
Cdd:PRK10139   90 GLGSGVIIDaAKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAI--ADSDKLRVGDF 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 250 VLAIGNPFGLERTLTTGIVSGLGRPVQQDSKtiIRDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYSPSGGSVGVGFA 329
Cdd:PRK10139  168 AVAVGNPFGLGQTATSGIISALGRSGLNLEG--LENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFA 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 330 VPVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRggttpvryyqs 409
Cdd:PRK10139  246 IPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFN-----LDVQRGAFVSEVLPNSGSAKAGVK----------- 309

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1308502472 410 vfnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVL 462
Cdd:PRK10139  310 ----AGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTL 358
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 173-312 4.63e-32

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 119.45  E-value: 4.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 173 GSGSIIDRRGYVLTNDHVVKDA-----YKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPkDMTLTVVPYGDSSNLKVG 247
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAeeaavELVSVVLADGREYPATVVARDPDLDLALLRVSGD-GRGLPPLPLGDSEPLVGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308502472 248 QKVLAIGNPFGLER-TLTTGIVSGLGRPVQQDSKtiiRDMIQTDASINPGNSGGPLLNSRGEIIGV 312
Cdd:pfam13365  80 ERVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDD---GRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 374-462 3.02e-13

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: 65.68  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 374 SLPVDKGLLVSTARKGGNADRSGVRGgTTPVRYYQSVFnvgGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGT 453
Cdd:cd00990    18 QLGVRSGVLVLDVPPGGPAAKAGLRG-TKRDEFGRIVL---GDVIVAVDGKPVKNESDLYRALDEYKVGDVVTLKVLRGG 93


                  ....*....
gi 1308502472 454 KRMGIDVVL 462
Cdd:cd00990    94 TKVDLKVTL 102
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 52-342 1.17e-12

MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens.


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 69.44  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472  52 RLRRRIHVRlySRRQL------IVSVVASAAVGILVAIGIGILPVGGRGAG-------TVVDAESPAPVSSPASGSVAAV 118
Cdd:NF033740   80 ALRRRIRWR--PLRAVdsvlgaVLQVVAVLLVAWLVASPLASSGLPGLAQAvrgsrvlGTVDRVMPDPALRALPSLRALL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 119 EAT---QVLSEAGGGYTQD------ERENIEVYERLNSGVVNVTTEVVAINWFLEpvpkeggsGSGSIIDRrGYVLTNDH 189
Cdd:NF033740  158 DDSgfpQVFGPFGRTPIPEveppdpALATSPAVRRARPSVVKVRGTAPSCGRALE--------GSGFVVAP-DRVMTNAH 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 190 VVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFD----PPKDMTLTVVPYGDSsnlkvgqkvlAI------GNPFGL 259
Cdd:NF033740  229 VVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLAVPglglPPLPFADEPAETGDD----------AIvlgypeGGPFTA 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 260 E--RTLTTGIVSGlgrPVQQDSKTIIRDMIQTDASINPGNSGGPLLNSRGEIIGVntmIYSPSGGSVGVGFAVpvnTAKR 337
Cdd:NF033740  299 TpaRVRERIALSG---PDIYGSGTVTREVYTLRGTVRPGNSGGPLLDPDGRVLGV---VFAAAVDDSDTGYAL---TADE 369


                  ....*
gi 1308502472 338 IVPDL 342
Cdd:NF033740  370 VRPDL 374
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 373-452 5.04e-03

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: 36.20  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472  373 GSLPVDKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRG 452
Cdd:smart00228  20 GGKDEGGGVVVSSVVPGSPAAKAGLRVG---------------DVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRG 84
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 171-467 6.97e-113

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: 333.65  E-value: 6.97e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 171 GSGSGSIIDRRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKdmtLTVVPYGDSSNLKVGQKV 250
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKD---LPAAPLGDSDKLRVGDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 251 LAIGNPFGLERTLTTGIVSGLGRPVQQDSKTIIRDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYSPSGGSVGVGFAV 330
Cdd:COG0265    78 LAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 331 PVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRggttpvryyqsv 410
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALG-----LPEPEGVLVARVEPGSPAAKAGLR------------ 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1308502472 411 fnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVLSDRAE 467
Cdd:COG0265   221 ---PGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 168-462 1.14e-91

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: 284.88  E-value: 1.14e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 168 KEGGSGSGSIIDRRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKDmtLTVVPYGDSSNLKVG 247
Cdd:TIGR02037  55 KVRGLGSGVIISADGYVLTNNHVVDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKN--LPVIKLGDSDKLRVG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 248 QKVLAIGNPFGLERTLTTGIVSGLGRpVQQDSKTIiRDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYSPSGGSVGVG 327
Cdd:TIGR02037 133 DWVLAIGNPFGLGQTVTSGIVSALGR-SGLGIGDY-ENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIG 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 328 FAVPVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRggttpvryy 407
Cdd:TIGR02037 211 FAIPSNMAKNVVDQLIEGGKVKRGWLGVTIQEVTSDLAKSLG-----LEKQRGALVAQVLPGSPAEKAGLK--------- 276

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308502472 408 qsvfnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVL 462
Cdd:TIGR02037 277 ------AGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKEKTITVTL 325
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 169-460 1.23e-74

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: 237.76  E-value: 1.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 169 EGGSGSGSIIDRRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKdmtLTVVPYGDSSNLKVGQ 248
Cdd:NF041521   54 ERGTGSGFIISSDGIILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKN---LPTVPLGNSDQLQPGE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 249 KVLAIGNPFGLERTLTTGIVSGLGRPVQQ----DsKTIirDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYspsGGSV 324
Cdd:NF041521  131 WAIAIGNPLGLDNTVTLGIISATGRSSSQvgvpD-KRV--DFIQTDAAINPGNSGGPLLNARGEVIGINTAIR---AGAQ 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 325 GVGFAVPVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPAL---IEYMKDKGGSLPVDKGLLVSTARKGGNADRSGVRggt 401
Cdd:NF041521  205 GLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVTLTPELkqeINSDPNSGFTVPEDEGVLIVRVVPNSPAARAGLR--- 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1308502472 402 tpvryyqsvfnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDV 460
Cdd:NF041521  282 ------------AGDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQTLTV 328
PRK10139 PRK10139
serine endoprotease DegQ;
171-462 6.99e-62

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 208.26  E-value: 6.99e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 171 GSGSGSIID-RRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKDMTLTVVpyGDSSNLKVGQK 249
Cdd:PRK10139   90 GLGSGVIIDaAKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAI--ADSDKLRVGDF 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 250 VLAIGNPFGLERTLTTGIVSGLGRPVQQDSKtiIRDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYSPSGGSVGVGFA 329
Cdd:PRK10139  168 AVAVGNPFGLGQTATSGIISALGRSGLNLEG--LENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFA 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 330 VPVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRggttpvryyqs 409
Cdd:PRK10139  246 IPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFN-----LDVQRGAFVSEVLPNSGSAKAGVK----------- 309

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1308502472 410 vfnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVL 462
Cdd:PRK10139  310 ----AGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTL 358
PRK10942 PRK10942
serine endoprotease DegP;
173-462 3.01e-61

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 206.93  E-value: 3.01e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 173 GSGSIID-RRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKDmtLTVVPYGDSSNLKVGQKVL 251
Cdd:PRK10942  113 GSGVIIDaDKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKN--LTAIKMADSDALRVGDYTV 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 252 AIGNPFGLERTLTTGIVSGLGRpvqqdSKTIIR---DMIQTDASINPGNSGGPLLNSRGEIIGVNTMIYSPSGGSVGVGF 328
Cdd:PRK10942  191 AIGNPYGLGETVTSGIVSALGR-----SGLNVEnyeNFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGF 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 329 AVPVNTAKRIVPDLIKFGMVKRGWIDAEYVQLFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRggttpvryyq 408
Cdd:PRK10942  266 AIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMK-----VDAQRGAFVSQVLPNSSAAKAGIK---------- 330

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1308502472 409 svfnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVL 462
Cdd:PRK10942  331 -----AGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVEL 379
PRK10898 PRK10898
serine endoprotease DegS;
173-464 2.60e-52

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 180.20  E-value: 2.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 173 GSGSIIDRRGYVLTNDHVVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPKdmtLTVVPYGDSSNLKVGQKVLA 252
Cdd:PRK10898   80 GSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATN---LPVIPINPKRVPHIGDVVLA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 253 IGNPFGLERTLTTGIVSGLGRPVQQDSKTiiRDMIQTDASINPGNSGGPLLNSRGEIIGVNTMIY--SPSGGSV-GVGFA 329
Cdd:PRK10898  157 IGNPYNLGQTITQGIISATGRIGLSPTGR--QNFLQTDASINHGNSGGALVNSLGELMGINTLSFdkSNDGETPeGIGFA 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 330 VPVNTAKRIVPDLIKFGMVKRGWIDAEYVQlfpalIEYMKDKGGSLPVDKGLLVSTARKGGNADRSGVRggttpvryyqs 409
Cdd:PRK10898  235 IPTQLATKIMDKLIRDGRVIRGYIGIGGRE-----IAPLHAQGGGIDQLQGIVVNEVSPDGPAAKAGIQ----------- 298

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308502472 410 vfnvGGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVLSD 464
Cdd:PRK10898  299 ----VNDLIISVNNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQE 349
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 173-312 4.63e-32

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 119.45  E-value: 4.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 173 GSGSIIDRRGYVLTNDHVVKDA-----YKVFVNLASGERLEGKVIGSDSENDLAVIKFDPPkDMTLTVVPYGDSSNLKVG 247
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAeeaavELVSVVLADGREYPATVVARDPDLDLALLRVSGD-GRGLPPLPLGDSEPLVGG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308502472 248 QKVLAIGNPFGLER-TLTTGIVSGLGRPVQQDSKtiiRDMIQTDASINPGNSGGPLLNSRGEIIGV 312
Cdd:pfam13365  80 ERVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDD---GRVIQTDAALSPGSSGGPVFDADGRVVGI 142
Trypsin pfam00089
Trypsin;
175-336 1.71e-21

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 92.51  E-value: 1.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 175 GSIIDRRgYVLTNDHVVKDAYKVFV---------NLASGERLEGKVI-------GSDSENDLAVIKFDPPKDMTLTVVPY 238
Cdd:pfam00089  29 GSLISEN-WVLTAAHCVSGASDVKVvlgahnivlREGGEQKFDVEKIivhpnynPDTLDNDIALLKLESPVTLGDTVRPI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 239 G---DSSNLKVGQKVLAIG----NPFGLERTLTTGIVSGLGRPV--QQDSKTIIRDMIQTDA---SINPGNSGGPLLNSR 306
Cdd:pfam00089 108 ClpdASSDLPVGTTCTVSGwgntKTLGPSDTLQEVTVPVVSRETcrSAYGGTVTDTMICAGAggkDACQGDSGGPLVCSD 187

                         170       180       190
                  ....*....|....*....|....*....|
gi 1308502472 307 GEIIGVNTMIYSPSGGSVGvGFAVPVNTAK 336
Cdd:pfam00089 188 GELIGIVSWGYGCASGNYP-GVYTPVSSYL 216
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 374-462 3.02e-13

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: 65.68  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 374 SLPVDKGLLVSTARKGGNADRSGVRGgTTPVRYYQSVFnvgGDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGT 453
Cdd:cd00990    18 QLGVRSGVLVLDVPPGGPAAKAGLRG-TKRDEFGRIVL---GDVIVAVDGKPVKNESDLYRALDEYKVGDVVTLKVLRGG 93


                  ....*....
gi 1308502472 454 KRMGIDVVL 462
Cdd:cd00990    94 TKVDLKVTL 102
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 52-342 1.17e-12

MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens.


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 69.44  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472  52 RLRRRIHVRlySRRQL------IVSVVASAAVGILVAIGIGILPVGGRGAG-------TVVDAESPAPVSSPASGSVAAV 118
Cdd:NF033740   80 ALRRRIRWR--PLRAVdsvlgaVLQVVAVLLVAWLVASPLASSGLPGLAQAvrgsrvlGTVDRVMPDPALRALPSLRALL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 119 EAT---QVLSEAGGGYTQD------ERENIEVYERLNSGVVNVTTEVVAINWFLEpvpkeggsGSGSIIDRrGYVLTNDH 189
Cdd:NF033740  158 DDSgfpQVFGPFGRTPIPEveppdpALATSPAVRRARPSVVKVRGTAPSCGRALE--------GSGFVVAP-DRVMTNAH 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 190 VVKDAYKVFVNLASGERLEGKVIGSDSENDLAVIKFD----PPKDMTLTVVPYGDSsnlkvgqkvlAI------GNPFGL 259
Cdd:NF033740  229 VVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLAVPglglPPLPFADEPAETGDD----------AIvlgypeGGPFTA 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 260 E--RTLTTGIVSGlgrPVQQDSKTIIRDMIQTDASINPGNSGGPLLNSRGEIIGVntmIYSPSGGSVGVGFAVpvnTAKR 337
Cdd:NF033740  299 TpaRVRERIALSG---PDIYGSGTVTREVYTLRGTVRPGNSGGPLLDPDGRVLGV---VFAAAVDDSDTGYAL---TADE 369


                  ....*
gi 1308502472 338 IVPDL 342
Cdd:NF033740  370 VRPDL 374
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 170-345 1.95e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.08  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 170 GGSGSGSIIDRRgYVLTNDHVVKDAYK-------VFV--------NLASGERL---EGKVIGSDSENDLAVIKFDPPKDM 231
Cdd:COG3591    11 GGVCTGTLIGPN-LVLTAGHCVYDGAGggwatniVFVpgynggpyGTATATRFrvpPGWVASGDAGYDYALLRLDEPLGD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 232 TLTVVPYGDSSNLKVGQKVLAIGNPFGLERTLTtgivsglgrpvQQDSKTIIR---DMIQTDASINPGNSGGPLLN---S 305
Cdd:COG3591    90 TTGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLS-----------LDCSGRVTGvqgNRLSYDCDTTGGSSGSPVLDdsdG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1308502472 306 RGEIIGVNTmiyspSGGSVGVGFAVPVNTAkrIVPDLIKF 345
Cdd:COG3591   159 GGRVVGVHS-----AGGADRANTGVRLTSA--IVAALRAW 191
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 350-460 4.81e-09

permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 53.45  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 350 RGWIDAEYVqlfpaLIEYMKDKGGSLPVDKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVGSL 429
Cdd:cd06779     1 RPYLGIEME-----NISPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEG---------------DVILSVNGKPVTSF 60

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308502472 430 ADLYSSLEDNKPGDTVKVEFYRGTKRMGIDV 460
Cdd:cd06779    61 NDLRAALDTKKPGDSLNLTILRDGKTLTVTV 91
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 377-462 1.11e-08

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: 52.64  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 377 VDKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRM 456
Cdd:cd06781    28 VNKGVYVAQVQSNSPAEKAGLKKG---------------DVITKLDGKKVESSSDLRQILYSHKVGDTVKVTIYRDGKEK 92


                  ....*.
gi 1308502472 457 GIDVVL 462
Cdd:cd06781    93 TLNIKL 98
PDZ_2 pfam13180
PDZ domain;
376-462 6.19e-08

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 49.58  E-value: 6.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 376 PVDKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKR 455
Cdd:pfam13180   3 DLEGGVVVVSVKSSGPAAKAGLKAG---------------DVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDGKL 67


                  ....*..
gi 1308502472 456 MGIDVVL 462
Cdd:pfam13180  68 LTVEVKL 74
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
376-462 7.40e-07

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 50.96  E-value: 7.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 376 PVDKGLLVSTARKGGNADRsgvrggttpvryyqsVFNVGgDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKR 455
Cdd:COG3480   135 PVTEGVYVASVLEGSPADG---------------VLQPG-DVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKE 198


                  ....*..
gi 1308502472 456 MGIDVVL 462
Cdd:COG3480   199 KTVTVTL 205
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 350-460 1.22e-06

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: 46.32  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 350 RGWIDAeYVQ-LFPALIEYMKdkggsLPVDKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVGS 428
Cdd:cd10839     1 RGWLGV-QIQeLTPDLAESFG-----LKEPKGALVAQVLPDSPAAKAGLKAG---------------DVILSLNGKPITS 59

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308502472 429 LADLYSSLEDNKPGDTVKVEFYRGTKRMGIDV 460
Cdd:cd10839    60 SADLRNRVATTKPGTKVELKILRDGKEKTLTV 91
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 350-454 2.48e-05

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: 43.22  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 350 RGWIDAEYVQLFPALIEYMKDKGGSLP-VDKGLLVSTARKGGNADRSGVRggttpvryyqsvfnvGGDIIVSVDGMTVGS 428
Cdd:cd23085     1 RPWLGMKMLELNEHIIAQLKERDPMFPdVKAGVLVPQVIPGSPAERAGLR---------------PGDVIVEFDGKPVDS 65

                          90       100
                  ....*....|....*....|....*.
gi 1308502472 429 LADLYSSLEDnKPGDTVKVEFYRGTK 454
Cdd:cd23085    66 TKQIIDALGD-KVGKPFKVVVKRANK 90
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 375-460 1.12e-04

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: 41.15  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 375 LPVDKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTK 454
Cdd:cd10838    29 IPEVDGVLIMQVLPNSPAARAGLRRG---------------DVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGDR 93


                  ....*.
gi 1308502472 455 RMGIDV 460
Cdd:cd10838    94 RQTLAV 99
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 361-472 4.06e-04

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


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 42.55  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 361 FPALIEYMKDKGGSLPV-----DKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVG--SLADLY 433
Cdd:COG0793    48 YEDFQESTSGEFGGLGAelgeeDGKVVVVSVIPGSPAEKAGIKPG---------------DIILAIDGKSVAglTLDDAV 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1308502472 434 SSLEdNKPGDTVKVEFYRGTKRMGIDVVL--------SDRAEYLGGK 472
Cdd:COG0793   113 KLLR-GKAGTKVTLTIKRPGEGEPITVTLtraeiklpSVEAKLLEGK 158
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 350-462 1.50e-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: 37.76  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 350 RGWIDAEYVQLFPALieymkDKGGSLPVDKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVGSL 429
Cdd:cd06777     1 RGYLGITLSEIPPAM-----ARGGGIDQLQGALVKGVSPDSPAAKAGIQVG---------------DIILQFDNKPVISV 60

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1308502472 430 ADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVL 462
Cdd:cd06777    61 LELMDLVAEIRPGTVIPVVVLRDGKQLTLEVTI 93
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 181-335 2.42e-03

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 39.21  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 181 RGYVLTNDHVVKDAYKVFVNLASGERLeGKVIGSD-SENDLAVIKFDPPKD--------MTLTVVPYGDSSNLKVGQKVL 251
Cdd:cd21112    27 TPYFLTAGHCGNGGGTVYADGALGVPI-GTVVASSfPGNDYALVRVTNPGWtpppevrtYGGGTVPITGSAEPVVGAPVC 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472 252 AIGnpfgleRT--LTTGIVSGLGRPVQQDSKTIIRdMIQTDASINPGNSGGPLLnSRGEIIGVNTMIYSPSGGSVGVGFA 329
Cdd:cd21112   106 KSG------RTtgWTCGTVTAVNVTVNYPGGTVTG-LTRTNACAEPGDSGGPVF-SGTQALGITSGGSGNCGSGGGTSYF 177


                  ....*.
gi 1308502472 330 VPVNTA 335
Cdd:cd21112   178 QPVNPV 183
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 373-452 5.04e-03

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: 36.20  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308502472  373 GSLPVDKGLLVSTARKGGNADRSGVRGGttpvryyqsvfnvggDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRG 452
Cdd:smart00228  20 GGKDEGGGVVVSSVVPGSPAAKAGLRVG---------------DVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRG 84
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 415-462 6.08e-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: 35.93  E-value: 6.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1308502472 415 GDIIVSVDGMTVGSLADLYSSLEDNKPGDTVKVEFYRGTKRMGIDVVL 462
Cdd:cd23080    20 GDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKL 67
 
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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