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Conserved domains on  [gi|446416926|ref|WP_000494781|]
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MULTISPECIES: S1C family serine protease [Bacillus]

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
SCOP:  4001790

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 ...
 113-397 1.03e-110

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: 325.57  E-value: 1.03e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 113 GSGSGVIYKKNGnkaFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADVkRVATLGDSEKIRTGET 192
Cdd:COG0265    1 GLGSGVIISPDG---YILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 193 VIAIGNPLGLEGSVTKGIISSKEREIPVSTLGDQQvdwqaQVIQTDAAINPGNSGGALFNEQGEVIGINSSKIAQQ-AVE 271
Cdd:COG0265   77 VLAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYD-----DFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSgGSQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 272 GIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDVekmTDSARNQLKLPKeiSNGAVLRNISYQSPAEKGGLQQYDVVI 351
Cdd:COG0265  152 GIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPV---TPELAEALGLPE--PEGVLVARVEPGSPAAKAGLRPGDVIL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446416926 352 ALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKLAD 397
Cdd:COG0265  227 AVDGKPVTSARDLQ-RLLASLKPGDTVTLTVLRGGKELTVTVTLGE 271
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 113-397 1.03e-110

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: 325.57  E-value: 1.03e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 113 GSGSGVIYKKNGnkaFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADVkRVATLGDSEKIRTGET 192
Cdd:COG0265    1 GLGSGVIISPDG---YILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 193 VIAIGNPLGLEGSVTKGIISSKEREIPVSTLGDQQvdwqaQVIQTDAAINPGNSGGALFNEQGEVIGINSSKIAQQ-AVE 271
Cdd:COG0265   77 VLAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYD-----DFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSgGSQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 272 GIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDVekmTDSARNQLKLPKeiSNGAVLRNISYQSPAEKGGLQQYDVVI 351
Cdd:COG0265  152 GIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPV---TPELAEALGLPE--PEGVLVARVEPGSPAAKAGLRPGDVIL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446416926 352 ALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKLAD 397
Cdd:COG0265  227 AVDGKPVTSARDLQ-RLLASLKPGDTVTLTVLRGGKELTVTVTLGE 271
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 96-395 2.33e-83

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: 261.00  E-value: 2.33e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926   96 YKQNAGSFNTQNQSEE-AGSGSGVIYKKNGnkaFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGAD 174
Cdd:TIGR02037  40 FGDDMPDFPRQQREQKvRGLGSGVIISADG---YVLTNNHVVDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  175 VKRVATLGDSEKIRTGETVIAIGNPLGLEGSVTKGIISSKEReipvSTLGDQQVDwqaQVIQTDAAINPGNSGGALFNEQ 254
Cdd:TIGR02037 117 NLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGR----SGLGIGDYE---NFIQTDAAINPGNSGGPLVNLR 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  255 GEVIGINSSKIAQ-QAVEGIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDVekmTDSARNQLKLPKeiSNGAVLRNI 333
Cdd:TIGR02037 190 GEVIGINTAILSPsGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGWLGVTIQEV---TSDLAKSLGLEK--QRGALVAQV 264

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446416926  334 SYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKL 395
Cdd:TIGR02037 265 LPGSPAEKAGLKAGDVITSVNGKPISSFADLR-RAIGTLKPGKKVTLGILRKGKEKTITVTL 325
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 111-396 2.22e-78

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: 245.08  E-value: 2.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 111 EAGSGSGVIYKKNGNkafIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADVKrVATLGDSEKIRTG 190
Cdd:NF041521  54 ERGTGSGFIISSDGI---ILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNLP-TVPLGNSDQLQPG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 191 ETVIAIGNPLGLEGSVTKGIISSKEReiPVSTLG--DQQVDWqaqvIQTDAAINPGNSGGALFNEQGEVIGINSSkIAQQ 268
Cdd:NF041521 130 EWAIAIGNPLGLDNTVTLGIISATGR--SSSQVGvpDKRVDF----IQTDAAINPGNSGGPLLNARGEVIGINTA-IRAG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 269 AvEGIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDV-----EKMTDSARNQLKLPKEisNGAVLRNISYQSPAEKGG 343
Cdd:NF041521 203 A-QGLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVTLtpelkQEINSDPNSGFTVPED--EGVLIVRVVPNSPAARAG 279

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446416926 344 LQQYDVVIALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKLA 396
Cdd:NF041521 280 LRAGDVIQKINGQPVTTAEQVQ-QIVENSQVGQTLQLEVQRNGQTQTLTVRPG 331
PRK10898 PRK10898
serine endoprotease DegS;
32-393 3.96e-57

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 190.60  E-value: 3.96e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  32 SAVIGAITIGLTTPYINEIKGSAGQSSKHNEVNQATPISYKPEdvsnpqnmIESAKEVVVGVinYKQNAGSFNtQNQSEE 111
Cdd:PRK10898   8 SVAIGLIVAAILLVAMPSLRSLNPLSTPQFDSTDETPASYNQA--------VRRAAPAVVNV--YNRSLNSTS-HNQLEI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 112 AGSGSGVIYKkngNKAFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADV-------KRVATLGDs 184
Cdd:PRK10898  77 RTLGSGVIMD---QRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATNLpvipinpKRVPHIGD- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 185 ekirtgeTVIAIGNPLGLEGSVTKGIISSKEReIPVSTLGDQqvdwqaQVIQTDAAINPGNSGGALFNEQGEVIGINSSK 264
Cdd:PRK10898 153 -------VVLAIGNPYNLGQTITQGIISATGR-IGLSPTGRQ------NFLQTDASINHGNSGGALVNSLGELMGINTLS 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 265 IAQ----QAVEGIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDVEKMTDSARNQLKLPkeisnGAVLRNISYQSPAE 340
Cdd:PRK10898 219 FDKsndgETPEGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQ-----GIVVNEVSPDGPAA 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 341 KGGLQQYDVVIALDGQK-------IENVVQFRkylykkkkLGDTIKVTVYRNGEKLIKNV 393
Cdd:PRK10898 294 KAGIQVNDLIISVNNKPaisaletMDQVAEIR--------PGSVIPVVVMRDDKQLTLQV 345
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 115-260 6.91e-35

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 125.61  E-value: 6.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  115 GSGVIYKKNGnkaFIVTNNHVIDGANKVEVKLN-----NGKKVQAKVVGTDPLLDLAVLEIDGADVK-RVATLGDSEKIR 188
Cdd:pfam13365   1 GTGFVVSSDG---LVLTNAHVVDDAEEAAVELVsvvlaDGREYPATVVARDPDLDLALLRVSGDGRGlPPLPLGDSEPLV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446416926  189 TGETVIAIGNPLGLEG-SVTKGIISSKEREIPVSTLGDqqvdwqaqVIQTDAAINPGNSGGALFNEQGEVIGI 260
Cdd:pfam13365  78 GGERVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDDGR--------VIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 297-395 3.18e-22

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: 90.00  E-value: 3.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 297 RPMMGVQLLDVEKMTDSARNQLKLPKEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGD 376
Cdd:cd06781    1 RPSLGISMVDLSDVPEYEQQSLKLPSNVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLR-QILYSHKVGD 79

                         90
                 ....*....|....*....
gi 446416926 377 TIKVTVYRNGEKLIKNVKL 395
Cdd:cd06781   80 TVKVTIYRDGKEKTLNIKL 98
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 317-386 2.37e-04

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 39.67  E-value: 2.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926   317 QLKLPKEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNG 386
Cdd:smart00228  17 SLVGGKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLE-AVDLLKKAGGKVTLTVLRGG 85
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 113-397 1.03e-110

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: 325.57  E-value: 1.03e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 113 GSGSGVIYKKNGnkaFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADVkRVATLGDSEKIRTGET 192
Cdd:COG0265    1 GLGSGVIISPDG---YILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 193 VIAIGNPLGLEGSVTKGIISSKEREIPVSTLGDQQvdwqaQVIQTDAAINPGNSGGALFNEQGEVIGINSSKIAQQ-AVE 271
Cdd:COG0265   77 VLAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYD-----DFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSgGSQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 272 GIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDVekmTDSARNQLKLPKeiSNGAVLRNISYQSPAEKGGLQQYDVVI 351
Cdd:COG0265  152 GIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPV---TPELAEALGLPE--PEGVLVARVEPGSPAAKAGLRPGDVIL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446416926 352 ALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKLAD 397
Cdd:COG0265  227 AVDGKPVTSARDLQ-RLLASLKPGDTVTLTVLRGGKELTVTVTLGE 271
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 96-395 2.33e-83

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: 261.00  E-value: 2.33e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926   96 YKQNAGSFNTQNQSEE-AGSGSGVIYKKNGnkaFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGAD 174
Cdd:TIGR02037  40 FGDDMPDFPRQQREQKvRGLGSGVIISADG---YVLTNNHVVDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  175 VKRVATLGDSEKIRTGETVIAIGNPLGLEGSVTKGIISSKEReipvSTLGDQQVDwqaQVIQTDAAINPGNSGGALFNEQ 254
Cdd:TIGR02037 117 NLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGR----SGLGIGDYE---NFIQTDAAINPGNSGGPLVNLR 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  255 GEVIGINSSKIAQ-QAVEGIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDVekmTDSARNQLKLPKeiSNGAVLRNI 333
Cdd:TIGR02037 190 GEVIGINTAILSPsGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGWLGVTIQEV---TSDLAKSLGLEK--QRGALVAQV 264

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446416926  334 SYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKL 395
Cdd:TIGR02037 265 LPGSPAEKAGLKAGDVITSVNGKPISSFADLR-RAIGTLKPGKKVTLGILRKGKEKTITVTL 325
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 111-396 2.22e-78

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: 245.08  E-value: 2.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 111 EAGSGSGVIYKKNGNkafIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADVKrVATLGDSEKIRTG 190
Cdd:NF041521  54 ERGTGSGFIISSDGI---ILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNLP-TVPLGNSDQLQPG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 191 ETVIAIGNPLGLEGSVTKGIISSKEReiPVSTLG--DQQVDWqaqvIQTDAAINPGNSGGALFNEQGEVIGINSSkIAQQ 268
Cdd:NF041521 130 EWAIAIGNPLGLDNTVTLGIISATGR--SSSQVGvpDKRVDF----IQTDAAINPGNSGGPLLNARGEVIGINTA-IRAG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 269 AvEGIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDV-----EKMTDSARNQLKLPKEisNGAVLRNISYQSPAEKGG 343
Cdd:NF041521 203 A-QGLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVTLtpelkQEINSDPNSGFTVPED--EGVLIVRVVPNSPAARAG 279

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446416926 344 LQQYDVVIALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKLA 396
Cdd:NF041521 280 LRAGDVIQKINGQPVTTAEQVQ-QIVENSQVGQTLQLEVQRNGQTQTLTVRPG 331
PRK10898 PRK10898
serine endoprotease DegS;
32-393 3.96e-57

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 190.60  E-value: 3.96e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  32 SAVIGAITIGLTTPYINEIKGSAGQSSKHNEVNQATPISYKPEdvsnpqnmIESAKEVVVGVinYKQNAGSFNtQNQSEE 111
Cdd:PRK10898   8 SVAIGLIVAAILLVAMPSLRSLNPLSTPQFDSTDETPASYNQA--------VRRAAPAVVNV--YNRSLNSTS-HNQLEI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 112 AGSGSGVIYKkngNKAFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADV-------KRVATLGDs 184
Cdd:PRK10898  77 RTLGSGVIMD---QRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATNLpvipinpKRVPHIGD- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 185 ekirtgeTVIAIGNPLGLEGSVTKGIISSKEReIPVSTLGDQqvdwqaQVIQTDAAINPGNSGGALFNEQGEVIGINSSK 264
Cdd:PRK10898 153 -------VVLAIGNPYNLGQTITQGIISATGR-IGLSPTGRQ------NFLQTDASINHGNSGGALVNSLGELMGINTLS 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 265 IAQ----QAVEGIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDVEKMTDSARNQLKLPkeisnGAVLRNISYQSPAE 340
Cdd:PRK10898 219 FDKsndgETPEGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQ-----GIVVNEVSPDGPAA 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 341 KGGLQQYDVVIALDGQK-------IENVVQFRkylykkkkLGDTIKVTVYRNGEKLIKNV 393
Cdd:PRK10898 294 KAGIQVNDLIISVNNKPaisaletMDQVAEIR--------PGSVIPVVVMRDDKQLTLQV 345
PRK10942 PRK10942
serine endoprotease DegP;
115-395 8.25e-48

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 169.18  E-value: 8.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 115 GSGVIYkkNGNKAFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADVKRVATLGDSEKIRTGETVI 194
Cdd:PRK10942 113 GSGVII--DADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDALRVGDYTV 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 195 AIGNPLGLEGSVTKGIISSKEReipvSTLgdqQVDWQAQVIQTDAAINPGNSGGALFNEQGEVIGINSSKIAQQAVE-GI 273
Cdd:PRK10942 191 AIGNPYGLGETVTSGIVSALGR----SGL---NVENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNiGI 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 274 GFAIPIHIAKTILESLEKDGTVKRPMMGVqlLDVEKMTDSARnQLKLpkEISNGAVLRNISYQSPAEKGGLQQYDVVIAL 353
Cdd:PRK10942 264 GFAIPSNMVKNLTSQMVEYGQVKRGELGI--MGTELNSELAK-AMKV--DAQRGAFVSQVLPNSSAAKAGIKAGDVITSL 338

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446416926 354 DGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKL 395
Cdd:PRK10942 339 NGKPISSFAALR-AQVGTMPVGSKLTLGLLRDGKPVNVNVEL 379
PRK10139 PRK10139
serine endoprotease DegQ;
113-395 2.91e-46

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 164.73  E-value: 2.91e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 113 GSGSGVIYkkNGNKAFIVTNNHVIDGANKVEVKLNNGKKVQAKVVGTDPLLDLAVLEIDGADVKRVATLGDSEKIRTGET 192
Cdd:PRK10139  90 GLGSGVII--DAAKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDF 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 193 VIAIGNPLGLEGSVTKGIISSKEReipvSTLGDQQVDwqaQVIQTDAAINPGNSGGALFNEQGEVIGINSSKIAQQAVE- 271
Cdd:PRK10139 168 AVAVGNPFGLGQTATSGIISALGR----SGLNLEGLE---NFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSv 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 272 GIGFAIPIHIAKTILESLEKDGTVKRPMMGVQLLDvekMTDSARNQLKLpkEISNGAVLRNISYQSPAEKGGLQQYDVVI 351
Cdd:PRK10139 241 GIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTE---MSADIAKAFNL--DVQRGAFVSEVLPNSGSAKAGVKAGDIIT 315

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 446416926 352 ALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKL 395
Cdd:PRK10139 316 SLNGKPLNSFAELR-SRIATTEPGTKVKLGLLRNGKPLEVEVTL 358
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 115-260 6.91e-35

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 125.61  E-value: 6.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  115 GSGVIYKKNGnkaFIVTNNHVIDGANKVEVKLN-----NGKKVQAKVVGTDPLLDLAVLEIDGADVK-RVATLGDSEKIR 188
Cdd:pfam13365   1 GTGFVVSSDG---LVLTNAHVVDDAEEAAVELVsvvlaDGREYPATVVARDPDLDLALLRVSGDGRGlPPLPLGDSEPLV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446416926  189 TGETVIAIGNPLGLEG-SVTKGIISSKEREIPVSTLGDqqvdwqaqVIQTDAAINPGNSGGALFNEQGEVIGI 260
Cdd:pfam13365  78 GGERVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDDGR--------VIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 297-395 3.18e-22

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: 90.00  E-value: 3.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 297 RPMMGVQLLDVEKMTDSARNQLKLPKEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGD 376
Cdd:cd06781    1 RPSLGISMVDLSDVPEYEQQSLKLPSNVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLR-QILYSHKVGD 79

                         90
                 ....*....|....*....
gi 446416926 377 TIKVTVYRNGEKLIKNVKL 395
Cdd:cd06781   80 TVKVTIYRDGKEKTLNIKL 98
Trypsin pfam00089
Trypsin;
125-286 2.56e-14

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 71.70  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  125 NKAFIVTNNHVIDGANKVEVKL-------NNGKKVQAKV---------VGTDPLLDLAVLEID-----GADVK--RVATL 181
Cdd:pfam00089  33 SENWVLTAAHCVSGASDVKVVLgahnivlREGGEQKFDVekiivhpnyNPDTLDNDIALLKLEspvtlGDTVRpiCLPDA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926  182 GDSEKIRTGETVIAIGNP--LGLEGSVTKGIISSKEREIPVSTLGDqqvDWQAQVIQTDA---AINPGNSGGALFNEQGE 256
Cdd:pfam00089 113 SSDLPVGTTCTVSGWGNTktLGPSDTLQEVTVPVVSRETCRSAYGG---TVTDTMICAGAggkDACQGDSGGPLVCSDGE 189

                         170       180       190
                  ....*....|....*....|....*....|
gi 446416926  257 VIGINSSKIAQQAVEGIGFAIPIHIAKTIL 286
Cdd:pfam00089 190 LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 297-393 5.17e-09

circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do) and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for combining with other DegP monomers to form a stable oligomer structure. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegP family PDZ domain 1 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467630 [Multi-domain]  Cd Length: 91  Bit Score: 52.87  E-value: 5.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 297 RPMMGVQLLDVEKmtDSArNQLKLpkEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGD 376
Cdd:cd10839    1 RGWLGVQIQELTP--DLA-ESFGL--KEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADLR-NRVATTKPGT 74

                         90
                 ....*....|....*..
gi 446416926 377 TIKVTVYRNGEKLIKNV 393
Cdd:cd10839   75 KVELKILRDGKEKTLTV 91
PDZ_2 pfam13180
PDZ domain;
322-395 4.19e-08

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 49.96  E-value: 4.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446416926  322 KEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNGEKLIKNVKL 395
Cdd:pfam13180   2 VDLEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLE-SALYGHKPGDTVTLQVYRDGKLLTVEVKL 74
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 307-390 1.53e-07

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


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 48.83  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 307 VEKMTDSARNQLKLPKEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNG 386
Cdd:cd06779    6 IEMENISPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLR-AALDTKKPGDSLNLTILRDG 84


                 ....
gi 446416926 387 EKLI 390
Cdd:cd06779   85 KTLT 88
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 298-397 2.32e-07

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: 48.85  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 298 PMMGVQLLDVE-KMTDSARNQLKLPKEI--SNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKL 374
Cdd:cd10838    2 PYLGIQMTTLTpELAQQNNRNPNSPVRIpeVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQ-RIVEQAGV 80

                         90       100
                 ....*....|....*....|...
gi 446416926 375 GDTIKVTVYRNGEKLIKNVKLAD 397
Cdd:cd10838   81 GEELELTVLRGDRRQTLAVKPGD 103
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 129-273 5.10e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.67  E-value: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 129 IVTNNHVIDGAN--------KVEVKLNNGKKVQAKVV----------GTDPLLDLAVLEIDGADVKRVATLG--DSEKIR 188
Cdd:COG3591   24 VLTAGHCVYDGAgggwatniVFVPGYNGGPYGTATATrfrvppgwvaSGDAGYDYALLRLDEPLGDTTGWLGlaFNDAPL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 189 TGETVIAIGNPLGlegsvtKGIISSKEREIPVstlgdqqVDWQAQVIQTDAAINPGNSGGALFN---EQGEVIGINSSKI 265
Cdd:COG3591  104 AGEPVTIIGYPGD------RPKDLSLDCSGRV-------TGVQGNRLSYDCDTTGGSSGSPVLDdsdGGGRVVGVHSAGG 170


                 ....*...
gi 446416926 266 AQQAVEGI 273
Cdd:COG3591  171 ADRANTGV 178
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 328-396 1.29e-06

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 49.70  E-value: 1.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446416926 328 AVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkyLYKKKKLGDTIKVTVYRNGEKLIKNVKLA 396
Cdd:COG0750  130 PVVGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLV--DIIRASPGKPLTLTVERDGEELTLTVTPR 196
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 328-394 4.02e-06

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: 44.49  E-value: 4.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446416926 328 AVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkyLYKKKKLGDTIKVTVYRNGEKLIKNVK 394
Cdd:cd23081    1 PVVGEVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIV--RIVRENPGKPLTLKIERDGKILTVTVT 65
Peptidase_M50 pfam02163
Peptidase family M50;
329-393 8.98e-05

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 44.02  E-value: 8.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446416926  329 VLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFrkYLYKKKKLGDTIKVTVYRNGEKLIKNV 393
Cdd:pfam02163  96 VIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDL--VEALAKSPGKPITLTVERGGQTLTVTI 158
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
300-396 9.05e-05

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 44.43  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 300 MGVQLLDVEKMTDSARNQLKLpKEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKI-----ENVVQfrkylykKKKL 374
Cdd:COG3975  469 FGLKLVYEDAPSLKPSLGLRV-SADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVtadnlDDALA-------AYKP 540

                         90       100
                 ....*....|....*....|..
gi 446416926 375 GDTIKVTVYRNGEKLIKNVKLA 396
Cdd:COG3975  541 GDPIELLVFRRDELRTVTVTLA 562
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 295-395 1.04e-04

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: 41.02  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 295 VKRPMMGVQLLDvekmtDSARNQLKLPkeisNGAVLRNISYQSPAEKGGLQQY-----------DVVIALDGQKIENVVQ 363
Cdd:cd00990    1 VVRPGLGISFAP-----DQVARQLGVR----SGVLVLDVPPGGPAAKAGLRGTkrdefgrivlgDVIVAVDGKPVKNESD 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446416926 364 -FRKYLYKKKklGDTIKVTVYRNGEKLIKNVKL 395
Cdd:cd00990   72 lYRALDEYKV--GDVVTLKVLRGGTKVDLKVTL 102
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 317-386 2.37e-04

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 39.67  E-value: 2.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926   317 QLKLPKEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFRkYLYKKKKLGDTIKVTVYRNG 386
Cdd:smart00228  17 SLVGGKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLE-AVDLLKKAGGKVTLTVLRGG 85
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 297-391 4.10e-04

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: 39.37  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 297 RPMMGVQLLDVEKMTDSarnQLK-----LPkEISNGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFrkylykK 371
Cdd:cd23085    1 RPWLGMKMLELNEHIIA---QLKerdpmFP-DVKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQI------I 70

                         90       100
                 ....*....|....*....|....
gi 446416926 372 KKLGDTI----KVTVYRNGEKLIK 391
Cdd:cd23085   71 DALGDKVgkpfKVVVKRANKVQVT 94
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 326-395 7.31e-04

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: 38.53  E-value: 7.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416926 326 NGAVLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQFrKYLYKKKKLGDTIKVTVYRNGEKLIKNVKL 395
Cdd:cd06777   25 QGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLEL-MDLVAEIRPGTVIPVVVLRDGKQLTLEVTI 93
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 337-395 9.55e-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: 41.01  E-value: 9.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446416926 337 SPAEKGGLQQYDVVIALDGQKIENVVQFRKYLYKKKKLGDTIKVTVYRNGEKLIKNVKL 395
Cdd:COG0793   82 SPAEKAGIKPGDIILAIDGKSVAGLTLDDAVKLLRGKAGTKVTLTIKRPGEGEPITVTL 140
cpPDZ2_EcRseP-like cd23083
circularly permuted PDZ domain 2 (PDZ-C) of Escherichia coli Regulator of sigma-E protease ...
 329-364 1.56e-03

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: 37.49  E-value: 1.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446416926 329 VLRNISYQSPAEKGGLQQYDVVIALDGQKIENVVQF 364
Cdd:cd23083    2 VLANVQPNSAAEKAGLQAGDRIVKVDGQPLTQWQTF 37
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 337-359 8.46e-03

PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS3, and related domains. RGS3 down-regulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. It downregulates G-protein-mediated release of inositol phosphates and activation of MAP kinases. In Eph/ephrin signaling, RGS3 binds via its PDZ domain to the cytoplasmic C terminus of Eph receptor tyrosine kinase EphB. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467195 [Multi-domain]  Cd Length: 77  Bit Score: 35.06  E-value: 8.46e-03
                         10        20
                 ....*....|....*....|...
gi 446416926 337 SPAEKGGLQQYDVVIALDGQKIE 359
Cdd:cd06711   31 GPAEQAGLQQGDTVLQINGQPVE 53
 
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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