NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2573660348|ref|WP_308440957|]
View 

MULTISPECIES: S1C family serine protease [Roseivirga]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 108-381 6.78e-130

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: 377.57  E-value: 6.78e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 108 STGSGVLISADGYIATNYHVVEDADELEVRLDDNRRIDAELIGVDPDTDLALIKIDAKNLPHVEFGNSDQVEIGEWVLAV 187
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 188 GNPFDLNNTVTAGIVSAKARNInliqsGQVNNYGIESFIQTDAVVNRGNSGGALVNLDGELIGINTAIATNTGTFNGYSF 267
Cdd:COG0265    81 GNPFGLGQTVTAGIVSALGRSI-----GSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 268 AVPSILVKKVMDDLLEFGKVQRGLLGVQITDADGRFTNEL-----SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRT 342
Cdd:COG0265   156 AIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALglpepEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTS 235

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2573660348 343 TSELQELVARKRPGDEILVKYKRDGKLKETKLKLRKKDE 381
Cdd:COG0265   236 ARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 108-381 6.78e-130

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: 377.57  E-value: 6.78e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 108 STGSGVLISADGYIATNYHVVEDADELEVRLDDNRRIDAELIGVDPDTDLALIKIDAKNLPHVEFGNSDQVEIGEWVLAV 187
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 188 GNPFDLNNTVTAGIVSAKARNInliqsGQVNNYGIESFIQTDAVVNRGNSGGALVNLDGELIGINTAIATNTGTFNGYSF 267
Cdd:COG0265    81 GNPFGLGQTVTAGIVSALGRSI-----GSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 268 AVPSILVKKVMDDLLEFGKVQRGLLGVQITDADGRFTNEL-----SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRT 342
Cdd:COG0265   156 AIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALglpepEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTS 235

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2573660348 343 TSELQELVARKRPGDEILVKYKRDGKLKETKLKLRKKDE 381
Cdd:COG0265   236 ARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 67-467 6.38e-125

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: 370.40  E-value: 6.38e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348  67 NFIKASRKAVPAVVHITNTSISSRNSSSWS------RLFG-------RERRAR--QSTGSGVLISADGYIATNYHVVEDA 131
Cdd:TIGR02037   2 SFAPLVEKVAPAVVNISVEGTVKRRNRPPAlppffrQFFGddmpdfpRQQREQkvRGLGSGVIISADGYVLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 132 DELEVRLDDNRRIDAELIGVDPDTDLALIKIDAK-NLPHVEFGNSDQVEIGEWVLAVGNPFDLNNTVTAGIVSAKARNin 210
Cdd:TIGR02037  82 DEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKkNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRS-- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 211 liqsgQVNNYGIESFIQTDAVVNRGNSGGALVNLDGELIGINTAIATNTGTFNGYSFAVPSILVKKVMDDLLEFGKVQRG 290
Cdd:TIGR02037 160 -----GLGIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 291 LLGVQITDADGRFTNEL-----SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKR 365
Cdd:TIGR02037 235 WLGVTIQEVTSDLAKSLglekqRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 366 DGKLKETKLKLrkkdefiaGVPEEVTLSYKIE--GSTFIDINENIKTRLKIEGGVQLVEMGE----GAWKEAGIKEGFVI 439
Cdd:TIGR02037 315 KGKEKTITVTL--------GASPEEQASSSNPflGLTVANLSPEIRKELRLKGDVKGVVVTKvvsgSPAARAGLQPGDVI 386

                         410       420
                  ....*....|....*....|....*...
gi 2573660348 440 TKVGDVDIKGLSDFQELLDAKTRDFYVM 467
Cdd:TIGR02037 387 LSVNQQPVSSVAELRKVLARAKKGGRVA 414
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 67-368 2.75e-85

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: 265.49  E-value: 2.75e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348  67 NFI-KASRKAVPAVVHItNTSISSRNSSSWS-------RLFGRE-------RRARQSTGSGVLISADGYIATNYHVVEDA 131
Cdd:NF041521    1 NFVaAAVEKVGPAVVRI-DAERTVVTQVPPFfndpffrRFFGSDipppppqERVERGTGSGFIISSDGIILTNAHVVDGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 132 DELEVRLDDNRRIDAELIGVDPDTDLALIKIDAKNLPHVEFGNSDQVEIGEWVLAVGNPFDLNNTVTAGIVSAKARNinl 211
Cdd:NF041521   80 DTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNLPTVPLGNSDQLQPGEWAIAIGNPLGLDNTVTLGIISATGRS--- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 212 iqSGQVnnyGIE----SFIQTDAVVNRGNSGGALVNLDGELIGINTAIATNTgtfNGYSFAVPSILVKKVMDDLLEFGKV 287
Cdd:NF041521  157 --SSQV---GVPdkrvDFIQTDAAINPGNSGGPLLNARGEVIGINTAIRAGA---QGLGFAIPINTAQRIADQLIAGGKV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 288 QRGLLGVQI------------TDADGRFT-NELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKR 354
Cdd:NF041521  229 EHPYLGIQMvtltpelkqeinSDPNSGFTvPEDEGVLIVRVVPNSPAARAGLRAGDVIQKINGQPVTTAEQVQQIVENSQ 308

                         330
                  ....*....|....
gi 2573660348 355 PGDEILVKYKRDGK 368
Cdd:NF041521  309 VGQTLQLEVQRNGQ 322
PRK10942 PRK10942
serine endoprotease DegP;
100-460 5.43e-76

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 246.22  E-value: 5.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 100 GRERRARQSTGSGVLISAD-GYIATNYHVVEDADELEVRLDDNRRIDAELIGVDPDTDLALIKI-DAKNLPHVEFGNSDQ 177
Cdd:PRK10942  103 GGQQQKFMALGSGVIIDADkGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLqNPKNLTAIKMADSDA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 178 VEIGEWVLAVGNPFDLNNTVTAGIVSAKARninliqSG-QVNNYgiESFIQTDAVVNRGNSGGALVNLDGELIGINTAIA 256
Cdd:PRK10942  183 LRVGDYTVAIGNPYGLGETVTSGIVSALGR------SGlNVENY--ENFIQTDAAINRGNSGGALVNLNGELIGINTAIL 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 257 TNTGTFNGYSFAVPSILVKKVMDDLLEFGKVQRGLLGVQITD-----ADGRFTNELSGVLISGVSPGGAAERAGIKIDDV 331
Cdd:PRK10942  255 APDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTElnselAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDV 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 332 IVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGKLKETKLKLRKKDEfiAGVpEEVTLSYKIEGSTFIDINEniktr 411
Cdd:PRK10942  335 ITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVELQQSSQ--NQV-DSSNIFNGIEGAELSNKGG----- 406

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2573660348 412 lkiEGGVQL--VEMGEGAWKeAGIKEGFVITKVGDVDIKGLSDFQELLDAK 460
Cdd:PRK10942  407 ---DKGVVVdnVKPGTPAAQ-IGLKKGDVIIGANQQPVKNIAELRKILDSK 453
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 110-251 2.31e-35

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 128.31  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 110 GSGVLISADGYIATNYHVVEDADELEV-----RLDDNRRIDAELIGVDPDTDLALIKI--DAKNLPHVEFGNSDQVEIGE 182
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVelvsvVLADGREYPATVVARDPDLDLALLRVsgDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 183 WVLAVGNPFDLN-NTVTAGIVSAKARNInliqsgqvNNYGIESFIQTDAVVNRGNSGGALVNLDGELIGI 251
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGR--------DGGDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 289-374 9.31e-17

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: 75.21  E-value: 9.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 289 RGLLGVQITD-----ADGRFTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKY 363
Cdd:cd10839     1 RGWLGVQIQEltpdlAESFGLKEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADLRNRVATTKPGTKVELKI 80

                          90
                  ....*....|.
gi 2573660348 364 KRDGKLKETKL 374
Cdd:cd10839    81 LRDGKEKTLTV 91
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 290-367 3.61e-10

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: 56.23  E-value: 3.61e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2573660348  290 GLLGVQITDADgrftNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDG 367
Cdd:smart00228  12 GGLGFSLVGGK----DEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 108-381 6.78e-130

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: 377.57  E-value: 6.78e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 108 STGSGVLISADGYIATNYHVVEDADELEVRLDDNRRIDAELIGVDPDTDLALIKIDAKNLPHVEFGNSDQVEIGEWVLAV 187
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 188 GNPFDLNNTVTAGIVSAKARNInliqsGQVNNYGIESFIQTDAVVNRGNSGGALVNLDGELIGINTAIATNTGTFNGYSF 267
Cdd:COG0265    81 GNPFGLGQTVTAGIVSALGRSI-----GSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 268 AVPSILVKKVMDDLLEFGKVQRGLLGVQITDADGRFTNEL-----SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRT 342
Cdd:COG0265   156 AIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALglpepEGVLVARVEPGSPAAKAGLRPGDVILAVDGKPVTS 235

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2573660348 343 TSELQELVARKRPGDEILVKYKRDGKLKETKLKLRKKDE 381
Cdd:COG0265   236 ARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 67-467 6.38e-125

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: 370.40  E-value: 6.38e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348  67 NFIKASRKAVPAVVHITNTSISSRNSSSWS------RLFG-------RERRAR--QSTGSGVLISADGYIATNYHVVEDA 131
Cdd:TIGR02037   2 SFAPLVEKVAPAVVNISVEGTVKRRNRPPAlppffrQFFGddmpdfpRQQREQkvRGLGSGVIISADGYVLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 132 DELEVRLDDNRRIDAELIGVDPDTDLALIKIDAK-NLPHVEFGNSDQVEIGEWVLAVGNPFDLNNTVTAGIVSAKARNin 210
Cdd:TIGR02037  82 DEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKkNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRS-- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 211 liqsgQVNNYGIESFIQTDAVVNRGNSGGALVNLDGELIGINTAIATNTGTFNGYSFAVPSILVKKVMDDLLEFGKVQRG 290
Cdd:TIGR02037 160 -----GLGIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 291 LLGVQITDADGRFTNEL-----SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKR 365
Cdd:TIGR02037 235 WLGVTIQEVTSDLAKSLglekqRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 366 DGKLKETKLKLrkkdefiaGVPEEVTLSYKIE--GSTFIDINENIKTRLKIEGGVQLVEMGE----GAWKEAGIKEGFVI 439
Cdd:TIGR02037 315 KGKEKTITVTL--------GASPEEQASSSNPflGLTVANLSPEIRKELRLKGDVKGVVVTKvvsgSPAARAGLQPGDVI 386

                         410       420
                  ....*....|....*....|....*...
gi 2573660348 440 TKVGDVDIKGLSDFQELLDAKTRDFYVM 467
Cdd:TIGR02037 387 LSVNQQPVSSVAELRKVLARAKKGGRVA 414
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 67-368 2.75e-85

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: 265.49  E-value: 2.75e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348  67 NFI-KASRKAVPAVVHItNTSISSRNSSSWS-------RLFGRE-------RRARQSTGSGVLISADGYIATNYHVVEDA 131
Cdd:NF041521    1 NFVaAAVEKVGPAVVRI-DAERTVVTQVPPFfndpffrRFFGSDipppppqERVERGTGSGFIISSDGIILTNAHVVDGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 132 DELEVRLDDNRRIDAELIGVDPDTDLALIKIDAKNLPHVEFGNSDQVEIGEWVLAVGNPFDLNNTVTAGIVSAKARNinl 211
Cdd:NF041521   80 DTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNLPTVPLGNSDQLQPGEWAIAIGNPLGLDNTVTLGIISATGRS--- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 212 iqSGQVnnyGIE----SFIQTDAVVNRGNSGGALVNLDGELIGINTAIATNTgtfNGYSFAVPSILVKKVMDDLLEFGKV 287
Cdd:NF041521  157 --SSQV---GVPdkrvDFIQTDAAINPGNSGGPLLNARGEVIGINTAIRAGA---QGLGFAIPINTAQRIADQLIAGGKV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 288 QRGLLGVQI------------TDADGRFT-NELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKR 354
Cdd:NF041521  229 EHPYLGIQMvtltpelkqeinSDPNSGFTvPEDEGVLIVRVVPNSPAARAGLRAGDVIQKINGQPVTTAEQVQQIVENSQ 308

                         330
                  ....*....|....
gi 2573660348 355 PGDEILVKYKRDGK 368
Cdd:NF041521  309 VGQTLQLEVQRNGQ 322
PRK10942 PRK10942
serine endoprotease DegP;
100-460 5.43e-76

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 246.22  E-value: 5.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 100 GRERRARQSTGSGVLISAD-GYIATNYHVVEDADELEVRLDDNRRIDAELIGVDPDTDLALIKI-DAKNLPHVEFGNSDQ 177
Cdd:PRK10942  103 GGQQQKFMALGSGVIIDADkGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLqNPKNLTAIKMADSDA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 178 VEIGEWVLAVGNPFDLNNTVTAGIVSAKARninliqSG-QVNNYgiESFIQTDAVVNRGNSGGALVNLDGELIGINTAIA 256
Cdd:PRK10942  183 LRVGDYTVAIGNPYGLGETVTSGIVSALGR------SGlNVENY--ENFIQTDAAINRGNSGGALVNLNGELIGINTAIL 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 257 TNTGTFNGYSFAVPSILVKKVMDDLLEFGKVQRGLLGVQITD-----ADGRFTNELSGVLISGVSPGGAAERAGIKIDDV 331
Cdd:PRK10942  255 APDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTElnselAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDV 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 332 IVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGKLKETKLKLRKKDEfiAGVpEEVTLSYKIEGSTFIDINEniktr 411
Cdd:PRK10942  335 ITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVELQQSSQ--NQV-DSSNIFNGIEGAELSNKGG----- 406

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2573660348 412 lkiEGGVQL--VEMGEGAWKeAGIKEGFVITKVGDVDIKGLSDFQELLDAK 460
Cdd:PRK10942  407 ---DKGVVVdnVKPGTPAAQ-IGLKKGDVIIGANQQPVKNIAELRKILDSK 453
protease_degS TIGR02038
periplasmic serine pepetdase DegS; This family consists of the periplasmic serine protease ...
 66-368 8.22e-76

periplasmic serine pepetdase DegS; This family consists of the periplasmic serine protease DegS (HhoB), a shorter paralog of protease DO (HtrA, DegP) and DegQ (HhoA). It is found in E. coli and several other Proteobacteria of the gamma subdivision. It contains a trypsin domain and a single copy of PDZ domain (in contrast to DegP with two copies). A critical role of this DegS is to sense stress in the periplasm and partially degrade an inhibitor of sigma(E). [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273939 [Multi-domain]  Cd Length: 351  Bit Score: 241.65  E-value: 8.22e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348  66 INFIKASRKAVPAVVHITNTSISSRNssswsrlfgRERRARQSTGSGVLISADGYIATNYHVVEDADELEVRLDDNRRID 145
Cdd:TIGR02038  45 ISFNKAVRRAAPAVVNIYNRSISQNS---------LNQLSIQGLGSGVIMSKEGYILTNYHVIKKADQIVVALQDGRKFE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 146 AELIGVDPDTDLALIKIDAKNLPHVEFGNSDQVEIGEWVLAVGNPFDLNNTVTAGIVSAKARNinliqsgQVNNYGIESF 225
Cdd:TIGR02038 116 AELVGSDPLTDLAVLKIEGDNLPTIPVNLDRPPHVGDVVLAIGNPYNLGQTITQGIISATGRN-------GLSSVGRQNF 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 226 IQTDAVVNRGNSGGALVNLDGELIGINTAI--ATNTGTFNGYSFAVPSILVKKVMDDLLEFGKVQRGLLGVQITD----- 298
Cdd:TIGR02038 189 IQTDAAINAGNSGGALINTNGELVGINTASfqKGGDEGGEGINFAIPIKLAHKIMGKIIRDGRVIRGYIGVSGEDinsvv 268

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 299 ADGRFTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGK 368
Cdd:TIGR02038 269 AQGLGLPDLRGIVITGVDPNGPAARAGILVRDVILKYDGKDVIGAEELMDRIAETRPGSKVMVTVLRQGK 338
PRK10898 PRK10898
serine endoprotease DegS;
66-368 7.69e-75

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 239.13  E-value: 7.69e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348  66 INFIKASRKAVPAVVHITNTSISSrnssswsrlFGRERRARQSTGSGVLISADGYIATNYHVVEDADELEVRLDDNRRID 145
Cdd:PRK10898   45 ASYNQAVRRAAPAVVNVYNRSLNS---------TSHNQLEIRTLGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 146 AELIGVDPDTDLALIKIDAKNLPHVEFGNSDQVEIGEWVLAVGNPFDLNNTVTAGIVSAKARnINLIQSGQVNnygiesF 225
Cdd:PRK10898  116 ALLVGSDSLTDLAVLKINATNLPVIPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGR-IGLSPTGRQN------F 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 226 IQTDAVVNRGNSGGALVNLDGELIGINTAI---ATNTGTFNGYSFAVPSILVKKVMDDLLEFGKVQRGLLGVQITD---- 298
Cdd:PRK10898  189 LQTDASINHGNSGGALVNSLGELMGINTLSfdkSNDGETPEGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIGGREiapl 268

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2573660348 299 -ADGRFTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGK 368
Cdd:PRK10898  269 hAQGGGIDQLQGIVVNEVSPDGPAAKAGIQVNDLIISVNNKPAISALETMDQVAEIRPGSVIPVVVMRDDK 339
PRK10139 PRK10139
serine endoprotease DegQ;
74-460 3.71e-70

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 230.22  E-value: 3.71e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348  74 KAVPAVVHIT---NTSISSRNSSSWSRLFGRERRARQST-----GSGVLI-SADGYIATNYHVVEDADELEVRLDDNRRI 144
Cdd:PRK10139   48 KVLPAVVSVRvegTASQGQKIPEEFKKFFGDDLPDQPAQpfeglGSGVIIdAAKGYVLTNNHVINQAQKISIQLNDGREF 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 145 DAELIGVDPDTDLALIKI-DAKNLPHVEFGNSDQVEIGEWVLAVGNPFDLNNTVTAGIVSAKARninliqSGqVNNYGIE 223
Cdd:PRK10139  128 DAKLIGSDDQSDIALLQIqNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGR------SG-LNLEGLE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 224 SFIQTDAVVNRGNSGGALVNLDGELIGINTAIATNTGTFNGYSFAVPSILVKKVMDDLLEFGKVQRGLLGVQITD----- 298
Cdd:PRK10139  201 NFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEmsadi 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 299 ADGRFTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGKLKETKLKLRK 378
Cdd:PRK10139  281 AKAFNLDVQRGAFVSEVLPNSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDT 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 379 KDEFIAGVPeevTLSYKIEGSTFIDINENIKTR-LKIEGgvqlVEMGEGAwKEAGIKEGFVITKVGDVDIKGLSDFQELL 457
Cdd:PRK10139  361 STSSSASAE---MITPALQGATLSDGQLKDGTKgIKIDE----VVKGSPA-AQAGLQKDDVIIGVNRDRVNSIAEMRKVL 432


                  ...
gi 2573660348 458 DAK 460
Cdd:PRK10139  433 AAK 435
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 110-251 2.31e-35

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 128.31  E-value: 2.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 110 GSGVLISADGYIATNYHVVEDADELEV-----RLDDNRRIDAELIGVDPDTDLALIKI--DAKNLPHVEFGNSDQVEIGE 182
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVelvsvVLADGREYPATVVARDPDLDLALLRVsgDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 183 WVLAVGNPFDLN-NTVTAGIVSAKARNInliqsgqvNNYGIESFIQTDAVVNRGNSGGALVNLDGELIGI 251
Cdd:pfam13365  81 RVYAVGYPLGGEkLSLSEGIVSGVDEGR--------DGGDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 289-374 9.31e-17

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: 75.21  E-value: 9.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 289 RGLLGVQITD-----ADGRFTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKY 363
Cdd:cd10839     1 RGWLGVQIQEltpdlAESFGLKEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADLRNRVATTKPGTKVELKI 80

                          90
                  ....*....|.
gi 2573660348 364 KRDGKLKETKL 374
Cdd:cd10839    81 LRDGKEKTLTV 91
Trypsin pfam00089
Trypsin;
112-278 1.66e-16

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 78.25  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 112 GVLISADgYIATNYHVVEDADELEVRLDDN---------RRIDAELI----GVDPDT---DLALIKIDAK---------- 165
Cdd:pfam00089  29 GSLISEN-WVLTAAHCVSGASDVKVVLGAHnivlreggeQKFDVEKIivhpNYNPDTldnDIALLKLESPvtlgdtvrpi 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 166 NLPHVefGNSDQVEIGEWVLAVGNPFDLN-----NTVTAGIVSAKARninliqSGQVNNYGIESFIQTDAV---VNRGNS 237
Cdd:pfam00089 108 CLPDA--SSDLPVGTTCTVSGWGNTKTLGpsdtlQEVTVPVVSRETC------RSAYGGTVTDTMICAGAGgkdACQGDS 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2573660348 238 GGALVNLDGELIGINTAIAtNTGTFNGYSFAVPSILVKKVM 278
Cdd:pfam00089 180 GGPLVCSDGELIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 292-376 2.88e-15

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: 71.13  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 292 LGVQITDADGRFTNELS----------GVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILV 361
Cdd:cd06781     4 LGISMVDLSDVPEYEQQslklpsnvnkGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDTVKV 83

                          90
                  ....*....|....*
gi 2573660348 362 KYKRDGKLKETKLKL 376
Cdd:cd06781    84 TIYRDGKEKTLNIKL 98
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
292-378 5.11e-15

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 77.55  E-value: 5.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 292 LGVQITDADGRftnelsgVLISGVSPGGAAERAGIKIDDVIVGIDDRTVrTTSELQELVARKRPGDEILVKYKRDGKLKE 371
Cdd:COG3975   485 LGLRVSADGGG-------LVVTSVLWGSPAYKAGLSAGDELLAIDGLRV-TADNLDDALAAYKPGDPIELLVFRRDELRT 556


                  ....*..
gi 2573660348 372 TKLKLRK 378
Cdd:COG3975   557 VTVTLAA 563
PDZ_2 pfam13180
PDZ domain;
303-376 5.14e-15

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 69.61  E-value: 5.14e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2573660348 303 FTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGKLKETKLKL 376
Cdd:pfam13180   1 FVDLEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDGKLLTVEVKL 74
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 289-368 1.34e-14

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: 69.24  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 289 RGLLGVQITDADGRFTNEL-----SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKY 363
Cdd:cd06779     1 RPYLGIEMENISPLLAKELglpvnRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDSLNLTI 80


                  ....*
gi 2573660348 364 KRDGK 368
Cdd:cd06779    81 LRDGK 85
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 287-376 5.21e-14

circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana DEGP1 (also known as protease Do-like 1, chloroplastic, protein DEGRADATION OF PERIPLASMIC PROTEINS 1, DEGP PROTEASE 1 and DEG1), and related domains. DEGP1 is a serine protease that is required at high temperature and may be involved in the degradation of damaged proteins. This family also includes Arabidopsis protease DEGP8/Do-like 8 (chloroplastic), a probable serine protease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This AtDEGP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467618 [Multi-domain]  Cd Length: 102  Bit Score: 67.99  E-value: 5.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 287 VQRGLLGVQIT-DADGRFTNELSGVLISGVSPGGAAERAGIK-----------IDDVIVGIDDRTVRTTSELQELVARKR 354
Cdd:cd00990     1 VVRPGLGISFApDQVARQLGVRSGVLVLDVPPGGPAAKAGLRgtkrdefgrivLGDVIVAVDGKPVKNESDLYRALDEYK 80

                          90       100
                  ....*....|....*....|..
gi 2573660348 355 PGDEILVKYKRDGKLKETKLKL 376
Cdd:cd00990    81 VGDVVTLKVLRGGTKVDLKVTL 102
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 312-381 1.14e-13

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 72.04  E-value: 1.14e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 312 ISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVaRKRPGDEILVKYKRDGKLKETKLKLRKKDE 381
Cdd:COG0750   132 VGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDII-RASPGKPLTLTVERDGEELTLTVTPRLVEE 200
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
309-378 4.01e-13

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 70.22  E-value: 4.01e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 309 GVLISGVSPGGAAERAgIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGKLKETKLKLRK 378
Cdd:COG3480   139 GVYVASVLEGSPADGV-LQPGDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVTLVK 207
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 312-387 4.01e-12

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


Pssm-ID: 467638 [Multi-domain]  Cd Length: 83  Bit Score: 61.82  E-value: 4.01e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2573660348 312 ISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVaRKRPGDEILVKYKRDGKLKETKLKLRKKDEFIAGVP 387
Cdd:cd23081     3 VGEVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIVRIV-RENPGKPLTLKIERDGKILTVTVTPELVEVEGKGVG 77
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 305-368 5.02e-12

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: 62.34  E-value: 5.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2573660348 305 NELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGK 368
Cdd:cd10838    30 PEVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGDR 93
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 289-368 6.63e-12

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: 61.64  E-value: 6.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 289 RGLLGV---QITDADGRFTNE--LSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKY 363
Cdd:cd06777     1 RGYLGItlsEIPPAMARGGGIdqLQGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLELMDLVAEIRPGTVIPVVV 80


                  ....*
gi 2573660348 364 KRDGK 368
Cdd:cd06777    81 LRDGK 85
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 281-362 2.89e-10

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 56.52  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 281 LLEFGKVQRGLLGVQITDADGrftNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEIL 360
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSD---QGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVT 77


                  ..
gi 2573660348 361 VK 362
Cdd:pfam00595  78 LT 79
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 290-367 3.61e-10

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: 56.23  E-value: 3.61e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2573660348  290 GLLGVQITDADgrftNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDG 367
Cdd:smart00228  12 GGLGFSLVGGK----DEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLRGG 85
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 275-379 3.98e-09

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: 57.96  E-value: 3.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 275 KKVMDDLLEFGKVQRGLLGVQITDADGRftnelsgVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSeLQELVARKR 354
Cdd:COG0793    45 PEEYEDFQESTSGEFGGLGAELGEEDGK-------VVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAGLT-LDDAVKLLR 116

                          90       100
                  ....*....|....*....|....*..
gi 2573660348 355 --PGDEILVKYKRDGKLKETKLKLRKK 379
Cdd:COG0793   117 gkAGTKVTLTIKRPGEGEPITVTLTRA 143
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 295-372 1.05e-08

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: 52.85  E-value: 1.05e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2573660348 295 QITDADGRFTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKrPGDEILVKYKRDGKLKET 372
Cdd:cd23085    18 QLKERDPMFPDVKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQIIDALGDK-VGKPFKVVVKRANKVQVT 94
Peptidase_M50 pfam02163
Peptidase family M50;
307-424 1.58e-08

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 55.96  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 307 LSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVaRKRPGDEILVKYKRDGKLKETKLKLRKKDEF---- 382
Cdd:pfam02163  92 PAPPVIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEAL-AKSPGKPITLTVERGGQTLTVTITPKSSEESkfig 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2573660348 383 IAGVPEEVTLSYKIEG---STFIDINENIKTRLKIEGGVQLVEMG 424
Cdd:pfam02163 171 IGPVYVKYGLLEALGFaleKTVNLVTLTLKALGKLITGVSLKNLG 215
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 308-355 1.90e-08

circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of HtrA family serine proteases including human HtrA1, HtrA2 (mitochondrial), HtrA3, and HtrA4, and related domains. These proteases are key enzymes associated with pregnancy. Their diverse biological functions include cell growth proliferation, migration and apoptosis. They are also implicated in disorders including Alzheimer's, Parkinson's, arthritis and cancer. HtrA1 (also known as high-temperature requirement A serine peptidase 1, L56, and serine protease 11) substrates include extracellular matrix proteins, proteoglycans, and insulin-like growth factor (IGF)-binding proteins. HtrA1 also inhibits signaling by members of the transforming growth factor beta (TGF-beta) family. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467624 [Multi-domain]  Cd Length: 98  Bit Score: 51.73  E-value: 1.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2573660348 308 SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRP 355
Cdd:cd06785    31 SGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSS 78
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 311-365 2.19e-08

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 50.22  E-value: 2.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2573660348 311 LISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVaRKRPGDEILVKYKR 365
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLL-QGSAGESVTLTVRR 54
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 292-376 6.24e-08

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


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 50.17  E-value: 6.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 292 LGVQITdadgrfTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSeLQELVARKR--PGDEILVKYKRDGKL 369
Cdd:cd06782     4 IGIEIG------KDDDGYLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVRGMS-LDEVVKLLRgpKGTKVKLTIRRGGEG 76


                  ....*..
gi 2573660348 370 KETKLKL 376
Cdd:cd06782    77 EPRDVTL 83
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 309-377 2.77e-06

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


Pssm-ID: 467637 [Multi-domain]  Cd Length: 83  Bit Score: 45.18  E-value: 2.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 309 GVLISGVSPGGAAerAGI-KIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGKLKETKLKLR 377
Cdd:cd23080     1 GVYVLSVVENMPA--KGIlEAGDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKLK 68
cpPDZ1_MamE-like cd23087
circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease ...
 292-374 5.54e-05

circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease MamE and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Magnetospirillum magneticum MamE (also known as magnetochrome MamE and magnetosome serine protease MamE), and related domains. MamE is a serine protease required to produce magnetite crystals in the magnetotactic bacterium M. magneticum. It is involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome, and likely cleaves at least itself, MamO and MamP. MamE-PDZ1 may bind MamB. Its autoproteolysis is stimulated by exogenous substrates or peptides that bind to its PDZ domains. Peptide binding to either the first or the second PDZ domain of MamE can activate proteolysis; activation through PDZ2 is much weaker. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This MamE-like PDZ domain 1 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467634 [Multi-domain]  Cd Length: 91  Bit Score: 41.78  E-value: 5.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 292 LGVQITDADGRftnelsGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGKLKE 371
Cdd:cd23087    15 LGQQTNLPAGR------GVFVSGVTPNTPAAAAGLRPGDVILKVDGRPVHQPEEVSAIMAEMPNGRSVRLGVLRDGDVRN 88


                  ...
gi 2573660348 372 TKL 374
Cdd:cd23087    89 MSL 91
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 308-360 7.33e-05

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. 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 rhophilin-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: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 41.03  E-value: 7.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2573660348 308 SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVR--TTSELQELVarKRPGDEIL 360
Cdd:cd06712    21 SPVQVASVDPGSCAAEAGLKEGDYIVSVGGVDCKwsKHSEVVKLL--KSAGEEGL 73
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 305-377 2.14e-04

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 42.66  E-value: 2.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2573660348 305 NELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQELVARKRPGDEILVKYKRDGKLKETKLKLR 377
Cdd:COG3031   148 GKLVGYRVNPGRPGSLFSKLGLQPGDVITSINGQDLTDPAQALELLQQLRDASEVTLTVERNGQPVTLTYNLR 220
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 290-348 2.81e-04

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


Pssm-ID: 467631 [Multi-domain]  Cd Length: 83  Bit Score: 39.53  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2573660348 290 GLLGvqITDADGRFTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSELQE 348
Cdd:cd23084     2 ALEG--ATVSNVTDEDGGKGVVVTEVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRK 58
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
 293-344 5.03e-04

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 42.42  E-value: 5.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2573660348 293 GVQI--TDADGRFTNELsgVLISGVsPGGAAERAGIKIDDVIVGIDDRTVRTTS 344
Cdd:PLN00049   88 GLEVgyPTGSDGPPAGL--VVVAPA-PGGPAARAGIRPGDVILAIDGTSTEGLS 138
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 303-359 6.85e-04

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 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: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 38.78  E-value: 6.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2573660348 303 FTNELSGVLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTSElQELV-ARKRPGDEI 359
Cdd:cd06702    27 FGVDEPGIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHATH-QEAVsALLSPGQEI 83
cpPDZ2_EcRseP-like cd23083
circularly permuted PDZ domain 2 (PDZ-C) of Escherichia coli Regulator of sigma-E protease ...
 312-386 1.72e-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: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 312 ISGVSPGGAAERAGIKIDDVIVGIDDRTVrttSELQELV--ARKRPGDEILVKYKRDGK------LKETKLKLRKKDEFI 383
Cdd:cd23083     3 LANVQPNSAAEKAGLQAGDRIVKVDGQPL---TQWQTFVmaVRDNPGKPLALEIERQGSplsltlIPDSKELNQGKAIGF 79


                  ...
gi 2573660348 384 AGV 386
Cdd:cd23083    80 AGI 82
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 294-344 1.85e-03

PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. 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 delphilin-like family PDZ2 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: 467226 [Multi-domain]  Cd Length: 75  Bit Score: 36.87  E-value: 1.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2573660348 294 VQITDADGRFTNELSG---VLISGVSPGGAAERAGIKIDDVIVGIDDRTVRTTS 344
Cdd:cd06744     2 VRVYRGNGSFGFTLRGhapVYIESVDPGSAAERAGLKPGDRILFLNGLDVRNCS 55
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 153-270 2.22e-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: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2573660348 153 PDTDLALIKIDAKNL---PHVEFGNSDQVEI--------GEWVLAVGNpfdlnnT--VTAGIVSAKARNINlIQSGQVNN 219
Cdd:cd21112    62 PGNDYALVRVTNPGWtppPEVRTYGGGTVPItgsaepvvGAPVCKSGR------TtgWTCGTVTAVNVTVN-YPGGTVTG 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2573660348 220 ygiesFIQTDAVVNRGNSGGALVNlDGELIGINTAIATNTGTFNGYSFAVP 270
Cdd:cd21112   135 -----LTRTNACAEPGDSGGPVFS-GTQALGITSGGSGNCGSGGGTSYFQP 179
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 312-337 3.30e-03

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). 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 PDLIM-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: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 36.35  E-value: 3.30e-03
                          10        20
                  ....*....|....*....|....*.
gi 2573660348 312 ISGVSPGGAAERAGIKIDDVIVGIDD 337
Cdd:cd06753    26 ISRVTPGGKAAQANLRPGDVILAING 51
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 292-341 7.88e-03

PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. 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 MUPP1-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: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 35.67  E-value: 7.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2573660348 292 LGVQITD-ADGRFTNELSGVLISGVSPGGAAERAG-IKIDDVIVGIDDRTVR 341
Cdd:cd06791    14 LGITIAGyVGEKASGELSGIFVKSIIPGSAADQDGrIQVNDQIIAVDGVNLQ 65
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 308-361 9.34e-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: 9.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2573660348 308 SGVLISGVSPGGAAERAGIKIDDVIVGIDDRTV-RTTSELQELVARKRPGDEILV 361
Cdd:cd06711    20 SPVRVQAVDPGGPAEQAGLQQGDTVLQINGQPVeRSKCVELAHAIRNCPSEIILL 74
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH