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Conserved domains on  [gi|1002271965|ref|XP_015640296|]
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protease Do-like 1, chloroplastic [Oryza sativa Japonica Group]

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 ...
 153-435 3.47e-119

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: 348.68  E-value: 3.47e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 153 GSGSGFVWDKSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRIKAptDKLRPVPVGVSADLLVGQKVF 232
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDA--KDLPAAPLGDSDKLRVGDWVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 233 AIGNPFGLDHTLTTGVISGLRREISSAAtGRPIQDVIQTDAAINPGNSGGPLLDSSGNLIGVNTAIYSPSGASSGVGFSI 312
Cdd:COG0265    79 AIGNPFGLGQTVTAGIVSALGRSIGSSG-GGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 313 PVDTVGGIVDQLIKFGKVTRPILGIKFAP--DQSVEQLGLS---GVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIIT 387
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQPvtPELAEALGLPepeGVLVARVEPGSPAAKAGLRP-----------GDVIL 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1002271965 388 SVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEPKPD 435
Cdd:COG0265   227 AVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 153-435 3.47e-119

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: 348.68  E-value: 3.47e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 153 GSGSGFVWDKSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRIKAptDKLRPVPVGVSADLLVGQKVF 232
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDA--KDLPAAPLGDSDKLRVGDWVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 233 AIGNPFGLDHTLTTGVISGLRREISSAAtGRPIQDVIQTDAAINPGNSGGPLLDSSGNLIGVNTAIYSPSGASSGVGFSI 312
Cdd:COG0265    79 AIGNPFGLGQTVTAGIVSALGRSIGSSG-GGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 313 PVDTVGGIVDQLIKFGKVTRPILGIKFAP--DQSVEQLGLS---GVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIIT 387
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQPvtPELAEALGLPepeGVLVARVEPGSPAAKAGLRP-----------GDVIL 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1002271965 388 SVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEPKPD 435
Cdd:COG0265   227 AVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 120-436 3.71e-95

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: 292.59  E-value: 3.71e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 120 VRLFQENTPSVVYITNLAVRQDAFTLDVL---------------------EVPQGSGSGFVWDKSGHIVTNFHVIRGASD 178
Cdd:TIGR02037   4 APLVEKVAPAVVNISVEGTVKRRNRPPALppffrqffgddmpdfprqqreQKVRGLGSGVIISADGYVLTNNHVVDGADE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 179 LRVTLADQTVYEAQVVGFDQDKDVAVLRIKAPtDKLRPVPVGVSADLLVGQKVFAIGNPFGLDHTLTTGVISGLRREISS 258
Cdd:TIGR02037  84 ITVTLSDGREFKAKLVGKDPRTDIAVLKIDAK-KNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSGLG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 259 AATgrpIQDVIQTDAAINPGNSGGPLLDSSGNLIGVNTAIYSPSGASSGVGFSIPVDTVGGIVDQLIKFGKVTRPILGIK 338
Cdd:TIGR02037 163 IGD---YENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGWLGVT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 339 FAPDQS--VEQLGL---SGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKV 413
Cdd:TIGR02037 240 IQEVTSdlAKSLGLekqRGALVAQVLPGSPAEKAGLKA-----------GDVITSVNGKPISSFADLRRAIGTLKPGKKV 308

                         330       340
                  ....*....|....*....|...
gi 1002271965 414 TVEVLRGDQKEKIPVILEPKPDE 436
Cdd:TIGR02037 309 TLGILRKGKEKTITVTLGASPEE 331
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 149-434 8.78e-82

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: 255.09  E-value: 8.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 149 EVPQGSGSGFVWDKSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRIKAptDKLRPVPVGVSADLLVG 228
Cdd:NF041521   52 RVERGTGSGFIISSDGIILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEA--KNLPTVPLGNSDQLQPG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 229 QKVFAIGNPFGLDHTLTTGVISGLRReiSSAATGRPIQDV--IQTDAAINPGNSGGPLLDSSGNLIGVNTAIYspSGAsS 306
Cdd:NF041521  130 EWAIAIGNPLGLDNTVTLGIISATGR--SSSQVGVPDKRVdfIQTDAAINPGNSGGPLLNARGEVIGINTAIR--AGA-Q 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 307 GVGFSIPVDTVGGIVDQLIKFGKVTRPILGIKFA---PDQ-----SVEQLGL-----SGVLVLDAPPNGPAGKAGLQStk 373
Cdd:NF041521  205 GLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVtltPELkqeinSDPNSGFtvpedEGVLIVRVVPNSPAARAGLRA-- 282

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002271965 374 rdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEPKP 434
Cdd:NF041521  283 ---------GDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQTLTVRPGALP 334
PRK10898 PRK10898
serine endoprotease DegS;
128-436 4.64e-52

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 178.66  E-value: 4.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 128 PSVVYITNLAVrqDAFTLDVLEVpQGSGSGFVWDKSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRI 207
Cdd:PRK10898   56 PAVVNVYNRSL--NSTSHNQLEI-RTLGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 208 KAptDKLRPVPVGVSADLLVGQKVFAIGNPFGLDHTLTTGVISGLRReISSAATGRpiQDVIQTDAAINPGNSGGPLLDS 287
Cdd:PRK10898  133 NA--TNLPVIPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGR-IGLSPTGR--QNFLQTDASINHGNSGGALVNS 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 288 SGNLIGVNTAIYSPS---GASSGVGFSIPVDTVGGIVDQLIKFGKVTRPILGIK-------FAPDQSVEQlgLSGVLVLD 357
Cdd:PRK10898  208 LGELMGINTLSFDKSndgETPEGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIGgreiaplHAQGGGIDQ--LQGIVVNE 285

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002271965 358 APPNGPAGKAGLQstkrdsygrliLGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEPKPDE 436
Cdd:PRK10898  286 VSPDGPAAKAGIQ-----------VNDLIISVNNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPAT 353
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 330-430 1.71e-47

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: 158.12  E-value: 1.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 330 VTRPILGIKFAPDQSVEQLGL-SGVLVLDAPPNGPAGKAGLQSTKRDSYGRLILGDIITSVNGTKVTNGSDLYRILDQCK 408
Cdd:cd00990     1 VVRPGLGISFAPDQVARQLGVrSGVLVLDVPPGGPAAKAGLRGTKRDEFGRIVLGDVIVAVDGKPVKNESDLYRALDEYK 80

                          90       100
                  ....*....|....*....|..
gi 1002271965 409 VGEKVTVEVLRGDQKEKIPVIL 430
Cdd:cd00990    81 VGDVVTLKVLRGGTKVDLKVTL 102
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 155-294 8.18e-36

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 129.08  E-value: 8.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 155 GSGFVWDKSGHIVTNFHVIRGASDLRV-----TLADQTVYEAQVVGFDQDKDVAVLRIKAPTDKLRPVPVGVSADLLVGQ 229
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVelvsvVLADGREYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002271965 230 KVFAIGNPFGLDH-TLTTGVISGLRREISSAATGRpiqdVIQTDAAINPGNSGGPLLDSSGNLIGV 294
Cdd:pfam13365  81 RVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDDGR----VIQTDAALSPGSSGGPVFDADGRVVGI 142
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 67-317 1.07e-18

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


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 87.16  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965  67 DLLPDETGRILSSATGslivALASAALI--LGDAGSASAFVVATPrklqADELATVRLFQENTPSVVYITNLAvrqdaft 144
Cdd:NF033740  140 RVMPDPALRALPSLRA----LLDDSGFPqvFGPFGRTPIPEVEPP----DPALATSPAVRRARPSVVKVRGTA------- 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 145 ldvlevPQGS----GSGFVWDkSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRikAPTDKLRPVPVG 220
Cdd:NF033740  205 ------PSCGraleGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLA--VPGLGLPPLPFA 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 221 vSADLLVGQKVFAIGNPFGLDHTLTTGVISGlRREISSA---ATGRPIQDVIQTDAAINPGNSGGPLLDSSGNLIGVnta 297
Cdd:NF033740  276 -DEPAETGDDAIVLGYPEGGPFTATPARVRE-RIALSGPdiyGSGTVTREVYTLRGTVRPGNSGGPLLDPDGRVLGV--- 350

                         250       260
                  ....*....|....*....|
gi 1002271965 298 IYSPSGASSGVGFSIPVDTV 317
Cdd:NF033740  351 VFAAAVDDSDTGYALTADEV 370
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 335-421 2.43e-08

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: 51.23  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965  335 LGIKFAPDQSVEQlglsGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKVT 414
Cdd:smart00228  14 LGFSLVGGKDEGG----GVVVSSVVPGSPAAKAGLRV-----------GDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78


                   ....*..
gi 1002271965  415 VEVLRGD 421
Cdd:smart00228  79 LTVLRGG 85
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 153-435 3.47e-119

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: 348.68  E-value: 3.47e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 153 GSGSGFVWDKSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRIKAptDKLRPVPVGVSADLLVGQKVF 232
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDA--KDLPAAPLGDSDKLRVGDWVL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 233 AIGNPFGLDHTLTTGVISGLRREISSAAtGRPIQDVIQTDAAINPGNSGGPLLDSSGNLIGVNTAIYSPSGASSGVGFSI 312
Cdd:COG0265    79 AIGNPFGLGQTVTAGIVSALGRSIGSSG-GGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 313 PVDTVGGIVDQLIKFGKVTRPILGIKFAP--DQSVEQLGLS---GVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIIT 387
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQPvtPELAEALGLPepeGVLVARVEPGSPAAKAGLRP-----------GDVIL 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1002271965 388 SVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEPKPD 435
Cdd:COG0265   227 AVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGERPE 274
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 120-436 3.71e-95

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: 292.59  E-value: 3.71e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 120 VRLFQENTPSVVYITNLAVRQDAFTLDVL---------------------EVPQGSGSGFVWDKSGHIVTNFHVIRGASD 178
Cdd:TIGR02037   4 APLVEKVAPAVVNISVEGTVKRRNRPPALppffrqffgddmpdfprqqreQKVRGLGSGVIISADGYVLTNNHVVDGADE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 179 LRVTLADQTVYEAQVVGFDQDKDVAVLRIKAPtDKLRPVPVGVSADLLVGQKVFAIGNPFGLDHTLTTGVISGLRREISS 258
Cdd:TIGR02037  84 ITVTLSDGREFKAKLVGKDPRTDIAVLKIDAK-KNLPVIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGRSGLG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 259 AATgrpIQDVIQTDAAINPGNSGGPLLDSSGNLIGVNTAIYSPSGASSGVGFSIPVDTVGGIVDQLIKFGKVTRPILGIK 338
Cdd:TIGR02037 163 IGD---YENFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGWLGVT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 339 FAPDQS--VEQLGL---SGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKV 413
Cdd:TIGR02037 240 IQEVTSdlAKSLGLekqRGALVAQVLPGSPAEKAGLKA-----------GDVITSVNGKPISSFADLRRAIGTLKPGKKV 308

                         330       340
                  ....*....|....*....|...
gi 1002271965 414 TVEVLRGDQKEKIPVILEPKPDE 436
Cdd:TIGR02037 309 TLGILRKGKEKTITVTLGASPEE 331
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 149-434 8.78e-82

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: 255.09  E-value: 8.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 149 EVPQGSGSGFVWDKSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRIKAptDKLRPVPVGVSADLLVG 228
Cdd:NF041521   52 RVERGTGSGFIISSDGIILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEA--KNLPTVPLGNSDQLQPG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 229 QKVFAIGNPFGLDHTLTTGVISGLRReiSSAATGRPIQDV--IQTDAAINPGNSGGPLLDSSGNLIGVNTAIYspSGAsS 306
Cdd:NF041521  130 EWAIAIGNPLGLDNTVTLGIISATGR--SSSQVGVPDKRVdfIQTDAAINPGNSGGPLLNARGEVIGINTAIR--AGA-Q 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 307 GVGFSIPVDTVGGIVDQLIKFGKVTRPILGIKFA---PDQ-----SVEQLGL-----SGVLVLDAPPNGPAGKAGLQStk 373
Cdd:NF041521  205 GLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVtltPELkqeinSDPNSGFtvpedEGVLIVRVVPNSPAARAGLRA-- 282

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002271965 374 rdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEPKP 434
Cdd:NF041521  283 ---------GDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQTLTVRPGALP 334
PRK10898 PRK10898
serine endoprotease DegS;
128-436 4.64e-52

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 178.66  E-value: 4.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 128 PSVVYITNLAVrqDAFTLDVLEVpQGSGSGFVWDKSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRI 207
Cdd:PRK10898   56 PAVVNVYNRSL--NSTSHNQLEI-RTLGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 208 KAptDKLRPVPVGVSADLLVGQKVFAIGNPFGLDHTLTTGVISGLRReISSAATGRpiQDVIQTDAAINPGNSGGPLLDS 287
Cdd:PRK10898  133 NA--TNLPVIPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGR-IGLSPTGR--QNFLQTDASINHGNSGGALVNS 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 288 SGNLIGVNTAIYSPS---GASSGVGFSIPVDTVGGIVDQLIKFGKVTRPILGIK-------FAPDQSVEQlgLSGVLVLD 357
Cdd:PRK10898  208 LGELMGINTLSFDKSndgETPEGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIGgreiaplHAQGGGIDQ--LQGIVVNE 285

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002271965 358 APPNGPAGKAGLQstkrdsygrliLGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEPKPDE 436
Cdd:PRK10898  286 VSPDGPAAKAGIQ-----------VNDLIISVNNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPAT 353
PRK10942 PRK10942
serine endoprotease DegP;
152-432 2.43e-49

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 174.57  E-value: 2.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 152 QGSGSGFVWDKS-GHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRIKAPTDkLRPVPVGVSADLLVGQK 230
Cdd:PRK10942  110 MALGSGVIIDADkGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKN-LTAIKMADSDALRVGDY 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 231 VFAIGNPFGLDHTLTTGVISGLRReisSAATGRPIQDVIQTDAAINPGNSGGPLLDSSGNLIGVNTAIYSPSGASSGVGF 310
Cdd:PRK10942  189 TVAIGNPYGLGETVTSGIVSALGR---SGLNVENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGF 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 311 SIPVDTVGGIVDQLIKFGKVTRPILGI-------KFAPDQSVEqlGLSGVLVLDAPPNGPAGKAGLQStkrdsygrlilG 383
Cdd:PRK10942  266 AIPSNMVKNLTSQMVEYGQVKRGELGImgtelnsELAKAMKVD--AQRGAFVSQVLPNSSAAKAGIKA-----------G 332

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1002271965 384 DIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEP 432
Cdd:PRK10942  333 DVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVELQQ 381
PRK10139 PRK10139
serine endoprotease DegQ;
152-437 1.25e-48

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 172.05  E-value: 1.25e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 152 QGSGSGFVWDKS-GHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRIKAPtDKLRPVPVGVSADLLVGQK 230
Cdd:PRK10139   89 EGLGSGVIIDAAkGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNP-SKLTQIAIADSDKLRVGDF 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 231 VFAIGNPFGLDHTLTTGVISGLRReisSAATGRPIQDVIQTDAAINPGNSGGPLLDSSGNLIGVNTAIYSPSGASSGVGF 310
Cdd:PRK10139  168 AVAVGNPFGLGQTATSGIISALGR---SGLNLEGLENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGF 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 311 SIPVDTVGGIVDQLIKFGKVTRPILGIK----FAPDQSVEQLGLS-GVLVLDAPPNGPAGKAGLQStkrdsygrlilGDI 385
Cdd:PRK10139  245 AIPSNMARTLAQQLIDFGEIKRGLLGIKgtemSADIAKAFNLDVQrGAFVSEVLPNSGSAKAGVKA-----------GDI 313

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002271965 386 ITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILEPKPDES 437
Cdd:PRK10139  314 ITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDTSTSSS 365
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 330-430 1.71e-47

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: 158.12  E-value: 1.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 330 VTRPILGIKFAPDQSVEQLGL-SGVLVLDAPPNGPAGKAGLQSTKRDSYGRLILGDIITSVNGTKVTNGSDLYRILDQCK 408
Cdd:cd00990     1 VVRPGLGISFAPDQVARQLGVrSGVLVLDVPPGGPAAKAGLRGTKRDEFGRIVLGDVIVAVDGKPVKNESDLYRALDEYK 80

                          90       100
                  ....*....|....*....|..
gi 1002271965 409 VGEKVTVEVLRGDQKEKIPVIL 430
Cdd:cd00990    81 VGDVVTLKVLRGGTKVDLKVTL 102
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 155-294 8.18e-36

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 129.08  E-value: 8.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 155 GSGFVWDKSGHIVTNFHVIRGASDLRV-----TLADQTVYEAQVVGFDQDKDVAVLRIKAPTDKLRPVPVGVSADLLVGQ 229
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVelvsvVLADGREYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002271965 230 KVFAIGNPFGLDH-TLTTGVISGLRREISSAATGRpiqdVIQTDAAINPGNSGGPLLDSSGNLIGV 294
Cdd:pfam13365  81 RVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDDGR----VIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 332-428 6.97e-19

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: 81.19  E-value: 6.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 332 RPILGIKFAPDQSVEQLGL-----SGVLVLDAPPNGPAGKAGLQstkrdsygrliLGDIITSVNGTKVTNGSDLYRILDQ 406
Cdd:cd06779     1 RPYLGIEMENISPLLAKELglpvnRGVLVAEVIPGSPAAKAGLK-----------EGDVILSVNGKPVTSFNDLRAALDT 69

                          90       100
                  ....*....|....*....|..
gi 1002271965 407 CKVGEKVTVEVLRGDQKEKIPV 428
Cdd:cd06779    70 KKPGDSLNLTILRDGKTLTVTV 91
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 67-317 1.07e-18

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


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 87.16  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965  67 DLLPDETGRILSSATGslivALASAALI--LGDAGSASAFVVATPrklqADELATVRLFQENTPSVVYITNLAvrqdaft 144
Cdd:NF033740  140 RVMPDPALRALPSLRA----LLDDSGFPqvFGPFGRTPIPEVEPP----DPALATSPAVRRARPSVVKVRGTA------- 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 145 ldvlevPQGS----GSGFVWDkSGHIVTNFHVIRGASDLRVTLADQTVYEAQVVGFDQDKDVAVLRikAPTDKLRPVPVG 220
Cdd:NF033740  205 ------PSCGraleGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLA--VPGLGLPPLPFA 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 221 vSADLLVGQKVFAIGNPFGLDHTLTTGVISGlRREISSA---ATGRPIQDVIQTDAAINPGNSGGPLLDSSGNLIGVnta 297
Cdd:NF033740  276 -DEPAETGDDAIVLGYPEGGPFTATPARVRE-RIALSGPdiyGSGTVTREVYTLRGTVRPGNSGGPLLDPDGRVLGV--- 350

                         250       260
                  ....*....|....*....|
gi 1002271965 298 IYSPSGASSGVGFSIPVDTV 317
Cdd:NF033740  351 VFAAAVDDSDTGYALTADEV 370
Trypsin pfam00089
Trypsin;
166-317 1.18e-17

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 81.33  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 166 IVTNFHVIRGASDLRVTLADQTV--YEAQVVGFD--------------QDKDVAVLRIKAP---TDKLRPVPVG-VSADL 225
Cdd:pfam00089  37 VLTAAHCVSGASDVKVVLGAHNIvlREGGEQKFDvekiivhpnynpdtLDNDIALLKLESPvtlGDTVRPICLPdASSDL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 226 LVGQKVFAIG----NPFGLDHTLTTGVISGL-RREISSAATGRPIQDVIQTDA---AINPGNSGGPLLDSSGNLIGVNTA 297
Cdd:pfam00089 117 PVGTTCTVSGwgntKTLGPSDTLQEVTVPVVsRETCRSAYGGTVTDTMICAGAggkDACQGDSGGPLVCSDGELIGIVSW 196

                         170       180
                  ....*....|....*....|
gi 1002271965 298 IYSPSGASSGvGFSIPVDTV 317
Cdd:pfam00089 197 GYGCASGNYP-GVYTPVSSY 215
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 351-432 4.56e-15

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: 70.81  E-value: 4.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 351 SGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVIL 430
Cdd:cd10838    33 DGVLIMQVLPNSPAARAGLRR-----------GDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGDRRQTLAVKP 101


                  ..
gi 1002271965 431 EP 432
Cdd:cd10838   102 GD 103
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 346-428 7.40e-15

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: 69.82  E-value: 7.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 346 EQLGLS---GVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQ 422
Cdd:cd10839    17 ESFGLKepkGALVAQVLPDSPAAKAGLKA-----------GDVILSLNGKPITSSADLRNRVATTKPGTKVELKILRDGK 85


                  ....*.
gi 1002271965 423 KEKIPV 428
Cdd:cd10839    86 EKTLTV 91
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 332-430 1.95e-14

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: 68.82  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 332 RPILGIKF---APDQSVEQLGL-------SGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLY 401
Cdd:cd06781     1 RPSLGISMvdlSDVPEYEQQSLklpsnvnKGVYVAQVQSNSPAEKAGLKK-----------GDVITKLDGKKVESSSDLR 69

                          90       100
                  ....*....|....*....|....*....
gi 1002271965 402 RILDQCKVGEKVTVEVLRGDQKEKIPVIL 430
Cdd:cd06781    70 QILYSHKVGDTVKVTIYRDGKEKTLNIKL 98
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
352-436 8.73e-12

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 65.99  E-value: 8.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 352 GVLVLDAPPNGPAgkaglqstkrdsYGRLILGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILE 431
Cdd:COG3480   139 GVYVASVLEGSPA------------DGVLQPGDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVTLV 206


                  ....*
gi 1002271965 432 PKPDE 436
Cdd:COG3480   207 KLPDD 211
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 153-327 5.63e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.53  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 153 GSGSGFVWDKSgHIVTNFHVI------RGASDLRVTLADQ------------TVYEAQVVGFDQDKDVAVLRIKAP-TDK 213
Cdd:COG3591    12 GVCTGTLIGPN-LVLTAGHCVydgaggGWATNIVFVPGYNggpygtatatrfRVPPGWVASGDAGYDYALLRLDEPlGDT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 214 LRPVPVGVSADLLVGQKVFAIGNPFGLDHTLTTGvisglrreiSSAATGRPIQDVIQTDAAINPGNSGGPLLDSSGN--- 290
Cdd:COG3591    91 TGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSLD---------CSGRVTGVQGNRLSYDCDTTGGSSGSPVLDDSDGggr 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1002271965 291 LIGVNTAiyspsGASSGVGFSIPVDTvgGIVDQLIKF 327
Cdd:COG3591   162 VVGVHSA-----GGADRANTGVRLTS--AIVAALRAW 191
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 351-432 1.02e-09

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: 55.20  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 351 SGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILdqcKVGEKVTVEVLRGDQKEKIPVIL 430
Cdd:cd06785    31 SGVYVHKVIPGSPAQRAGLKD-----------GDVIISINGKPVKSSSDVYEAV---KSGSSLLVVVRRGNEDLLLTVTP 96


                  ..
gi 1002271965 431 EP 432
Cdd:cd06785    97 EE 98
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 360-434 1.44e-09

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 59.33  E-value: 1.44e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002271965 360 PNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKvGEKVTVEVLRGDQKEKIPVILEPKP 434
Cdd:COG0750   137 PGSPAAKAGLQP-----------GDRIVAINGQPVTSWDDLVDIIRASP-GKPLTLTVERDGEELTLTVTPRLVE 199
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
331-434 2.06e-09

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 59.45  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 331 TRPILGIKFAPDQSveqlglsGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTnGSDLYRILDQCKVG 410
Cdd:COG3975   481 LKPSLGLRVSADGG-------GLVVTSVLWGSPAYKAGLSA-----------GDELLAIDGLRVT-ADNLDDALAAYKPG 541

                          90       100
                  ....*....|....*....|....
gi 1002271965 411 EKVTVEVLRGDQKEKIPVILEPKP 434
Cdd:COG3975   542 DPIELLVFRRDELRTVTVTLAAAP 565
PDZ_2 pfam13180
PDZ domain;
351-430 4.48e-09

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 52.66  E-value: 4.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 351 SGVLVLDAPPNGPAGKAGLQstkrdsygrliLGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVIL 430
Cdd:pfam13180   6 GGVVVVSVKSSGPAAKAGLK-----------AGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDGKLLTVEVKL 74
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 335-421 2.43e-08

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: 51.23  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965  335 LGIKFAPDQSVEQlglsGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKVT 414
Cdd:smart00228  14 LGFSLVGGKDEGG----GVVVSSVVPGSPAAKAGLRV-----------GDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78


                   ....*..
gi 1002271965  415 VEVLRGD 421
Cdd:smart00228  79 LTVLRGG 85
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 334-422 6.49e-08

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: 49.93  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 334 ILGIKFAPDQsvEQLGLSGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDqcKVGEKV 413
Cdd:cd23084     3 LEGATVSNVT--DEDGGKGVVVTEVDPGSPAAQSGLKK-----------GDVIIGVNRQPVKSIAELRKVLK--SKPSAV 67


                  ....*....
gi 1002271965 414 TVEVLRGDQ 422
Cdd:cd23084    68 LLQIKRGDS 76
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 352-431 4.58e-07

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: 47.48  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 352 GVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTnGSDLYRILD--QCKVGEKVTVEVLRGDQKEKIPVI 429
Cdd:cd06782    15 YLVVVSPIPGGPAEKAGIKP-----------GDVIVAVDGESVR-GMSLDEVVKllRGPKGTKVKLTIRRGGEGEPRDVT 82


                  ..
gi 1002271965 430 LE 431
Cdd:cd06782    83 LT 84
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 352-430 2.08e-06

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: 49.48  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 352 GVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGS--DLYRILDQcKVGEKVTVEVLRGDQKEKIPVI 429
Cdd:COG0793    72 KVVVVSVIPGSPAEKAGIKP-----------GDIILAIDGKSVAGLTldDAVKLLRG-KAGTKVTLTIKRPGEGEPITVT 139


                  .
gi 1002271965 430 L 430
Cdd:COG0793   140 L 140
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 360-419 2.28e-06

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 44.44  E-value: 2.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 360 PNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILdQCKVGEKVTVEVLR 419
Cdd:pfam17820   7 PGSPAERAGLRV-----------GDVILAVNGKPVRSLEDVARLL-QGSAGESVTLTVRR 54
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 360-431 5.27e-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: 5.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002271965 360 PNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKvGEKVTVEVLRGDQKEKIPVILE 431
Cdd:cd23081     8 ANSPAAEAGLKP-----------GDRILKIDGQKVRTWEDIVRIVRENP-GKPLTLKIERDGKILTVTVTPE 67
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 350-426 9.22e-06

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 46.51  E-value: 9.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002271965 350 LSGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKI 426
Cdd:COG3031   150 LVGYRVNPGRPGSLFSKLGLQP-----------GDVITSINGQDLTDPAQALELLQQLRDASEVTLTVERNGQPVTL 215
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 332-430 1.62e-05

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: 43.15  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 332 RPILGIKFAP-----DQSVEQLGLSGVLVLDAPPNGPAGKAGLQstkrdsygrliLGDIITSVNGTKVTNGSDLYRILDQ 406
Cdd:cd06777     1 RGYLGITLSEippamARGGGIDQLQGALVKGVSPDSPAAKAGIQ-----------VGDIILQFDNKPVISVLELMDLVAE 69

                          90       100
                  ....*....|....*....|....
gi 1002271965 407 CKVGEKVTVEVLRGDQKEKIPVIL 430
Cdd:cd06777    70 IRPGTVIPVVVLRDGKQLTLEVTI 93
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 352-436 1.63e-05

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: 42.87  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 352 GVLVLDAPPNGPAGkaglqstkrdsyGRLILGDIITSVNGTKVTNGSDLYRILDQCKVGEKVTVEVLRGDQKEKIPVILE 431
Cdd:cd23080     1 GVYVLSVVENMPAK------------GILEAGDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKLK 68


                  ....*
gi 1002271965 432 PKPDE 436
Cdd:cd23080    69 QFPDE 73
Peptidase_M50 pfam02163
Peptidase family M50;
350-436 2.98e-04

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 42.48  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 350 LSGVLVLDAPPNGPAGKAGLQstkrdsygrliLGDIITSVNGTKVTNGSDLYRILDQcKVGEKVTVEVLRGDQKEKIPVI 429
Cdd:pfam02163  92 PAPPVIGGVAPGSPAAKAGLK-----------PGDVILSINGKKITSWQDLVEALAK-SPGKPITLTVERGGQTLTVTIT 159


                  ....*..
gi 1002271965 430 LEPKPDE 436
Cdd:pfam02163 160 PKSSEES 166
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 201-317 6.99e-04

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: 40.37  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 201 DVAVLRIKAPTDKLRP---------VPVGVSADLLVGQKVFAIGNpfgldhtlTTGVISG--LRREISSAATGRPIQDVI 269
Cdd:cd21112    65 DYALVRVTNPGWTPPPevrtygggtVPITGSAEPVVGAPVCKSGR--------TTGWTCGtvTAVNVTVNYPGGTVTGLT 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1002271965 270 QTDAAINPGNSGGPLLdSSGNLIGVNTAIYSPSGASSGVGFSIPVDTV 317
Cdd:cd21112   137 RTNACAEPGDSGGPVF-SGTQALGITSGGSGNCGSGGGTSYFQPVNPV 183
PDZ5_INAD-like cd23066
PDZ domain 5 of inactivation no after potential D (INAD), and related domains; PDZ (PSD-95 ...
 327-419 8.64e-04

PDZ domain 5 of inactivation no after potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ45 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. 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 INAD-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: 467279 [Multi-domain]  Cd Length: 80  Bit Score: 37.87  E-value: 8.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 327 FGKVTRPiLGIKFAPDQSVeqlglsGVLVLDAPPNGPAgkaglqstkrDSYGRLILGDIITSVNGTKVTNGS--DLYRIL 404
Cdd:cd23066     5 MKKAGKE-LGLSLSPNEGI------GCTIADLLPGGYA----------EIDGKLQKGDIITKFNGDALSGLPfqVCYALF 67

                          90
                  ....*....|....*
gi 1002271965 405 DQCKvgEKVTVEVLR 419
Cdd:cd23066    68 KGAN--GKISLEVTR 80
PDZ4_PDZD2-PDZ2_hPro-IL-16-like cd06760
PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 ...
 378-419 2.43e-03

PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the second PDZ domain (PDZ2) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers 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 PDZD2-like family PDZ4 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: 467241 [Multi-domain]  Cd Length: 90  Bit Score: 36.86  E-value: 2.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002271965 378 GRLILGDIITSVNGTKVTNG--SDLYRILDQCKVGEkVTVEVLR 419
Cdd:cd06760    48 GRLRRGDQILEINGTSLRNVtlNEAYAILSQCKPGP-VTLIISR 90
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
 351-420 2.87e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 39.72  E-value: 2.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002271965 351 SGVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKvTNGSDLYRILD--QCKVGEKVTVEVLRG 420
Cdd:PLN00049  102 AGLVVVAPAPGGPAARAGIRP-----------GDVILAIDGTS-TEGLSLYEAADrlQGPEGSSVELTLRRG 161
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 352-432 3.39e-03

circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana putative protease DEGP14 and related domains. DEGP14 is a putative protease belonging to the HtrA family of housekeeping proteases. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This AtDEGP14-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467632 [Multi-domain]  Cd Length: 101  Bit Score: 37.06  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271965 352 GVLVLDAPPNGPAGKAGLQStkrdsygrlilGDIITSVNGTKVTNGSDLYRILDQcKVGEKVTVEVLRG-DQKEKIPVIL 430
Cdd:cd23085    32 GVLVPQVIPGSPAERAGLRP-----------GDVIVEFDGKPVDSTKQIIDALGD-KVGKPFKVVVKRAnKVQVTLTVTP 99


                  ..
gi 1002271965 431 EP 432
Cdd:cd23085   100 EE 101
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 360-419 5.26e-03

PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. 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 MAGI family PDZ1 domain is a canonical PDZ domain containing 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.


Pssm-ID: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 36.03  E-value: 5.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002271965 360 PNGPAgkaglqstkrDSYGRLILGDIITSVNGTKVTNGS--DLYRILDQCKVGEKVTVEVLR 419
Cdd:cd06731    34 PDGPA----------ALDGKLRTGDVLVSVNDTCVLGYThaDVVKLFQSIPIGQSVNLEVCR 85
cpPDZ1_ScNma111-like cd06786
circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine ...
 352-422 5.88e-03

circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine protease Nma111p and related domains; First PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the HtrA-type protease Saccharomyces cerevisiae Nma111p (also known as Ynm3p), and related domains. Nma111p is a nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor Bir1p. Nma111p is composed of two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-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 ScNma111-like PDZ1 domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation places both beta-strands A and B on the C-terminus.


Pssm-ID: 467625 [Multi-domain]  Cd Length: 89  Bit Score: 36.01  E-value: 5.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002271965 352 GVLVLDAP-PNGPAgkaglqstkrdsYGRLILGDIITSVNGTKVTNGSDLYRILDQcKVGEKVTVEVLRGDQ 422
Cdd:cd06786    23 GMLVAETVlPEGPA------------DGKLEEGDVLISVNGELITQFIRLEEILDE-NVGKTVELVVQRGGE 81
 
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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