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Conserved domains on  [gi|2735145462|ref|WP_346770706|]
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S1C family serine protease [Novosphingobium panipatense]

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 ...
 77-357 4.01e-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: 345.60  E-value: 4.01e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  77 GSGSGFIWDDAGHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRI-GVGLRrprPVPLGTSADLKVGQKV 155
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIdAKDLP---AAPLGDSDKLRVGDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 156 FAIGNPFGLDWTFTTGIISALNRTLPSESGPDIQQLIQTDAAINPGNSGGPLLDSSGRLIGINTAIYSPSGASAGIGFAV 235
Cdd:COG0265    78 LAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 236 PVDTVRRVIPQLARSGRYVRPSLGIEVDEqVNARLNERTG---AKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIIT 312
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQP-VTPELAEALGlpePEGVLVARVEPGSPAAKAGLR----------PGDVIL 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2735145462 313 AVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVELGA 357
Cdd:COG0265   227 AVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGE 271
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 77-357 4.01e-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: 345.60  E-value: 4.01e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  77 GSGSGFIWDDAGHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRI-GVGLRrprPVPLGTSADLKVGQKV 155
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIdAKDLP---AAPLGDSDKLRVGDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 156 FAIGNPFGLDWTFTTGIISALNRTLPSESGPDIQQLIQTDAAINPGNSGGPLLDSSGRLIGINTAIYSPSGASAGIGFAV 235
Cdd:COG0265    78 LAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 236 PVDTVRRVIPQLARSGRYVRPSLGIEVDEqVNARLNERTG---AKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIIT 312
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQP-VTPELAEALGlpePEGVLVARVEPGSPAAKAGLR----------PGDVIL 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2735145462 313 AVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVELGA 357
Cdd:COG0265   227 AVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGE 271
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 45-358 2.86e-90

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: 277.57  E-value: 2.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  45 ELFEKSRGSVVFISTSQLVQDA----------------WTRNIFSTPQ-----GSGSGFIWDDAGHVVTNFHVIQGASGA 103
Cdd:TIGR02037   5 PLVEKVAPAVVNISVEGTVKRRnrppalppffrqffgdDMPDFPRQQReqkvrGLGSGVIISADGYVLTNNHVVDGADEI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 104 TVQLADGRKYQAALVGVSPQHDLALLRIGVGLRRPrPVPLGTSADLKVGQKVFAIGNPFGLDWTFTTGIISALNRtlpse 183
Cdd:TIGR02037  85 TVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLP-VIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGR----- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 184 SGPDIQQ---LIQTDAAINPGNSGGPLLDSSGRLIGINTAIYSPSGASAGIGFAVPVDTVRRVIPQLARSGRYVRPSLGI 260
Cdd:TIGR02037 159 SGLGIGDyenFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGWLGV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 261 EVDEqVNARLNERTG---AKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGDV 337
Cdd:TIGR02037 239 TIQE-VTSDLAKSLGlekQRGALVAQVLPGSPAEKAGLK----------AGDVITSVNGKPISSFADLRRAIGTLKPGKK 307

                         330       340
                  ....*....|....*....|.
gi 2735145462 338 VTLTVMKQEQERQVRVELGAD 358
Cdd:TIGR02037 308 VTLGILRKGKEKTITVTLGAS 328
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 76-357 1.63e-77

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: 241.61  E-value: 1.63e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  76 QGSGSGFIWDDAGHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRI-GVGLrrprP-VPLGTSADLKVGQ 153
Cdd:NF041521   55 RGTGSGFIISSDGIILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIeAKNL----PtVPLGNSDQLQPGE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 154 KVFAIGNPFGLDWTFTTGIISALNRTlPSESG-PDIQ-QLIQTDAAINPGNSGGPLLDSSGRLIGINTAIYspSGASaGI 231
Cdd:NF041521  131 WAIAIGNPLGLDNTVTLGIISATGRS-SSQVGvPDKRvDFIQTDAAINPGNSGGPLLNARGEVIGINTAIR--AGAQ-GL 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 232 GFAVPVDTVRRVIPQLARSGRYVRPSLGI-------EVDEQVNARLNER---TGAKGVFVLAVQSGSPAAAAGLSgmatg 301
Cdd:NF041521  207 GFAIPINTAQRIADQLIAGGKVEHPYLGIqmvtltpELKQEINSDPNSGftvPEDEGVLIVRVVPNSPAARAGLR----- 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2735145462 302 pqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVELGA 357
Cdd:NF041521  282 -----AGDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQTLTVRPGA 332
PRK10942 PRK10942
serine endoprotease DegP;
76-355 1.85e-55

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 188.44  E-value: 1.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  76 QGSGSGFIWDDA-GHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRIgVGLRRPRPVPLGTSADLKVGQK 154
Cdd:PRK10942  110 MALGSGVIIDADkGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQL-QNPKNLTAIKMADSDALRVGDY 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 155 VFAIGNPFGLDWTFTTGIISALNRtlpseSGPDIQQ---LIQTDAAINPGNSGGPLLDSSGRLIGINTAIYSPSGASAGI 231
Cdd:PRK10942  189 TVAIGNPYGLGETVTSGIVSALGR-----SGLNVENyenFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGI 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 232 GFAVPVDTVRRVIPQLARSGRYVRPSLGI---EVDEQVnARLNERTGAKGVFVLAVQSGSPAAAAglsgmatgpqGVTPG 308
Cdd:PRK10942  264 GFAIPSNMVKNLTSQMVEYGQVKRGELGImgtELNSEL-AKAMKVDAQRGAFVSQVLPNSSAAKA----------GIKAG 332

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2735145462 309 DIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVEL 355
Cdd:PRK10942  333 DVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVEL 379
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 79-217 2.16e-37

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 131.39  E-value: 2.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  79 GSGFIWDDAGHVVTNFHVIQGASGATVQ-----LADGRKYQAALVGVSPQHDLALLRIGVGLRRPRPVPLGTSADLKVGQ 153
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVElvsvvLADGREYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735145462 154 KVFAIGNPFGLDW-TFTTGIISALNRTLPSESGPDIqqlIQTDAAINPGNSGGPLLDSSGRLIGI 217
Cdd:pfam13365  81 RVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDDGRV---IQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 254-355 4.76e-19

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: 81.08  E-value: 4.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 254 VRPSLGIEV-DEQVNARLNERtgaKGVFVLAVQSGSPAAAAGLSGMATGPQG-VTPGDIITAVEGREVPTVGALLSRLDD 331
Cdd:cd00990     2 VRPGLGISFaPDQVARQLGVR---SGVLVLDVPPGGPAAKAGLRGTKRDEFGrIVLGDVIVAVDGKPVKNESDLYRALDE 78

                          90       100
                  ....*....|....*....|....
gi 2735145462 332 FKVGDVVTLTVMKQEQERQVRVEL 355
Cdd:cd00990    79 YKVGDVVTLKVLRGGTKVDLKVTL 102
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 78-256 4.43e-13

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


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 69.83  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  78 SGSGFIWDDaGHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRIGvGLRRPrPVPLGTSAdLKVGQKVFA 157
Cdd:NF033740  212 EGSGFVVAP-DRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLAVP-GLGLP-PLPFADEP-AETGDDAIV 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 158 IGNPFGLDWTFTtgiiSALNRTLPSESGPDI-------QQLIQTDAAINPGNSGGPLLDSSGRLIGIntaIYSPSGASAG 230
Cdd:NF033740  288 LGYPEGGPFTAT----PARVRERIALSGPDIygsgtvtREVYTLRGTVRPGNSGGPLLDPDGRVLGV---VFAAAVDDSD 360

                         170       180
                  ....*....|....*....|....*.
gi 2735145462 231 IGFAVPVDTVRrviPQLARSGRYVRP 256
Cdd:NF033740  361 TGYALTADEVR---PDLAAAAALTTP 383
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 277-343 5.03e-05

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 41.21  E-value: 5.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735145462  277 KGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVM 343
Cdd:smart00228  26 GGVVVSSVVPGSPAAKAGLR----------VGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 77-357 4.01e-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: 345.60  E-value: 4.01e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  77 GSGSGFIWDDAGHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRI-GVGLRrprPVPLGTSADLKVGQKV 155
Cdd:COG0265     1 GLGSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIdAKDLP---AAPLGDSDKLRVGDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 156 FAIGNPFGLDWTFTTGIISALNRTLPSESGPDIQQLIQTDAAINPGNSGGPLLDSSGRLIGINTAIYSPSGASAGIGFAV 235
Cdd:COG0265    78 LAIGNPFGLGQTVTAGIVSALGRSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGGSQGIGFAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 236 PVDTVRRVIPQLARSGRYVRPSLGIEVDEqVNARLNERTG---AKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIIT 312
Cdd:COG0265   158 PINLAKRVVEQLIETGRVRRGWLGVTIQP-VTPELAEALGlpePEGVLVARVEPGSPAAKAGLR----------PGDVIL 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2735145462 313 AVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVELGA 357
Cdd:COG0265   227 AVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGE 271
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 45-358 2.86e-90

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: 277.57  E-value: 2.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  45 ELFEKSRGSVVFISTSQLVQDA----------------WTRNIFSTPQ-----GSGSGFIWDDAGHVVTNFHVIQGASGA 103
Cdd:TIGR02037   5 PLVEKVAPAVVNISVEGTVKRRnrppalppffrqffgdDMPDFPRQQReqkvrGLGSGVIISADGYVLTNNHVVDGADEI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 104 TVQLADGRKYQAALVGVSPQHDLALLRIGVGLRRPrPVPLGTSADLKVGQKVFAIGNPFGLDWTFTTGIISALNRtlpse 183
Cdd:TIGR02037  85 TVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLP-VIKLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGR----- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 184 SGPDIQQ---LIQTDAAINPGNSGGPLLDSSGRLIGINTAIYSPSGASAGIGFAVPVDTVRRVIPQLARSGRYVRPSLGI 260
Cdd:TIGR02037 159 SGLGIGDyenFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPSGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGWLGV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 261 EVDEqVNARLNERTG---AKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGDV 337
Cdd:TIGR02037 239 TIQE-VTSDLAKSLGlekQRGALVAQVLPGSPAEKAGLK----------AGDVITSVNGKPISSFADLRRAIGTLKPGKK 307

                         330       340
                  ....*....|....*....|.
gi 2735145462 338 VTLTVMKQEQERQVRVELGAD 358
Cdd:TIGR02037 308 VTLGILRKGKEKTITVTLGAS 328
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 76-357 1.63e-77

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: 241.61  E-value: 1.63e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  76 QGSGSGFIWDDAGHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRI-GVGLrrprP-VPLGTSADLKVGQ 153
Cdd:NF041521   55 RGTGSGFIISSDGIILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIeAKNL----PtVPLGNSDQLQPGE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 154 KVFAIGNPFGLDWTFTTGIISALNRTlPSESG-PDIQ-QLIQTDAAINPGNSGGPLLDSSGRLIGINTAIYspSGASaGI 231
Cdd:NF041521  131 WAIAIGNPLGLDNTVTLGIISATGRS-SSQVGvPDKRvDFIQTDAAINPGNSGGPLLNARGEVIGINTAIR--AGAQ-GL 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 232 GFAVPVDTVRRVIPQLARSGRYVRPSLGI-------EVDEQVNARLNER---TGAKGVFVLAVQSGSPAAAAGLSgmatg 301
Cdd:NF041521  207 GFAIPINTAQRIADQLIAGGKVEHPYLGIqmvtltpELKQEINSDPNSGftvPEDEGVLIVRVVPNSPAARAGLR----- 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2735145462 302 pqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVELGA 357
Cdd:NF041521  282 -----AGDVIQKINGQPVTTAEQVQQIVENSQVGQTLQLEVQRNGQTQTLTVRPGA 332
PRK10942 PRK10942
serine endoprotease DegP;
76-355 1.85e-55

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 188.44  E-value: 1.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  76 QGSGSGFIWDDA-GHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRIgVGLRRPRPVPLGTSADLKVGQK 154
Cdd:PRK10942  110 MALGSGVIIDADkGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQL-QNPKNLTAIKMADSDALRVGDY 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 155 VFAIGNPFGLDWTFTTGIISALNRtlpseSGPDIQQ---LIQTDAAINPGNSGGPLLDSSGRLIGINTAIYSPSGASAGI 231
Cdd:PRK10942  189 TVAIGNPYGLGETVTSGIVSALGR-----SGLNVENyenFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGI 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 232 GFAVPVDTVRRVIPQLARSGRYVRPSLGI---EVDEQVnARLNERTGAKGVFVLAVQSGSPAAAAglsgmatgpqGVTPG 308
Cdd:PRK10942  264 GFAIPSNMVKNLTSQMVEYGQVKRGELGImgtELNSEL-AKAMKVDAQRGAFVSQVLPNSSAAKA----------GIKAG 332

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2735145462 309 DIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVEL 355
Cdd:PRK10942  333 DVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVEL 379
PRK10139 PRK10139
serine endoprotease DegQ;
76-362 8.30e-51

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 175.90  E-value: 8.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  76 QGSGSGFIWDDA-GHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRIgVGLRRPRPVPLGTSADLKVGQK 154
Cdd:PRK10139   89 EGLGSGVIIDAAkGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQI-QNPSKLTQIAIADSDKLRVGDF 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 155 VFAIGNPFGLDWTFTTGIISALNRTLPSESGpdIQQLIQTDAAINPGNSGGPLLDSSGRLIGINTAIYSPSGASAGIGFA 234
Cdd:PRK10139  168 AVAVGNPFGLGQTATSGIISALGRSGLNLEG--LENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFA 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 235 VPVDTVRRVIPQLARSGRYVRPSLGI---EVDEQVNARLNERTgAKGVFVLAVQSGSPAAAAglsgmatgpqGVTPGDII 311
Cdd:PRK10139  246 IPSNMARTLAQQLIDFGEIKRGLLGIkgtEMSADIAKAFNLDV-QRGAFVSEVLPNSGSAKA----------GVKAGDII 314

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2735145462 312 TAVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVELGADGSAS 362
Cdd:PRK10139  315 TSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDTSTSSS 365
PRK10898 PRK10898
serine endoprotease DegS;
63-353 1.87e-47

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 164.40  E-value: 1.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  63 VQDAWTRNIFSTPQGS------GSGFIWDDAGHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRI-GVGL 135
Cdd:PRK10898   58 VVNVYNRSLNSTSHNQleirtlGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKInATNL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 136 rrprPV-PLGTSADLKVGQKVFAIGNPFGLDWTFTTGIISALNRTLPSESGPdiQQLIQTDAAINPGNSGGPLLDSSGRL 214
Cdd:PRK10898  138 ----PViPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLSPTGR--QNFLQTDASINHGNSGGALVNSLGEL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 215 IGINTAIY--SPSGASA-GIGFAVPVDTVRRVIPQLARSGRYVRPSLGIEVDEQVNARlNERTGAK---GVFVLAVQSGS 288
Cdd:PRK10898  212 MGINTLSFdkSNDGETPeGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIGGREIAPLH-AQGGGIDqlqGIVVNEVSPDG 290

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735145462 289 PAAAAGLSgmatgpqgvtPGDIITAVEGRevPTVGAL--LSRLDDFKVGDVVTLTVMKQEQERQVRV 353
Cdd:PRK10898  291 PAAKAGIQ----------VNDLIISVNNK--PAISALetMDQVAEIRPGSVIPVVVMRDDKQLTLQV 345
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 79-217 2.16e-37

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 131.39  E-value: 2.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  79 GSGFIWDDAGHVVTNFHVIQGASGATVQ-----LADGRKYQAALVGVSPQHDLALLRIGVGLRRPRPVPLGTSADLKVGQ 153
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVElvsvvLADGREYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2735145462 154 KVFAIGNPFGLDW-TFTTGIISALNRTLPSESGPDIqqlIQTDAAINPGNSGGPLLDSSGRLIGI 217
Cdd:pfam13365  81 RVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDDGRV---IQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 254-355 4.76e-19

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: 81.08  E-value: 4.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 254 VRPSLGIEV-DEQVNARLNERtgaKGVFVLAVQSGSPAAAAGLSGMATGPQG-VTPGDIITAVEGREVPTVGALLSRLDD 331
Cdd:cd00990     2 VRPGLGISFaPDQVARQLGVR---SGVLVLDVPPGGPAAKAGLRGTKRDEFGrIVLGDVIVAVDGKPVKNESDLYRALDE 78

                          90       100
                  ....*....|....*....|....
gi 2735145462 332 FKVGDVVTLTVMKQEQERQVRVEL 355
Cdd:cd00990    79 YKVGDVVTLKVLRGGTKVDLKVTL 102
Trypsin pfam00089
Trypsin;
87-244 6.83e-15

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 72.86  E-value: 6.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  87 AGHVVTNFHVIQGASGA-TVQLADGRKYQAALVGV---------SPQHDLALLRigvgLRRP-------RPVPLGT-SAD 148
Cdd:pfam00089  40 AAHCVSGASDVKVVLGAhNIVLREGGEQKFDVEKIivhpnynpdTLDNDIALLK----LESPvtlgdtvRPICLPDaSSD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 149 LKVGQKVFAIG----NPFGLDWTFTTGIISALNRTLPSESGPD--IQQLIQTDA---AINPGNSGGPLLDSSGRLIGINT 219
Cdd:pfam00089 116 LPVGTTCTVSGwgntKTLGPSDTLQEVTVPVVSRETCRSAYGGtvTDTMICAGAggkDACQGDSGGPLVCSDGELIGIVS 195

                         170       180
                  ....*....|....*....|....*
gi 2735145462 220 AIYSPSGASaGIGFAVPVDTVRRVI 244
Cdd:pfam00089 196 WGYGCASGN-YPGVYTPVSSYLDWI 219
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 78-256 4.43e-13

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


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 69.83  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  78 SGSGFIWDDaGHVVTNFHVIQGASGATVQLADGRKYQAALVGVSPQHDLALLRIGvGLRRPrPVPLGTSAdLKVGQKVFA 157
Cdd:NF033740  212 EGSGFVVAP-DRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLAVP-GLGLP-PLPFADEP-AETGDDAIV 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 158 IGNPFGLDWTFTtgiiSALNRTLPSESGPDI-------QQLIQTDAAINPGNSGGPLLDSSGRLIGIntaIYSPSGASAG 230
Cdd:NF033740  288 LGYPEGGPFTAT----PARVRERIALSGPDIygsgtvtREVYTLRGTVRPGNSGGPLLDPDGRVLGV---VFAAAVDDSD 360

                         170       180
                  ....*....|....*....|....*.
gi 2735145462 231 IGFAVPVDTVRrviPQLARSGRYVRP 256
Cdd:NF033740  361 TGYALTADEVR---PDLAAAAALTTP 383
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
255-358 3.06e-12

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 67.54  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 255 RPSLGIEVDEQvnarlnertgAKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVpTVGALLSRLDDFKV 334
Cdd:COG3975   482 KPSLGLRVSAD----------GGGLVVTSVLWGSPAYKAGLS----------AGDELLAIDGLRV-TADNLDDALAAYKP 540

                          90       100
                  ....*....|....*....|....
gi 2735145462 335 GDVVTLTVMKQEQERQVRVELGAD 358
Cdd:COG3975   541 GDPIELLVFRRDELRTVTVTLAAA 564
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 255-355 1.28e-11

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: 60.34  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 255 RPSLGIE-VD-EQVNARLNERT-----GAKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLS 327
Cdd:cd06781     1 RPSLGISmVDlSDVPEYEQQSLklpsnVNKGVYVAQVQSNSPAEKAGLK----------KGDVITKLDGKKVESSSDLRQ 70

                          90       100
                  ....*....|....*....|....*...
gi 2735145462 328 RLDDFKVGDVVTLTVMKQEQERQVRVEL 355
Cdd:cd06781    71 ILYSHKVGDTVKVTIYRDGKEKTLNIKL 98
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 255-353 1.54e-11

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: 60.00  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 255 RPSLGIEV--DEQVNARLNERTGAKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDF 332
Cdd:cd06779     1 RPYLGIEMenISPLLAKELGLPVNRGVLVAEVIPGSPAAKAGLK----------EGDVILSVNGKPVTSFNDLRAALDTK 70

                          90       100
                  ....*....|....*....|.
gi 2735145462 333 KVGDVVTLTVMKQEQERQVRV 353
Cdd:cd06779    71 KPGDSLNLTILRDGKTLTVTV 91
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 263-357 5.75e-10

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: 55.79  E-value: 5.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 263 DEQVNARLNErtgAKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGDVVTLTV 342
Cdd:cd10838    22 NPNSPVRIPE---VDGVLIMQVLPNSPAARAGLR----------RGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTV 88

                          90
                  ....*....|....*
gi 2735145462 343 MKQEQERQVRVELGA 357
Cdd:cd10838    89 LRGDRRQTLAVKPGD 103
PDZ_2 pfam13180
PDZ domain;
278-355 4.39e-09

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 52.66  E-value: 4.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735145462 278 GVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVEL 355
Cdd:pfam13180   7 GVVVVSVKSSGPAAKAGLK----------AGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDGKLLTVEVKL 74
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 255-353 3.57e-08

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: 50.56  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 255 RPSLGIEVDEqVNARLNERTG---AKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDD 331
Cdd:cd10839     1 RGWLGVQIQE-LTPDLAESFGlkePKGALVAQVLPDSPAAKAGLK----------AGDVILSLNGKPITSSADLRNRVAT 69

                          90       100
                  ....*....|....*....|..
gi 2735145462 332 FKVGDVVTLTVMKQEQERQVRV 353
Cdd:cd10839    70 TKPGTKVELKILRDGKEKTLTV 91
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 87-249 1.20e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.22  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462  87 AGHVVTNFHVIQGASGATV----QLADGRKYQAALVGVSPQ--------HDLALLRIGVGLRRPR-PVPLGTSADLKVGQ 153
Cdd:COG3591    27 AGHCVYDGAGGGWATNIVFvpgyNGGPYGTATATRFRVPPGwvasgdagYDYALLRLDEPLGDTTgWLGLAFNDAPLAGE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 154 KVFAIGNPFGLDWTFT---TGIISALNrtlpsesgpdiQQLIQTDAAINPGNSGGPLL---DSSGRLIGINTAiyspsGA 227
Cdd:COG3591   107 PVTIIGYPGDRPKDLSldcSGRVTGVQ-----------GNRLSYDCDTTGGSSGSPVLddsDGGGRVVGVHSA-----GG 170

                         170       180
                  ....*....|....*....|..
gi 2735145462 228 SAGIGFAVPVDTvrRVIPQLAR 249
Cdd:COG3591   171 ADRANTGVRLTS--AIVAALRA 190
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 250-355 8.59e-07

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


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 50.25  E-value: 8.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 250 SGRYvrPSLGIEVDEQvnarlnertgAKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGreVPTVGALLSRL 329
Cdd:COG0793    56 SGEF--GGLGAELGEE----------DGKVVVVSVIPGSPAEKAGIK----------PGDIILAIDG--KSVAGLTLDDA 111

                          90       100
                  ....*....|....*....|....*....
gi 2735145462 330 DDF---KVGDVVTLTVMKQEQERQVRVEL 355
Cdd:COG0793   112 VKLlrgKAGTKVTLTIKRPGEGEPITVTL 140
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 119-240 2.87e-06

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: 47.30  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 119 GVSPQHDLALLRI---------GVGLRRPRPVPLGTSADLKVGQKVFAIGNPFGldwtFTTGIISALNRTLPSESGpDIQ 189
Cdd:cd21112    59 SSFPGNDYALVRVtnpgwtpppEVRTYGGGTVPITGSAEPVVGAPVCKSGRTTG----WTCGTVTAVNVTVNYPGG-TVT 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2735145462 190 QLIQTDAAINPGNSGGPLLdSSGRLIGINTAIYSPSGASAGIGFAVPVDTV 240
Cdd:cd21112   134 GLTRTNACAEPGDSGGPVF-SGTQALGITSGGSGNCGSGGGTSYFQPVNPV 183
cpPDZ_RseP_YlbL-like cd10824
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), ...
 279-357 4.31e-06

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), Bacillus subtilis YlbL protease, 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), Bacillus subtilis YlbL, and related domains, including archaeal and chloroplast PDZ domains. RseP participates in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmaE) protein RseA. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. 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 beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP-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: 467636 [Multi-domain]  Cd Length: 82  Bit Score: 44.49  E-value: 4.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2735145462 279 VFVLAVQSGSPAAAAGlsgmatgpqgvTPGDIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVELGA 357
Cdd:cd10824     1 VVVLSVKPNSPAAKAL-----------HAGDLITEIDGQPTKSWQTFIDYIHDKKVGESVKITYKHGNKNEEASLKLTA 68
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 281-358 1.48e-05

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 46.23  E-value: 1.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735145462 281 VLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKvGDVVTLTVMKQEQERQVRVELGAD 358
Cdd:COG0750   132 VGEVVPGSPAAKAGLQ----------PGDRIVAINGQPVTSWDDLVDIIRASP-GKPLTLTVERDGEELTLTVTPRLV 198
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 277-343 5.03e-05

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 41.21  E-value: 5.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2735145462  277 KGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVM 343
Cdd:smart00228  26 GGVVVSSVVPGSPAAKAGLR----------VGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 284-353 8.49e-05

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: 40.64  E-value: 8.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 284 VQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKvGDVVTLTVMKQEQERQVRV 353
Cdd:cd23081     6 VVANSPAAEAGLK----------PGDRILKIDGQKVRTWEDIVRIVRENP-GKPLTLKIERDGKILTVTV 64
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 255-346 9.16e-05

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


Pssm-ID: 467632 [Multi-domain]  Cd Length: 101  Bit Score: 40.91  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 255 RPSLGI---EVDEQVNARLNERTGA-----KGVFVLAVQSGSPAAAAGLsgmatgpqgvTPGDIITAVEGREVPTVGALL 326
Cdd:cd23085     1 RPWLGMkmlELNEHIIAQLKERDPMfpdvkAGVLVPQVIPGSPAERAGL----------RPGDVIVEFDGKPVDSTKQII 70

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2735145462 327 SRLDD-----FKV------GDVVTLTVMKQE 346
Cdd:cd23085    71 DALGDkvgkpFKVvvkranKVQVTLTVTPEE 101
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 258-349 1.52e-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: 39.92  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 258 LGIEVDEqvnarLNERTGAKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKvgDV 337
Cdd:cd23084     4 EGATVSN-----VTDEDGGKGVVVTEVDPGSPAAQSGLK----------KGDVIIGVNRQPVKSIAELRKVLKSKP--SA 66

                          90
                  ....*....|..
gi 2735145462 338 VTLTVMKQEQER 349
Cdd:cd23084    67 VLLQIKRGDSSR 78
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 280-342 3.86e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 37.89  E-value: 3.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2735145462 280 FVLAVQSGSPAAAAGLsgmatgpqgvTPGDIITAVEGREVPTVGALLSRLDDfKVGDVVTLTV 342
Cdd:pfam17820   1 VVTAVVPGSPAERAGL----------RVGDVILAVNGKPVRSLEDVARLLQG-SAGESVTLTV 52
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 255-355 4.04e-04

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


Pssm-ID: 467620 [Multi-domain]  Cd Length: 93  Bit Score: 38.91  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 255 RPSLGIEVDEQ--VNARLNERTGAKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDF 332
Cdd:cd06777     1 RGYLGITLSEIppAMARGGGIDQLQGALVKGVSPDSPAAKAGIQ----------VGDIILQFDNKPVISVLELMDLVAEI 70

                          90       100
                  ....*....|....*....|...
gi 2735145462 333 KVGDVVTLTVMKQEQERQVRVEL 355
Cdd:cd06777    71 RPGTVIPVVVLRDGKQLTLEVTI 93
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 278-355 4.42e-04

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: 38.63  E-value: 4.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735145462 278 GVFVLAVQSGSPAAAAglsgmatgpqgVTPGDIITAVEGREVPTVGALLSRLDDFKVGDVVTLTVMKQEQERQVRVEL 355
Cdd:cd23080     1 GVYVLSVVENMPAKGI-----------LEAGDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKL 67
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 257-343 7.69e-04

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 38.03  E-value: 7.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 257 SLGIEVDEQVNARlnertgAKGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPTVGALLSRLDDFKVGD 336
Cdd:pfam00595  11 GLGFSLKGGSDQG------DPGIFVSEVLPGGAAEAGGLK----------VGDRILSINGQDVENMTHEEAVLALKGSGG 74


                  ....*..
gi 2735145462 337 VVTLTVM 343
Cdd:pfam00595  75 KVTLTIL 81
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 277-355 2.21e-03

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: 36.69  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735145462 277 KGVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGreVPTVGALLSRLDDF---KVGDVVTLTVMKQEQERQVRV 353
Cdd:cd06782    14 GYLVVVSPIPGGPAEKAGIK----------PGDVIVAVDG--ESVRGMSLDEVVKLlrgPKGTKVKLTIRRGGEGEPRDV 81


                  ..
gi 2735145462 354 EL 355
Cdd:cd06782    82 TL 83
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 278-321 4.39e-03

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: 36.32  E-value: 4.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2735145462 278 GVFVLAVQSGSPAAAAGLSgmatgpqgvtPGDIITAVEGREVPT 321
Cdd:cd06785    32 GVYVHKVIPGSPAQRAGLK----------DGDVIISINGKPVKS 65
Peptidase_M50 pfam02163
Peptidase family M50;
279-354 8.58e-03

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 37.47  E-value: 8.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2735145462 279 VFVLAVQSGSPAAAAGLsgmatgpqgvTPGDIITAVEGREVPTVGALLSRLDDfKVGDVVTLTVMKQEQERQVRVE 354
Cdd:pfam02163  95 PVIGGVAPGSPAAKAGL----------KPGDVILSINGKKITSWQDLVEALAK-SPGKPITLTVERGGQTLTVTIT 159
 
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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