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Conserved domains on  [gi|21614538|ref|NP_659540|]
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serine protease HTRA2, mitochondrial isoform 2 preproprotein [Homo sapiens]

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 ...
 182-358 1.25e-31

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: 120.25  E-value: 1.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 182 GSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTK------------------------ 237
Cdd:COG0265   3 GSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKdlpaaplgdsdklrvgdwvlaign 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 238 ------------------------------F---------GNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSDRL 273
Cdd:COG0265  83 pfglgqtvtagivsalgrsigssgggtyddFiqtdaainpGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPINLA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 274 REFLHRGEKKnsssgisGSQRR-YIGVMMLTLSP--------------------------RAGLRPGDVILAIGEQMVQN 326
Cdd:COG0265 163 KRVVEQLIET-------GRVRRgWLGVTIQPVTPelaealglpepegvlvarvepgspaaKAGLRPGDVILAVDGKPVTS 235

                       250       260       270
                ....*....|....*....|....*....|....*
gi 21614538 327 AEDVYEAVRTQ---SQLAVQIRRGRETLTLYVTPE 358
Cdd:COG0265 236 ARDLQRLLASLkpgDTVTLTVLRGGKELTVTVTLG 270
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 182-358 1.25e-31

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: 120.25  E-value: 1.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 182 GSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTK------------------------ 237
Cdd:COG0265   3 GSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKdlpaaplgdsdklrvgdwvlaign 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 238 ------------------------------F---------GNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSDRL 273
Cdd:COG0265  83 pfglgqtvtagivsalgrsigssgggtyddFiqtdaainpGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPINLA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 274 REFLHRGEKKnsssgisGSQRR-YIGVMMLTLSP--------------------------RAGLRPGDVILAIGEQMVQN 326
Cdd:COG0265 163 KRVVEQLIET-------GRVRRgWLGVTIQPVTPelaealglpepegvlvarvepgspaaKAGLRPGDVILAVDGKPVTS 235

                       250       260       270
                ....*....|....*....|....*....|....*
gi 21614538 327 AEDVYEAVRTQ---SQLAVQIRRGRETLTLYVTPE 358
Cdd:COG0265 236 ARDLQRLLASLkpgDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 150-356 3.94e-25

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: 105.38  E-value: 3.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   150 IADVVEKTAPAVVYIE---------ILDRHP-----FLGREVPISN-----------GSGFVVAADGLIVTNAHVVADRR 204
Cdd:TIGR02037   3 FAPLVEKVAPAVVNISvegtvkrrnRPPALPpffrqFFGDDMPDFPrqqreqkvrglGSGVIISADGYVLTNNHVVDGAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   205 RVRVRLLSGDTYEAVVTAVDPVADIATLRIQTK----------------------------------------------- 237
Cdd:TIGR02037  83 EITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKknlpviklgdsdklrvgdwvlaignpfglgqtvtsgivsalgrsglg 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   238 ------F---------GNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSD---RLREFLHRGEKknsssgisgSQR 294
Cdd:TIGR02037 163 igdyenFiqtdaainpGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNmakNVVDQLIEGGK---------VKR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   295 RYIGVMMLTLSP--------------------------RAGLRPGDVILAIGEQMVQNAEDVYEAVRTQ---SQLAVQIR 345
Cdd:TIGR02037 234 GWLGVTIQEVTSdlakslglekqrgalvaqvlpgspaeKAGLKAGDVITSVNGKPISSFADLRRAIGTLkpgKKVTLGIL 313

                         330
                  ....*....|.
gi 21614538   346 RGRETLTLYVT 356
Cdd:TIGR02037 314 RKGKEKTITVT 324
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 294-359 1.37e-24

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: 96.03  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 294 RRYIGVMMLTLSP--------------------------------RAGLRPGDVILAIGEQMVQNAEDVYEAVRTQSQLA 341
Cdd:cd06785   1 KRYIGIRMLTLTPslleelkqrnpdfpdvssgvyvhkvipgspaqRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSSLL 80

                        90
                ....*....|....*...
gi 21614538 342 VQIRRGRETLTLYVTPEV 359
Cdd:cd06785  81 VVVRRGNEDLLLTVTPEE 98
PRK10898 PRK10898
serine endoprotease DegS;
154-356 2.62e-12

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 66.95  E-value: 2.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  154 VEKTAPAVVYI--EILDRHPFLGREVPiSNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIAT 231
Cdd:PRK10898  51 VRRAAPAVVNVynRSLNSTSHNQLEIR-TLGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  232 LRI--------------------------------QT--------------------KF---------GNSGGPLVNLDG 250
Cdd:PRK10898 130 LKInatnlpvipinpkrvphigdvvlaignpynlgQTitqgiisatgriglsptgrqNFlqtdasinhGNSGGALVNSLG 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  251 EVIGVNTM--------KVTAGISFAIPSD---RLREFLHR-GEKKNSSSGISGSQRRYI-----------GVMMLTLSP- 306
Cdd:PRK10898 210 ELMGINTLsfdksndgETPEGIGFAIPTQlatKIMDKLIRdGRVIRGYIGIGGREIAPLhaqgggidqlqGIVVNEVSPd 289

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21614538  307 ----RAGLRPGDVILAIG--------EQMVQNAEdvyeaVRTQSQLAVQIRRGRETLTLYVT 356
Cdd:PRK10898 290 gpaaKAGIQVNDLIISVNnkpaisalETMDQVAE-----IRPGSVIPVVVMRDDKQLTLQVT 346
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 182-255 1.25e-07

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 50.50  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   182 GSGFVVAADGLIVTNAH-----VVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRI---------------------- 234
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHvvddaEEAAVELVSVVLADGREYPATVVARDPDLDLALLRVsgdgrglpplplgdseplvgge 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21614538   235 -----------------------------------------QTKFGNSGGPLVNLDGEVIGV 255
Cdd:pfam13365  81 rvyavgyplggeklslsegivsgvdegrdggddgrviqtdaALSPGSSGGPVFDADGRVVGI 142
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 151-255 1.13e-05

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: 46.72  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  151 ADVVEKTAPAVVYIeiLDRHPFLGRevpISNGSGFVVAaDGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIA 230
Cdd:NF033740 187 SPAVRRARPSVVKV--RGTAPSCGR---ALEGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  231 TL---------------------------------------RIQTKF--------------------------GNSGGPL 245
Cdd:NF033740 261 VLavpglglpplpfadepaetgddaivlgypeggpftatpaRVRERIalsgpdiygsgtvtrevytlrgtvrpGNSGGPL 340

                        170
                 ....*....|
gi 21614538  246 VNLDGEVIGV 255
Cdd:NF033740 341 LDPDGRVLGV 350
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 307-355 9.73e-04

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 37.74  E-value: 9.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 21614538    307 RAGLRPGDVILAIGEQMVQNAedvyeavrTQSQLAVQIRRGRETLTLYV 355
Cdd:smart00228  41 KAGLRVGDVILEVNGTSVEGL--------THLEAVDLLKKAGGKVTLTV 81
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 182-358 1.25e-31

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: 120.25  E-value: 1.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 182 GSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTK------------------------ 237
Cdd:COG0265   3 GSGVIISPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKdlpaaplgdsdklrvgdwvlaign 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 238 ------------------------------F---------GNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSDRL 273
Cdd:COG0265  83 pfglgqtvtagivsalgrsigssgggtyddFiqtdaainpGNSGGPLVNLNGEVIGINTAIISrsggsQGIGFAIPINLA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 274 REFLHRGEKKnsssgisGSQRR-YIGVMMLTLSP--------------------------RAGLRPGDVILAIGEQMVQN 326
Cdd:COG0265 163 KRVVEQLIET-------GRVRRgWLGVTIQPVTPelaealglpepegvlvarvepgspaaKAGLRPGDVILAVDGKPVTS 235

                       250       260       270
                ....*....|....*....|....*....|....*
gi 21614538 327 AEDVYEAVRTQ---SQLAVQIRRGRETLTLYVTPE 358
Cdd:COG0265 236 ARDLQRLLASLkpgDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 150-356 3.94e-25

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: 105.38  E-value: 3.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   150 IADVVEKTAPAVVYIE---------ILDRHP-----FLGREVPISN-----------GSGFVVAADGLIVTNAHVVADRR 204
Cdd:TIGR02037   3 FAPLVEKVAPAVVNISvegtvkrrnRPPALPpffrqFFGDDMPDFPrqqreqkvrglGSGVIISADGYVLTNNHVVDGAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   205 RVRVRLLSGDTYEAVVTAVDPVADIATLRIQTK----------------------------------------------- 237
Cdd:TIGR02037  83 EITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKknlpviklgdsdklrvgdwvlaignpfglgqtvtsgivsalgrsglg 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   238 ------F---------GNSGGPLVNLDGEVIGVNTMKVT-----AGISFAIPSD---RLREFLHRGEKknsssgisgSQR 294
Cdd:TIGR02037 163 igdyenFiqtdaainpGNSGGPLVNLRGEVIGINTAILSpsggnVGIGFAIPSNmakNVVDQLIEGGK---------VKR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   295 RYIGVMMLTLSP--------------------------RAGLRPGDVILAIGEQMVQNAEDVYEAVRTQ---SQLAVQIR 345
Cdd:TIGR02037 234 GWLGVTIQEVTSdlakslglekqrgalvaqvlpgspaeKAGLKAGDVITSVNGKPISSFADLRRAIGTLkpgKKVTLGIL 313

                         330
                  ....*....|.
gi 21614538   346 RGRETLTLYVT 356
Cdd:TIGR02037 314 RKGKEKTITVT 324
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 294-359 1.37e-24

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: 96.03  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 294 RRYIGVMMLTLSP--------------------------------RAGLRPGDVILAIGEQMVQNAEDVYEAVRTQSQLA 341
Cdd:cd06785   1 KRYIGIRMLTLTPslleelkqrnpdfpdvssgvyvhkvipgspaqRAGLKDGDVIISINGKPVKSSSDVYEAVKSGSSLL 80

                        90
                ....*....|....*...
gi 21614538 342 VQIRRGRETLTLYVTPEV 359
Cdd:cd06785  81 VVVRRGNEDLLLTVTPEE 98
PRK10898 PRK10898
serine endoprotease DegS;
154-356 2.62e-12

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 66.95  E-value: 2.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  154 VEKTAPAVVYI--EILDRHPFLGREVPiSNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIAT 231
Cdd:PRK10898  51 VRRAAPAVVNVynRSLNSTSHNQLEIR-TLGSGVIMDQRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  232 LRI--------------------------------QT--------------------KF---------GNSGGPLVNLDG 250
Cdd:PRK10898 130 LKInatnlpvipinpkrvphigdvvlaignpynlgQTitqgiisatgriglsptgrqNFlqtdasinhGNSGGALVNSLG 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  251 EVIGVNTM--------KVTAGISFAIPSD---RLREFLHR-GEKKNSSSGISGSQRRYI-----------GVMMLTLSP- 306
Cdd:PRK10898 210 ELMGINTLsfdksndgETPEGIGFAIPTQlatKIMDKLIRdGRVIRGYIGIGGREIAPLhaqgggidqlqGIVVNEVSPd 289

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21614538  307 ----RAGLRPGDVILAIG--------EQMVQNAEdvyeaVRTQSQLAVQIRRGRETLTLYVT 356
Cdd:PRK10898 290 gpaaKAGIQVNDLIISVNnkpaisalETMDQVAE-----IRPGSVIPVVVMRDDKQLTLQVT 346
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 294-355 2.47e-10

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: 56.53  E-value: 2.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538 294 RRYIGVMMLTLSP--------------------------RAGLRPGDVILAIGEQMVQNAEDVYEAVRTQ---SQLAVQI 344
Cdd:cd06779   1 RPYLGIEMENISPllakelglpvnrgvlvaevipgspaaKAGLKEGDVILSVNGKPVTSFNDLRAALDTKkpgDSLNLTI 80

                        90
                ....*....|.
gi 21614538 345 RRGRETLTLYV 355
Cdd:cd06779  81 LRDGKTLTVTV 91
PRK10942 PRK10942
serine endoprotease DegP;
182-319 1.10e-09

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 59.39  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  182 GSGFVV-AADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIA-------------------TLR-------- 233
Cdd:PRK10942 113 GSGVIIdADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIAliqlqnpknltaikmadsdALRvgdytvai 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  234 -------------------------------IQTKF----GNSGGPLVNLDGEVIGVNTMKVTA-----GISFAIPSDRL 273
Cdd:PRK10942 193 gnpyglgetvtsgivsalgrsglnvenyenfIQTDAainrGNSGGALVNLNGELIGINTAILAPdggniGIGFAIPSNMV 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21614538  274 R----EFLHRGEKKNSSSGISG--------------SQR-RYIG-VMMLTLSPRAGLRPGDVILAI 319
Cdd:PRK10942 273 KnltsQMVEYGQVKRGELGIMGtelnselakamkvdAQRgAFVSqVLPNSSAAKAGIKAGDVITSL 338
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 305-361 1.63e-08

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 55.48  E-value: 1.63e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21614538 305 SP--RAGLRPGDVILAIGEQMVQNAEDVYEAVRT--QSQLAVQIRRGRETLTLYVTPEVTE 361
Cdd:COG0750 139 SPaaKAGLQPGDRIVAINGQPVTSWDDLVDIIRAspGKPLTLTVERDGEELTLTVTPRLVE 199
PRK10139 PRK10139
serine endoprotease DegQ;
150-319 8.10e-08

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 53.80  E-value: 8.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  150 IADVVEKTAPAVVYIEI------LDRHP-----FLGREVPISN-------GSGFVV-AADGLIVTNAHVVADRRRVRVRL 210
Cdd:PRK10139  42 LAPMLEKVLPAVVSVRVegtasqGQKIPeefkkFFGDDLPDQPaqpfeglGSGVIIdAAKGYVLTNNHVINQAQKISIQL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  211 LSGDTYEAVVTAVDPVADIATLRIQT------------------------------------------------------ 236
Cdd:PRK10139 122 NDGREFDAKLIGSDDQSDIALLQIQNpskltqiaiadsdklrvgdfavavgnpfglgqtatsgiisalgrsglnleglen 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  237 --------KFGNSGGPLVNLDGEVIGVNTMKV-----TAGISFAIPSDRLR----EFLHRGEKKNSSSGISGS------- 292
Cdd:PRK10139 202 fiqtdasiNRGNSGGALLNLNGELIGINTAILapgggSVGIGFAIPSNMARtlaqQLIDFGEIKRGLLGIKGTemsadia 281

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 21614538  293 -------QR-RYIG-VMMLTLSPRAGLRPGDVILAI 319
Cdd:PRK10139 282 kafnldvQRgAFVSeVLPNSGSAKAGVKAGDIITSL 317
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 182-255 1.25e-07

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 50.50  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538   182 GSGFVVAADGLIVTNAH-----VVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRI---------------------- 234
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHvvddaEEAAVELVSVVLADGREYPATVVARDPDLDLALLRVsgdgrglpplplgdseplvgge 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21614538   235 -----------------------------------------QTKFGNSGGPLVNLDGEVIGV 255
Cdd:pfam13365  81 rvyavgyplggeklslsegivsgvdegrdggddgrviqtdaALSPGSSGGPVFDADGRVVGI 142
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 307-361 1.85e-07

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: 48.34  E-value: 1.85e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21614538 307 RAGLRPGDVILAIGEQMVQNAEDVYEAVR--TQSQLAVQIRRGRETLTLYVTPEVTE 361
Cdd:cd23081  14 EAGLKPGDRILKIDGQKVRTWEDIVRIVRenPGKPLTLKIERDGKILTVTVTPELVE 70
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 298-358 6.48e-07

circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 47.31  E-value: 6.48e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614538 298 GVMMLTLSP-----RAGLRPGDVILAIGEQMVQNAEDVYEAV-RTQ--SQLAVQIRRGRETLTLYVTPE 358
Cdd:cd10838  34 GVLIMQVLPnspaaRAGLRRGDVIQAVDGQPVTTADDVQRIVeQAGvgEELELTVLRGDRRQTLAVKPG 102
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 151-255 1.13e-05

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: 46.72  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  151 ADVVEKTAPAVVYIeiLDRHPFLGRevpISNGSGFVVAaDGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIA 230
Cdd:NF033740 187 SPAVRRARPSVVKV--RGTAPSCGR---ALEGSGFVVA-PDRVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614538  231 TL---------------------------------------RIQTKF--------------------------GNSGGPL 245
Cdd:NF033740 261 VLavpglglpplpfadepaetgddaivlgypeggpftatpaRVRERIalsgpdiygsgtvtrevytlrgtvrpGNSGGPL 340

                        170
                 ....*....|
gi 21614538  246 VNLDGEVIGV 255
Cdd:NF033740 341 LDPDGRVLGV 350
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 298-356 2.11e-05

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: 42.95  E-value: 2.11e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21614538 298 GVMMLTLSP-----RAGLRP-----------GDVILAIGEQMVQNAEDVYEAVRTQS---QLAVQIRRGRETLTLYVT 356
Cdd:cd00990  24 GVLVLDVPPggpaaKAGLRGtkrdefgrivlGDVIVAVDGKPVKNESDLYRALDEYKvgdVVTLKVLRGGTKVDLKVT 101
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 307-356 3.42e-05

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 44.59  E-value: 3.42e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21614538 307 RAGLRPGDVILAIGEQMVQNAED---VYEAVRTQSQLAVQIRRGRETLTLYVT 356
Cdd:COG3031 166 KLGLQPGDVITSINGQDLTDPAQaleLLQQLRDASEVTLTVERNGQPVTLTYN 218
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 307-353 2.01e-04

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


Pssm-ID: 467631 [Multi-domain]  Cd Length: 83  Bit Score: 39.53  E-value: 2.01e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21614538 307 RAGLRPGDVILAIGEQMVQNAEDVYEAVRTQ-SQLAVQIRRGRETLTL 353
Cdd:cd23084  33 QSGLKKGDVIIGVNRQPVKSIAELRKVLKSKpSAVLLQIKRGDSSRYL 80
Trypsin pfam00089
Trypsin;
238-277 2.02e-04

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 42.04  E-value: 2.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 21614538   238 FGNSGGPLVNLDGEVIGVNTMK----VTAGISFAIPSDRLREFL 277
Cdd:pfam00089 176 QGDSGGPLVCSDGELIGIVSWGygcaSGNYPGVYTPVSSYLDWI 219
Peptidase_M50 pfam02163
Peptidase family M50;
307-361 2.05e-04

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 42.48  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21614538   307 RAGLRPGDVILAIGEQMVQNAEDVYEAVRTQ--SQLAVQIRRGRETLTLYVTPEVTE 361
Cdd:pfam02163 108 KAGLKPGDVILSINGKKITSWQDLVEALAKSpgKPITLTVERGGQTLTVTITPKSSE 164
PDZ_2 pfam13180
PDZ domain;
307-356 5.56e-04

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 38.02  E-value: 5.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 21614538   307 RAGLRPGDVILAIGEQMVQNAEDVYEAVRT---QSQLAVQIRRGRETLTLYVT 356
Cdd:pfam13180  21 KAGLKAGDVILSIDGRKINDLTDLESALYGhkpGDTVTLQVYRDGKLLTVEVK 73
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 307-346 7.75e-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: 37.12  E-value: 7.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 21614538   307 RAGLRPGDVILAIGEQMVQNAEDVYEAVRTQ--SQLAVQIRR 346
Cdd:pfam17820  13 RAGLRVGDVILAVNGKPVRSLEDVARLLQGSagESVTLTVRR 54
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 307-355 9.73e-04

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


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 37.74  E-value: 9.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 21614538    307 RAGLRPGDVILAIGEQMVQNAedvyeavrTQSQLAVQIRRGRETLTLYV 355
Cdd:smart00228  41 KAGLRVGDVILEVNGTSVEGL--------THLEAVDLLKKAGGKVTLTV 81
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
 305-358 2.97e-03

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 39.33  E-value: 2.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21614538  305 SPRAGLRPGDVILAIGEQMVQNAeDVYEAVR-----TQSQLAVQIRRGRETLTLYVTPE 358
Cdd:PLN00049 115 AARAGIRPGDVILAIDGTSTEGL-SLYEAADrlqgpEGSSVELTLRRGPETRLVTLTRE 172
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 298-358 4.90e-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: 36.28  E-value: 4.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21614538 298 GVMMLTLSP-----RAGLRPGDVILAIGEQMVQNAEDVYEAV--RTQSQLAVQIRRG-RETLTLYVTPE 358
Cdd:cd23085  32 GVLVPQVIPgspaeRAGLRPGDVIVEFDGKPVDSTKQIIDALgdKVGKPFKVVVKRAnKVQVTLTVTPE 100
 
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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