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Conserved domains on  [gi|192451461|ref|NP_001122182|]
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peroxisomal leader peptide-processing protease [Danio rerio]

Protein Classification

serine protease( domain architecture ID 10595581)

serine protease such as Arabidopsis thaliana DegS which functions as a trimer to catalyze the initial rate-limiting step in a proteolytic cascade that ultimately activates transcription of stress response genes in the cytoplasm

Gene Ontology:  GO:0008236|GO:0008233|GO:0006508
PubMed:  29180814

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
317-456 5.99e-19

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


:

Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 83.24  E-value: 5.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  317 GSGVLLNQN-LVLTCRHVVDEKSELTVKVNSGGRF--HTVRGKVLYssvVSSPYDIAIVELQEALTDKRTPRFTKH--FH 391
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLAdgREYPATVVA---RDPDLDLALLRVSGDGRGLPPLPLGDSepLV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 192451461  392 TGEDVVVVGYGALGSRcgPSLTSGILSRVITHQSQPV---MLQTTCAVQSGASGGAVIrSDTGELLGI 456
Cdd:pfam13365  78 GGERVYAVGYPLGGEK--LSLSEGIVSGVDEGRDGGDdgrVIQTDAALSPGSSGGPVF-DADGRVVGI 142
degP_htrA_DO super family cl37035
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
145-242 5.93e-07

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]


The actual alignment was detected with superfamily member TIGR02037:

Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 51.84  E-value: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  145 ALLKVPTSPNCPckeTIPWMKSGSLKKGCHVIACGSPFGglcpdlFMNTISKGIVSNLA------GDENALILTDARCLP 218
Cdd:TIGR02037 108 AVLKIDAKKNLP---VIKLGDSDKLRVGDWVLAIGNPFG------LGQTVTSGIVSALGrsglgiGDYENFIQTDAAINP 178
                          90       100
                  ....*....|....*....|....*..
gi 192451461  219 GTEGGGVFISKGgtsYLVGL---IASP 242
Cdd:TIGR02037 179 GNSGGPLVNLRG---EVIGIntaILSP 202
 
Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
317-456 5.99e-19

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 83.24  E-value: 5.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  317 GSGVLLNQN-LVLTCRHVVDEKSELTVKVNSGGRF--HTVRGKVLYssvVSSPYDIAIVELQEALTDKRTPRFTKH--FH 391
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLAdgREYPATVVA---RDPDLDLALLRVSGDGRGLPPLPLGDSepLV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 192451461  392 TGEDVVVVGYGALGSRcgPSLTSGILSRVITHQSQPV---MLQTTCAVQSGASGGAVIrSDTGELLGI 456
Cdd:pfam13365  78 GGERVYAVGYPLGGEK--LSLSEGIVSGVDEGRDGGDdgrVIQTDAALSPGSSGGPVF-DADGRVVGI 142
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
317-493 7.15e-18

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: 83.66  E-value: 7.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 317 GSGVLLNQN-LVLTCRHVVDEKSELTVKVNSGgrfHTVRGKVLYSSVVSspyDIAIVELQEA------LTDKRTPRftkh 389
Cdd:COG0265    3 GSGVIISPDgYILTNNHVVEGADEITVTLADG---REYPAKVVGRDPLT---DLAVLKIDAKdlpaapLGDSDKLR---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 390 fhTGEDVVVVGYgALGSrcGPSLTSGILSRviTHQSQPVM--------LQTTCAVQSGASGGAVIRSDtGELLGIvssNT 461
Cdd:COG0265   73 --VGDWVLAIGN-PFGL--GQTVTAGIVSA--LGRSIGSSgggtyddfIQTDAAINPGNSGGPLVNLN-GEVIGI---NT 141
                        170       180       190
                 ....*....|....*....|....*....|..
gi 192451461 462 RDYAAKVTYPHLNFSIPVTLLEPLLRRFAQTG 493
Cdd:COG0265  142 AIISRSGGSQGIGFAIPINLAKRVVEQLIETG 173
PRK10139 PRK10139
serine endoprotease DegQ;
317-494 3.89e-08

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 55.72  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 317 GSGVLLN--QNLVLTCRHVVDEKSELTVKVNSGGRFHtvrGKVLYSSVVSspyDIAIVELQEA--LTDKRTPRFTKhFHT 392
Cdd:PRK10139  92 GSGVIIDaaKGYVLTNNHVINQAQKISIQLNDGREFD---AKLIGSDDQS---DIALLQIQNPskLTQIAIADSDK-LRV 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 393 GEDVVVVG--YGalgsrCGPSLTSGILSRV----ITHQSQPVMLQTTCAVQSGASGGAVIRSDtGELLGIvssNTRDYAA 466
Cdd:PRK10139 165 GDFAVAVGnpFG-----LGQTATSGIISALgrsgLNLEGLENFIQTDASINRGNSGGALLNLN-GELIGI---NTAILAP 235
                        170       180
                 ....*....|....*....|....*...
gi 192451461 467 KVTYPHLNFSIPVTLLEPLLRRFAQTGD 494
Cdd:PRK10139 236 GGGSVGIGFAIPSNMARTLAQQLIDFGE 263
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
317-479 1.35e-07

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: 53.76  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  317 GSGVLLNQN-LVLTCRHVVDEKSELTVKVNSGGRFhtvRGKVLYSSVVSspyDIAIVELqEALTDKRTPRFT--KHFHTG 393
Cdd:TIGR02037  60 GSGVIISADgYVLTNNHVVDGADEITVTLSDGREF---KAKLVGKDPRT---DIAVLKI-DAKKNLPVIKLGdsDKLRVG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  394 EDVVVVG--YGaLGSrcgpSLTSGILS---RVITHQSQPV-MLQTTCAVQSGASGGAVIRSDtGELLGIvssNTRDYAAK 467
Cdd:TIGR02037 133 DWVLAIGnpFG-LGQ----TVTSGIVSalgRSGLGIGDYEnFIQTDAAINPGNSGGPLVNLR-GEVIGI---NTAILSPS 203
                         170
                  ....*....|..
gi 192451461  468 VTYPHLNFSIPV 479
Cdd:TIGR02037 204 GGNVGIGFAIPS 215
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
145-242 5.93e-07

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: 51.84  E-value: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  145 ALLKVPTSPNCPckeTIPWMKSGSLKKGCHVIACGSPFGglcpdlFMNTISKGIVSNLA------GDENALILTDARCLP 218
Cdd:TIGR02037 108 AVLKIDAKKNLP---VIKLGDSDKLRVGDWVLAIGNPFG------LGQTVTSGIVSALGrsglgiGDYENFIQTDAAINP 178
                          90       100
                  ....*....|....*....|....*..
gi 192451461  219 GTEGGGVFISKGgtsYLVGL---IASP 242
Cdd:TIGR02037 179 GNSGGPLVNLRG---EVIGIntaILSP 202
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
144-238 1.62e-05

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 44.72  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  144 FALLKVPTSPNCPckETIPWMKSGSLKKGCHVIACGSPFGGLcpdlfMNTISKGIVSNL-----AGDENALILTDARCLP 218
Cdd:pfam13365  53 LALLRVSGDGRGL--PPLPLGDSEPLVGGERVYAVGYPLGGE-----KLSLSEGIVSGVdegrdGGDDGRVIQTDAALSP 125
                          90       100
                  ....*....|....*....|
gi 192451461  219 GTEGGGVFISKGgtsYLVGL 238
Cdd:pfam13365 126 GSSGGPVFDADG---RVVGI 142
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
145-242 1.49e-04

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: 43.60  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 145 ALLKVPTSPNcpckETIPWMKSGSLKKGCHVIACGSPFGglcpdlFMNTISKGIVSNLAGDENA--------LILTDARC 216
Cdd:COG0265   51 AVLKIDAKDL----PAAPLGDSDKLRVGDWVLAIGNPFG------LGQTVTAGIVSALGRSIGSsgggtyddFIQTDAAI 120
                         90       100
                 ....*....|....*....|....*....
gi 192451461 217 LPGTEGGGVFISKGGtsyLVGL---IASP 242
Cdd:COG0265  121 NPGNSGGPLVNLNGE---VIGIntaIISR 146
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
319-458 1.49e-04

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 43.44  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461   319 GVLLNQNLVLTCRHVVDEKSELTVKVNSGGRFHTVRGKVLYSSVVS-----------SPYDIAIVELQEALTDKRT---- 383
Cdd:smart00020  30 GSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIKVSKviihpnynpstYDNDIALLKLKEPVTLSDNvrpi 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461   384 --PRFTKHFHTGEDVVVVGYGALgsrcgpSLTSGILSRVITHQSQPVMLQTTCAVQSGA--------------------- 440
Cdd:smart00020 110 clPSSNYNVPAGTTCTVSGWGRT------SEGAGSLPDTLQEVNVPIVSNATCRRAYSGggaitdnmlcaggleggkdac 183
                          170       180
                   ....*....|....*....|..
gi 192451461   441 ---SGGA-VIRSDTGELLGIVS 458
Cdd:smart00020 184 qgdSGGPlVCNDGRWVLVGIVS 205
 
Name Accession Description Interval E-value
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
317-456 5.99e-19

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 83.24  E-value: 5.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  317 GSGVLLNQN-LVLTCRHVVDEKSELTVKVNSGGRF--HTVRGKVLYssvVSSPYDIAIVELQEALTDKRTPRFTKH--FH 391
Cdd:pfam13365   1 GTGFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLAdgREYPATVVA---RDPDLDLALLRVSGDGRGLPPLPLGDSepLV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 192451461  392 TGEDVVVVGYGALGSRcgPSLTSGILSRVITHQSQPV---MLQTTCAVQSGASGGAVIrSDTGELLGI 456
Cdd:pfam13365  78 GGERVYAVGYPLGGEK--LSLSEGIVSGVDEGRDGGDdgrVIQTDAALSPGSSGGPVF-DADGRVVGI 142
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
317-493 7.15e-18

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: 83.66  E-value: 7.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 317 GSGVLLNQN-LVLTCRHVVDEKSELTVKVNSGgrfHTVRGKVLYSSVVSspyDIAIVELQEA------LTDKRTPRftkh 389
Cdd:COG0265    3 GSGVIISPDgYILTNNHVVEGADEITVTLADG---REYPAKVVGRDPLT---DLAVLKIDAKdlpaapLGDSDKLR---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 390 fhTGEDVVVVGYgALGSrcGPSLTSGILSRviTHQSQPVM--------LQTTCAVQSGASGGAVIRSDtGELLGIvssNT 461
Cdd:COG0265   73 --VGDWVLAIGN-PFGL--GQTVTAGIVSA--LGRSIGSSgggtyddfIQTDAAINPGNSGGPLVNLN-GEVIGI---NT 141
                        170       180       190
                 ....*....|....*....|....*....|..
gi 192451461 462 RDYAAKVTYPHLNFSIPVTLLEPLLRRFAQTG 493
Cdd:COG0265  142 AIISRSGGSQGIGFAIPINLAKRVVEQLIETG 173
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
306-480 1.95e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 63.16  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 306 GVVLVETGWLWGSGVLLNQNLVLTCRHVVDEKSELTVKVN-------SGGRFHTVRGKVL-----YSSVVSSPYDIAIVE 373
Cdd:COG3591    3 GRLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNivfvpgyNGGPYGTATATRFrvppgWVASGDAGYDYALLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 374 LQEALTDKRTP---RFTKHFHTGEDVVVVGYGalGSRcGPSLTSGILSRVITHQSQpvMLQTTCAVQSGASGGAVIRSDT 450
Cdd:COG3591   83 LDEPLGDTTGWlglAFNDAPLAGEPVTIIGYP--GDR-PKDLSLDCSGRVTGVQGN--RLSYDCDTTGGSSGSPVLDDSD 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 192451461 451 G--ELLGIVSSNTRDYAakvtyphlNFSIPVT 480
Cdd:COG3591  158 GggRVVGVHSAGGADRA--------NTGVRLT 181
Trypsin pfam00089
Trypsin;
304-470 3.43e-09

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 57.07  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  304 YPGVVLVETGWLWGSGVLLNQNLVLTCRHVVDEKSELTV--------KVNSGGRFHTVRGKVLYSSVVSS--PYDIAIVE 373
Cdd:pfam00089  14 WQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVvlgahnivLREGGEQKFDVEKIIVHPNYNPDtlDNDIALLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  374 LQEALT------DKRTPRFTKHFHTGEDVVVVGYGaLGSRCGPS-----LTSGILSRVITHQSQPVMLQTT--CA----- 435
Cdd:pfam00089  94 LESPVTlgdtvrPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSdtlqeVTVPVVSRETCRSAYGGTVTDTmiCAgaggk 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 192451461  436 -VQSGASGGAVIRSDtGELLGIVS-------SNTRDYAAKVTY 470
Cdd:pfam00089 173 dACQGDSGGPLVCSD-GELIGIVSwgygcasGNYPGVYTPVSS 214
PRK10139 PRK10139
serine endoprotease DegQ;
317-494 3.89e-08

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 55.72  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 317 GSGVLLN--QNLVLTCRHVVDEKSELTVKVNSGGRFHtvrGKVLYSSVVSspyDIAIVELQEA--LTDKRTPRFTKhFHT 392
Cdd:PRK10139  92 GSGVIIDaaKGYVLTNNHVINQAQKISIQLNDGREFD---AKLIGSDDQS---DIALLQIQNPskLTQIAIADSDK-LRV 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 393 GEDVVVVG--YGalgsrCGPSLTSGILSRV----ITHQSQPVMLQTTCAVQSGASGGAVIRSDtGELLGIvssNTRDYAA 466
Cdd:PRK10139 165 GDFAVAVGnpFG-----LGQTATSGIISALgrsgLNLEGLENFIQTDASINRGNSGGALLNLN-GELIGI---NTAILAP 235
                        170       180
                 ....*....|....*....|....*...
gi 192451461 467 KVTYPHLNFSIPVTLLEPLLRRFAQTGD 494
Cdd:PRK10139 236 GGGSVGIGFAIPSNMARTLAQQLIDFGE 263
PRK10942 PRK10942
serine endoprotease DegP;
317-493 6.19e-08

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 55.16  E-value: 6.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 317 GSGVLLN--QNLVLTCRHVVDEKSELTVKVNSGGRFHT-VRGKVLYSsvvsspyDIAIVELQEA-------LTDKRTPRf 386
Cdd:PRK10942 113 GSGVIIDadKGYVVTNNHVVDNATKIKVQLSDGRKFDAkVVGKDPRS-------DIALIQLQNPknltaikMADSDALR- 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 387 tkhfhTGEDVVVVG--YGalgsrCGPSLTSGILSRV----ITHQSQPVMLQTTCAVQSGASGGAVIRSDtGELLGIvssN 460
Cdd:PRK10942 185 -----VGDYTVAIGnpYG-----LGETVTSGIVSALgrsgLNVENYENFIQTDAAINRGNSGGALVNLN-GELIGI---N 250
                        170       180       190
                 ....*....|....*....|....*....|...
gi 192451461 461 TRDYAAKVTYPHLNFSIPVTLLEPLLRRFAQTG 493
Cdd:PRK10942 251 TAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYG 283
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
317-479 1.35e-07

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: 53.76  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  317 GSGVLLNQN-LVLTCRHVVDEKSELTVKVNSGGRFhtvRGKVLYSSVVSspyDIAIVELqEALTDKRTPRFT--KHFHTG 393
Cdd:TIGR02037  60 GSGVIISADgYVLTNNHVVDGADEITVTLSDGREF---KAKLVGKDPRT---DIAVLKI-DAKKNLPVIKLGdsDKLRVG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  394 EDVVVVG--YGaLGSrcgpSLTSGILS---RVITHQSQPV-MLQTTCAVQSGASGGAVIRSDtGELLGIvssNTRDYAAK 467
Cdd:TIGR02037 133 DWVLAIGnpFG-LGQ----TVTSGIVSalgRSGLGIGDYEnFIQTDAAINPGNSGGPLVNLR-GEVIGI---NTAILSPS 203
                         170
                  ....*....|..
gi 192451461  468 VTYPHLNFSIPV 479
Cdd:TIGR02037 204 GGNVGIGFAIPS 215
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
145-242 5.93e-07

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: 51.84  E-value: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  145 ALLKVPTSPNCPckeTIPWMKSGSLKKGCHVIACGSPFGglcpdlFMNTISKGIVSNLA------GDENALILTDARCLP 218
Cdd:TIGR02037 108 AVLKIDAKKNLP---VIKLGDSDKLRVGDWVLAIGNPFG------LGQTVTSGIVSALGrsglgiGDYENFIQTDAAINP 178
                          90       100
                  ....*....|....*....|....*..
gi 192451461  219 GTEGGGVFISKGgtsYLVGL---IASP 242
Cdd:TIGR02037 179 GNSGGPLVNLRG---EVIGIntaILSP 202
PRK10898 PRK10898
serine endoprotease DegS;
317-481 1.30e-06

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 50.39  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 317 GSGVLLNQN-LVLTCRHVVDEKSELTVKVNSGGRFHTVrgkvLYSSvvSSPYDIAIVELQEA------LTDKRTPrftkh 389
Cdd:PRK10898  80 GSGVIMDQRgYILTNKHVINDADQIIVALQDGRVFEAL----LVGS--DSLTDLAVLKINATnlpvipINPKRVP----- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 390 fHTGeDVVVvgygALGS--RCGPSLTSGILS---RV----ITHQSqpvMLQTTCAVQSGASGGAVIRSdTGELLGIvssN 460
Cdd:PRK10898 149 -HIG-DVVL----AIGNpyNLGQTITQGIISatgRIglspTGRQN---FLQTDASINHGNSGGALVNS-LGELMGI---N 215
                        170       180
                 ....*....|....*....|....
gi 192451461 461 TR--DYAAKVTYPH-LNFSIPVTL 481
Cdd:PRK10898 216 TLsfDKSNDGETPEgIGFAIPTQL 239
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
144-238 1.62e-05

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 44.72  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461  144 FALLKVPTSPNCPckETIPWMKSGSLKKGCHVIACGSPFGGLcpdlfMNTISKGIVSNL-----AGDENALILTDARCLP 218
Cdd:pfam13365  53 LALLRVSGDGRGL--PPLPLGDSEPLVGGERVYAVGYPLGGE-----KLSLSEGIVSGVdegrdGGDDGRVIQTDAALSP 125
                          90       100
                  ....*....|....*....|
gi 192451461  219 GTEGGGVFISKGgtsYLVGL 238
Cdd:pfam13365 126 GSSGGPVFDADG---RVVGI 142
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
145-242 1.49e-04

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: 43.60  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461 145 ALLKVPTSPNcpckETIPWMKSGSLKKGCHVIACGSPFGglcpdlFMNTISKGIVSNLAGDENA--------LILTDARC 216
Cdd:COG0265   51 AVLKIDAKDL----PAAPLGDSDKLRVGDWVLAIGNPFG------LGQTVTAGIVSALGRSIGSsgggtyddFIQTDAAI 120
                         90       100
                 ....*....|....*....|....*....
gi 192451461 217 LPGTEGGGVFISKGGtsyLVGL---IASP 242
Cdd:COG0265  121 NPGNSGGPLVNLNGE---VIGIntaIISR 146
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
319-458 1.49e-04

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 43.44  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461   319 GVLLNQNLVLTCRHVVDEKSELTVKVNSGGRFHTVRGKVLYSSVVS-----------SPYDIAIVELQEALTDKRT---- 383
Cdd:smart00020  30 GSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEGQVIKVSKviihpnynpstYDNDIALLKLKEPVTLSDNvrpi 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192451461   384 --PRFTKHFHTGEDVVVVGYGALgsrcgpSLTSGILSRVITHQSQPVMLQTTCAVQSGA--------------------- 440
Cdd:smart00020 110 clPSSNYNVPAGTTCTVSGWGRT------SEGAGSLPDTLQEVNVPIVSNATCRRAYSGggaitdnmlcaggleggkdac 183
                          170       180
                   ....*....|....*....|..
gi 192451461   441 ---SGGA-VIRSDTGELLGIVS 458
Cdd:smart00020 184 qgdSGGPlVCNDGRWVLVGIVS 205
 
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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