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Conserved domains on  [gi|194374209|dbj|BAG57000|]
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unnamed protein product [Homo sapiens]

Protein Classification

S53 family serine peptidase( domain architecture ID 10183546)

S53 family serine peptidase similar to Bacillus kumamolisin, an extracellular proteinase that belongs to the sedolisin family of endopeptidases characterized by a subtilisin-like fold and a Ser-Glu-Asp catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidases_S53 cd04056
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
 166-340 7.02e-65

Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.


:

Pssm-ID: 173788 [Multi-domain]  Cd Length: 361  Bit Score: 209.48  E-value: 7.02e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 166 PYVTTVGGTSFQEP--------FLITNEIVDYISGGGFSNVFPRPSYQEEAVTKflsssphLPPSSYFNASGRAYPDVAA 237
Cdd:cd04056  186 PYVTAVGGTTLYTGgtgssaesTVWSSEGGWGGSGGGFSNYFPRPSYQSGAVLG-------LPPSGLYNGSGRGVPDVAA 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 238 LSD---GYWVVSNrVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQ---QHGAGLFDVTRGCHESCLd 311
Cdd:cd04056  259 NADpgtGYLVVVN-GQWYLVGGTSAAAPLFAGLIALINQARLAAGKPPLGFLNPLLYQlaaTAPSAFNDITSGNNGGCG- 336

                        170       180
                 ....*....|....*....|....*....
gi 194374209 312 eeveGQGFCSGPGWDPVTGWGTPNFPALL 340
Cdd:cd04056  337 ----GAGYPAGPGWDPVTGLGTPNFAKLL 361
Pro-peptidase_S53 cd11377
Activation domain of S53 peptidases; Members of this family are found in various subtilase ...
 34-174 3.36e-40

Activation domain of S53 peptidases; Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.


:

Pssm-ID: 206778  Cd Length: 139  Bit Score: 138.15  E-value: 3.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209  34 GWVSLGRADPEEELSPTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHS 113
Cdd:cd11377    1 GWVDVGRADPSTPITLTIALKQRNLAELEQLLLEVSDPGSPNYGKFLSPEEVAALFAPSPADVAAVTAWLESHGFTITSV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194374209 114 VITQDFLTCWLSIRQAELLLpGAEFHHYVGGPTETHVVRSPHPYQLPHILeVPYVTTVGGT 174
Cdd:cd11377   81 AANRDWIVFTGTVAQVEKAF-GTSLHVYSHKGSGGTYIRTPGNYSVPASL-ADHVDFVLGL 139
 
Name Accession Description Interval E-value
Peptidases_S53 cd04056
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
 166-340 7.02e-65

Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.


Pssm-ID: 173788 [Multi-domain]  Cd Length: 361  Bit Score: 209.48  E-value: 7.02e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 166 PYVTTVGGTSFQEP--------FLITNEIVDYISGGGFSNVFPRPSYQEEAVTKflsssphLPPSSYFNASGRAYPDVAA 237
Cdd:cd04056  186 PYVTAVGGTTLYTGgtgssaesTVWSSEGGWGGSGGGFSNYFPRPSYQSGAVLG-------LPPSGLYNGSGRGVPDVAA 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 238 LSD---GYWVVSNrVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQ---QHGAGLFDVTRGCHESCLd 311
Cdd:cd04056  259 NADpgtGYLVVVN-GQWYLVGGTSAAAPLFAGLIALINQARLAAGKPPLGFLNPLLYQlaaTAPSAFNDITSGNNGGCG- 336

                        170       180
                 ....*....|....*....|....*....
gi 194374209 312 eeveGQGFCSGPGWDPVTGWGTPNFPALL 340
Cdd:cd04056  337 ----GAGYPAGPGWDPVTGLGTPNFAKLL 361
Pro-peptidase_S53 cd11377
Activation domain of S53 peptidases; Members of this family are found in various subtilase ...
 34-174 3.36e-40

Activation domain of S53 peptidases; Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.


Pssm-ID: 206778  Cd Length: 139  Bit Score: 138.15  E-value: 3.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209  34 GWVSLGRADPEEELSPTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHS 113
Cdd:cd11377    1 GWVDVGRADPSTPITLTIALKQRNLAELEQLLLEVSDPGSPNYGKFLSPEEVAALFAPSPADVAAVTAWLESHGFTITSV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194374209 114 VITQDFLTCWLSIRQAELLLpGAEFHHYVGGPTETHVVRSPHPYQLPHILeVPYVTTVGGT 174
Cdd:cd11377   81 AANRDWIVFTGTVAQVEKAF-GTSLHVYSHKGSGGTYIRTPGNYSVPASL-ADHVDFVLGL 139
Pro-kuma_activ smart00944
Pro-kumamolisin, activation domain; This domain is found at the N-terminus of peptidases ...
 36-175 6.08e-38

Pro-kumamolisin, activation domain; This domain is found at the N-terminus of peptidases belonging to MEROPS peptidase family S53 (sedolisin, clan SB). The domain adopts a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.


Pssm-ID: 214928  Cd Length: 136  Bit Score: 132.38  E-value: 6.08e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209    36 VSLGRADPEEELSPTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVI 115
Cdd:smart00944   1 VDLGRLDPNETVSVTIALKQRNLAQLEQLVQEVSDPGSPNYGKFLSPEEFASLFGPSPADVNAVLAWLESHGLTVIEVAP 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194374209   116 TQDFLTCWLSIRQAELLLpGAEFHHY-VGGpteTHVVRSPHPYQLPHILEvPYVTTVGGTS 175
Cdd:smart00944  81 TRDFITFSGTVAQAEKAF-GTELHRYsHNG---KTYFANTGPPSIPAALA-GHVDGVLGLD 136
Pro-kuma_activ pfam09286
Pro-kumamolisin, activation domain; Members of this family are found in various subtilase ...
 33-176 1.07e-37

Pro-kumamolisin, activation domain; Members of this family are found in various subtilase propeptides, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptide.


Pssm-ID: 401284  Cd Length: 142  Bit Score: 131.96  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209   33 PGWVSLGRADPEEELSPTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCH 112
Cdd:pfam09286   1 PGWVKVGRADPSETIRLRIALKQRNLDQLEQLLMDVSTPGSPNYGKHLSPEEVASLFAPSDETVNAVLAWLESAGITITR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194374209  113 SVITQDFLTCWLSIRQAELLLpGAEFHHYVGGPTETHVVRSPHPyQLPHILeVPYVTTVGGTSF 176
Cdd:pfam09286  81 ISANGDWITFTGTVAQAESLF-GTEFHYYSHKNGGTTRLRTLEP-SVPAAL-ADHVDGIQPLTR 141
COG4934 COG4934
Serine protease, subtilase family [Posttranslational modification, protein turnover, ...
 166-343 6.31e-34

Serine protease, subtilase family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443961 [Multi-domain]  Cd Length: 519  Bit Score: 130.86  E-value: 6.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 166 PYVTTVGGTSFQepflIT-----------NEIVDYI----SGGGFSNVFPRPSYQEEAVTkflsssphlppssyFNASGR 230
Cdd:COG4934  346 PYVTAVGGTTLS----VDsngryssetawNDGSSYGgyggSGGGVSTVFPKPSWQTGTGV--------------PAGGGR 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 231 AYPDVAALSD---GYWVVSNRVPIPWVSGTSASTPVFGGILSLINEhrilSGRPPLGFLNPRLYQQHGAG-----LFDVT 302
Cdd:COG4934  408 GVPDVSADADpntGYLVYVTGSGWGVVGGTSAAAPLWAGLLALINQ----ALGHRLGFINPLLYALANSAaypsaFHDVT 483

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 194374209 303 RGCHESCldeevEGQGFCSGPGWDPVTGWGTPNFPALLKTL 343
Cdd:COG4934  484 SGNNGSC-----GGYGYTAGPGYDLVTGLGSPNGAALAAAL 519
 
Name Accession Description Interval E-value
Peptidases_S53 cd04056
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
 166-340 7.02e-65

Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.


Pssm-ID: 173788 [Multi-domain]  Cd Length: 361  Bit Score: 209.48  E-value: 7.02e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 166 PYVTTVGGTSFQEP--------FLITNEIVDYISGGGFSNVFPRPSYQEEAVTKflsssphLPPSSYFNASGRAYPDVAA 237
Cdd:cd04056  186 PYVTAVGGTTLYTGgtgssaesTVWSSEGGWGGSGGGFSNYFPRPSYQSGAVLG-------LPPSGLYNGSGRGVPDVAA 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 238 LSD---GYWVVSNrVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQ---QHGAGLFDVTRGCHESCLd 311
Cdd:cd04056  259 NADpgtGYLVVVN-GQWYLVGGTSAAAPLFAGLIALINQARLAAGKPPLGFLNPLLYQlaaTAPSAFNDITSGNNGGCG- 336

                        170       180
                 ....*....|....*....|....*....
gi 194374209 312 eeveGQGFCSGPGWDPVTGWGTPNFPALL 340
Cdd:cd04056  337 ----GAGYPAGPGWDPVTGLGTPNFAKLL 361
Pro-peptidase_S53 cd11377
Activation domain of S53 peptidases; Members of this family are found in various subtilase ...
 34-174 3.36e-40

Activation domain of S53 peptidases; Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.


Pssm-ID: 206778  Cd Length: 139  Bit Score: 138.15  E-value: 3.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209  34 GWVSLGRADPEEELSPTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHS 113
Cdd:cd11377    1 GWVDVGRADPSTPITLTIALKQRNLAELEQLLLEVSDPGSPNYGKFLSPEEVAALFAPSPADVAAVTAWLESHGFTITSV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194374209 114 VITQDFLTCWLSIRQAELLLpGAEFHHYVGGPTETHVVRSPHPYQLPHILeVPYVTTVGGT 174
Cdd:cd11377   81 AANRDWIVFTGTVAQVEKAF-GTSLHVYSHKGSGGTYIRTPGNYSVPASL-ADHVDFVLGL 139
Pro-kuma_activ smart00944
Pro-kumamolisin, activation domain; This domain is found at the N-terminus of peptidases ...
 36-175 6.08e-38

Pro-kumamolisin, activation domain; This domain is found at the N-terminus of peptidases belonging to MEROPS peptidase family S53 (sedolisin, clan SB). The domain adopts a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.


Pssm-ID: 214928  Cd Length: 136  Bit Score: 132.38  E-value: 6.08e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209    36 VSLGRADPEEELSPTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVI 115
Cdd:smart00944   1 VDLGRLDPNETVSVTIALKQRNLAQLEQLVQEVSDPGSPNYGKFLSPEEFASLFGPSPADVNAVLAWLESHGLTVIEVAP 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194374209   116 TQDFLTCWLSIRQAELLLpGAEFHHY-VGGpteTHVVRSPHPYQLPHILEvPYVTTVGGTS 175
Cdd:smart00944  81 TRDFITFSGTVAQAEKAF-GTELHRYsHNG---KTYFANTGPPSIPAALA-GHVDGVLGLD 136
Pro-kuma_activ pfam09286
Pro-kumamolisin, activation domain; Members of this family are found in various subtilase ...
 33-176 1.07e-37

Pro-kumamolisin, activation domain; Members of this family are found in various subtilase propeptides, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptide.


Pssm-ID: 401284  Cd Length: 142  Bit Score: 131.96  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209   33 PGWVSLGRADPEEELSPTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCH 112
Cdd:pfam09286   1 PGWVKVGRADPSETIRLRIALKQRNLDQLEQLLMDVSTPGSPNYGKHLSPEEVASLFAPSDETVNAVLAWLESAGITITR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194374209  113 SVITQDFLTCWLSIRQAELLLpGAEFHHYVGGPTETHVVRSPHPyQLPHILeVPYVTTVGGTSF 176
Cdd:pfam09286  81 ISANGDWITFTGTVAQAESLF-GTEFHYYSHKNGGTTRLRTLEP-SVPAAL-ADHVDGIQPLTR 141
COG4934 COG4934
Serine protease, subtilase family [Posttranslational modification, protein turnover, ...
 166-343 6.31e-34

Serine protease, subtilase family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443961 [Multi-domain]  Cd Length: 519  Bit Score: 130.86  E-value: 6.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 166 PYVTTVGGTSFQepflIT-----------NEIVDYI----SGGGFSNVFPRPSYQEEAVTkflsssphlppssyFNASGR 230
Cdd:COG4934  346 PYVTAVGGTTLS----VDsngryssetawNDGSSYGgyggSGGGVSTVFPKPSWQTGTGV--------------PAGGGR 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194374209 231 AYPDVAALSD---GYWVVSNRVPIPWVSGTSASTPVFGGILSLINEhrilSGRPPLGFLNPRLYQQHGAG-----LFDVT 302
Cdd:COG4934  408 GVPDVSADADpntGYLVYVTGSGWGVVGGTSAAAPLWAGLLALINQ----ALGHRLGFINPLLYALANSAaypsaFHDVT 483

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 194374209 303 RGCHESCldeevEGQGFCSGPGWDPVTGWGTPNFPALLKTL 343
Cdd:COG4934  484 SGNNGSC-----GGYGYTAGPGYDLVTGLGSPNGAALAAAL 519
 
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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