Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002856  422 LEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYfNTGTL 501
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG-DTGTL 79

                  ....*
gi 768002856  502 YRYTL 506
Cdd:pfam01483  80 NSWQL 84

Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to family S8.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002856   37 SWAVQVSQGNREVERLARKFGFVNLGPIFPDGQYFHLRHRGVVQQSLTPHWGHRLHLKKNPKtrpgpksiqqeeagrpry 116
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPK------------------ 62

                          90       100
                  ....*....|....*....|....
gi 768002856  117 gnhgacqglVQWFQQQTLQRRVKR 140
Cdd:pfam16470  63 ---------VKWAEQQRGKKRVKR 77

Giardia variant-specific surface protein;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002856  525 TSSACVQRDTEGLCQACDGPAYILGQlclaycpprffnhtrlvtagpghtaapalrVCSSCHASCYTCRGGSPRDCTSCP 604
Cdd:pfam03302  80 TVANCKTCEDQGQCQACNDGFYKSGD------------------------------ACSPCHESCKTCSGGTASDCTECL 129

                          90
                  ....*....|....*.
gi 768002856  605 PSSTL----DQQQGSC 616
Cdd:pfam03302 130 TGKALrygnDGTKGTC 145

Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002856  422 LEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYfNTGTL 501
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG-DTGTL 79

                  ....*
gi 768002856  502 YRYTL 506
Cdd:pfam01483  80 NSWQL 84

Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to family S8.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002856   37 SWAVQVSQGNREVERLARKFGFVNLGPIFPDGQYFHLRHRGVVQQSLTPHWGHRLHLKKNPKtrpgpksiqqeeagrpry 116
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPK------------------ 62

                          90       100
                  ....*....|....*....|....
gi 768002856  117 gnhgacqglVQWFQQQTLQRRVKR 140
Cdd:pfam16470  63 ---------VKWAEQQRGKKRVKR 77

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002856 141 SVVVPTDPWFSKQWYMNSEAQPDLSILQAWSQGLSGQGIVVSVLDDGIEKDHPDLWANYdpLASYDFNDYDPDPQ 215
Cdd:COG1404   73 PAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRV--VGGYDFVDGDGDPS 145

Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 768002856  176 GQGIVVSVLDDGIEKDHPDLWANYDPLASYDFNDYDPDPQPRYTP 220
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDFNNEWDDP 45

Giardia variant-specific surface protein;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002856  525 TSSACVQRDTEGLCQACDGPAYILGQlclaycpprffnhtrlvtagpghtaapalrVCSSCHASCYTCRGGSPRDCTSCP 604
Cdd:pfam03302  80 TVANCKTCEDQGQCQACNDGFYKSGD------------------------------ACSPCHESCKTCSGGTASDCTECL 129

                          90
                  ....*....|....*.
gi 768002856  605 PSSTL----DQQQGSC 616
Cdd:pfam03302 130 TGKALrygnDGTKGTC 145

Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002856  422 LEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYfNTGTL 501
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG-DTGTL 79

                  ....*
gi 768002856  502 YRYTL 506
Cdd:pfam01483  80 NSWQL 84

Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to family S8.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002856   37 SWAVQVSQGNREVERLARKFGFVNLGPIFPDGQYFHLRHRGVVQQSLTPHWGHRLHLKKNPKtrpgpksiqqeeagrpry 116
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPK------------------ 62

                          90       100
                  ....*....|....*....|....
gi 768002856  117 gnhgacqglVQWFQQQTLQRRVKR 140
Cdd:pfam16470  63 ---------VKWAEQQRGKKRVKR 77

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768002856 141 SVVVPTDPWFSKQWYMNSEAQPDLSILQAWSQGLSGQGIVVSVLDDGIEKDHPDLWANYdpLASYDFNDYDPDPQ 215
Cdd:COG1404   73 PAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRV--VGGYDFVDGDGDPS 145

Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. 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. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768002856 144 VPTDPWFSKQWYMNseaqpDLSILQAWSQgLSGQGIVVSVLDDGIEKDHPDlWANYDPLASYDFNDYDPDPQP 216
Cdd:cd07484    1 TPNDPYYSYQWNLD-----QIGAPKAWDI-TGGSGVTVAVVDTGVDPTHPD-LLKVKFVLGYDFVDNDSDAMD 66

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 768002856 585 CHASCYTCRGGSPRDCTSCPPSSTLDqqQGSCM 617
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCV 32

Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768002856 176 GQGIVVSVLDDGIEKDHPDLWANYDPLAS----YDF--NDYDP-DPQPRYTPSKENRRTDAG 230
Cdd:cd07474    1 GKGVKVAVIDTGIDYTHPDLGGPGFPNDKvkggYDFvdDDYDPmDTRPYPSPLGDASAGDAT 62

Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. 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.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 768002856 178 GIVVSVLDDGIEKDHPDLWANYdpLASYDFNDYDPD 213
Cdd:cd07477    1 GVKVAVIDTGIDSSHPDLKLNI--VGGANFTGDDNN 34

Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases 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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 768002856 176 GQGIVVSVLDDGIEKDHPDLWAnydplASYDFNDYDPDPQPRYTPSKEN 224
Cdd:cd07487    1 GKGITVAVLDTGIDAPHPDFDG-----RIIRFADFVNTVNGRTTPYDDN 44