Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family 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, 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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961374264   1 TSMASPFIAGTQALVKQAMSDKkgtfynlYQKMSASEKTAFVKNIEMNTASIEPDVSHENVIVSPRRQGAG 71
Cdd:cd07475  274 TSMASPHVAGASALVKQRLKEK-------YPKLSGEELVDLVKNLLMNTATPPLDSEDTKTYYSPRRQGAG 337

Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases 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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961374264   1 TSMASPFIAGTQALVKQAMSDKkgtfynlYQKMSASEKTAFVKNIEMNTASIEPDVSHENVIVSPRRQGAG 71
Cdd:cd07475  274 TSMASPHVAGASALVKQRLKEK-------YPKLSGEELVDLVKNLLMNTATPPLDSEDTKTYYSPRRQGAG 337

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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961374264    1 TSMASPFIAGTQALVKQAmsdkkgtfynlYQKMSASEktafVKNIEMNTASIEPDvshenvIVSPRRQGAG 71
Cdd:pfam00082 238 TSMATPHVAGAAALLKQA-----------YPNLTPET----LKALLVNTATDLGD------AGLDRLFGYG 287

Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases 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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961374264   1 TSMASPFIAGTQALVKQAMSDKkgtfynlYQKMSASEKTAFVKNIEMNTASIEPDVSHENVIVSPRRQGAG 71
Cdd:cd07475  274 TSMASPHVAGASALVKQRLKEK-------YPKLSGEELVDLVKNLLMNTATPPLDSEDTKTYYSPRRQGAG 337

Fn3-like domain; Fn3_5 is an fn3-like domain which is frequently found as the first of three on streptococcal C5a peptidase (SCP), a highly specific protease and adhesin/invasin. The family is found in conjunction with pfam00082, pfam02225 and pfam00746.

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                  ....*....|....*....|....*....|....*....|....*..
gi 961374264   98 VELKDFkENTKTFTVKFTNRTNKPLTYKLANNGkdsdVYTSATDKNA 144
Cdd:pfam06280   1 VELKEI-GDFFSFTLTLHNTGKKAVTYAVSHNG----VLTDQTDTNE 42

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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961374264    1 TSMASPFIAGTQALVKQAmsdkkgtfynlYQKMSASEktafVKNIEMNTASIEPDvshenvIVSPRRQGAG 71
Cdd:pfam00082 238 TSMATPHVAGAAALLKQA-----------YPNLTPET----LKALLVNTATDLGD------AGLDRLFGYG 287

Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases

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                 ....*....|....*....|....*....|....*....|....*....|
gi 961374264   1 TSMASPFIAGTQALVKQAMSDkkgTFYNLYQKMSAsektAFVKNIEMNTA 50
Cdd:cd04842  250 TSMATPLVAGAAALLRQYFVD---GYYPTKFNPSA----ALLKALLINSA 292