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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657    1 MAAFSSKGPNIITPdiLKPDITAPGVSIIAAYTEAQGPTNQmFDKRRVLFNSVSGTSMSCPHISGICGLLKTLYPHWSPA 80
Cdd:pfam00082 186 LASFSSYGPTLDGR--LKPDIVAPGGNITGGNISSTLLTTT-SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPE 262

                          90
                  ....*....|.
gi 645306657   81 AIKSAIMTTAT 91
Cdd:pfam00082 263 TLKALLVNTAT 273

bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 645306657    5 SSKGPNIItpDILKPDITAPGVSIIAAYteaqgPTNQmfdkrrvlFNSVSGTSMSCPHISGICGL 69
Cdd:NF040809  994 SSRGPTIR--NIQKPDIVAPGVNIIAPY-----PGNT--------YATITGTSAAAAHVSGVAAL 1043

bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 645306657    2 AAFSSKGPniITPDILKPDITAPGVSIIAaYTEAqGPTNqmfdkrrvlfnSVSGTSMSCPHISGICGLL 70
Cdd:NF040809  419 SVFSGEGD--IENGIYKPDLLAPGENIVS-YLPG-GTTG-----------ALTGTSMATPHVTGVCSLL 472

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   2 AAFSSKGPnIITPDILKPDITAPGVSIIAAyteAQGPTNQmfdkrrvlFNSVSGTSMSCPHISGICGLLKTLYPHWSPAA 81
Cdd:cd07474  193 GPSSSRGP-PTSDSAIKPDIVAPGVDIMST---APGSGTG--------YARMSGTSMAAPHVAGAAALLKQAHPDWSPAQ 260

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 645306657  82 IKSAIMTTATTQDNSREPVlnasfyrATPFSYGAGHVNPNSA 123
Cdd:cd07474  261 IKAALMNTAKPLYDSDGVV-------YPVSRQGAGRVDALRA 295

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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657    1 MAAFSSKGPNIITPdiLKPDITAPGVSIIAAYTEAQGPTNQmFDKRRVLFNSVSGTSMSCPHISGICGLLKTLYPHWSPA 80
Cdd:pfam00082 186 LASFSSYGPTLDGR--LKPDIVAPGGNITGGNISSTLLTTT-SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPE 262

                          90
                  ....*....|.
gi 645306657   81 AIKSAIMTTAT 91
Cdd:pfam00082 263 TLKALLVNTAT 273

Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. 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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   1 MAAFSSKGPNIitPDILKPDITAPGVSIIAAYteaqgPTNQmfdkrrvlFNSVSGTSMSCPHISGICGLL------KTLY 74
Cdd:cd07478  359 IAIFSGRGPTR--DGRIKPDIAAPGVNILTAS-----PGGG--------YTTRSGTSVAAAIVAGACALLlqwgivRGND 423

                         90
                 ....*....|....*..
gi 645306657  75 PHWSPAAIKSAIMTTAT 91
Cdd:cd07478  424 PYLYGEKIKTYLIRGAR 440

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   1 MAAFSSKGPniiTPDI-LKPDITAPGVSIIAAYteaqgPTNQmfdkrrvlFNSVSGTSMSCPHISGICGL----LKTLYP 75
Cdd:cd07475  234 MSGFSSWGP---TPDLdLKPDITAPGGNIYSTV-----NDNT--------YGYMSGTSMASPHVAGASALvkqrLKEKYP 297

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 645306657  76 HWSPA----AIKSAIMTTATTQDNSREPvlnasfyrATPFS---YGAGHVN 119
Cdd:cd07475  298 KLSGEelvdLVKNLLMNTATPPLDSEDT--------KTYYSprrQGAGLID 340

Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq 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        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   4 FSSKGPniiTPD-ILKPDITAPGVSIIAAYTEAQGPtnqmfdkrrvlFNSVSGTSMSCPHISGICGLLKTLYPH-WSPAA 81
Cdd:cd07489  191 FSSWGP---TNElYLKPDVAAPGGNILSTYPLAGGG-----------YAVLSGTSMATPYVAGAAALLIQARHGkLSPAE 256

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 645306657  82 IKSAIMTTATTQDNSREPvlNASFYRATPFSYGAGHVN 119
Cdd:cd07489  257 LRDLLASTAKPLPWSDGT--SALPDLAPVAQQGAGLVN 292

Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   1 MAAFSSKGPNIitpdilkpDITAPGVSIIAAYteAQGPTNqmfdkrrvlFNSVSGTSMSCPHISGICGLLKTLYPHWSPA 80
Cdd:cd04077  183 RASFSNYGSCV--------DIFAPGVDILSAW--IGSDTA---------TATLSGTSMAAPHVAGLAAYLLSLGPDLSPA 243

                         90
                 ....*....|.
gi 645306657  81 AIKSAIMTTAT 91
Cdd:cd04077  244 EVKARLLNLAT 254

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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   2 AAFSSKGPNIitpdilkpDITAPGVSIIAAYteaqgPTNQmfdkrrvlFNSVSGTSMSCPHISGICGLLKTLYPHWSPAA 81
Cdd:cd07477  163 ASFSSTGPEV--------ELAAPGVDILSTY-----PNND--------YAYLSGTSMATPHVAGVAALVWSKRPELTNAQ 221

                 ....*...
gi 645306657  82 IKSAIMTT 89
Cdd:cd07477  222 VRQALNKT 229

Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F, encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a 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 these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 645306657   1 MAAFSSKGPniITPDILKPDITAPGVSIIAAYTEaqgptnqmfdkrrVLFNSVSGTSMSCPHISGICGLLKTLYP 75
Cdd:cd07481  187 LADFSSRGP--STYGRIKPDISAPGVNIRSAVPG-------------GGYGSSSGTSMAAPHVAGVAALLWSANP 246

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   2 AAFSSKGPNIitpdilkpDITAPGVSIIAAYteaqgPTNQmfdkrrvlFNSVSGTSMSCPHISGICGLLKTLYPhWSPAA 81
Cdd:cd07484  190 ASFSNYGKWV--------DVSAPGGGILSTT-----PDGD--------YAYMSGTSMATPHVAGVAALLYSQGP-LSASE 247

                         90
                 ....*....|.
gi 645306657  82 IKSAIMTTATT 92
Cdd:cd07484  248 VRDALKKTADD 258

Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of alkaline proteinases originating from different strains of Bacillus subtilis. Novo is one of the strains that produced enzymes belonging to this group. The enzymes obtained from the Novo and BPN' strains are identical. The Carlsburg and Novo subtilisins are thought to have arisen from a common ancestral protein. They have similar peptidase and esterase activities, pH profiles, catalyze transesterification reactions, and are both inhibited by diispropyl fluorophosphate, though they differ in 85 positions in the amino acid sequence. 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 with an additional acidic residue Asp in the oxyanion hole, similar to that of 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   1 MAAFSSKGPNIItpdilkpDITAPGVSIIAAYteaqgPTNQmfdkrrvlFNSVSGTSMSCPHISGICGLLKTLYPHWSPA 80
Cdd:cd07483  221 VANFSNYGKKNV-------DVFAPGERIYSTT-----PDNE--------YETDSGTSMAAPVVSGVAALIWSYYPNLTAK 280

                         90
                 ....*....|.
gi 645306657  81 AIKSAIMTTAT 91
Cdd:cd07483  281 EVKQIILESGV 291

Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans is an extracellular subtilisin-like keratinase. It is contains a signal peptide, a propeptide, and a catalytic region. The tertiary structure of fervidolysin is similar to that of subtilisin. It contains a Asp/His/Ser catalytic triad and is a member of the peptidase S8 (subtilisin and kexin) family. The catalytic triad is similar to that found in trypsin-like proteases, but it does 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 645306657  20 DITAPGV-SIIAAYTEAQGPTNQMFDKrrvlfnsVSGTSMSCPHISGICGLLKTLYP-HWSPAAIKSAIMTT 89
Cdd:cd07485  209 DIAAPGVgTILSTVPKLDGDGGGNYEY-------LSGTSMAAPHVSGVAALVLSKFPdVFTPEQIRKLLEES 273

Peptidase S8 family domain, uncharacterized subfamily 15; 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        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   2 AAFSSKGPNIitpdilkpDITAPGVSIiaaYTEAQGPTNQmFDKRRVLFNSVSGTSMSCPHISGICGLLKTLYPHWSPAA 81
Cdd:cd07498  167 ASYSNYGNYV--------DLVAPGVGI---WTTGTGRGSA-GDYPGGGYGSFSGTSFASPVAAGVAALILSANPNLTPAE 234

                 ....*...
gi 645306657  82 IKSAIMTT 89
Cdd:cd07498  235 VEDILTST 242

Peptidase S8 family domain, uncharacterized subfamily 10; 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
                 ....*....|....*....|....*....|....*..
gi 645306657  54 SGTSMSCPHISGICGLLKTLYPHWSPAAIKSAIMTTA 90
Cdd:cd07494  246 SGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTA 282

Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II are member of the peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, 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). Tripeptidyl aminopeptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl aminopeptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645306657   5 SSKGPniiTPD-ILKPDITAPGVSIIAAYTEAQGPTNQMfdkrrvlfnsvSGTSMSCPHISGICGL----LKTLYPHWSP 79
Cdd:cd04857  333 SSRGP---TADgALGVSISAPGGAIASVPNWTLQGSQLM-----------NGTSMSSPNACGGIALllsgLKAEGIPYTP 398

                         90
                 ....*....|..
gi 645306657  80 AAIKSAIMTTAT 91
Cdd:cd04857  399 YSVRRALENTAK 410

Peptidase S8 family domain, uncharacterized subfamily 8; 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        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 645306657  21 ITAPGVSIIAayteaqgPTNQMFDKRrvlfnsVSGTSMSCPHISGICGLLKTLYPHWSPAAIKSAIMTTAT 91
Cdd:cd07492  165 FSADGVDIIA-------PAPHGRYLT------VSGNSFAAPHVTGMVALLLSEKPDIDANDLKRLLQRLAV 222