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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931396844   2 TAVDQNDRRASFANYGAGCVDISAPGTRIVSTQVheprqagfDQPYgGYFNGTSVAASVVSGSVALIWALDRNLTPRQIQ 81
Cdd:cd07473  181 AATDSNDALASFSNYGKKTVDLAAPGVDILSTSP--------GGGY-GYMSGTSMATPHVAGAAALLLSLNPNLTAAQIK 251

                 ....*..
gi 931396844  82 NILLESS 88
Cdd:cd07473  252 DAILSSA 258

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931396844  288 DLDGDGRAEIVVSHGSGSAARLGVFDGQGTELAEFAPVGlsGRGSLSVSAVDLNGDGRAEIVA 350
Cdd:pfam13517   1 DLDGDGKLDLVVANDGGLRLYLNNGDGTFTFITSVSLGG--GGGGLSVAVGDLDGDGRLDLLV 61

Peptidase S8 family domain in Subtilisin-like proteins; 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 931396844   2 TAVDQNDRRASFANYGAGCVDISAPGTRIVSTQVheprqagfDQPYgGYFNGTSVAASVVSGSVALIWALDRNLTPRQIQ 81
Cdd:cd07473  181 AATDSNDALASFSNYGKKTVDLAAPGVDILSTSP--------GGGY-GYMSGTSMATPHVAGAAALLLSLNPNLTAAQIK 251

                 ....*..
gi 931396844  82 NILLESS 88
Cdd:cd07473  252 DAILSSA 258

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 931396844    6 QNDRRASFANYGAGC-----VDISAPGTRIVSTQVHEPRQAGFDQPYGGYF---NGTSVAASVVSGSVALIWALDRNLTP 77
Cdd:pfam00082 182 SEGNLASFSSYGPTLdgrlkPDIVAPGGNITGGNISSTLLTTTSDPPNQGYdsmSGTSMATPHVAGAAALLKQAYPNLTP 261

                          90       100
                  ....*....|....*....|....*...
gi 931396844   78 RQIQNILLESSFPIDDlnPGLFGKLGRG 105
Cdd:pfam00082 262 ETLKALLVNTATDLGD--AGLDRLFGYG 287

type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931396844    2 TAVDQNDRRASFANYGAGcVDISAPGTRIVSTQvheprqagfdqPYGGYF---NGTSVAASVVSGSVALIWALDRNLTPR 78
Cdd:TIGR03921 182 GSIDRDGTPSSFSLPGPW-VDLAAPGENIVSLS-----------PGGDGLattSGTSFAAPFVSGTAALVRSRFPDLTAA 249

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 931396844   79 QIQNILLESSfpiddLNPGLFGK---LGRGRIDAARAV 113
Cdd:TIGR03921 250 QVRRRIEATA-----DHPARGGRddyVGYGVVDPVAAL 282

Peptidase S8 family domain in Subtilisin-like proteins; 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 931396844   2 TAVDQNDRRASFANYGAGCVDISAPGTRIVSTQVheprqagfDQPYgGYFNGTSVAASVVSGSVALIWALDRNLTPRQIQ 81
Cdd:cd07473  181 AATDSNDALASFSNYGKKTVDLAAPGVDILSTSP--------GGGY-GYMSGTSMATPHVAGAAALLLSLNPNLTAAQIK 251

                 ....*..
gi 931396844  82 NILLESS 88
Cdd:cd07473  252 DAILSSA 258

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 931396844   3 AVDQNDRRASFANYGAgCVDISAPGTRIVSTQvheprqagfdqPYGGY--FNGTSVAASVVSGSVALIWALDRNLTPRQI 80
Cdd:cd07477  155 AVDSNNNRASFSSTGP-EVELAAPGVDILSTY-----------PNNDYayLSGTSMATPHVAGVAALVWSKRPELTNAQV 222

                 ....*..
gi 931396844  81 QNILLES 87
Cdd:cd07477  223 RQALNKT 229

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 931396844   3 AVDQNDRRASFANYGAgCVDISAPGTRIVSTQvhEPRQAGFDQPYGGY--FNGTSVAASVVSGSVALIWALDRNLTPRQI 80
Cdd:cd07498  159 ATDSNDARASYSNYGN-YVDLVAPGVGIWTTG--TGRGSAGDYPGGGYgsFSGTSFASPVAAGVAALILSANPNLTPAEV 235

                 ....
gi 931396844  81 QNIL 84
Cdd:cd07498  236 EDIL 239

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931396844   2 TAVDQNDRRASFANYGAGCVDISAPGTRIVSTqvheprqAGFDQPYGGYFNGTSVAASVVSGSVALIWALDRNLTPRQIQ 81
Cdd:cd00306  163 GAVDRDGTPASPSSNGGAGVDIAAPGGDILSS-------PTTGGGGYATLSGTSMAAPIVAGVAALLLSANPDLTPAQVK 235

                 ....*.
gi 931396844  82 NILLES 87
Cdd:cd00306  236 AALLST 241

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 931396844   2 TAVDQNDRRASFANYGAgCVDISAPGTRIVSTqvheprqagfdQPYGGY--FNGTSVAASVVSGSVALIWALDRnLTPRQ 79
Cdd:cd07484  181 AATDQDDKRASFSNYGK-WVDVSAPGGGILST-----------TPDGDYayMSGTSMATPHVAGVAALLYSQGP-LSASE 247

                 ....*...
gi 931396844  80 IQNILLES 87
Cdd:cd07484  248 VRDALKKT 255

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 931396844    6 QNDRRASFANYGAGC-----VDISAPGTRIVSTQVHEPRQAGFDQPYGGYF---NGTSVAASVVSGSVALIWALDRNLTP 77
Cdd:pfam00082 182 SEGNLASFSSYGPTLdgrlkPDIVAPGGNITGGNISSTLLTTTSDPPNQGYdsmSGTSMATPHVAGAAALLKQAYPNLTP 261

                          90       100
                  ....*....|....*....|....*...
gi 931396844   78 RQIQNILLESSFPIDDlnPGLFGKLGRG 105
Cdd:pfam00082 262 ETLKALLVNTATDLGD--AGLDRLFGYG 287

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931396844  288 DLDGDGRAEIVVSHGSGSAARLGVFDGQGTELAEFAPVGlsGRGSLSVSAVDLNGDGRAEIVA 350
Cdd:pfam13517   1 DLDGDGKLDLVVANDGGLRLYLNNGDGTFTFITSVSLGG--GGGGLSVAVGDLDGDGRLDLLV 61

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 931396844  22 DISAPGTRIVSTQvheprqAGFDQPYGgYFNGTSVAASVVSGSVALIWALDRNLTPRQIQNILLESSFPIDDLNPGLFGK 101
Cdd:cd07474  210 DIVAPGVDIMSTA------PGSGTGYA-RMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLYDSDGVVYPV 282

                         90
                 ....*....|...
gi 931396844 102 L--GRGRIDAARA 112
Cdd:cd07474  283 SrqGAGRVDALRA 295

Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. 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 931396844   3 AVDQNDRRASFANYGAGCVDISAPG-----------TRIVSTQVHEPRQAGFDQPYGGY--FNGTSVAASVVSGSVALIw 69
Cdd:cd07482  196 ATDNNGNLSSFSNYGNSRIDLAAPGgdfllldqygkEKWVNNGLMTKEQILTTAPEGGYayMYGTSLAAPKVSGALALI- 274

                         90       100
                 ....*....|....*....|.
gi 931396844  70 aLDRN---LTPRQIQNILLES 87
Cdd:cd07482  275 -IDKNplkKPPDEAIRILYNT 294

Peptidase S8 family domain, uncharacterized subfamily 9; 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 931396844   3 AVDQNDRRASFANYGA---GCV--DISAPGTRIVstqvheprqagFDQPYGGYF--NGTSVAASVVSGSVALIWALDRNL 75
Cdd:cd07493  179 AVDANGNKASFSSIGPtadGRLkpDVMALGTGIY-----------VINGDGNITyaNGTSFSCPLIAGLIACLWQAHPNW 247

                         90
                 ....*....|..
gi 931396844  76 TPRQIQNILLES 87
Cdd:cd07493  248 TNLQIKEAILKS 259

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 931396844   3 AVDQNDRRASFANYGAGCV-----DISAPGTRIVSTQvheprqagfdqPYGGY--FNGTSVAASVVSGSVALIWALD 72
Cdd:cd07481  180 ATDRNDVLADFSSRGPSTYgrikpDISAPGVNIRSAV-----------PGGGYgsSSGTSMAAPHVAGVAALLWSAN 245

Peptidase S8 family domain, uncharacterized subfamily 6; 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931396844  22 DISAPGTRIVSTQVHEPRQAGFDqpyggYFNGTSVAASVVSGSVALIWALDRNLTPRQIQNILLESS 88
Cdd:cd07490  192 DVAAPGVDVYSARQGANGDGQYT-----RLSGTSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETA 253

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 931396844  22 DISAPGTRIVSTqvheprqaGFDQPYGgYFNGTSVAASVVSGSVALIW-ALDR---NLTPRQ----IQNILLESSFPIDD 93
Cdd:cd07475  251 DITAPGGNIYST--------VNDNTYG-YMSGTSMASPHVAGASALVKqRLKEkypKLSGEElvdlVKNLLMNTATPPLD 321

                         90       100
                 ....*....|....*....|....
gi 931396844  94 LN-PGLF---GKLGRGRIDAARAV 113
Cdd:cd07475  322 SEdTKTYyspRRQGAGLIDVAKAI 345

Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931396844  51 FNGTSVAASVVSGSVALIWALDRNLTPRQIQNILLESSFPIDdlNPGLFGKLGRGRIDAARAV 113
Cdd:cd05562  213 FFGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMG--EPGYDNASGSGLVDADRAV 273