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Conserved domains on  [gi|189065499|dbj|BAG35338|]
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unnamed protein product [Homo sapiens]

Protein Classification

S8 family peptidase( domain architecture ID 11242990)

S8 family peptidase is a subtilisin-like serine protease containing a Asp/His/Ser catalytic triad that is not homologous to trypsin; similar to human neuroendocrine convertase 2 that is involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues

CATH:  3.40.50.200
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S8
PubMed:  8439290|9070434

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 145-440 5.18e-155

Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation.


:

Pssm-ID: 173789 [Multi-domain]  Cd Length: 297  Bit Score: 453.17  E-value: 5.18e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 145 FNDPKYPQQWHLNNRRS----PGRDINVTGVWERNVTGRGVTVVVVDDGVEHTIQDIAPNYSPEGSYDLNSNDPDPMPHP 220
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQaggtPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 221 DveNGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQINDIYSCSWGPDDDGKTVDGP 300
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 301 HQLGKAALQHGVIAGRQGFGSIFVVASGNGGQHNDNCNYDGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGDK 380
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189065499 381 M-LRSIVTTDWdlQKGTGCTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTAT 440
Cdd:cd04059  239 NpEASIVTTDL--GGNCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 525-612 7.33e-34

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.


:

Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 124.30  E-value: 7.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  525 LEHVAVTVSITHPRRGSLELKLFCPSGMMSLIGAPRSMDSDPNGFNDWTFSTVRCWGERARGTYRLVIRDVGDEsfQVGI 604
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG--DTGT 78


                  ....*...
gi 189065499  605 LRQWQLTL 612
Cdd:pfam01483  79 LNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 53-141 1.88e-14

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


:

Pssm-ID: 465126  Cd Length: 77  Bit Score: 68.79  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499   53 SWAVHLESLEGDGE---EETleqqadalaqaaGLVNAGRIGELQGHYLFVQP-AGHRPALEVEAirqqVEAVLAGHEAVR 128
Cdd:pfam16470   1 EWAVHLEGGPEEADriaEKH------------GFINLGQIGGLEDYYHFRHRrVSKRSKRSLRH----KHSRLKKDPKVK 64

                          90
                  ....*....|...
gi 189065499  129 WHSEQRLLRRAKR 141
Cdd:pfam16470  65 WAEQQRGKKRVKR 77
 
Name Accession Description Interval E-value
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 145-440 5.18e-155

Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation.


Pssm-ID: 173789 [Multi-domain]  Cd Length: 297  Bit Score: 453.17  E-value: 5.18e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 145 FNDPKYPQQWHLNNRRS----PGRDINVTGVWERNVTGRGVTVVVVDDGVEHTIQDIAPNYSPEGSYDLNSNDPDPMPHP 220
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQaggtPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 221 DveNGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQINDIYSCSWGPDDDGKTVDGP 300
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 301 HQLGKAALQHGVIAGRQGFGSIFVVASGNGGQHNDNCNYDGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGDK 380
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189065499 381 M-LRSIVTTDWdlQKGTGCTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTAT 440
Cdd:cd04059  239 NpEASIVTTDL--GGNCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 196-465 1.23e-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.


Pssm-ID: 395035 [Multi-domain]  Cd Length: 287  Bit Score: 156.47  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  196 DIAPNYSPEGSYDLNSNDPDPmpHPDVENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGP---LTDSMEAV 272
Cdd:pfam00082  25 DNDPSDDPEASVDFNNEWDDP--RDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGAKILGVRVFGDGggtDAITAQAI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  273 AFNKHyQINDIYSCSWGPDddgKTVDGPHQLGKAALQHGviaGRQGFGSIFVVASGNGGQhNDNCNYDGY--ANSIYTVT 350
Cdd:pfam00082 103 SWAIP-QGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGSP-GGNNGSSVGypAQYKNVIA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  351 IGAVDE--EGRMPFYAE---ECASMLAVTFS--------GGDKMLRSIVTTDWdlqkGTGCTEGHTGTSAAAPLAAGMIA 417
Cdd:pfam00082 175 VGAVDEasEGNLASFSSygpTLDGRLKPDIVapggnitgGNISSTLLTTTSDP----PNQGYDSMSGTSMATPHVAGAAA 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 189065499  418 LMLQVRPCLTWRDVQHIIVFTATRyedrraewvTNEAGFSHShqHGFG 465
Cdd:pfam00082 251 LLKQAYPNLTPETLKALLVNTATD---------LGDAGLDRL--FGYG 287
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 525-612 7.33e-34

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.


Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 124.30  E-value: 7.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  525 LEHVAVTVSITHPRRGSLELKLFCPSGMMSLIGAPRSMDSDPNGFNDWTFSTVRCWGERARGTYRLVIRDVGDEsfQVGI 604
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG--DTGT 78


                  ....*...
gi 189065499  605 LRQWQLTL 612
Cdd:pfam01483  79 LNSWQLTL 86
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 84-444 5.11e-28

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 118.28  E-value: 5.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  84 VNAGRIGELQGHYLFVQPAGHRPALEVEAIRQQVEAVLAGHEAVRWHSEQRLLRRAKRSVHFNDPKYPQQWHLNNRRSPG 163
Cdd:COG1404   29 AALLVVLAAGVAVAAAAAALVAAAAAAAVAAALAAPLAPAALAAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 164 RDINV----TGVwernvtgrgvtvvvvddgvEHTIQDIAPNYSpeGSYDLNSNDPDPMphpdveNGNHHGTRCAGEIAAV 239
Cdd:COG1404  109 AGVTVavidTGV-------------------DADHPDLAGRVV--GGYDFVDGDGDPS------DDNGHGTHVAGIIAAN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 240 PNNSFCAVGVAYGSRIAGIRVLD----GPLTDSMEAVAFNKHYQInDIYSCSWGPDDDGKTvDGPHQLGKAALQHGViag 315
Cdd:COG1404  162 GNNGGGVAGVAPGAKLLPVRVLDdngsGTTSDIAAAIDWAADNGA-DVINLSLGGPADGYS-DALAAAVDYAVDKGV--- 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 316 rqgfgsIFVVASGNGGQhNDNCNYD--GYANSIytvTIGAVDEEGRMPFYAeecASMLAVTFS--GGDkmlrsIVTTDwd 391
Cdd:COG1404  237 ------LVVAAAGNSGS-DDATVSYpaAYPNVI---AVGAVDANGQLASFS---NYGPKVDVAapGVD-----ILSTY-- 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189065499 392 lqKGTGcTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTATRYED 444
Cdd:COG1404  297 --PGGG-YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGA 346
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 53-141 1.88e-14

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


Pssm-ID: 465126  Cd Length: 77  Bit Score: 68.79  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499   53 SWAVHLESLEGDGE---EETleqqadalaqaaGLVNAGRIGELQGHYLFVQP-AGHRPALEVEAirqqVEAVLAGHEAVR 128
Cdd:pfam16470   1 EWAVHLEGGPEEADriaEKH------------GFINLGQIGGLEDYYHFRHRrVSKRSKRSLRH----KHSRLKKDPKVK 64

                          90
                  ....*....|...
gi 189065499  129 WHSEQRLLRRAKR 141
Cdd:pfam16470  65 WAEQQRGKKRVKR 77
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 228-510 8.53e-11

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]


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 64.27  E-value: 8.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  228 HGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLD--------GPLTDSMEAVAFNKHYQIN---DIYSCSWGpddDGKT 296
Cdd:TIGR03921  53 HGTLVAGIIAGRPGEGDGFSGVAPDARILPIRQTSaafepdegTSGVGDLGTLAKAIRRAADlgaDVINISLV---ACLP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  297 VDGPHQ---LGKA---ALQHGViagrqgfgsIFVVASGNGGQhNDNCNYDGY-ANSIYTVTIGAVDEEGrMPFYAEECAS 369
Cdd:TIGR03921 130 AGSGADdpeLGAAvryALDKGV---------VVVAAAGNTGG-DGQKTTVVYpAWYPGVLAVGSIDRDG-TPSSFSLPGP 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  370 MLAVTFSGGDkmlrsIVTTDWDlqkGTGcTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTAtryedRRAew 449
Cdd:TIGR03921 199 WVDLAAPGEN-----IVSLSPG---GDG-LATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEATA-----DHP-- 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189065499  450 vtneAGFSHSHQHGFGLLN-----AWRLVNAAKiwTSVPYLASYVSPVLKENKAIPQS--PRSLEVLW 510
Cdd:TIGR03921 263 ----ARGGRDDYVGYGVVDpvaalTGELPPEDG--RPLRPAPAPARPVAAPAPPPPPDdtPRGRVALW 324
 
Name Accession Description Interval E-value
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 145-440 5.18e-155

Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation.


Pssm-ID: 173789 [Multi-domain]  Cd Length: 297  Bit Score: 453.17  E-value: 5.18e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 145 FNDPKYPQQWHLNNRRS----PGRDINVTGVWERNVTGRGVTVVVVDDGVEHTIQDIAPNYSPEGSYDLNSNDPDPMPHP 220
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQaggtPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 221 DveNGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQINDIYSCSWGPDDDGKTVDGP 300
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 301 HQLGKAALQHGVIAGRQGFGSIFVVASGNGGQHNDNCNYDGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGDK 380
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189065499 381 M-LRSIVTTDWdlQKGTGCTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTAT 440
Cdd:cd04059  239 NpEASIVTTDL--GGNCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 196-465 1.23e-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.


Pssm-ID: 395035 [Multi-domain]  Cd Length: 287  Bit Score: 156.47  E-value: 1.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  196 DIAPNYSPEGSYDLNSNDPDPmpHPDVENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGP---LTDSMEAV 272
Cdd:pfam00082  25 DNDPSDDPEASVDFNNEWDDP--RDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGAKILGVRVFGDGggtDAITAQAI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  273 AFNKHyQINDIYSCSWGPDddgKTVDGPHQLGKAALQHGviaGRQGFGSIFVVASGNGGQhNDNCNYDGY--ANSIYTVT 350
Cdd:pfam00082 103 SWAIP-QGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGSP-GGNNGSSVGypAQYKNVIA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  351 IGAVDE--EGRMPFYAE---ECASMLAVTFS--------GGDKMLRSIVTTDWdlqkGTGCTEGHTGTSAAAPLAAGMIA 417
Cdd:pfam00082 175 VGAVDEasEGNLASFSSygpTLDGRLKPDIVapggnitgGNISSTLLTTTSDP----PNQGYDSMSGTSMATPHVAGAAA 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 189065499  418 LMLQVRPCLTWRDVQHIIVFTATRyedrraewvTNEAGFSHShqHGFG 465
Cdd:pfam00082 251 LLKQAYPNLTPETLKALLVNTATD---------LGDAGLDRL--FGYG 287
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 525-612 7.33e-34

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.


Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 124.30  E-value: 7.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  525 LEHVAVTVSITHPRRGSLELKLFCPSGMMSLIGAPRSMDSDPNGFNDWTFSTVRCWGERARGTYRLVIRDVGDEsfQVGI 604
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG--DTGT 78


                  ....*...
gi 189065499  605 LRQWQLTL 612
Cdd:pfam01483  79 LNSWQLTL 86
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 203-438 5.37e-30

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.


Pssm-ID: 173787 [Multi-domain]  Cd Length: 241  Bit Score: 118.84  E-value: 5.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 203 PEGSYDLNSNDPDPMPHPDVENGNHHGTRCAGEIAAVPNNSFCaVGVAYGSRIAGIRVLD----GPLTDSMEAVAFNKHY 278
Cdd:cd00306   21 FGGGDGGNDDDDNENGPTDPDDGNGHGTHVAGIIAASANNGGG-VGVAPGAKLIPVKVLDgdgsGSSSDIAAAIDYAAAD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 279 QINDIYSCSWGPDDDGKTVDGPHQLGKAALQHGVIagrqgfgsiFVVASGNGGQHNDNcNYDGYANSIYTVTIGAVDEEG 358
Cdd:cd00306  100 QGADVINLSLGGPGSPPSSALSEAIDYALAKLGVL---------VVAAAGNDGPDGGT-NIGYPAASPNVIAVGAVDRDG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 359 RMPFYAEECASMLAVTFSGGDkmlrsIVTTDWDlqkGTGCTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFT 438
Cdd:cd00306  170 TPASPSSNGGAGVDIAAPGGD-----ILSSPTT---GGGGYATLSGTSMAAPIVAGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 207-440 1.21e-28

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.


Pssm-ID: 173799 [Multi-domain]  Cd Length: 259  Bit Score: 115.37  E-value: 1.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 207 YDLNSNDPDPMPhpdvENGnhHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLD----GPLTDSMEAVAfnkhYQIN- 281
Cdd:cd07473   50 WNFVNNDNDPMD----DNG--HGTHVAGIIGAVGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAID----YAVDm 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 282 --DIYSCSWGPdddgktvDGPHQLGKAALQHGVIAgrqgfGSIFVVASGNGGQHNDN-----CNYDgYANSIytvTIGAV 354
Cdd:cd07473  120 gaKIINNSWGG-------GGPSQALRDAIARAIDA-----GILFVAAAGNDGTNNDKtptypASYD-LDNII---SVAAT 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 355 DEEGRMPfyaeecasmlavTFSG-----------GDKMLRSIVTTDWDLQkgtgcteghTGTSAAAPLAAGMIALMLQVR 423
Cdd:cd07473  184 DSNDALA------------SFSNygkktvdlaapGVDILSTSPGGGYGYM---------SGTSMATPHVAGAAALLLSLN 242

                        250
                 ....*....|....*..
gi 189065499 424 PCLTWRDVQHIIVFTAT 440
Cdd:cd07473  243 PNLTAAQIKDAILSSAD 259
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 199-435 1.47e-28

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.


Pssm-ID: 173822 [Multi-domain]  Cd Length: 242  Bit Score: 114.75  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 199 PNYSPEGSYDLNSNDPDPMPHPDVENGnhHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLD--GPLTDSMEAVAFNK 276
Cdd:cd07498   15 PDLSGKPKLVPGWNFVSNNDPTSDIDG--HGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRIADslGYAYWSDIAQAITW 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 277 HYQIN-DIYSCSWGPDDDGKTVdgphqlgKAALQHGVIAGRQGFGSIFVVASGNGGQHNDNcnydGYANSIYTVTIGAVD 355
Cdd:cd07498   93 AADNGaDVISNSWGGSDSTESI-------SSAIDNAATYGRNGKGGVVLFAAGNSGRSVSS----GYAANPSVIAVAATD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 356 EEGRMPFYAEEcASMLAVTFSGGDkmlrsIVTTD-WDLQKG---TGCTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDV 431
Cdd:cd07498  162 SNDARASYSNY-GNYVDLVAPGVG-----IWTTGtGRGSAGdypGGGYGSFSGTSFASPVAAGVAALILSANPNLTPAEV 235


                 ....
gi 189065499 432 QHII 435
Cdd:cd07498  236 EDIL 239
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 84-444 5.11e-28

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 118.28  E-value: 5.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  84 VNAGRIGELQGHYLFVQPAGHRPALEVEAIRQQVEAVLAGHEAVRWHSEQRLLRRAKRSVHFNDPKYPQQWHLNNRRSPG 163
Cdd:COG1404   29 AALLVVLAAGVAVAAAAAALVAAAAAAAVAAALAAPLAPAALAAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 164 RDINV----TGVwernvtgrgvtvvvvddgvEHTIQDIAPNYSpeGSYDLNSNDPDPMphpdveNGNHHGTRCAGEIAAV 239
Cdd:COG1404  109 AGVTVavidTGV-------------------DADHPDLAGRVV--GGYDFVDGDGDPS------DDNGHGTHVAGIIAAN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 240 PNNSFCAVGVAYGSRIAGIRVLD----GPLTDSMEAVAFNKHYQInDIYSCSWGPDDDGKTvDGPHQLGKAALQHGViag 315
Cdd:COG1404  162 GNNGGGVAGVAPGAKLLPVRVLDdngsGTTSDIAAAIDWAADNGA-DVINLSLGGPADGYS-DALAAAVDYAVDKGV--- 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 316 rqgfgsIFVVASGNGGQhNDNCNYD--GYANSIytvTIGAVDEEGRMPFYAeecASMLAVTFS--GGDkmlrsIVTTDwd 391
Cdd:COG1404  237 ------LVVAAAGNSGS-DDATVSYpaAYPNVI---AVGAVDANGQLASFS---NYGPKVDVAapGVD-----ILSTY-- 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189065499 392 lqKGTGcTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTATRYED 444
Cdd:COG1404  297 --PGGG-YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGA 346
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 204-440 2.82e-22

Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to 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). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.


Pssm-ID: 173794 [Multi-domain]  Cd Length: 267  Bit Score: 97.39  E-value: 2.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 204 EGSYDLNSNDPDPMPHPDVENgnhHGTRCAGEIAAVPNNSFcAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQIND- 282
Cdd:cd04848   27 EASYYVAVNDAGYASNGDGDS---HGTHVAGVIAAARDGGG-MHGVAPDATLYSARASASAGSTFSDADIAAAYDFLAAs 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 283 ---IYSCSWGPDDDGKTVDGPHQLGKAALQHGVIAGRQGF---GSIFVVASGNGGQHNDNCN-------YDGYANSIYTV 349
Cdd:cd04848  103 gvrIINNSWGGNPAIDTVSTTYKGSAATQGNTLLAALARAanaGGLFVFAAGNDGQANPSLAaaalpylEPELEGGWIAV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 350 tiGAVDEEGRMPFY--AEEC--ASMLAVTFSGGDkmlrsIVTTDWDLQKGTGcteGHTGTSAAAPLAAGMIALMLQVRPC 425
Cdd:cd04848  183 --VAVDPNGTIASYsySNRCgvAANWCLAAPGEN-----IYSTDPDGGNGYG---RVSGTSFAAPHVSGAAALLAQKFPW 252

                        250
                 ....*....|....*
gi 189065499 426 LTWRDVQHIIVFTAT 440
Cdd:cd04848  253 LTADQVRQTLLTTAT 267
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 146-441 3.93e-20

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.


Pssm-ID: 173810 [Multi-domain]  Cd Length: 260  Bit Score: 90.78  E-value: 3.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 146 NDPKYPQQWHLNNRRSP-------GRDINV----TGVwernvtgrgvtvvvvddgvehtiqdiAPNYsPE-------GSY 207
Cdd:cd07484    3 NDPYYSYQWNLDQIGAPkawditgGSGVTVavvdTGV--------------------------DPTH-PDllkvkfvLGY 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 208 DLNSNDPDPMPhpdvENGnhHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAfnkhyqiNDIYscs 287
Cdd:cd07484   56 DFVDNDSDAMD----DNG--HGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDANGSGSLADIA-------NGIR--- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 288 WGPDDDGKTVD----GPhqLGKAALQHGVI-AGRQgfGSIFVVASGNGGQhnDNCNYDgyANSIYTVTIGAVDEEGRMPF 362
Cdd:cd07484  120 YAADKGAKVINlslgGG--LGSTALQEAINyAWNK--GVVVVAAAGNEGV--SSVSYP--AAYPGAIAVAATDQDDKRAS 191

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189065499 363 YAEEcASMLAVTFSGGDkmlrsIVTTDWDlqkgtGCTEGHTGTSAAAPLAAGMIALMLQVRPcLTWRDVQHIIVFTATR 441
Cdd:cd07484  192 FSNY-GKWVDVSAPGGG-----ILSTTPD-----GDYAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDALKKTADD 258
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 199-427 1.02e-16

Peptidase S8 family domain, uncharacterized subfamily 13; 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.


Pssm-ID: 173820 [Multi-domain]  Cd Length: 285  Bit Score: 81.19  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 199 PNYSPEGSYDLNSNDPDPMPHP-DVENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVL---DGPLTDSMEAVAF 274
Cdd:cd07496   43 SDPTDPGDWVTGDDVPPGGFCGsGVSPSSWHGTHVAGTIAAVTNNGVGVAGVAWGARILPVRVLgkcGGTLSDIVDGMRW 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 275 nkhyqindiyscSWGPDDDGKTVD-----------GPHQLGKAALQHGVIAGRQGfGSIFVVASGNGGQHNDN---CNYD 340
Cdd:cd07496  123 ------------AAGLPVPGVPVNpnpakvinlslGGDGACSATMQNAINDVRAR-GVLVVVAAGNEGSSASVdapANCR 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 341 GyansiyTVTIGAVDEEGRMPFYAEeCASMLAVTFSGGDkmLRSIVTTDWDLQKGTGCTEGHT-------GTSAAAPLAA 413
Cdd:cd07496  190 G------VIAVGATDLRGQRASYSN-YGPAVDVSAPGGD--CASDVNGDGYPDSNTGTTSPGGstygflqGTSMAAPHVA 260

                        250
                 ....*....|....
gi 189065499 414 GMIALMLQVRPCLT 427
Cdd:cd07496  261 GVAALMKSVNPSLT 274
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 212-440 1.39e-16

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.


Pssm-ID: 173812 [Multi-domain]  Cd Length: 264  Bit Score: 80.32  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 212 NDPDPMPHPDVENGnhHGTRCAGEIA---AVPNNSFCavGVAYGSRIAGIRVLD----GPLTDSMEA----VAFNKHYQI 280
Cdd:cd07487   32 NTVNGRTTPYDDNG--HGTHVAGIIAgsgRASNGKYK--GVAPGANLVGVKVLDdsgsGSESDIIAGidwvVENNEKYNI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 281 NDI-----YSCSWGPDDDgKTVDGPHQLGKAalqhgviagrqgfGSIFVVASGNGGQHNDNCNYDGyaNSIYTVTIGAVD 355
Cdd:cd07487  108 RVVnlslgAPPDPSYGED-PLCQAVERLWDA-------------GIVVVVAAGNSGPGPGTITSPG--NSPKVITVGAVD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 356 EEGRMPFYAEECASmLAVTFSG---------GDKMLrSIVTTDWDLQKGTGCTEG-HTGTSAAAPLAAGMIALMLQVRPC 425
Cdd:cd07487  172 DNGPHDDGISYFSS-RGPTGDGrikpdvvapGENIV-SCRSPGGNPGAGVGSGYFeMSGTSMATPHVSGAIALLLQANPI 249

                        250
                 ....*....|....*
gi 189065499 426 LTWRDVQHIIVFTAT 440
Cdd:cd07487  250 LTPDEVKCILRDTAT 264
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 193-424 3.72e-15

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.


Pssm-ID: 173811 [Multi-domain]  Cd Length: 273  Bit Score: 76.37  E-value: 3.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 193 TIQDIAPNYSPEGsYDLNSNDPDPMPHP-----DVENGNHHGTRCAGEIAAVPNNSF------CAVGVAYGSRIAGIRVL 261
Cdd:cd07485   24 THPDLQGNGDGDG-YDPAVNGYNFVPNVgdidnDVSVGGGHGTHVAGTIAAVNNNGGgvggiaGAGGVAPGVKIMSIQIF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 262 DG--PLTDSMEAVAFnkhYQIND----IYSCSWGpdddGKTVDGPHQLGKAALQHGVIAGRQGF--GSIFVVASGN--GG 331
Cdd:cd07485  103 AGryYVGDDAVAAAI---VYAADngavILQNSWG----GTGGGIYSPLLKDAFDYFIENAGGSPldGGIVVFSAGNsyTD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 332 QHNDNCNYDGyansiyTVTIGAVDEEGRMPFYAEECASMlAVTFSGGDKMLRSIVTTDWDlqkGTGCTEGHTGTSAAAPL 411
Cdd:cd07485  176 EHRFPAAYPG------VIAVAALDTNDNKASFSNYGRWV-DIAAPGVGTILSTVPKLDGD---GGGNYEYLSGTSMAAPH 245

                        250
                 ....*....|...
gi 189065499 412 AAGMIALMLQVRP 424
Cdd:cd07485  246 VSGVAALVLSKFP 258
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 150-614 8.45e-15

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443962 [Multi-domain]  Cd Length: 641  Bit Score: 78.32  E-value: 8.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 150 YPQQWHLNNRRSPGRDINVTGVWERNVTGRGVTVVVVDDGVEHTIQDIAPNYSPEGSYDLNSNDPDPMPHPDVENGNHHG 229
Cdd:COG4935  222 GGAGLAAAGGGGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVG 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 230 TRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLDGPLTDSMEAVAFNKHYQINDIYSCSWGPDDDGKTVDGPHQLGKAALq 309
Cdd:COG4935  302 AAGTGNAAAAAAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAA- 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 310 hGVIAGRQGFGSIFVVASGNGGQHNDNCNYDGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGDKMLRSIVTTD 389
Cdd:COG4935  381 -AGAAAGAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTG 459

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 390 WDLQKGTGcteghTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTATRYEDRRAEWVTNEAGFSHSHQHGFGLLNa 469
Cdd:COG4935  460 SAAGAAGG-----TTTATSGLASSTTAAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTT- 533

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 470 wrlvnaakiwtsvpylasyvspvlkeNKAIPQSPRSlevlwNVSRmDLEMSGLKTLEHVAVTVSITHPRRGSLELKLFCP 549
Cdd:COG4935  534 --------------------------DVAIPDNGPA-----GVTS-TITVSGGGAVEDVTVTVDITHTYRGDLVITLISP 581

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189065499 550 SGMMSLIgAPRSMDSDPNGfnDWTFSTVRCWGERARGTYRLVIRDVGdeSFQVGILRQWQLTLYG 614
Cdd:COG4935  582 DGTTVVL-KNRSGGSADNI--NATFDVANFSGESANGTWTLRVVDTA--GGDTGTLNSWSLTFTG 641
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 205-440 1.47e-14

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.


Pssm-ID: 173800 [Multi-domain]  Cd Length: 295  Bit Score: 75.06  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 205 GSYDLNSNDPDPM---------PHPDVENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLD----GPLTDSMEA 271
Cdd:cd07474   32 GGYDFVDDDYDPMdtrpypsplGDASAGDATGHGTHVAGIIAGNGVNVGTIKGVAPKADLYAYKVLGpggsGTTDVIIAA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 272 V--AFNKHYQINDIYScswgpdddGKTVDGPHQLGKAALQHGVIAGrqgfgsIFVVAS-GNGGqhNDNCNYDGYANSIYT 348
Cdd:cd07474  112 IeqAVDDGMDVINLSL--------GSSVNGPDDPDAIAINNAVKAG------VVVVAAaGNSG--PAPYTIGSPATAPSA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 349 VTIGAVDeeGRMPFYAEECASMLAVTFSGGDKMLR--------SIVTTDwdlQKGTGCTEGHTGTSAAAPLAAGMIALML 420
Cdd:cd07474  176 ITVGAST--VADVAEADTVGPSSSRGPPTSDSAIKpdivapgvDIMSTA---PGSGTGYARMSGTSMAAPHVAGAAALLK 250

                        250       260
                 ....*....|....*....|
gi 189065499 421 QVRPCLTWRDVQHIIVFTAT 440
Cdd:cd07474  251 QAHPDWSPAQIKAALMNTAK 270
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 53-141 1.88e-14

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


Pssm-ID: 465126  Cd Length: 77  Bit Score: 68.79  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499   53 SWAVHLESLEGDGE---EETleqqadalaqaaGLVNAGRIGELQGHYLFVQP-AGHRPALEVEAirqqVEAVLAGHEAVR 128
Cdd:pfam16470   1 EWAVHLEGGPEEADriaEKH------------GFINLGQIGGLEDYYHFRHRrVSKRSKRSLRH----KHSRLKKDPKVK 64

                          90
                  ....*....|...
gi 189065499  129 WHSEQRLLRRAKR 141
Cdd:pfam16470  65 WAEQQRGKKRVKR 77
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 196-438 2.29e-13

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.


Pssm-ID: 173803 [Multi-domain]  Cd Length: 229  Bit Score: 70.25  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 196 DIAPNYspEGSYDLNSNDPDpmphpDVENGNHHGTRCAGEIAAVPNNsFCAVGVAYGSRIAGIRVLD----GPLTDSMEA 271
Cdd:cd07477   17 DLKLNI--VGGANFTGDDNN-----DYQDGNGHGTHVAGIIAALDNG-VGVVGVAPEADLYAVKVLNddgsGTYSDIIAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 272 V--AFNKHYqinDIYSCSWGPDDDGKTVdgpHQLGKAALQHGViagrqgfgsIFVVASGNGGQHNDNCNYDGYANSiyTV 349
Cdd:cd07477   89 IewAIENGM---DIINMSLGGPSDSPAL---REAIKKAYAAGI---------LVVAAAGNSGNGDSSYDYPAKYPS--VI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 350 TIGAVDEEGRMPFYAeecASMLAVTFSG-GDKMLRSIVTTDWDLQkgtgcteghTGTSAAAPLAAGMIALMLQVRPCLTW 428
Cdd:cd07477  152 AVGAVDSNNNRASFS---STGPEVELAApGVDILSTYPNNDYAYL---------SGTSMATPHVAGVAALVWSKRPELTN 219

                        250
                 ....*....|
gi 189065499 429 RDVQHIIVFT 438
Cdd:cd07477  220 AQVRQALNKT 229
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 204-475 9.19e-13

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.


Pssm-ID: 173814 [Multi-domain]  Cd Length: 312  Bit Score: 69.94  E-value: 9.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 204 EGSYDL--NSNDPDPMPHPDV----ENGnhHGTRCAGEIAAVPNNsFCAVGVAYGSRIAGIRVLD--GPLTDSMEAVAFN 275
Cdd:cd07489   42 AGGYDFvgDDYDGTNPPVPDDdpmdCQG--HGTHVAGIIAANPNA-YGFTGVAPEATLGAYRVFGcsGSTTEDTIIAAFL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 276 KHYQIN-DIYSCSWGpdddgktvdGPHQLGKAALqhGVIAGR-QGFGSIFVVASGNGGQhndncnyDG--YA----NSIY 347
Cdd:cd07489  119 RAYEDGaDVITASLG---------GPSGWSEDPW--AVVASRiVDAGVVVTIAAGNDGE-------RGpfYAsspaSGRG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 348 TVTIGAVDeegrmpfyaeecasmlaVTFS--GGDKMLR----------SIVTTdWDLQKGTGCTEghTGTSAAAPLAAGM 415
Cdd:cd07489  181 VIAVASVD-----------------SYFSswGPTNELYlkpdvaapggNILST-YPLAGGGYAVL--SGTSMATPYVAGA 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189065499 416 IALMLQVR-PCLTWRDVQHIIVFTAtryedRRAEWVTNEA---GFSHSHQHGFGLLNAWRLVNA 475
Cdd:cd07489  241 AALLIQARhGKLSPAELRDLLASTA-----KPLPWSDGTSalpDLAPVAQQGAGLVNAYKALYA 299
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 228-510 8.53e-11

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]


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 64.27  E-value: 8.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  228 HGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLD--------GPLTDSMEAVAFNKHYQIN---DIYSCSWGpddDGKT 296
Cdd:TIGR03921  53 HGTLVAGIIAGRPGEGDGFSGVAPDARILPIRQTSaafepdegTSGVGDLGTLAKAIRRAADlgaDVINISLV---ACLP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  297 VDGPHQ---LGKA---ALQHGViagrqgfgsIFVVASGNGGQhNDNCNYDGY-ANSIYTVTIGAVDEEGrMPFYAEECAS 369
Cdd:TIGR03921 130 AGSGADdpeLGAAvryALDKGV---------VVVAAAGNTGG-DGQKTTVVYpAWYPGVLAVGSIDRDG-TPSSFSLPGP 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499  370 MLAVTFSGGDkmlrsIVTTDWDlqkGTGcTEGHTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTAtryedRRAew 449
Cdd:TIGR03921 199 WVDLAAPGEN-----IVSLSPG---GDG-LATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEATA-----DHP-- 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189065499  450 vtneAGFSHSHQHGFGLLN-----AWRLVNAAKiwTSVPYLASYVSPVLKENKAIPQS--PRSLEVLW 510
Cdd:TIGR03921 263 ----ARGGRDDYVGYGVVDpvaalTGELPPEDG--RPLRPAPAPARPVAAPAPPPPPDdtPRGRVALW 324
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 218-439 1.72e-09

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.


Pssm-ID: 173819 [Multi-domain]  Cd Length: 298  Bit Score: 59.80  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 218 PHPDvENGnhHGT-RCAGEIAAVPNNSFCAVGvaygsriAGIRVLDGPLtdsmeaVAFNKHYQIN-DIYSCSWGPDDDGK 295
Cdd:cd07494   56 PACD-ENG--HGTgESANLFAIAPGAQFIGVK-------LGGPDLVNSV------GAFKKAISLSpDIISNSWGYDLRSP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 296 TVDGPHQLGKAA-LQHGVIAGRQGFGSIFVVASGNG-----GQHNDncnydgyansiyTVTIGAV--DEEGRMPfYAEEC 367
Cdd:cd07494  120 GTSWSRSLPNALkALAATLQDAVARGIVVVFSAGNGgwsfpAQHPE------------VIAAGGVfvDEDGARR-ASSYA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 368 ASMLAVTFSG----------GDK------ML-----RSIVTTDWDLQKGTGCTEG---HTGTSAAAPLAAGMIALMLQVR 423
Cdd:cd07494  187 SGFRSKIYPGrqvpdvcglvGMLphaaylMLpvppgSQLDRSCAAFPDGTPPNDGwgvFSGTSAAAPQVAGVCALMLQAN 266

                        250
                 ....*....|....*.
gi 189065499 424 PCLTWRDVQHIIVFTA 439
Cdd:cd07494  267 PGLSPERARSLLNKTA 282
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 206-427 4.70e-09

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.


Pssm-ID: 173815 [Multi-domain]  Cd Length: 254  Bit Score: 57.94  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 206 SYDLNSNDPDPMPHpdveNGNHHGTRCAGEIAaVPNNSFCAVGVAYGSRIAGIRVLDG------PLTDSME-AVAfnkhy 278
Cdd:cd07490   27 DFDENRRISATEVF----DAGGHGTHVSGTIG-GGGAKGVYIGVAPEADLLHGKVLDDgggslsQIIAGMEwAVE----- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 279 QINDIYSCSWGPDDdgkTVDGPhqlgkaaLQHGVIAGRQGFGSIFVVASGNGGQHNDNCNYDGYAnsiyTVTIGAVDEEG 358
Cdd:cd07490   97 KDADVVSMSLGGTY---YSEDP-------LEEAVEALSNQTGALFVVSAGNEGHGTSGSPGSAYA----ALSVGAVDRDD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 359 RMPFYaEECASMLAVTFSGGDKMLRSIVTTDWDLQ-----------KGTGCTEGHTGTSAAAPLAAGMIALMLQVRPCLT 427
Cdd:cd07490  163 EDAWF-SSFGSSGASLVSAPDSPPDEYTKPDVAAPgvdvysarqgaNGDGQYTRLSGTSMAAPHVAGVAALLAAAHPDLS 241
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 192-427 7.44e-08

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.


Pssm-ID: 173808 [Multi-domain]  Cd Length: 294  Bit Score: 54.68  E-value: 7.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 192 HTIQDIAPNYSPEGSYDLNSNDpDPMPHPDVENGNHHGTRCAGEIAAVPNNSfcavGVAYGSRIAGIRVLD----GPLTD 267
Cdd:cd07482   20 NSISSYSKNLVPKGGYDGKEAG-ETGDINDIVDKLGHGTAVAGQIAANGNIK----GVAPGIGIVSYRVFGscgsAESSW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 268 SMEAV--AFNKHyqiNDIYSCSWG-----PDDDGKTVDGPHQLGKA---ALQHGVI----AGRQG-----------FGSI 322
Cdd:cd07482   95 IIKAIidAADDG---VDVINLSLGgyliiGGEYEDDDVEYNAYKKAinyAKSKGSIvvaaAGNDGldvsnkqelldFLSS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 323 FVVASGNGGQhndncnYDGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGD-KMLRSIVTTDWDLQKG------ 395
Cdd:cd07482  172 GDDFSVNGEV------YDVPASLPNVITVSATDNNGNLSSFSNYGNSRIDLAAPGGDfLLLDQYGKEKWVNNGLmtkeqi 245

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 189065499 396 -----TGCTEGHTGTSAAAPLAAGMIALMLQVRPCLT 427
Cdd:cd07482  246 lttapEGGYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
 205-439 1.54e-07

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.


Pssm-ID: 173818 [Multi-domain]  Cd Length: 261  Bit Score: 53.46  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 205 GSYDLNSNDPDPMphpdvENGNHHGTRCAGEIAA-VPNNsfcAVGVAYGSR--------------------IAGIRVldg 263
Cdd:cd07493   31 GEYDFVDNSNNTN-----YTDDDHGTAVLSTMAGyTPGV---MVGTAPNASyylartedvasetpveednwVAAAEW--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 264 plTDSMEAVAFNKH--YQINDIYSCSWGPDD-DGKTVdgphQLGKAAlqhgVIAGRQGfgsIFVVAS-GNGGqhNDNCNY 339
Cdd:cd07493  100 --ADSLGVDIISSSlgYTTFDNPTYSYTYADmDGKTS----FISRAA----NIAASKG---MLVVNSaGNEG--STQWKG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 340 DGY-ANSIYTVTIGAVDEEGRMpfyaeecasmlaVTFSG----GDKMLRSIVTTdwdlqKGTGCTEGHT--------GTS 406
Cdd:cd07493  165 IGApADAENVLSVGAVDANGNK------------ASFSSigptADGRLKPDVMA-----LGTGIYVINGdgnityanGTS 227

                        250       260       270
                 ....*....|....*....|....*....|...
gi 189065499 407 AAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTA 439
Cdd:cd07493  228 FSCPLIAGLIACLWQAHPNWTNLQIKEAILKSA 260
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
 223-440 7.79e-07

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.


Pssm-ID: 173809 [Multi-domain]  Cd Length: 291  Bit Score: 51.60  E-value: 7.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 223 ENGNHHGTRCAGEIAAVPNNSFCAVGVAYGSRIAGIRVLdgPLTDSME---------AV---------AFNKHYQINDiy 284
Cdd:cd07483   82 ISDADHGTHVAGIIAAVRDNGIGIDGVADNVKIMPLRIV--PNGDERDkdianairyAVdngakvinmSFGKSFSPNK-- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 285 scswgpdddgKTVDgphQLGKAALQHGVIagrqgfgsiFVVASGNggQHNDNCNYDGYANSIYT---------VTIGAVD 355
Cdd:cd07483  158 ----------EWVD---DAIKYAESKGVL---------IVHAAGN--DGLDLDITPNFPNDYDKnggepannfITVGASS 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 356 EEGrmpfyaeecASMLAVTFSGGDKM--------LRSIVTTDWDlqkgtgCTEGHTGTSAAAPLAAGMIALMLQVRPCLT 427
Cdd:cd07483  214 KKY---------ENNLVANFSNYGKKnvdvfapgERIYSTTPDN------EYETDSGTSMAAPVVSGVAALIWSYYPNLT 278

                        250
                 ....*....|...
gi 189065499 428 WRDVQHIIVFTAT 440
Cdd:cd07483  279 AKEVKQIILESGV 291
Peptidases_S53 cd04056
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
 246-423 9.33e-07

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: 51.93  E-value: 9.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 246 AVGVAYGSRI----AGIRVLDGPLTDSMEAVAFNkhYQINDIYSCSWG------PDDDGKTVDgpHQLGKAALQhGViag 315
Cdd:cd04056   83 AGAIAPGANItlyfAPGTVTNGPLLAFLAAVLDN--PNLPSVISISYGepeqslPPAYAQRVC--NLFAQAAAQ-GI--- 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 316 rqgfgSIFVvASGNGG---QHNDNCNYDGYAN--------------SIYTVTIGAVDEEGR------------------- 359
Cdd:cd04056  155 -----TVLA-ASGDSGaggCGGDGSGTGFSVSfpasspyvtavggtTLYTGGTGSSAESTVwsseggwggsgggfsnyfp 228

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189065499 360 MPFYAEECASMLAVTFSGGDKMlRSI--VTTDWDLqkGTG---CTEGHT----GTSAAAPLAAGMIALMLQVR 423
Cdd:cd04056  229 RPSYQSGAVLGLPPSGLYNGSG-RGVpdVAANADP--GTGylvVVNGQWylvgGTSAAAPLFAGLIALINQAR 298
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 320-475 2.48e-06

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.


Pssm-ID: 173798 [Multi-domain]  Cd Length: 275  Bit Score: 49.98  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 320 GSIFVVASGNGGQhndncnYD---GYANSIYTVTIGAVDEEGRMPFyaEECASMLAVTFSGGDKMLRSivTTDWDLQK-- 394
Cdd:cd05562  123 GVLYFSSAGNDGQ------SGsifGHAAAPGAIAVGAVDYGNTPAF--GSDPAPGGTPSSFDPVGIRL--PTPEVRQKpd 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 395 ----------GTGCTEGH---TGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTATryeDRRaewvtnEAGFSHShq 461
Cdd:cd05562  193 vtapdgvngtVDGDGDGPpnfFGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTAL---DMG------EPGYDNA-- 261

                        170
                 ....*....|....
gi 189065499 462 HGFGLLNAWRLVNA 475
Cdd:cd05562  262 SGSGLVDADRAVAA 275
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 221-421 5.44e-06

Peptidase S8 family domain, uncharacterized subfamily 12; 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.


Pssm-ID: 173806 [Multi-domain]  Cd Length: 297  Bit Score: 48.91  E-value: 5.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 221 DVENGNHHGTRCAGEIA--AVPNNSfcaVGVAYGSRIAGIRVL-------DGPLTDSME-AVAFNKHyqindIYSCSWGP 290
Cdd:cd07480   41 DVQDGHGHGTHCAGTIFgrDVPGPR---YGVARGAEIALIGKVlgdggggDGGILAGIQwAVANGAD-----VISMSLGA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 291 DDDGKTVDG--PHQLGKAALQH------------GVIAGRQGF--GSIFVVASGNGGQHNDNCNYDG-YANSIYTVTIGA 353
Cdd:cd07480  113 DFPGLVDQGwpPGLAFSRALEAyrqrarlfdalmTLVAAQAALarGTLIVAAAGNESQRPAGIPPVGnPAACPSAMGVAA 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189065499 354 VDEEGRMPFYAEecasmlAVTFSGGDKML----RSIVTTdwdlqKGTGCTEGHTGTSAAAPLAAGMIALMLQ 421
Cdd:cd07480  193 VGALGRTGNFSA------VANFSNGEVDIaapgVDIVSA-----APGGGYRSMSGTSMATPHVAGVAALWAE 253
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 183-441 9.81e-06

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.


Pssm-ID: 173790 [Multi-domain]  Cd Length: 255  Bit Score: 47.90  E-value: 9.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 183 VVvvddgvehtIQDIAPNYS-PEGS------YDLNSNDPDpmphpdvENGNHHGTRCAGEIAAVpnnsfcAVGVAYGSRI 255
Cdd:cd04077   29 VY---------VLDTGIRTThVEFGgraiwgADFVGGDPD-------SDCNGHGTHVAGTVGGK------TYGVAKKANL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 256 AGIRVLD----GPLTDSMEAVAfnkhYQINDIYSC--------SWGPDDDgKTVDgphqlgkAALQHGVIAgrqgfGSIF 323
Cdd:cd04077   87 VAVKVLDcngsGTLSGIIAGLE----WVANDATKRgkpavanmSLGGGAS-TALD-------AAVAAAVNA-----GVVV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 324 VVASGNGGQhnDNCNYDGyANSIYTVTIGAVDEEGRMPFYAE--ECASMLAvtfSGGDkmlrsIVTTDWDlqkGTGCTEG 401
Cdd:cd04077  150 VVAAGNSNQ--DACNYSP-ASAPEAITVGATDSDDARASFSNygSCVDIFA---PGVD-----ILSAWIG---SDTATAT 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 189065499 402 HTGTSAAAPLAAGMIALMLQVRPCLTWRDVQHIIVFTATR 441
Cdd:cd04077  216 LSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLATK 255
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 320-420 6.38e-04

Peptidase S8 family domain, uncharacterized subfamily 2; 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.


Pssm-ID: 173813  Cd Length: 247  Bit Score: 42.07  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 320 GSIFVVASGNGGQHNDNCNY-DGYANSIYTVTIGAVDEEGRMPFYAEECASMLAVTFSGGDKMLrsIVTTDWDLQKGTGC 398
Cdd:cd07488  123 EVINVFSAGNQGKEKEKFGGiSIPTLAYNSIVVGSTDRNGDRFFASDVSNAGSEINSYGRRKVL--IVAPGSNYNLPDGK 200

                         90       100
                 ....*....|....*....|..
gi 189065499 399 TEGHTGTSAAAPLAAGMIALML 420
Cdd:cd07488  201 DDFVSGTSFSAPLVTGIIALLL 222
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 403-449 2.27e-03

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.


Pssm-ID: 173804 [Multi-domain]  Cd Length: 455  Bit Score: 41.06  E-value: 2.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189065499 403 TGTSAAAPLAAGMIALMLQ---VR---PCLTWRDVQHIIVFTATRYEDRR---AEW 449
Cdd:cd07478  397 SGTSVAAAIVAGACALLLQwgiVRgndPYLYGEKIKTYLIRGARRRPGDEypnPEW 452
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 183-421 5.25e-03

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


Pssm-ID: 173791 [Multi-domain]  Cd Length: 293  Bit Score: 39.62  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 183 VvvvddgvehTIQDIAPNYSPEGSYDLNSNDPDPmPH------------PDVENGnhHGTRCAGEIAAVPNNSFCAV--- 247
Cdd:cd04842   11 V---------GVADTGLDTNHCFFYDPNFNKTNL-FHrkivrydslsdtKDDVDG--HGTHVAGIIAGKGNDSSSISlyk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 248 GVAYGSRIAGIRVLDGPLTDSMEaVAFNKHYQ-IND----IYSCSWGPDDDG------KTVDgphqlgKAALQHgviagr 316
Cdd:cd04842   79 GVAPKAKLYFQDIGDTSGNLSSP-PDLNKLFSpMYDagarISSNSWGSPVNNgytllaRAYD------QFAYNN------ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 317 QGFgsIFVVASGNGGqhNDNCNYDGY-ANSIYTVTIGAVD----EEGRMPFYAEECASMLAVTFSGG---DKMLR----- 383
Cdd:cd04842  146 PDI--LFVFSAGNDG--NDGSNTIGSpATAKNVLTVGASNnpsvSNGEGGLGQSDNSDTVASFSSRGptyDGRIKpdlva 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 189065499 384 ---SIVTTDWDLQKGTGCTEGH----TGTSAAAPLAAGMIALMLQ 421
Cdd:cd04842  222 pgtGILSARSGGGGIGDTSDSAytskSGTSMATPLVAGAAALLRQ 266
Peptidase_S8_N pfam16361
N-terminal of Subtilase family; This is the N-terminal of Peptidase_S8 of subtilase family. It ...
 110-158 8.05e-03

N-terminal of Subtilase family; This is the N-terminal of Peptidase_S8 of subtilase family. It is around 100 residues in length from various Bacteroides species. The function of this family is unknown.


Pssm-ID: 435299  Cd Length: 142  Bit Score: 37.66  E-value: 8.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 189065499  110 VEAIRQQVEAvlAGHEAVRWHSEQRLLRRAKRSVHFNDPKYPQQWHLNN 158
Cdd:pfam16361  94 VEPVYRIKLA--AEESYTPAAAAAAAPAAAATEMPFNDPGLSQQWHYNN 140
Peptidases_S8_Subtilisin_like_2 cd04847
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 203-424 8.55e-03

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.


Pssm-ID: 173793 [Multi-domain]  Cd Length: 291  Bit Score: 38.82  E-value: 8.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 203 PEGSYDLNSNDPDPMPHPDVENGNH----HGTRCAGEI----AAVPNNSFcavgVAYGSRIAGIRVLD----------GP 264
Cdd:cd04847   11 NRGHPLLAPALAEDDLDSDEPGWTAddlgHGTAVAGLAlygdLTLPGNGL----PRPGCRLESVRVLPpngendpelyGD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 265 LT-DSMEAVAFNKHYqINDIYSCSWGPDDDGKTvDGPHQLGKA----ALQHGVIagrqgfgsiFVVASGNGGQHN--DNC 337
Cdd:cd04847   87 ITlRAIRRAVIQNPD-IVRVFNLSLGSPLPIDD-GRPSSWAAAldqlAAEYDVL---------FVVSAGNLGDDDaaDGP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189065499 338 NYDGY------ANSIYTVTIGAVDEEGRMPFYAEECASMLA-------------------VTFSGG----DKMLRSIVTT 388
Cdd:cd04847  156 PRIQDdeiedpADSVNALTVGAITSDDDITDRARYSAVGPApagattssgpgspgpikpdVVAFGGnlayDPSGNAADGD 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 189065499 389 DWDLQKGTGCTEGHT----GTSAAAPLAAGMIALMLQVRP 424
Cdd:cd04847  236 LSLLTTLSSPSGGGFvtvgGTSFAAPLAARLAAGLFAELP 275
 
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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