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Conserved domains on  [gi|568983154|ref|XP_006517217|]
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neuroendocrine convertase 1 isoform X1 [Mus musculus]

Protein Classification

neuroendocrine convertase 1( domain architecture ID 11243030)

neuroendocrine convertase 1 is an S8 family peptidase, containing an Asp/His/Ser catalytic triad that is not homologous to trypsin, 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:  3.4.21.93
Gene Symbol:  PCSK1
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S8
PubMed:  8439290|9070434
SCOP:  3000226

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 ...
 121-415 1.66e-176

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: 507.10  E-value: 1.66e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 121 FNDPMWNQQWYLQDTRMTAALPKLDLHVIPVWEKGITGKGVVITVLDDGLEWNHTDIYANYDPEASYDFNDNDHDPFPRY 200
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 201 DltNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRMLDGIVTDAIEASSIGFNPGHVDIYSASWGPNDDGKTVEGP 280
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 281 GRLAQKAFEYGVKQGRQGKGSIFVWASGNGGRQGDNCDCDGYTDSIYTISISSASQQGLSPWYAEKCSSTLATSYSSGDY 360
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983154 361 TDQR-ITSADLH--NDCTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTS 415
Cdd:cd04059  239 NPEAsIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTA 296
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 504-591 5.13e-35

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: 127.77  E-value: 5.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  504 LEHVQFEATIEYSRRGDLHVTLTSAVGTSTVLLAERERDTSPNGFKNWDFMSVHTWGENPVGTWTLKITDmsGRMQNEGR 583
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD--TAPGDTGT 78


                  ....*...
gi 568983154  584 IVNWKLIL 591
Cdd:pfam01483  79 LNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 34-110 6.54e-34

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: 124.25  E-value: 6.54e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983154   34 EWAAEIPGGQEAASAIAEELGYDLLGQIGSLENHYLFKHKSHPRRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR 110
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
Proho_convert pfam12177
Prohormone convertase enzyme; This domain family is found in eukaryotes, and is approximately ...
 713-751 3.61e-19

Prohormone convertase enzyme; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam01483, pfam00082. There are two completely conserved residues (Y and D) that may be functionally important. This protein is the C terminal domain of a prohormone convertase enzyme which targets hormones in dense core secretory granules. This C terminal tail domain is the domain responsible for targeting these dense core secretory granules. The domain adopts an alpha helical structure.


:

Pssm-ID: 463483  Cd Length: 39  Bit Score: 80.94  E-value: 3.61e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568983154  713 LEGSEDSLYSDYVDVFYNTKPYKHRDDRLLQALMDILNE 751
Cdd:pfam12177   1 YRGPEDSLYSDYSDGFYNTKPYRHRDDRLLQALFDMLDD 39
 
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 ...
 121-415 1.66e-176

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: 507.10  E-value: 1.66e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 121 FNDPMWNQQWYLQDTRMTAALPKLDLHVIPVWEKGITGKGVVITVLDDGLEWNHTDIYANYDPEASYDFNDNDHDPFPRY 200
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 201 DltNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRMLDGIVTDAIEASSIGFNPGHVDIYSASWGPNDDGKTVEGP 280
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 281 GRLAQKAFEYGVKQGRQGKGSIFVWASGNGGRQGDNCDCDGYTDSIYTISISSASQQGLSPWYAEKCSSTLATSYSSGDY 360
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983154 361 TDQR-ITSADLH--NDCTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTS 415
Cdd:cd04059  239 NPEAsIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTA 296
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 158-442 3.61e-67

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: 223.49  E-value: 3.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  158 GKGVVITVLDDGLEWNHTDIYANYDPEASYD----FNDNDHDPFPRYDLTNENKHGTRCAGEIAMQANNHKCGVGVAYNS 233
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDpeasVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  234 KVGGIRML-DGIVTDAIEASSIGFN-PGHVDIYSASWGPNddgKTVEGPGRLAQKAFEYGvkqGRQGKGSIFVWASGNGG 311
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  312 RQGDNCDCDGY-TDSIYTISISSASQqglspwyaekCSSTLATSYSS-----------------------GDYTDQRITS 367
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVDE----------ASEGNLASFSSygptldgrlkpdivapggnitggNISSTLLTTT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568983154  368 ADLHNDCTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTSEYDPlasnpgwkkngaGLMVNSRFGFG 442
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLG------------DAGLDRLFGYG 287
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 504-591 5.13e-35

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: 127.77  E-value: 5.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  504 LEHVQFEATIEYSRRGDLHVTLTSAVGTSTVLLAERERDTSPNGFKNWDFMSVHTWGENPVGTWTLKITDmsGRMQNEGR 583
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD--TAPGDTGT 78


                  ....*...
gi 568983154  584 IVNWKLIL 591
Cdd:pfam01483  79 LNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 34-110 6.54e-34

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: 124.25  E-value: 6.54e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983154   34 EWAAEIPGGQEAASAIAEELGYDLLGQIGSLENHYLFKHKSHPRRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR 110
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 139-458 7.72e-34

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 135.61  E-value: 7.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 139 AALPKLDLHVIPVWEKGITGKGVVITVLDDGLEWNHTDIYANYDpeASYDFNDNDHDPfprydlTNENKHGTRCAGEIAM 218
Cdd:COG1404   89 AQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVV--GGYDFVDGDGDP------SDDNGHGTHVAGIIAA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 219 QANNHKCGVGVAYNSKVGGIRMLDG-------IVTDAIE-ASSIGfnpghVDIYSASWGPNDDGKTvegpgRLAQKAFEY 290
Cdd:COG1404  161 NGNNGGGVAGVAPGAKLLPVRVLDDngsgttsDIAAAIDwAADNG-----ADVINLSLGGPADGYS-----DALAAAVDY 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 291 GVkqgrqGKGSIFVWASGNGGrqgDNCDCDGYTDSIY-TISISSASQQGlspwyaekcssTLAtSYSS-GDYTD-----Q 363
Cdd:COG1404  231 AV-----DKGVLVVAAAGNSG---SDDATVSYPAAYPnVIAVGAVDANG-----------QLA-SFSNyGPKVDvaapgV 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 364 RITSADLHNDcTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTSEYDPLASNpgwkKNGAGLMVNSRFGFGL 443
Cdd:COG1404  291 DILSTYPGGG-YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGP----YYGYGLLADGAAGATS 365

                        330
                 ....*....|....*
gi 568983154 444 LNAKALVDLADPRTW 458
Cdd:COG1404  366 AGAGLAAAAGAAGAA 380
Proho_convert pfam12177
Prohormone convertase enzyme; This domain family is found in eukaryotes, and is approximately ...
 713-751 3.61e-19

Prohormone convertase enzyme; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam01483, pfam00082. There are two completely conserved residues (Y and D) that may be functionally important. This protein is the C terminal domain of a prohormone convertase enzyme which targets hormones in dense core secretory granules. This C terminal tail domain is the domain responsible for targeting these dense core secretory granules. The domain adopts an alpha helical structure.


Pssm-ID: 463483  Cd Length: 39  Bit Score: 80.94  E-value: 3.61e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568983154  713 LEGSEDSLYSDYVDVFYNTKPYKHRDDRLLQALMDILNE 751
Cdd:pfam12177   1 YRGPEDSLYSDYSDGFYNTKPYRHRDDRLLQALFDMLDD 39
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 49-407 6.83e-06

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 49.58  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  49 IAEELGYDLLGQIGSLENHYLFKHKSHPRRSRRSALHITKRLSDDDRVTWAEQQYEKERSKRSvqkdsaldLFNDPMWNQ 128
Cdd:PTZ00262 223 VIWESGMDDMIPIKEEGHIRGEAPVRNGNSLRGNSSNYDDHPGSDGSFSLSNQMAFNNFLGKY--------QFNDEGRNL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 129 QWYLQDTRMTAALPKLDLHVIPVwekgitgkgVVITVLDDGLEWNHTDIYANY---------------------DPEASY 187
Cdd:PTZ00262 295 QWGLDLTRLDETQELIEPHEVND---------TNICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGA 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 188 DFNDNDHDPFprydltNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVggirmldgIVTDAIEASSIGFNPghvDIYSA- 266
Cdd:PTZ00262 366 NFVNNDGGPM------DDNYHGTHVSGIISAIGNNNIGIVGVDKRSKL--------IICKALDSHKLGRLG---DMFKCf 428

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 267 SWGPNDDGKTVEGPGRLAQKA--FEYGVKQGRQgKGSIFVWASGN----GGRQGDNCDCDGYTDSIY----------TIS 330
Cdd:PTZ00262 429 DYCISREAHMINGSFSFDEYSgiFNESVKYLEE-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYppilskklrnVIT 507

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983154 331 ISSASQQgLSPWYAEKCSSTLATSYSSGDYTDQRITSADLHNDCTEThTGTSASAPLAAGIFALALEANPNLTWRDM 407
Cdd:PTZ00262 508 VSNLIKD-KNNQYSLSPNSFYSAKYCQLAAPGTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
 
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 ...
 121-415 1.66e-176

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: 507.10  E-value: 1.66e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 121 FNDPMWNQQWYLQDTRMTAALPKLDLHVIPVWEKGITGKGVVITVLDDGLEWNHTDIYANYDPEASYDFNDNDHDPFPRY 200
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 201 DltNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRMLDGIVTDAIEASSIGFNPGHVDIYSASWGPNDDGKTVEGP 280
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 281 GRLAQKAFEYGVKQGRQGKGSIFVWASGNGGRQGDNCDCDGYTDSIYTISISSASQQGLSPWYAEKCSSTLATSYSSGDY 360
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568983154 361 TDQR-ITSADLH--NDCTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTS 415
Cdd:cd04059  239 NPEAsIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTA 296
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 158-442 3.61e-67

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: 223.49  E-value: 3.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  158 GKGVVITVLDDGLEWNHTDIYANYDPEASYD----FNDNDHDPFPRYDLTNENKHGTRCAGEIAMQANNHKCGVGVAYNS 233
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDpeasVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  234 KVGGIRML-DGIVTDAIEASSIGFN-PGHVDIYSASWGPNddgKTVEGPGRLAQKAFEYGvkqGRQGKGSIFVWASGNGG 311
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  312 RQGDNCDCDGY-TDSIYTISISSASQqglspwyaekCSSTLATSYSS-----------------------GDYTDQRITS 367
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVDE----------ASEGNLASFSSygptldgrlkpdivapggnitggNISSTLLTTT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568983154  368 ADLHNDCTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTSEYDPlasnpgwkkngaGLMVNSRFGFG 442
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLG------------DAGLDRLFGYG 287
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 504-591 5.13e-35

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: 127.77  E-value: 5.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  504 LEHVQFEATIEYSRRGDLHVTLTSAVGTSTVLLAERERDTSPNGFKNWDFMSVHTWGENPVGTWTLKITDmsGRMQNEGR 583
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD--TAPGDTGT 78


                  ....*...
gi 568983154  584 IVNWKLIL 591
Cdd:pfam01483  79 LNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 34-110 6.54e-34

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: 124.25  E-value: 6.54e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983154   34 EWAAEIPGGQEAASAIAEELGYDLLGQIGSLENHYLFKHKSHPRRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR 110
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 139-458 7.72e-34

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 135.61  E-value: 7.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 139 AALPKLDLHVIPVWEKGITGKGVVITVLDDGLEWNHTDIYANYDpeASYDFNDNDHDPfprydlTNENKHGTRCAGEIAM 218
Cdd:COG1404   89 AQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVV--GGYDFVDGDGDP------SDDNGHGTHVAGIIAA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 219 QANNHKCGVGVAYNSKVGGIRMLDG-------IVTDAIE-ASSIGfnpghVDIYSASWGPNDDGKTvegpgRLAQKAFEY 290
Cdd:COG1404  161 NGNNGGGVAGVAPGAKLLPVRVLDDngsgttsDIAAAIDwAADNG-----ADVINLSLGGPADGYS-----DALAAAVDY 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 291 GVkqgrqGKGSIFVWASGNGGrqgDNCDCDGYTDSIY-TISISSASQQGlspwyaekcssTLAtSYSS-GDYTD-----Q 363
Cdd:COG1404  231 AV-----DKGVLVVAAAGNSG---SDDATVSYPAAYPnVIAVGAVDANG-----------QLA-SFSNyGPKVDvaapgV 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 364 RITSADLHNDcTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLVVWTSEYDPLASNpgwkKNGAGLMVNSRFGFGL 443
Cdd:COG1404  291 DILSTYPGGG-YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGP----YYGYGLLADGAAGATS 365

                        330
                 ....*....|....*
gi 568983154 444 LNAKALVDLADPRTW 458
Cdd:COG1404  366 AGAGLAAAAGAAGAA 380
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 161-406 8.62e-33

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: 127.07  E-value: 8.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 161 VVITVLDDGLEWNHTDIYANYDPEASYDFNDNDHDPFprydltNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRM 240
Cdd:cd07498    1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPTS------DIDGHGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 241 LDGIVTDAIEASSIGFN----PGhVDIYSASWGPNDDGKTVEgpgrlaqKAFEYGVKQGRQGKGSIFVWASGNGGRQGDN 316
Cdd:cd07498   75 ADSLGYAYWSDIAQAITwaadNG-ADVISNSWGGSDSTESIS-------SAIDNAATYGRNGKGGVVLFAAGNSGRSVSS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 317 cdcdGYTDSIYTISISSASQQGLSPWYAEKCSSTLATSYSSGDYTDQRITSADLHN--DCTETHTGTSASAPLAAGIFAL 394
Cdd:cd07498  147 ----GYAANPSVIAVAATDSNDARASYSNYGNYVDLVAPGVGIWTTGTGRGSAGDYpgGGYGSFSGTSFASPVAAGVAAL 222

                        250
                 ....*....|..
gi 568983154 395 ALEANPNLTWRD 406
Cdd:cd07498  223 ILSANPNLTPAE 234
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 161-414 5.11e-29

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: 116.15  E-value: 5.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 161 VVITVLDDGLEWNHTDIYANYDPEA-SYDFNDNDHDPFPRYDltnENKHGTRCAGEIAMQANNHKcGVGVAYNSKVGGIR 239
Cdd:cd00306    1 VTVAVIDTGVDPDHPDLDGLFGGGDgGNDDDDNENGPTDPDD---GNGHGTHVAGIIAASANNGG-GVGVAPGAKLIPVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 240 MLD----GIVTDAIEASSIGFNPGHVDIYSASWGPNDDGktvegPGRLAQKAFEYGVKQgrqgKGSIFVWASGNGGrQGD 315
Cdd:cd00306   77 VLDgdgsGSSSDIAAAIDYAAADQGADVINLSLGGPGSP-----PSSALSEAIDYALAK----LGVLVVAAAGNDG-PDG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 316 NCDCDGYTDSIYTISISSASQQGlspwyaekcssTLATSYSS-GDYTD-----QRITSADLH-NDCTETHTGTSASAPLA 388
Cdd:cd00306  147 GTNIGYPAASPNVIAVGAVDRDG-----------TPASPSSNgGAGVDiaapgGDILSSPTTgGGGYATLSGTSMAAPIV 215

                        250       260
                 ....*....|....*....|....*.
gi 568983154 389 AGIFALALEANPNLTWRDMQHLVVWT 414
Cdd:cd00306  216 AGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 159-406 5.80e-23

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: 98.80  E-value: 5.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 159 KGVVITVLDDGLEWNHTD----IYANYDPEAS----------------YDFNDNDHDPFPrydltnENKHGTRCAGEIAM 218
Cdd:cd07473    2 GDVVVAVIDTGVDYNHPDlkdnMWVNPGEIPGngidddgngyvddiygWNFVNNDNDPMD------DNGHGTHVAGIIGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 219 QANNHKCGVGVAYNSKVGGIRMLD----GIVTDAIEASSIGFNPGhVDIYSASWGPnddgktvEGPGRLAQKAFEYGVKq 294
Cdd:cd07473   76 VGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAIDYAVDMG-AKIINNSWGG-------GGPSQALRDAIARAID- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 295 grqgKGSIFVWASGNGGRqgdNCDCDGYTDSIYT----ISISSASQQGlspwyaekcssTLATSYSSGDYT-D-----QR 364
Cdd:cd07473  147 ----AGILFVAAAGNDGT---NNDKTPTYPASYDldniISVAATDSND-----------ALASFSNYGKKTvDlaapgVD 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568983154 365 ITSADLhNDCTETHTGTSASAPLAAGIFALALEANPNLTWRD 406
Cdd:cd07473  209 ILSTSP-GGGYGYMSGTSMATPHVAGAAALLLSLNPNLTAAQ 249
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 122-400 3.47e-22

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: 96.56  E-value: 3.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 122 NDPMWNQQWYLQDTRMTAAlpkldlhvipvWEKgITGKGVVITVLDDGLEWNHTDIyANYDPEASYDFNDNDHDPfpryd 201
Cdd:cd07484    3 NDPYYSYQWNLDQIGAPKA-----------WDI-TGGSGVTVAVVDTGVDPTHPDL-LKVKFVLGYDFVDNDSDA----- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 202 lTNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRMLD----GIVTDAIEAssIGFNPGH-VDIYSASWGPNddgkt 276
Cdd:cd07484   65 -MDDNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANG--IRYAADKgAKVINLSLGGG----- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 277 veGPGRLAQKAFEYGVKqgrqgKGSIFVWASGNGGRQgdncDCDGYTDSIYTISISSASQQGlspwyaekcssTLAtSYS 356
Cdd:cd07484  137 --LGSTALQEAINYAWN-----KGVVVVAAAGNEGVS----SVSYPAAYPGAIAVAATDQDD-----------KRA-SFS 193

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568983154 357 S-GDYTD-----QRITSADLHNDcTETHTGTSASAPLAAGIFALALEANP 400
Cdd:cd07484  194 NyGKWVDvsapgGGILSTTPDGD-YAYMSGTSMATPHVAGVAALLYSQGP 242
Proho_convert pfam12177
Prohormone convertase enzyme; This domain family is found in eukaryotes, and is approximately ...
 713-751 3.61e-19

Prohormone convertase enzyme; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam01483, pfam00082. There are two completely conserved residues (Y and D) that may be functionally important. This protein is the C terminal domain of a prohormone convertase enzyme which targets hormones in dense core secretory granules. This C terminal tail domain is the domain responsible for targeting these dense core secretory granules. The domain adopts an alpha helical structure.


Pssm-ID: 463483  Cd Length: 39  Bit Score: 80.94  E-value: 3.61e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568983154  713 LEGSEDSLYSDYVDVFYNTKPYKHRDDRLLQALMDILNE 751
Cdd:pfam12177   1 YRGPEDSLYSDYSDGFYNTKPYRHRDDRLLQALFDMLDD 39
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 158-403 1.60e-18

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: 86.62  E-value: 1.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 158 GKGVVITVLDDGLEWNHTDIYANYDPEAS----YDFNDNDHDPFPRYDLTNENK---------HGTRCAGEIAMQANNHK 224
Cdd:cd07474    1 GKGVKVAVIDTGIDYTHPDLGGPGFPNDKvkggYDFVDDDYDPMDTRPYPSPLGdasagdatgHGTHVAGIIAGNGVNVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 225 CGVGVAYNSKVGGIRMLD-------GIVTDAIEASsigFNPGhVDIYSASWGPNddgktVEGPGRLAQKAFEYGVKQGrq 297
Cdd:cd07474   81 TIKGVAPKADLYAYKVLGpggsgttDVIIAAIEQA---VDDG-MDVINLSLGSS-----VNGPDDPDAIAINNAVKAG-- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 298 gkgsIFVWASGngGRQGDNCDCDGyTDSIYTISISSASQQGLSPWYAEkcssTLATSYSSGDYTDQRITSADL------- 370
Cdd:cd07474  150 ----VVVVAAA--GNSGPAPYTIG-SPATAPSAITVGASTVADVAEAD----TVGPSSSRGPPTSDSAIKPDIvapgvdi 218

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568983154 371 ------HNDCTETHTGTSASAPLAAGIFALALEANPNLT 403
Cdd:cd07474  219 mstapgSGTGYARMSGTSMAAPHVAGAAALLKQAHPDWS 257
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 157-403 2.04e-17

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: 82.76  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 157 TGKGVVITVLDDGLEWNHTDIYANYDPeASYDFNDNDHDPFPRYDltnENKHGTRCAGEIAMQANNHKCGvGVAYNSKVG 236
Cdd:cd04848    1 TGAGVKVGVIDSGIDLSHPEFAGRVSE-ASYYVAVNDAGYASNGD---GDSHGTHVAGVIAAARDGGGMH-GVAPDATLY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 237 GIRMLDG---IVTDAIEASSIGFNPGH-VDIYSASWGPNDDGKTVEGPGRL---AQKAFEYGVKQGRQGKGSIFVWASGN 309
Cdd:cd04848   76 SARASASagsTFSDADIAAAYDFLAASgVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVFAAGN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 310 GGR--QGDNCDCDGYT--------------DSIYTISISSASQQGLSpwYAEKCSSTLATSYSSgdytdqriTSADLHND 373
Cdd:cd04848  156 DGQanPSLAAAALPYLepeleggwiavvavDPNGTIASYSYSNRCGV--AANWCLAAPGENIYS--------TDPDGGNG 225

                        250       260       270
                 ....*....|....*....|....*....|
gi 568983154 374 CTeTHTGTSASAPLAAGIFALALEANPNLT 403
Cdd:cd04848  226 YG-RVSGTSFAAPHVSGAAALLAQKFPWLT 254
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 150-401 2.22e-17

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: 82.92  E-value: 2.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 150 PVWEKGITGKGVVITVLDDGLEWNHTDIYANYDPEAsYDFNDNDHDP-FPRYDLTNE----NKHGTRCAGEIAmQANNHK 224
Cdd:cd07485    1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDG-YDPAVNGYNFvPNVGDIDNDvsvgGGHGTHVAGTIA-AVNNNG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 225 CGVG-------VAYNSKVGGIRMLDGI--VTDAIEASSI--GFNPGHVdIYSASWGpnddGKTVEGPGRLAQKAFEYGVK 293
Cdd:cd07485   79 GGVGgiagaggVAPGVKIMSIQIFAGRyyVGDDAVAAAIvyAADNGAV-ILQNSWG----GTGGGIYSPLLKDAFDYFIE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 294 QGRQG--KGSIFVWASGNggrqgDNCDCDGYTDSIYTISISSASQQGLSPwyaekcsstlaTSYSS-GDYTD------QR 364
Cdd:cd07485  154 NAGGSplDGGIVVFSAGN-----SYTDEHRFPAAYPGVIAVAALDTNDNK-----------ASFSNyGRWVDiaapgvGT 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 568983154 365 ITSADLHNDCT-----ETHTGTSASAPLAAGIFALALEANPN 401
Cdd:cd07485  218 ILSTVPKLDGDgggnyEYLSGTSMAAPHVSGVAALVLSKFPD 259
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 160-403 5.38e-17

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: 80.65  E-value: 5.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 160 GVVITVLDDGLEWNHTDIYANYdpEASYDFNDNDHDPFprydlTNENKHGTRCAGEIAMQaNNHKCGVGVAYNSKVGGIR 239
Cdd:cd07477    1 GVKVAVIDTGIDSSHPDLKLNI--VGGANFTGDDNNDY-----QDGNGHGTHVAGIIAAL-DNGVGVVGVAPEADLYAVK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 240 MLD--GI-----VTDAIEASSIgfnpGHVDIYSASWGPNDDGKTVegpgrlaQKAFEYGVKQGrqgkgsIF-VWASGNGG 311
Cdd:cd07477   73 VLNddGSgtysdIIAGIEWAIE----NGMDIINMSLGGPSDSPAL-------REAIKKAYAAG------ILvVAAAGNSG 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 312 RQGDNCDCDGYTDSiyTISISSASQqglspwyaekcSSTLATSYSSGDYTD-----QRITSADLHNDCTEThTGTSASAP 386
Cdd:cd07477  136 NGDSSYDYPAKYPS--VIAVGAVDS-----------NNNRASFSSTGPEVElaapgVDILSTYPNNDYAYL-SGTSMATP 201

                        250
                 ....*....|....*..
gi 568983154 387 LAAGIFALALEANPNLT 403
Cdd:cd07477  202 HVAGVAALVWSKRPELT 218
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 160-403 1.25e-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: 80.80  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 160 GVVITVLDDGLEWNHTDI----YANYD----PEASYDFNDNDHDP----------------FPRYDLTNENKHGTRCAGE 215
Cdd:cd07496    1 GVVVAVLDTGVLFHHPDLagvlLPGYDfisdPAIANDGDGRDSDPtdpgdwvtgddvppggFCGSGVSPSSWHGTHVAGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 216 IAMQANNHKcGV-GVAYNSKVGGIRML---DGIVTDAIEA---------SSIGFNPGHVDIYSASWGpnddgktveGPGR 282
Cdd:cd07496   81 IAAVTNNGV-GVaGVAWGARILPVRVLgkcGGTLSDIVDGmrwaaglpvPGVPVNPNPAKVINLSLG---------GDGA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 283 L---AQKAFEYGVKqgrqgKGSIFVWASGNGGrqGDNC-----DCDGytdsiyTISISSASQQGLSPWYAEKCSS----- 349
Cdd:cd07496  151 CsatMQNAINDVRA-----RGVLVVVAAGNEG--SSASvdapaNCRG------VIAVGATDLRGQRASYSNYGPAvdvsa 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568983154 350 ----TLATSYSSGDYTDQRITSADlhNDCTETH-TGTSASAPLAAGIFALALEANPNLT 403
Cdd:cd07496  218 pggdCASDVNGDGYPDSNTGTTSP--GGSTYGFlQGTSMAAPHVAGVAALMKSVNPSLT 274
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 153-449 4.17e-15

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: 76.87  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 153 EKGITGKGVVITVLDDGLEWNHTD----IYANYDPEASYDF----NDNDHDPFPRYDLTNENKHGTRCAGEIAMQANNHK 224
Cdd:cd07489    7 AEGITGKGVKVAVVDTGIDYTHPAlggcFGPGCKVAGGYDFvgddYDGTNPPVPDDDPMDCQGHGTHVAGIIAANPNAYG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 225 CgVGVAYNSKVGGIRMLD--GIVTDA--IEASSIGFNPGhVDIYSASWGpnDDGKTVEGPG-----RLAQkafeygvkqg 295
Cdd:cd07489   87 F-TGVAPEATLGAYRVFGcsGSTTEDtiIAAFLRAYEDG-ADVITASLG--GPSGWSEDPWavvasRIVD---------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 296 rqgKGSIFVWASGNGGRQGdncdcDGYTDS----IYTISISSAsqqglspwyaekcSSTLaTSY-SSGDYTDQ------- 363
Cdd:cd07489  153 ---AGVVVTIAAGNDGERG-----PFYASSpasgRGVIAVASV-------------DSYF-SSWgPTNELYLKpdvaapg 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 364 -RITSADLHN-DCTETHTGTSASAPLAAGIFALALEA-NPNLTWRDMQHLVVWTSeyDPLASNPGwKKNGAGLMVNSRFG 440
Cdd:cd07489  211 gNILSTYPLAgGGYAVLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTA--KPLPWSDG-TSALPDLAPVAQQG 287

                        330
                 ....*....|
gi 568983154 441 FGLLNA-KAL 449
Cdd:cd07489  288 AGLVNAyKAL 297
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 155-593 5.77e-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: 78.71  E-value: 5.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 155 GITGKGVVITVLDDGLEWNHTDIYANYDPEASYDFNDNDHDPFPRYDLTNENKHGTRCAGEIAMQANNHKCGVGVAYNSK 234
Cdd:COG4935  205 GGGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGV 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 235 VGGIRMLDGIVTDAIEASSIGFNPGHVDIYSASWGPNDDGKTVEGPGRLAQKAFEYGVKQGRQGKGSIFVWASGNGGRQG 314
Cdd:COG4935  285 VGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAA 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 315 DNCDCDGYTDSIYTISISSASQQGLSPWYAEKCSSTLATSYSSGDYTDQRITSADLHNDCTETHTGTSASAPLAAGIFAL 394
Cdd:COG4935  365 AAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATG 444

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 395 ALEANPNLTWRDMQHLVVWTSEYDPLASNP--GWKKNGAGLMVNSRFGFGLLNAKALVDLADPRTWRNVPEKKECVVKDN 472
Cdd:COG4935  445 LGGGADAGSTSTGTGSAAGAAGGTTTATSGlaSSTTAAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTN 524

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 473 NFEPRALKANgeviVEIPTRACEGQENAI-----KSLEHVQFEATIEYSRRGDLHVTLTSAVGTsTVLLAERERDTSPNG 547
Cdd:COG4935  525 STATFSNTTD----VAIPDNGPAGVTSTItvsggGAVEDVTVTVDITHTYRGDLVITLISPDGT-TVVLKNRSGGSADNI 599

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 568983154 548 fkNWDFMSVHTWGENPVGTWTLKITDMSGrmQNEGRIVNWKLILHG 593
Cdd:COG4935  600 --NATFDVANFSGESANGTWTLRVVDTAG--GDTGTLNSWSLTFTG 641
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 154-437 6.82e-13

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: 70.05  E-value: 6.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 154 KGITGKGVVITVLDDGLEWNHTDiyaNYDPeaSYDFNDNDHDPFPRYDLTNENK-----HGTRCAGEIAMQANNHKCGV- 227
Cdd:cd04842    2 LGLTGKGQIVGVADTGLDTNHCF---FYDP--NFNKTNLFHRKIVRYDSLSDTKddvdgHGTHVAGIIAGKGNDSSSISl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 228 --GVAYNSKVGGIRMLDG-IVTDAIEASSIGFNPGH---VDIYSASWGPNDDGKTVEgpgrLAQkAFEYgvkQGRQGKGS 301
Cdd:cd04842   77 ykGVAPKAKLYFQDIGDTsGNLSSPPDLNKLFSPMYdagARISSNSWGSPVNNGYTL----LAR-AYDQ---FAYNNPDI 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 302 IFVWASGNGGRQGDNCdcdGYTDSIYTISISSASQQGLSPWYAEKC------SSTLATSYSSGDYTDQR----------- 364
Cdd:cd04842  149 LFVFSAGNDGNDGSNT---IGSPATAKNVLTVGASNNPSVSNGEGGlgqsdnSDTVASFSSRGPTYDGRikpdlvapgtg 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 365 ITSA----DLHNDCTETH----TGTSASAPLAAGIFALALEAnpnltwrdmqhlvvWTSEYDPLASNPgwkkNGA---GL 433
Cdd:cd04842  226 ILSArsggGGIGDTSDSAytskSGTSMATPLVAGAAALLRQY--------------FVDGYYPTKFNP----SAAllkAL 287


                 ....
gi 568983154 434 MVNS 437
Cdd:cd04842  288 LINS 291
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 150-434 2.00e-10

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.


Pssm-ID: 173801 [Multi-domain]  Cd Length: 346  Bit Score: 63.05  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 150 PVWEKGIT-GKGVVITVLDDGLEWNHTD------IYANYDPEAS---------------------YDFNDNDHDPfprYD 201
Cdd:cd07475    1 PLWDKGGYkGEGMVVAVIDSGVDPTHDAfrldddSKAKYSEEFEakkkkagigygkyynekvpfaYNYADNNDDI---LD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 202 LTNENKHGTRCAGEIAMQANNHKCG---VGVAYN---------SKVGGIRMLDGIVTDAIE-ASSIGfnpghVDIYSASW 268
Cdd:cd07475   78 EDDGSSHGMHVAGIVAGNGDEEDNGegiKGVAPEaqllamkvfSNPEGGSTYDDAYAKAIEdAVKLG-----ADVINMSL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 269 GpndDGKTVEGPGRLAQKAFEYGVKqgrqgKGSIFVWASGNGGRQGD-------NCDCDGYT---DSIYTISISSASQQG 338
Cdd:cd07475  153 G---STAGFVDLDDPEQQAIKRARE-----AGVVVVVAAGNDGNSGSgtskplaTNNPDTGTvgsPATADDVLTVASANK 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 339 LSPwYAEKcsSTLATSYSSGDYTDQR-----------ITSAdLHNDCTETHTGTSASAPLAAGIFALALEA----NPNLT 403
Cdd:cd07475  225 KVP-NPNG--GQMSGFSSWGPTPDLDlkpditapggnIYST-VNDNTYGYMSGTSMASPHVAGASALVKQRlkekYPKLS 300

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 568983154 404 WRDMQHLV----------VWTSEYDPLASNPgwKKNGAGLM 434
Cdd:cd07475  301 GEELVDLVknllmntatpPLDSEDTKTYYSP--RRQGAGLI 339
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 161-403 5.25e-09

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: 58.15  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 161 VVITVLDDGLEWNHTDI-------YANYDPEASYDFNDNDhDPFPRYDLTNENKHGTRCAGEIAMQANNhkcgVGVAYNS 233
Cdd:cd07482    2 VTVAVIDSGIDPDHPDLknsissySKNLVPKGGYDGKEAG-ETGDINDIVDKLGHGTAVAGQIAANGNI----KGVAPGI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 234 KVGGIRMLD---GIVTDAIEASSIGFNPGHVDIYSASWGPNDDGKTVEGPG----RLAQKAFEYGVKqgrqgKGSIFVWA 306
Cdd:cd07482   77 GIVSYRVFGscgSAESSWIIKAIIDAADDGVDVINLSLGGYLIIGGEYEDDdveyNAYKKAINYAKS-----KGSIVVAA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 307 SGNGGRQGDN--------------------CDCDGYTDSIytISISSASQQG-LSPWY----------AEKCSSTLATSY 355
Cdd:cd07482  152 AGNDGLDVSNkqelldflssgddfsvngevYDVPASLPNV--ITVSATDNNGnLSSFSnygnsridlaAPGGDFLLLDQY 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568983154 356 SSGDYTDQRITSADLH-----NDCTETHTGTSASAPLAAGIFALALEANPNLT 403
Cdd:cd07482  230 GKEKWVNNGLMTKEQIlttapEGGYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 158-403 6.86e-09

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: 57.60  E-value: 6.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 158 GKGVVITVLDDGLEWNHTDIYANydPEASYDFNDNDHDPFPRYDltnENKHGTRCAGEIA--MQANNHKcGVGVAYNSKV 235
Cdd:cd07487    1 GKGITVAVLDTGIDAPHPDFDGR--IIRFADFVNTVNGRTTPYD---DNGHGTHVAGIIAgsGRASNGK-YKGVAPGANL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 236 GGIRMLD----GIVTDAIEAssIGF-----NPGHVDIYSASWGPNDDGKTVEGPGRLA-QKAFEYGVkqgrqgkgsIFVW 305
Cdd:cd07487   75 VGVKVLDdsgsGSESDIIAG--IDWvvennEKYNIRVVNLSLGAPPDPSYGEDPLCQAvERLWDAGI---------VVVV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 306 ASGNGGrqgdncdcdgytDSIYTISissasqqglSPWYAEKC--------SSTL---ATSYSSGDYTDQ----------- 363
Cdd:cd07487  144 AAGNSG------------PGPGTIT---------SPGNSPKVitvgavddNGPHddgISYFSSRGPTGDgrikpdvvapg 202

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568983154 364 -RITSADLHNDCTETH--------TGTSASAPLAAGIFALALEANPNLT 403
Cdd:cd07487  203 eNIVSCRSPGGNPGAGvgsgyfemSGTSMATPHVSGAIALLLQANPILT 251
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 158-402 4.12e-08

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.


Pssm-ID: 173807 [Multi-domain]  Cd Length: 264  Bit Score: 55.08  E-value: 4.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 158 GKGVVITVLDDGLEWNHTDIYANYDPE--ASYDFNDNDHDPFPRYDL-TNENKHGTRCAGeiAMQANN-HKCGVGVAYNS 233
Cdd:cd07481    1 GTGIVVANIDTGVDWTHPALKNKYRGWggGSADHDYNWFDPVGNTPLpYDDNGHGTHTMG--TMVGNDgDGQQIGVAPGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 234 KVGGIRMLD---GIVTDAIEASSIGFNPGHV-----------DIYSASWGPNDDGKTVEGPGRLAQKAfeygvkqgrqgK 299
Cdd:cd07481   79 RWIACRALDrngGNDADYLRCAQWMLAPTDSagnpadpdlapDVINNSWGGPSGDNEWLQPAVAAWRA-----------A 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 300 GSIFVWASGNGGRQGDNCDCdgyTDSIYTISISSAsqqglspwyAEKCSSTLATSYSSGDYTDQRIT-----------SA 368
Cdd:cd07481  148 GIFPVFAAGNDGPRCSTLNA---PPANYPESFAVG---------ATDRNDVLADFSSRGPSTYGRIKpdisapgvnirSA 215

                        250       260       270
                 ....*....|....*....|....*....|....
gi 568983154 369 dLHNDCTETHTGTSASAPLAAGIFALALEANPNL 402
Cdd:cd07481  216 -VPGGGYGSSSGTSMAAPHVAGVAALLWSANPSL 248
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 157-403 5.27e-08

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: 54.83  E-value: 5.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 157 TGKGVVITVLDDGLEWNHTDIY--AnydpEASYDFNDNDHDpfprydlTNENKHGTRCAGEIAmqANNHkcgvGVAYNSK 234
Cdd:cd04077   23 TGSGVDVYVLDTGIRTTHVEFGgrA----IWGADFVGGDPD-------SDCNGHGTHVAGTVG--GKTY----GVAKKAN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 235 VGGIRMLD----GIVTDAIEassiGFNpghvdiYSASWGPNDDGKTV-----EGPG-----RLAQKAFEYGVkqgrqgkg 300
Cdd:cd04077   86 LVAVKVLDcngsGTLSGIIA----GLE------WVANDATKRGKPAVanmslGGGAstaldAAVAAAVNAGV-------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 301 sIFVWASGNGGRqgDNCDcdgytdsiytisISSASqqglspwyAEKC------SSTLATSYSS--GDYTD-----QRITS 367
Cdd:cd04077  148 -VVVVAAGNSNQ--DACN------------YSPAS--------APEAitvgatDSDDARASFSnyGSCVDifapgVDILS 204

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568983154 368 ADLHND-CTETHTGTSASAPLAAGIFALALEANPNLT 403
Cdd:cd04077  205 AWIGSDtATATLSGTSMAAPHVAGLAAYLLSLGPDLS 241
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 160-403 1.68e-07

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: 53.32  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 160 GVVITVLDDGLEWNHTDI------YANYDPeasyDFNDNDHDPFPRydltneNKHGTRCAGEIAMQANNHKcGVGVAyns 233
Cdd:cd07490    1 GVTVAVLDTGVDADHPDLagrvaqWADFDE----NRRISATEVFDA------GGHGTHVSGTIGGGGAKGV-YIGVA--- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 234 kvGGIRMLDGIVTDAIEASSIGFNPG-------HVDIYSASWGPNDdgkTVEGPgrlaqkaFEYGVKQGRQGKGSIFVWA 306
Cdd:cd07490   67 --PEADLLHGKVLDDGGGSLSQIIAGmewavekDADVVSMSLGGTY---YSEDP-------LEEAVEALSNQTGALFVVS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 307 SGNGGrqGDNCDCDGYTDSIYTISISSASQQGLSPwyaEKCSSTLATSYSSGDYTDQRITSADLH------NDCT----- 375
Cdd:cd07490  135 AGNEG--HGTSGSPGSAYAALSVGAVDRDDEDAWF---SSFGSSGASLVSAPDSPPDEYTKPDVAapgvdvYSARqgang 209

                        250       260       270
                 ....*....|....*....|....*....|..
gi 568983154 376 ----ETHTGTSASAPLAAGIFALALEANPNLT 403
Cdd:cd07490  210 dgqyTRLSGTSMAAPHVAGVAALLAAAHPDLS 241
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 157-406 3.02e-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: 49.68  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 157 TGKGVVITVLDDGLEWNHTDIYANYDPEASYDFNDNDHDpfprydltnENKHGTRCAGEIAMQANNhkcGV--GVAYNSK 234
Cdd:cd07480    6 TGAGVRVAVLDTGIDLTHPAFAGRDITTKSFVGGEDVQD---------GHGHGTHCAGTIFGRDVP---GPryGVARGAE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 235 --VGGI------RMLDGIVtDAIE----------ASSIGFN-PGHVDiysASWGPNDDG----KTVEGPGRLAQKAFEYG 291
Cdd:cd07480   74 iaLIGKvlgdggGGDGGIL-AGIQwavangadviSMSLGADfPGLVD---QGWPPGLAFsralEAYRQRARLFDALMTLV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 292 VKQGRQGKGSIFVWASGN-GGRQGdncdcdgytDSIYTISIS-SASQQGLSpwyAEKCSSTLATSYSSGDYTDQRITSA- 368
Cdd:cd07480  150 AAQAALARGTLIVAAAGNeSQRPA---------GIPPVGNPAaCPSAMGVA---AVGALGRTGNFSAVANFSNGEVDIAa 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568983154 369 ---DLHN----DCTETHTGTSASAPLAAGIFALALEANPNLTWRD 406
Cdd:cd07480  218 pgvDIVSaapgGGYRSMSGTSMATPHVAGVAALWAEALPKAGGRA 262
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 150-411 4.46e-06

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: 49.40  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 150 PVWEKGITGKGVVITVLDDGleWNHTDIYANYDPEASYDFNDNDHDPfprydLTNENKHGTrcageiAMQANNhkcgVGV 229
Cdd:cd07494   12 RVHQRGITGRGVRVAMVDTG--FYAHPFFESRGYQVRVVLAPGATDP-----ACDENGHGT------GESANL----FAI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 230 AYNSKVGGIRMLDGIVTDAIEA--SSIGFNPghvDIYSASWGPNDDGKTVEGPGRL--AQKAFEYGVkQGRQGKGSIFVW 305
Cdd:cd07494   75 APGAQFIGVKLGGPDLVNSVGAfkKAISLSP---DIISNSWGYDLRSPGTSWSRSLpnALKALAATL-QDAVARGIVVVF 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 306 ASGNGG----RQGDNCDCDG--YTDSIYTISISSASQQGLSPWYAEK-----C--------SSTLATSYSSGDYTDqrIT 366
Cdd:cd07494  151 SAGNGGwsfpAQHPEVIAAGgvFVDEDGARRASSYASGFRSKIYPGRqvpdvCglvgmlphAAYLMLPVPPGSQLD--RS 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 568983154 367 SADLHNDCTETH-----TGTSASAPLAAGIFALALEANPNLTWRDMQHLV 411
Cdd:cd07494  229 CAAFPDGTPPNDgwgvfSGTSAAAPQVAGVCALMLQANPGLSPERARSLL 278
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 49-407 6.83e-06

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 49.58  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154  49 IAEELGYDLLGQIGSLENHYLFKHKSHPRRSRRSALHITKRLSDDDRVTWAEQQYEKERSKRSvqkdsaldLFNDPMWNQ 128
Cdd:PTZ00262 223 VIWESGMDDMIPIKEEGHIRGEAPVRNGNSLRGNSSNYDDHPGSDGSFSLSNQMAFNNFLGKY--------QFNDEGRNL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 129 QWYLQDTRMTAALPKLDLHVIPVwekgitgkgVVITVLDDGLEWNHTDIYANY---------------------DPEASY 187
Cdd:PTZ00262 295 QWGLDLTRLDETQELIEPHEVND---------TNICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGA 365

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 188 DFNDNDHDPFprydltNENKHGTRCAGEIAMQANNHKCGVGVAYNSKVggirmldgIVTDAIEASSIGFNPghvDIYSA- 266
Cdd:PTZ00262 366 NFVNNDGGPM------DDNYHGTHVSGIISAIGNNNIGIVGVDKRSKL--------IICKALDSHKLGRLG---DMFKCf 428

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 267 SWGPNDDGKTVEGPGRLAQKA--FEYGVKQGRQgKGSIFVWASGN----GGRQGDNCDCDGYTDSIY----------TIS 330
Cdd:PTZ00262 429 DYCISREAHMINGSFSFDEYSgiFNESVKYLEE-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYppilskklrnVIT 507

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983154 331 ISSASQQgLSPWYAEKCSSTLATSYSSGDYTDQRITSADLHNDCTEThTGTSASAPLAAGIFALALEANPNLTWRDM 407
Cdd:PTZ00262 508 VSNLIKD-KNNQYSLSPNSFYSAKYCQLAAPGTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
 159-411 1.02e-05

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: 48.13  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 159 KGVVITVLDDGLEWNHTD----IYANYDPEASYDFNDN---------------DHDPFP-----RYDLTNEN-------- 206
Cdd:cd07483    1 KTVIVAVLDSGVDIDHEDlkgkLWINKKEIPGNGIDDDnngyiddvngwnflgQYDPRRivgddPYDLTEKGygnndvng 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 207 -----KHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRM------LDGIVTDAIEASsigfnpghVD----IYSASWG-- 269
Cdd:cd07483   81 pisdaDHGTHVAGIIAAVRDNGIGIDGVADNVKIMPLRIvpngdeRDKDIANAIRYA--------VDngakVINMSFGks 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 270 --PNDDgktvegpgrLAQKAFEYGVKqgrqgKGSIFVWASGNggrqgDNCDCDGYTDSIYTIS------ISSASQQGLSP 341
Cdd:cd07483  153 fsPNKE---------WVDDAIKYAES-----KGVLIVHAAGN-----DGLDLDITPNFPNDYDknggepANNFITVGASS 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983154 342 WYAEkcsSTLATSYSS-GDYT------DQRITSADLHNDcTETHTGTSASAPLAAGIFALALEANPNLTWRDMQHLV 411
Cdd:cd07483  214 KKYE---NNLVANFSNyGKKNvdvfapGERIYSTTPDNE-YETDSGTSMAAPVVSGVAALIWSYYPNLTAKEVKQII 286
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 379-452 3.00e-05

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: 46.52  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 379 TGTSASAPLAAGIFALALEANPNLTWRDMqhlvvwtseYDPLASN------PGWkkngaglmvNSRFGFGLLNAKALVDL 452
Cdd:cd05562  214 FGTSAAAPHAAGVAALVLSANPGLTPADI---------RDALRSTaldmgePGY---------DNASGSGLVDADRAVAA 275
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 152-396 6.58e-05

Peptidase S8 family domain, uncharacterized subfamily 11; 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: 173792  Cd Length: 277  Bit Score: 45.38  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 152 WEKGITGKGVviTVLDDGLEW--NHTDIYanydpeasydfnDNDHDPFPRYDLTNENKHGTRCAGEIAMqANNHKCGVGV 229
Cdd:cd04843    9 TKPGGSGQGV--TFVDIEQGWnlNHEDLV------------GNGITLISGLTDQADSDHGTAVLGIIVA-KDNGIGVTGI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 230 AYNSK--VGGIRMLDGIVtDAIEASSIGFNPGHVDIYSASWGPNDDGkTVEGPGRLAQKAFEyGVKQGRQgKGSIFVWAS 307
Cdd:cd04843   74 AHGAQaaVVSSTRVSNTA-DAILDAADYLSPGDVILLEMQTGGPNNG-YPPLPVEYEQANFD-AIRTATD-LGIIVVEAA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983154 308 GNGGRqgdncDCDGYTDSIYTIsissasqqgLSPWYAEK----------CSST--LATSYSS--GDYTD-----QRITSA 368
Cdd:cd04843  150 GNGGQ-----DLDAPVYNRGPI---------LNRFSPDFrdsgaimvgaGSSTtgHTRLAFSnyGSRVDvygwgENVTTT 215

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568983154 369 ---------DLHNDCTETHTGTSASAPLAAGifALAL 396
Cdd:cd04843  216 gygdlqdlgGENQDYTDSFSGTSSASPIVAG--AAAS 250
 
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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