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Conserved domains on  [gi|2104551491|ref|NP_001383042|]
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furin precursor [Gallus gallus]

Protein Classification

S8 family peptidase( domain architecture ID 13872935)

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

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 ...
 114-403 0e+00

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: 521.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 114 PTDPKFPQQWYLYNTNQR------DLNVRQAWEQGYTGKGIVVSILDDGIEKNHPDLEANYDPGASFDVNDQDPDPQPRY 187
Cdd:cd04059     1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 188 TqmNDNRHGTRCAGEVAAVANNGICGVGVAYNARIGGVRMLDGEVTDAVEAHSLGLNPNHIHIYSASWGPEDDGKTVDGP 267
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 268 ARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSTTQYGNVPWYSEACSSTLATTYSSGNQ 347
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2104551491 348 N-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSK 403
Cdd:cd04059   239 NpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 485-571 2.34e-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: 128.93  E-value: 2.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 485 LEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWLLEIENTsDANNYGTL 564
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79


                  ....*..
gi 2104551491 565 TKFTLVL 571
Cdd:pfam01483  80 NSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 34-108 2.24e-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: 125.80  E-value: 2.24e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2104551491  34 TWAVLVPAGPLEANRLARKHGFLNLGPIFG--DYYHFQHRGVVKRSLSPHQPWHSRLAREPQVHWLEQQVAKRRTKR 108
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
FU smart00261
Furin-like repeats;
644-681 1.33e-10

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.13  E-value: 1.33e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2104551491  644 CLPCHPSCATCTGPGPNQCLTCPahSHFSSLDLSCSHQ 681
Cdd:smart00261   4 CKPCHPECATCTGPGPDDCTSCK--HGFFLDGGKCVSE 39
GF_recep_IV super family cl37890
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 587-671 7.92e-06

Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).


The actual alignment was detected with superfamily member pfam14843:

Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 45.83  E-value: 7.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 587 SSGCKTLTPSQtCVVCEegYYLHQKSCLKRCPpgFAPGVQNTHYNlensmepiaPQLCLPCHPSC------ATCTGPGPN 660
Cdd:pfam14843   8 SEGCWGPGPDQ-CLSCR--NFSRGGTCVESCN--ILQGEPREYVV---------NSTCVPCHPEClpqngtATCSGPGAD 73

                          90
                  ....*....|.
gi 2104551491 661 QCLTCpahSHF 671
Cdd:pfam14843  74 NCTKC---AHF 81
 
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 ...
 114-403 0e+00

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: 521.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 114 PTDPKFPQQWYLYNTNQR------DLNVRQAWEQGYTGKGIVVSILDDGIEKNHPDLEANYDPGASFDVNDQDPDPQPRY 187
Cdd:cd04059     1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 188 TqmNDNRHGTRCAGEVAAVANNGICGVGVAYNARIGGVRMLDGEVTDAVEAHSLGLNPNHIHIYSASWGPEDDGKTVDGP 267
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 268 ARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSTTQYGNVPWYSEACSSTLATTYSSGNQ 347
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2104551491 348 N-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSK 403
Cdd:cd04059   239 NpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 145-428 5.96e-63

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: 212.70  E-value: 5.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 145 GKGIVVSILDDGIEKNHPDLEANYDPGASFD----VNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGICGVGVAYNA 220
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDpeasVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 221 RIGGVRML-DGEVTDAVEAHSLGLN-PNHIHIYSASWGPEddgKTVDGPARLAEEAFFRGvsqGRGGLGSIFVWASGNGG 298
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 299 REHDSCNCDGY-TNSIYTLSISSTTQY--GNVPWYSEACSS-------TLA----TTYSSGNQNEKQIVTTDLRQKCTES 364
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVDEAseGNLASFSSYGPTldgrlkpDIVapggNITGGNISSTLLTTTSDPPNQGYDS 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2104551491 365 HTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSKPAHLNAndwvtngvgrkVSHSYGYG 428
Cdd:pfam00082 235 MSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAG-----------LDRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 114-434 9.73e-40

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 152.95  E-value: 9.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 114 PTDPKFPQQWYLYNTNQRDLNVRQAWEQ--GYTGKGIVVSILDDGIEKNHPDLEANYDPGASFDVNDQDPDpqprytqmN 191
Cdd:COG1404    75 PLPVPAAAPAAVRAAQAALLAAAAAGSSaaGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDFVDGDGDPS--------D 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 192 DNRHGTRCAGEVAAVANNGICGVGVAYNARIGGVRMLD----GEVTDAVEAhslgLN---PNHIHIYSASWGPEDDGKTv 264
Cdd:COG1404   147 DNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDdngsGTTSDIAAA----IDwaaDNGADVINLSLGGPADGYS- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 265 DGPARLAEEAFFRGVsqgrgglgsIFVWASGNGGrehDSCNCDGYTNSIY-TLSISSTTQYGNVPWYSeacsstlattyS 343
Cdd:COG1404   222 DALAAAVDYAVDKGV---------LVVAAAGNSG---SDDATVSYPAAYPnVIAVGAVDANGQLASFS-----------N 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 344 SGNQNE-----KQIVTTDLRQKcTESHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSKPAHLNANDwvtngvg 418
Cdd:COG1404   279 YGPKVDvaapgVDILSTYPGGG-YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGPY------- 350

                         330
                  ....*....|....*.
gi 2104551491 419 rkvshsYGYGLLDAGA 434
Cdd:COG1404   351 ------YGYGLLADGA 360
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 485-571 2.34e-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: 128.93  E-value: 2.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 485 LEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWLLEIENTsDANNYGTL 564
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79


                  ....*..
gi 2104551491 565 TKFTLVL 571
Cdd:pfam01483  80 NSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 34-108 2.24e-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: 125.80  E-value: 2.24e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2104551491  34 TWAVLVPAGPLEANRLARKHGFLNLGPIFG--DYYHFQHRGVVKRSLSPHQPWHSRLAREPQVHWLEQQVAKRRTKR 108
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 133-437 9.85e-14

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: 73.51  E-value: 9.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 133 LNVRQAWEQGyTGKGIVVSILDDGIEKnHPDLEANYDPGASFdVNDQDpdpqprytQMND-NRHGTRCAGEVAAVANNGI 211
Cdd:TIGR03921   1 LSLEQAWKFS-TGAGVTVAVIDTGVDD-HPRLPGLVLPGGDF-VGSGD--------GTDDcDGHGTLVAGIIAGRPGEGD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 212 CGVGVAYNARIGGVRMLDGEVTDAVEAHSLGlNPNH---------------IHIYSASWGPEDDGktVDGPARLA--EEA 274
Cdd:TIGR03921  70 GFSGVAPDARILPIRQTSAAFEPDEGTSGVG-DLGTlakairraadlgadvINISLVACLPAGSG--ADDPELGAavRYA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 275 FFRGVsqgrgglgsIFVWASGNGGrehDSCNCDgyTNSI-----YTLSISSTTQYGNVPWYSEACSSTLATTYSSGnqne 349
Cdd:TIGR03921 147 LDKGV---------VVVAAAGNTG---GDGQKT--TVVYpawypGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGEN---- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 350 kqIVTTDLRQKCTESHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTskpAHLNAndwvtnGVGRkvSHSYGYGL 429
Cdd:TIGR03921 209 --IVSLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEAT---ADHPA------RGGR--DDYVGYGV 275


                  ....*...
gi 2104551491 430 LDAGAMVS 437
Cdd:TIGR03921 276 VDPVAALT 283
FU smart00261
Furin-like repeats;
644-681 1.33e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.13  E-value: 1.33e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2104551491  644 CLPCHPSCATCTGPGPNQCLTCPahSHFSSLDLSCSHQ 681
Cdd:smart00261   4 CKPCHPECATCTGPGPDDCTSCK--HGFFLDGGKCVSE 39
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 150-401 1.03e-09

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 61.91  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 150 VSILDDGIEKNHPDLEANYDP-----------------------GASFDVNDQDPdpqprytqMNDNRHGTRCAGEVAAV 206
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIDVnvkelhgrkgidddnngnvddeyGANFVNNDGGP--------MDDNYHGTHVSGIISAI 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 207 ANNGICGVGVAYNARIGGVRMLD----GEVTDAVEAHSLGLNPNhIHIYSASWGPEDDGKTVDGPARLAEEaffrgvsqg 282
Cdd:PTZ00262  392 GNNNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFNESVKYLEE--------- 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 283 rggLGSIFVWASGNGGREHDSCN----CDGYTNSIYTLSISSTtqYGNV-----------PWYSEACSSTLATTYSSGNQ 347
Cdd:PTZ00262  462 ---KGILFVVSASNCSHTKESKPdipkCDLDVNKVYPPILSKK--LRNVitvsnlikdknNQYSLSPNSFYSAKYCQLAA 536

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104551491 348 NEKQIVTTDLRQKCTEShTGTSASAPLAAGIIALALEANKNLTWRD----MQHLVVQT 401
Cdd:PTZ00262  537 PGTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEviriLKESIVQL 593
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 646-670 4.05e-09

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 52.91  E-value: 4.05e-09
                          10        20
                  ....*....|....*....|....*
gi 2104551491 646 PCHPSCATCTGPGPNQCLTCPAHSH 670
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFY 25
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 587-671 7.92e-06

Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 45.83  E-value: 7.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 587 SSGCKTLTPSQtCVVCEegYYLHQKSCLKRCPpgFAPGVQNTHYNlensmepiaPQLCLPCHPSC------ATCTGPGPN 660
Cdd:pfam14843   8 SEGCWGPGPDQ-CLSCR--NFSRGGTCVESCN--ILQGEPREYVV---------NSTCVPCHPEClpqngtATCSGPGAD 73

                          90
                  ....*....|.
gi 2104551491 661 QCLTCpahSHF 671
Cdd:pfam14843  74 NCTKC---AHF 81
 
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 ...
 114-403 0e+00

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: 521.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 114 PTDPKFPQQWYLYNTNQR------DLNVRQAWEQGYTGKGIVVSILDDGIEKNHPDLEANYDPGASFDVNDQDPDPQPRY 187
Cdd:cd04059     1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 188 TqmNDNRHGTRCAGEVAAVANNGICGVGVAYNARIGGVRMLDGEVTDAVEAHSLGLNPNHIHIYSASWGPEDDGKTVDGP 267
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 268 ARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSTTQYGNVPWYSEACSSTLATTYSSGNQ 347
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2104551491 348 N-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSK 403
Cdd:cd04059   239 NpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 145-428 5.96e-63

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: 212.70  E-value: 5.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 145 GKGIVVSILDDGIEKNHPDLEANYDPGASFD----VNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGICGVGVAYNA 220
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDpeasVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 221 RIGGVRML-DGEVTDAVEAHSLGLN-PNHIHIYSASWGPEddgKTVDGPARLAEEAFFRGvsqGRGGLGSIFVWASGNGG 298
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 299 REHDSCNCDGY-TNSIYTLSISSTTQY--GNVPWYSEACSS-------TLA----TTYSSGNQNEKQIVTTDLRQKCTES 364
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVDEAseGNLASFSSYGPTldgrlkpDIVapggNITGGNISSTLLTTTSDPPNQGYDS 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2104551491 365 HTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSKPAHLNAndwvtngvgrkVSHSYGYG 428
Cdd:pfam00082 235 MSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAG-----------LDRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 114-434 9.73e-40

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 152.95  E-value: 9.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 114 PTDPKFPQQWYLYNTNQRDLNVRQAWEQ--GYTGKGIVVSILDDGIEKNHPDLEANYDPGASFDVNDQDPDpqprytqmN 191
Cdd:COG1404    75 PLPVPAAAPAAVRAAQAALLAAAAAGSSaaGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDFVDGDGDPS--------D 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 192 DNRHGTRCAGEVAAVANNGICGVGVAYNARIGGVRMLD----GEVTDAVEAhslgLN---PNHIHIYSASWGPEDDGKTv 264
Cdd:COG1404   147 DNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDdngsGTTSDIAAA----IDwaaDNGADVINLSLGGPADGYS- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 265 DGPARLAEEAFFRGVsqgrgglgsIFVWASGNGGrehDSCNCDGYTNSIY-TLSISSTTQYGNVPWYSeacsstlattyS 343
Cdd:COG1404   222 DALAAAVDYAVDKGV---------LVVAAAGNSG---SDDATVSYPAAYPnVIAVGAVDANGQLASFS-----------N 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 344 SGNQNE-----KQIVTTDLRQKcTESHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSKPAHLNANDwvtngvg 418
Cdd:COG1404   279 YGPKVDvaapgVDILSTYPGGG-YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGPY------- 350

                         330
                  ....*....|....*.
gi 2104551491 419 rkvshsYGYGLLDAGA 434
Cdd:COG1404   351 ------YGYGLLADGA 360
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 148-401 1.62e-35

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: 134.78  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 148 IVVSILDDGIEKNHPDLEA--NYDPGasFDVNDQDPDPQPRYTqmndnrHGTRCAGEVAAVANNGICGVGVAYNARIGGV 225
Cdd:cd07498     1 VVVAIIDTGVDLNHPDLSGkpKLVPG--WNFVSNNDPTSDIDG------HGTACAGVAAAVGNNGLGVAGVAPGAKLMPV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 226 RMLDGEVTDAVEAHSLGLN---PNHIHIYSASWGPEDdgktvdgPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHD 302
Cdd:cd07498    73 RIADSLGYAYWSDIAQAITwaaDNGADVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLFAAGNSGRSVS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 303 ScncdGYTNSIYTLSISSTTQYGNVPWYSE--------ACSSTLATTySSGNQNEKQIVTTDlrqkcTESHTGTSASAPL 374
Cdd:cd07498   146 S----GYAANPSVIAVAATDSNDARASYSNygnyvdlvAPGVGIWTT-GTGRGSAGDYPGGG-----YGSFSGTSFASPV 215

                         250       260
                  ....*....|....*....|....*..
gi 2104551491 375 AAGIIALALEANKNLTWRDMQHLVVQT 401
Cdd:cd07498   216 AAGVAALILSANPNLTPAEVEDILTST 242
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 485-571 2.34e-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: 128.93  E-value: 2.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 485 LEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWLLEIENTsDANNYGTL 564
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79


                  ....*..
gi 2104551491 565 TKFTLVL 571
Cdd:pfam01483  80 NSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 34-108 2.24e-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: 125.80  E-value: 2.24e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2104551491  34 TWAVLVPAGPLEANRLARKHGFLNLGPIFG--DYYHFQHRGVVKRSLSPHQPWHSRLAREPQVHWLEQQVAKRRTKR 108
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 146-403 8.70e-29

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: 116.14  E-value: 8.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 146 KGIVVSILDDGIEKNHPDLEAN------YDPGASFDvNDQ---------------DPDPqprytqMNDNRHGTRCAGEVA 204
Cdd:cd07473     2 GDVVVAVIDTGVDYNHPDLKDNmwvnpgEIPGNGID-DDGngyvddiygwnfvnnDNDP------MDDNGHGTHVAGIIG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 205 AVANNGICGVGVAYNARIGGVRMLD----GEVTDAVEAHSLGLNpNHIHIYSASWGPeddgktvDGPARLAEEAFFRGVS 280
Cdd:cd07473    75 AVGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAIDYAVD-MGAKIINNSWGG-------GGPSQALRDAIARAID 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 281 QgrgglGSIFVWASGNGGREHDSCNC--DGYTNSiYTLSISSTTQYGNVPWYSEACSST--LA-------TTYSSGNQNE 349
Cdd:cd07473   147 A-----GILFVAAAGNDGTNNDKTPTypASYDLD-NIISVAATDSNDALASFSNYGKKTvdLAapgvdilSTSPGGGYGY 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104551491 350 KqivttdlrqkcteshTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSK 403
Cdd:cd07473   221 M---------------SGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 148-401 2.76e-28

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: 113.83  E-value: 2.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 148 IVVSILDDGIEKNHPDLEANYDPGASFdvNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGIcGVGVAYNARIGGVRM 227
Cdd:cd00306     1 VTVAVIDTGVDPDHPDLDGLFGGGDGG--NDDDDNENGPTDPDDGNGHGTHVAGIIAASANNGG-GVGVAPGAKLIPVKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 228 LDGEVTDAVEAHSLGLN----PNHIHIYSASWGPEDDGKTvDGPARLAEEAFFRgvsqgrggLGSIFVWASGNGGREHDS 303
Cdd:cd00306    78 LDGDGSGSSSDIAAAIDyaaaDQGADVINLSLGGPGSPPS-SALSEAIDYALAK--------LGVLVVAAAGNDGPDGGT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 304 cNCDGYTNSIYTLSISSTTQYGNVPWYSeACSSTLATTYSSGNQnekQIVTTDLRQKCTESHTGTSASAPLAAGIIALAL 383
Cdd:cd00306   149 -NIGYPAASPNVIAVGAVDRDGTPASPS-SNGGAGVDIAAPGGD---ILSSPTTGGGGYATLSGTSMAAPIVAGVAALLL 223

                         250
                  ....*....|....*...
gi 2104551491 384 EANKNLTWRDMQHLVVQT 401
Cdd:cd00306   224 SANPDLTPAQVKAALLST 241
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 113-381 4.15e-27

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: 111.20  E-value: 4.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 113 EPTDPKFPQQWYLYNTNqrdlnVRQAWEQGyTGKGIVVSILDDGIEKNHPDLEA-NYDPGASFDVNDQDPdpqprytqMN 191
Cdd:cd07484     1 TPNDPYYSYQWNLDQIG-----APKAWDIT-GGSGVTVAVVDTGVDPTHPDLLKvKFVLGYDFVDNDSDA--------MD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 192 DNRHGTRCAGEVAAVANNGICGVGVAYNARIGGVRMLD----GEVTDAVEAhslglnpnhIhIYSAswgpeDDGKTV--- 264
Cdd:cd07484    67 DNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANG---------I-RYAA-----DKGAKVinl 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 265 ----DGPARLAEEAFFRGVSQgrgglGSIFVWASGNGGREHDScncdgYTNSI-YTLSISSTTQYGNVPWYSEAcSSTLA 339
Cdd:cd07484   132 slggGLGSTALQEAINYAWNK-----GVVVVAAAGNEGVSSVS-----YPAAYpGAIAVAATDQDDKRASFSNY-GKWVD 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2104551491 340 TTYSSGNqnekqIVTTDLRQKcTESHTGTSASAPLAAGIIAL 381
Cdd:cd07484   201 VSAPGGG-----ILSTTPDGD-YAYMSGTSMATPHVAGVAAL 236
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 147-390 7.00e-22

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: 94.91  E-value: 7.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 147 GIVVSILDDGIEKNHPDLEANYDPGASFdVNDQDPDPQprytqmNDNRHGTRCAGEVAAvANNGICGVGVAYNARIGGVR 226
Cdd:cd07477     1 GVKVAVIDTGIDSSHPDLKLNIVGGANF-TGDDNNDYQ------DGNGHGTHVAGIIAA-LDNGVGVVGVAPEADLYAVK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 227 MLD----GEVTDAVEAHSLGLNpNHIHIYSASWGPEDDGKTVdgparlaEEAFFRGVSQGrgglgsIF-VWASGNggreh 301
Cdd:cd07477    73 VLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLGGPSDSPAL-------REAIKKAYAAG------ILvVAAAGN----- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 302 dscncDGYTNSIYT--------LSISSTTQYGNVPWYSeacsstlattySSGNQNE-----KQIVTTDLRQKcTESHTGT 368
Cdd:cd07477   134 -----SGNGDSSYDypakypsvIAVGAVDSNNNRASFS-----------STGPEVElaapgVDILSTYPNND-YAYLSGT 196

                         250       260
                  ....*....|....*....|..
gi 2104551491 369 SASAPLAAGIIALALEANKNLT 390
Cdd:cd07477   197 SMATPHVAGVAALVWSKRPELT 218
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 137-388 6.56e-21

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: 93.32  E-value: 6.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 137 QAWEQGYTGKGIVVSILDDGIEKNHPDLEANYD-PGASFDVNDQDPDPQ---PRYTQMNDNRHGTRCAGEVAAVANN--G 210
Cdd:cd07485     1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDgDGYDPAVNGYNFVPNvgdIDNDVSVGGGHGTHVAGTIAAVNNNggG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 211 ICGV----GVAYNARIGGVRMLDGE--VTDAVEAHSLGLNPNH-IHIYSASWGpeddGKTVDGPARLAEEAFFRGVSQGR 283
Cdd:cd07485    81 VGGIagagGVAPGVKIMSIQIFAGRyyVGDDAVAAAIVYAADNgAVILQNSWG----GTGGGIYSPLLKDAFDYFIENAG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 284 GGL--GSIFVWASGNggrEHDSCncdGYTNSIY--TLSISSTTQYGNVPWYSeacssTLATTYSSGNQNEKQIVTTDLRQ 359
Cdd:cd07485   157 GSPldGGIVVFSAGN---SYTDE---HRFPAAYpgVIAVAALDTNDNKASFS-----NYGRWVDIAAPGVGTILSTVPKL 225

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2104551491 360 KCTESHT-----GTSASAPLAAGIIALALEANKN 388
Cdd:cd07485   226 DGDGGGNyeylsGTSMAAPHVSGVAALVLSKFPD 259
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 144-401 4.81e-20

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: 90.85  E-value: 4.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 144 TGKGIVVSILDDGIEKNHPDLEANYDP-GASFDVNDQDPDPQPRYtqmndNRHGTRCAGEVAAVANNGICGvGVAYNARI 222
Cdd:cd04848     1 TGAGVKVGVIDSGIDLSHPEFAGRVSEaSYYVAVNDAGYASNGDG-----DSHGTHVAGVIAAARDGGGMH-GVAPDATL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 223 GGVRMLDG----EVTDAVEAHSLGLNPNHIHIYSASWGPEDDGKTVDGPARL--------AEEAFFRGVSQgrgglGSIF 290
Cdd:cd04848    75 YSARASASagstFSDADIAAAYDFLAASGVRIINNSWGGNPAIDTVSTTYKGsaatqgntLLAALARAANA-----GGLF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 291 VWASGNGGREHDSCNCDGYT-------NSIytLSISSTTQYGNVP--WYSEAC----SSTLA-------TTYSSGNQNEK 350
Cdd:cd04848   150 VFAAGNDGQANPSLAAAALPylepeleGGW--IAVVAVDPNGTIAsySYSNRCgvaaNWCLAapgeniySTDPDGGNGYG 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2104551491 351 QIvttdlrqkcteshTGTSASAPLAAGIIALALEANKNLTwrdmQHLVVQT 401
Cdd:cd04848   228 RV-------------SGTSFAAPHVSGAAALLAQKFPWLT----ADQVRQT 261
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 145-411 2.75e-19

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: 89.31  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 145 GKGIVVSILDDGIEKNHPDLE------ANYDPGASFDVNDQDPDPQPRYTQMNDNR-------HGTRCAGEVAAVANNGI 211
Cdd:cd07474     1 GKGVKVAVIDTGIDYTHPDLGgpgfpnDKVKGGYDFVDDDYDPMDTRPYPSPLGDAsagdatgHGTHVAGIIAGNGVNVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 212 CGVGVAYNARIGGVRMLD--GEVT---------DAVEAH------SLGlnpnhihiysASWGPEDDgKTVDGPARLAEea 274
Cdd:cd07474    81 TIKGVAPKADLYAYKVLGpgGSGTtdviiaaieQAVDDGmdvinlSLG----------SSVNGPDD-PDAIAINNAVK-- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 275 ffrgvsqgrggLGSIFVWASGNGGrehDSCNCDG-YTNSIYTLSISSTTqyGNVPWYSEacssTLATTYSSGNQNEKQIV 353
Cdd:cd07474   148 -----------AGVVVVAAAGNSG---PAPYTIGsPATAPSAITVGAST--VADVAEAD----TVGPSSSRGPPTSDSAI 207

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2104551491 354 TTDL-------------RQKCTESHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSKPAHLNAND 411
Cdd:cd07474   208 KPDIvapgvdimstapgSGTGYARMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLYDSDGV 278
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 147-390 3.18e-18

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: 85.81  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 147 GIVVSILDDGIEKNHPDLEANYDPGASF----------DVNDQDP-DPQPRYTQMNDNR-------------HGTRCAGE 202
Cdd:cd07496     1 GVVVAVLDTGVLFHHPDLAGVLLPGYDFisdpaiandgDGRDSDPtDPGDWVTGDDVPPggfcgsgvspsswHGTHVAGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 203 VAAVANNGIcGV-GVAYNARIGGVRML---DGEVTDAVEAhslglnpnhihIYSASWGPEDDGKTVDGPAR-----LAEE 273
Cdd:cd07496    81 IAAVTNNGV-GVaGVAWGARILPVRVLgkcGGTLSDIVDG-----------MRWAAGLPVPGVPVNPNPAKvinlsLGGD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 274 AFFRGVSQ----GRGGLGSIFVWASGNGGR--EHDS-CNCDGytnsiyTLSISSTTQYGNVPWYSEACSST-LAT----T 341
Cdd:cd07496   149 GACSATMQnainDVRARGVLVVVAAGNEGSsaSVDApANCRG------VIAVGATDLRGQRASYSNYGPAVdVSApggdC 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2104551491 342 YSSGNQNEKQIVTTDLRQKCTESHT---GTSASAPLAAGIIALALEANKNLT 390
Cdd:cd07496   223 ASDVNGDGYPDSNTGTTSPGGSTYGflqGTSMAAPHVAGVAALMKSVNPSLT 274
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 145-390 5.13e-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: 78.78  E-value: 5.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 145 GKGIVVSILDDGIEKNHPDLEANYDPGASFdVNDQDPDPQPRytqmNDNRHGTRCAGEVAA--VANNGIcGVGVAYNARI 222
Cdd:cd07487     1 GKGITVAVLDTGIDAPHPDFDGRIIRFADF-VNTVNGRTTPY----DDNGHGTHVAGIIAGsgRASNGK-YKGVAPGANL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 223 GGVRMLD----GEVTDAVEA------HSLGLNpnhIHIYSASWGPEDDGKTVDGPARLA-EEAFFRGVsqgrgglgsIFV 291
Cdd:cd07487    75 VGVKVLDdsgsGSESDIIAGidwvveNNEKYN---IRVVNLSLGAPPDPSYGEDPLCQAvERLWDAGI---------VVV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 292 WASGNGGREHDSCNCDGytNSIYTLSISSTTQYGNVPWYSEACSS---TLA--------------TTYSSGNQNEKQIVT 354
Cdd:cd07487   143 VAAGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSSrgpTGDgrikpdvvapgeniVSCRSPGGNPGAGVG 220

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2104551491 355 TDLRQKcteshTGTSASAPLAAGIIALALEANKNLT 390
Cdd:cd07487   221 SGYFEM-----SGTSMATPHVSGAIALLLQANPILT 251
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 140-432 3.47e-14

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: 74.18  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 140 EQGYTGKGIVVSILDDGIEKNHPDLEANYDPGASF--------DVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANN-G 210
Cdd:cd07489     7 AEGITGKGVKVAVVDTGIDYTHPALGGCFGPGCKVaggydfvgDDYDGTNPPVPDDDPMDCQGHGTHVAGIIAANPNAyG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 211 IcgVGVAYNARIGGVRMLD--GEVTDAVE------AHSLGlnpnhIHIYSASWGpeDDGKTVDGPA-----RLAEEAFFR 277
Cdd:cd07489    87 F--TGVAPEATLGAYRVFGcsGSTTEDTIiaaflrAYEDG-----ADVITASLG--GPSGWSEDPWavvasRIVDAGVVV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 278 GVSQG-RGGLGSifvWASGNGGrehdscncdgytNSIYTLSISSttqygnvpwyseacsstLATTYSS-GNQNEKQ---- 351
Cdd:cd07489   158 TIAAGnDGERGP---FYASSPA------------SGRGVIAVAS-----------------VDSYFSSwGPTNELYlkpd 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 352 -------IVTTDLRQKCT-ESHTGTSASAPLAAGIIALALEA-NKNLTWRDMQHLVVQTSKPahLNANDWVTNGVGRKVS 422
Cdd:cd07489   206 vaapggnILSTYPLAGGGyAVLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKP--LPWSDGTSALPDLAPV 283

                         330
                  ....*....|
gi 2104551491 423 HSYGYGLLDA 432
Cdd:cd07489   284 AQQGAGLVNA 293
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 133-437 9.85e-14

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: 73.51  E-value: 9.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 133 LNVRQAWEQGyTGKGIVVSILDDGIEKnHPDLEANYDPGASFdVNDQDpdpqprytQMND-NRHGTRCAGEVAAVANNGI 211
Cdd:TIGR03921   1 LSLEQAWKFS-TGAGVTVAVIDTGVDD-HPRLPGLVLPGGDF-VGSGD--------GTDDcDGHGTLVAGIIAGRPGEGD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 212 CGVGVAYNARIGGVRMLDGEVTDAVEAHSLGlNPNH---------------IHIYSASWGPEDDGktVDGPARLA--EEA 274
Cdd:TIGR03921  70 GFSGVAPDARILPIRQTSAAFEPDEGTSGVG-DLGTlakairraadlgadvINISLVACLPAGSG--ADDPELGAavRYA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 275 FFRGVsqgrgglgsIFVWASGNGGrehDSCNCDgyTNSI-----YTLSISSTTQYGNVPWYSEACSSTLATTYSSGnqne 349
Cdd:TIGR03921 147 LDKGV---------VVVAAAGNTG---GDGQKT--TVVYpawypGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGEN---- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 350 kqIVTTDLRQKCTESHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTskpAHLNAndwvtnGVGRkvSHSYGYGL 429
Cdd:TIGR03921 209 --IVSLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEAT---ADHPA------RGGR--DDYVGYGV 275


                  ....*...
gi 2104551491 430 LDAGAMVS 437
Cdd:TIGR03921 276 VDPVAALT 283
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 123-390 1.78e-13

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: 71.01  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 123 WYLYNTNQRDLNVRQAW-EQGYTGKGIVVSILDDGIEKNHPDLEANYDPGASFDVNDQDPDPqprytqmndNRHGTRCAG 201
Cdd:cd04077     1 WGLDRISQRDLPLDGTYyYDSSTGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDC---------NGHGTHVAG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 202 EVAAVAnngicgVGVAYNARIGGVRMLD----GEVTDAVEahslGLNpnhihiYSASWGPEDDGKTV-----DGPARLAE 272
Cdd:cd04077    72 TVGGKT------YGVAKKANLVAVKVLDcngsGTLSGIIA----GLE------WVANDATKRGKPAVanmslGGGASTAL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 273 EAFFRGVSQGrgglGSIFVWASGNGGRehDSCNcdgYT--NSIYTLSISSTTQYGNVPWYSE--AC-------SSTLATT 341
Cdd:cd04077   136 DAAVAAAVNA----GVVVVVAAGNSNQ--DACN---YSpaSAPEAITVGATDSDDARASFSNygSCvdifapgVDILSAW 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2104551491 342 YSSGNqnekqivttdlrqkCTESHTGTSASAPLAAGIIALALEANKNLT 390
Cdd:cd04077   207 IGSDT--------------ATATLSGTSMAAPHVAGLAAYLLSLGPDLS 241
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 147-390 7.39e-13

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: 69.11  E-value: 7.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 147 GIVVSILDDGIEKNHPDLEANYDPGASFDVNDQDPDPQPrytqMNDNRHGTRCAGEVAAVANNGIcGVGVAynariGGVR 226
Cdd:cd07490     1 GVTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEV----FDAGGHGTHVSGTIGGGGAKGV-YIGVA-----PEAD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 227 MLDGEVTDAVEAHSLGLnpnhihIYSASWGPEDDGKTVD---GPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGreHDS 303
Cdd:cd07490    71 LLHGKVLDDGGGSLSQI------IAGMEWAVEKDADVVSmslGGTYYSEDPLEEAVEALSNQTGALFVVSAGNEG--HGT 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 304 CNCDGYTNSiyTLSISSTTQYGNVPWYSeACSSTLATTYSSGNQNEKQIVTTDLRQKCT---------------ESHTGT 368
Cdd:cd07490   143 SGSPGSAYA--ALSVGAVDRDDEDAWFS-SFGSSGASLVSAPDSPPDEYTKPDVAAPGVdvysarqgangdgqyTRLSGT 219

                         250       260
                  ....*....|....*....|..
gi 2104551491 369 SASAPLAAGIIALALEANKNLT 390
Cdd:cd07490   220 SMAAPHVAGVAALLAAAHPDLS 241
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 143-296 1.05e-10

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: 63.55  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 143 YTGKGIVVSILDDGIEKNHPDL------EANYDPGAsfDVNDQdpdpqprytqmndNRHGTRCAGEVAAVANNGIcGVGV 216
Cdd:cd07480     5 FTGAGVRVAVLDTGIDLTHPAFagrditTKSFVGGE--DVQDG-------------HGHGTHCAGTIFGRDVPGP-RYGV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 217 AYNARI--GGVRMLDGEVTDA--VEAHSLGLNpNHIHIYSASWG-----PEDDGKTVDGPARLAEEAFFRGV-------- 279
Cdd:cd07480    69 ARGAEIalIGKVLGDGGGGDGgiLAGIQWAVA-NGADVISMSLGadfpgLVDQGWPPGLAFSRALEAYRQRArlfdalmt 147

                         170       180
                  ....*....|....*....|
gi 2104551491 280 ---SQGRGGLGSIFVWASGN 296
Cdd:cd07480   148 lvaAQAALARGTLIVAAAGN 167
FU smart00261
Furin-like repeats;
644-681 1.33e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.13  E-value: 1.33e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2104551491  644 CLPCHPSCATCTGPGPNQCLTCPahSHFSSLDLSCSHQ 681
Cdd:smart00261   4 CKPCHPECATCTGPGPDDCTSCK--HGFFLDGGKCVSE 39
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 142-385 3.35e-10

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: 61.96  E-value: 3.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 142 GYTGKGIVVSILDDGIEKNHPDLeanYDPGASfDVNDQDP-----DPQPRYTQMNDNrHGTRCAGEVAAVANNGICGV-- 214
Cdd:cd04842     3 GLTGKGQIVGVADTGLDTNHCFF---YDPNFN-KTNLFHRkivryDSLSDTKDDVDG-HGTHVAGIIAGKGNDSSSISly 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 215 -GVAYNARIGGVRMLDGEVTDAVEAHSLGL----NPNHIHIYSASWGPEDDG------KTVDGPARLAEEAffrgvsqgr 283
Cdd:cd04842    78 kGVAPKAKLYFQDIGDTSGNLSSPPDLNKLfspmYDAGARISSNSWGSPVNNgytllaRAYDQFAYNNPDI--------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 284 gglgsIFVWASGNGGREHD---SCNCDG---------YTNSIYTLSISSTTQYGNVPWYSEACS---------------- 335
Cdd:cd04842   149 -----LFVFSAGNDGNDGSntiGSPATAknvltvgasNNPSVSNGEGGLGQSDNSDTVASFSSRgptydgrikpdlvapg 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2104551491 336 ----STLATTYSSGNQNekqivTTDLRQKcteshTGTSASAPLAAGIIALALEA 385
Cdd:cd04842   224 tgilSARSGGGGIGDTS-----DSAYTSK-----SGTSMATPLVAGAAALLRQY 267
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 166-573 4.22e-10

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: 63.30  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 166 ANYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGICGVGVAYNARIGGVRMLDGEVTDAVEAHSLGLNP 245
Cdd:COG4935   251 ATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAAAGA 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 246 NHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSTTQYG 325
Cdd:COG4935   331 AAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGGVASAAGAVGA 410

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 326 NVPWYSEACSSTLATTYSSGNQNEKQIVTTdlrqkcteshTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSKPA 405
Cdd:COG4935   411 GTAAGASATAAVSTGAASGSSTTSSTGTTA----------TATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTT 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 406 HLNANDWVTNGVGRKVSHSYGYGLLDAGAMVSLARNWITVGPQRKCVIDVLTEPKDI--GKRLEVRRKVDACLGKAnyis 483
Cdd:COG4935   481 AAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVAIpdNGPAGVTSTITVSGGGA---- 556

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 484 rLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAarPHDYSADGFNdWAFMTTHSWDEDPSGEWLLEIENTSDANNyGT 563
Cdd:COG4935   557 -VEDVTVTVDITHTYRGDLVITLISPDGTTVVLKN--RSGGSADNIN-ATFDVANFSGESANGTWTLRVVDTAGGDT-GT 631

                         410
                  ....*....|
gi 2104551491 564 LTKFTLVLYG 573
Cdd:COG4935   632 LNSWSLTFTG 641
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 145-389 5.58e-10

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: 60.85  E-value: 5.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 145 GKGIVVSILDDGIEKNHPDLEANYDP--GASFDVNDQDPDPQPRYTQMND-NRHGTRCAGevAAVANNGI-CGVGVAYNA 220
Cdd:cd07481     1 GTGIVVANIDTGVDWTHPALKNKYRGwgGGSADHDYNWFDPVGNTPLPYDdNGHGTHTMG--TMVGNDGDgQQIGVAPGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 221 RIGGVRMLD---GEVTDAVEAHSLGLNPNHI-----------HIYSASWGpeddgktvdGPARLAEeaFFRGVSQGRGGL 286
Cdd:cd07481    79 RWIACRALDrngGNDADYLRCAQWMLAPTDSagnpadpdlapDVINNSWG---------GPSGDNE--WLQPAVAAWRAA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 287 GSIFVWASGNGGREHDSCNCD--GYTNSIytlSISSTTQYGNVPWYseacSSTLATTYSSGNQNekqIVT--TDLRQKCT 362
Cdd:cd07481   148 GIFPVFAAGNDGPRCSTLNAPpaNYPESF---AVGATDRNDVLADF----SSRGPSTYGRIKPD---ISApgVNIRSAVP 217

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2104551491 363 E----SHTGTSASAPLAAGIIALALEANKNL 389
Cdd:cd07481   218 GggygSSSGTSMAAPHVAGVAALLWSANPSL 248
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 150-401 1.03e-09

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 61.91  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 150 VSILDDGIEKNHPDLEANYDP-----------------------GASFDVNDQDPdpqprytqMNDNRHGTRCAGEVAAV 206
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIDVnvkelhgrkgidddnngnvddeyGANFVNNDGGP--------MDDNYHGTHVSGIISAI 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 207 ANNGICGVGVAYNARIGGVRMLD----GEVTDAVEAHSLGLNPNhIHIYSASWGPEDDGKTVDGPARLAEEaffrgvsqg 282
Cdd:PTZ00262  392 GNNNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFNESVKYLEE--------- 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 283 rggLGSIFVWASGNGGREHDSCN----CDGYTNSIYTLSISSTtqYGNV-----------PWYSEACSSTLATTYSSGNQ 347
Cdd:PTZ00262  462 ---KGILFVVSASNCSHTKESKPdipkCDLDVNKVYPPILSKK--LRNVitvsnlikdknNQYSLSPNSFYSAKYCQLAA 536

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2104551491 348 NEKQIVTTDLRQKCTEShTGTSASAPLAAGIIALALEANKNLTWRD----MQHLVVQT 401
Cdd:PTZ00262  537 PGTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEviriLKESIVQL 593
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 137-411 4.04e-09

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: 59.20  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 137 QAWEQG-YTGKGIVVSILDDGIEKNHPDL-------------------EANYDPGA--------SFDVNDQDPDPQPRyt 188
Cdd:cd07475     1 PLWDKGgYKGEGMVVAVIDSGVDPTHDAFrldddskakyseefeakkkKAGIGYGKyynekvpfAYNYADNNDDILDE-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 189 qMNDNRHGTRCAGEVAAVANNGICG---VGVAYNARIGGVRMLD-----GEVTDAVEA---HSLGLNPNHIhiySASWGP 257
Cdd:cd07475    79 -DDGSSHGMHVAGIVAGNGDEEDNGegiKGVAPEAQLLAMKVFSnpeggSTYDDAYAKaieDAVKLGADVI---NMSLGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 258 EDDGKTVDGPARLA-EEAFFRGVsqgrgglgsIFVWASGNggrehdscncDGYTNSIYTLSISSTT-QYGNV--PWYSEA 333
Cdd:cd07475   155 TAGFVDLDDPEQQAiKRAREAGV---------VVVVAAGN----------DGNSGSGTSKPLATNNpDTGTVgsPATADD 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 334 CSSTLATTYSSGNQNEKQI-------VTTDLRQK-----------CT------ESHTGTSASAPLAAGIIALALEA---- 385
Cdd:cd07475   216 VLTVASANKKVPNPNGGQMsgfsswgPTPDLDLKpditapggniySTvndntyGYMSGTSMASPHVAGASALVKQRlkek 295

                         330       340       350
                  ....*....|....*....|....*....|
gi 2104551491 386 NKNLTWRDMQHLVVQ----TSKPAHLNAND 411
Cdd:cd07475   296 YPKLSGEELVDLVKNllmnTATPPLDSEDT 325
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 646-670 4.05e-09

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 52.91  E-value: 4.05e-09
                          10        20
                  ....*....|....*....|....*
gi 2104551491 646 PCHPSCATCTGPGPNQCLTCPAHSH 670
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFY 25
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 133-383 2.05e-08

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: 56.17  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 133 LNVRQAW-EQGYTGKGIVVSILDDGIEKNHPDLeanydPGASFDVNDQDPDPQprytqmnDNRHGTRCAGEVAAvANNGI 211
Cdd:cd04843     2 INARYAWtKPGGSGQGVTFVDIEQGWNLNHEDL-----VGNGITLISGLTDQA-------DSDHGTAVLGIIVA-KDNGI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 212 CGVGVAYNARIGGVRMLDGEVT-DAVEAHSLGLNPNHIHIYSASWGPEDdgktVDGPARLAE--EAFFRGVSQGRgGLGS 288
Cdd:cd04843    69 GVTGIAHGAQAAVVSSTRVSNTaDAILDAADYLSPGDVILLEMQTGGPN----NGYPPLPVEyeQANFDAIRTAT-DLGI 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 289 IFVWASGNGGREHDSC-NCDGYTNSIYTLSI-----------SSTTQygnvpwYSEACSST-------------LATTYS 343
Cdd:cd04843   144 IVVEAAGNGGQDLDAPvYNRGPILNRFSPDFrdsgaimvgagSSTTG------HTRLAFSNygsrvdvygwgenVTTTGY 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2104551491 344 SGNQNEKqivttDLRQKCTESHTGTSASAPLAAGiiALAL 383
Cdd:cd04843   218 GDLQDLG-----GENQDYTDSFSGTSSASPIVAG--AAAS 250
Peptidases_S8_7 cd07491
Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the ...
 148-383 6.45e-08

Peptidase S8 family domain, uncharacterized subfamily 7; 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: 173816  Cd Length: 247  Bit Score: 54.26  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 148 IVVSILDDGIEKNHPDLEANYDPGASFDVNDQDPD-PQPRYtqMNDNRHGT---RCAGEVAAVANNGICGVGVaYNARIG 223
Cdd:cd07491     5 IKVALIDDGVDILDSDLQGKIIGGKSFSPYEGDGNkVSPYY--VSADGHGTamaRMICRICPSAKLYVIKLED-RPSPDS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 224 GVRMLDGE-VTDAVEAHSlglnPNHIHIYSASWGPEDDGKTVDGPARLaEEAFFRGVSQGrgglgsIFVWAS----GNGG 298
Cdd:cd07491    82 NKRSITPQsAAKAIEAAV----EKKVDIISMSWTIKKPEDNDNDINEL-ENAIKEALDRG------ILLFCSasdqGAFT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 299 REHDSCnCDGYTNsiyTLSISSTTQYGNV--PWYSEacssTLATTYSSGNQnekqiVTTDLRQKCTES---HTGTSASAP 373
Cdd:cd07491   151 GDTYPP-PAARDR---IFRIGAADEDGGAdaPVGDE----DRVDYILPGEN-----VEARDRPPLSNSfvtHTGSSVATA 217

                         250
                  ....*....|
gi 2104551491 374 LAAGIIALAL 383
Cdd:cd07491   218 LAAGLAALIL 227
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 148-390 7.76e-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: 7.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 148 IVVSILDDGIEKNHPDLEANYDPGasfdVNDQDPDPQPRYTQMND----------NRHGTRCAGEVAAVANNGicgvGVA 217
Cdd:cd07482     2 VTVAVIDSGIDPDHPDLKNSISSY----SKNLVPKGGYDGKEAGEtgdindivdkLGHGTAVAGQIAANGNIK----GVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 218 YNARIGGVRMLD----GEVTDAVEAHSLGLNpNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGlGSIFVWA 293
Cdd:cd07482    74 PGIGIVSYRVFGscgsAESSWIIKAIIDAAD-DGVDVINLSLGGYLIIGGEYEDDDVEYNAYKKAINYAKSK-GSIVVAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 294 SGNGGRE---------HDSCNCDGYTNSIY---------TLSISSTTQYGNVPWYSEACSS--TLATTYSSGNQNEKQIV 353
Cdd:cd07482   152 AGNDGLDvsnkqelldFLSSGDDFSVNGEVydvpaslpnVITVSATDNNGNLSSFSNYGNSriDLAAPGGDFLLLDQYGK 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2104551491 354 TTDLRQK--------------CTESHTGTSASAPLAAGIIALALEANKNLT 390
Cdd:cd07482   232 EKWVNNGlmtkeqilttapegGYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 133-406 9.17e-08

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: 54.41  E-value: 9.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 133 LNVRQAWEQGYTGKGIVVSILDDGIEKNHPDLEANY------DPGASfdvndqDPdpqprytQMNDNRHGTrcaGEVAAV 206
Cdd:cd07494     8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYqvrvvlAPGAT------DP-------ACDENGHGT---GESANL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 207 anngicgVGVAYNARIGGVRMLDGEVTDAVEA--HSLGLNPNhihIYSASWGPEDDGKTVDGPARLA----------EEA 274
Cdd:cd07494    72 -------FAIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSPD---IISNSWGYDLRSPGTSWSRSLPnalkalaatlQDA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 275 FFRGV----SQGRGGL------------GSIFVwasGNGGREHDSCNCDGYTNSIYtlsiSSTTqygnVPwysEAC---- 334
Cdd:cd07494   142 VARGIvvvfSAGNGGWsfpaqhpeviaaGGVFV---DEDGARRASSYASGFRSKIY----PGRQ----VP---DVCglvg 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 335 ----SSTLATTYSSGNQNEkqiVTTDLRQKCTESH------TGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSKP 404
Cdd:cd07494   208 mlphAAYLMLPVPPGSQLD---RSCAAFPDGTPPNdgwgvfSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTARD 284


                  ..
gi 2104551491 405 AH 406
Cdd:cd07494   285 VT 286
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 587-671 7.92e-06

Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 45.83  E-value: 7.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 587 SSGCKTLTPSQtCVVCEegYYLHQKSCLKRCPpgFAPGVQNTHYNlensmepiaPQLCLPCHPSC------ATCTGPGPN 660
Cdd:pfam14843   8 SEGCWGPGPDQ-CLSCR--NFSRGGTCVESCN--ILQGEPREYVV---------NSTCVPCHPEClpqngtATCSGPGAD 73

                          90
                  ....*....|.
gi 2104551491 661 QCLTCpahSHF 671
Cdd:pfam14843  74 NCTKC---AHF 81
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 147-403 1.01e-05

Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173817 [Multi-domain]  Cd Length: 222  Bit Score: 47.33  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 147 GIVVSILDDGIEKNHPDLEAN------YDPGASFDVNDQDPDpqprytqmnDNRHGTRCAGEVAAVANNGIcgvgvayna 220
Cdd:cd07492     1 GVRVAVIDSGVDTDHPDLGNLaldgevTIDLEIIVVSAEGGD---------KDGHGTACAGIIKKYAPEAE--------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 221 rIGGVRML--DGEVTDAVEAHSLG-LNPNHIHIYSASWG-PEDDGKTVDGpaRLAEEAFFRGVsqgrgglgsIFVWASGN 296
Cdd:cd07492    63 -IGSIKILgeDGRCNSFVLEKALRaCVENDIRIVNLSLGgPGDRDFPLLK--ELLEYAYKAGG---------IIVAAAPN 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 297 GGREhdscncdGYTNSIYTLSI---SSTTQYGNVPWYSEACsstlattYSSGNQNekqiVTTDLRQKCTESHTGTSASAP 373
Cdd:cd07492   131 NNDI-------GTPPASFPNVIgvkSDTADDPKSFWYIYVE-------FSADGVD----IIAPAPHGRYLTVSGNSFAAP 192

                         250       260       270
                  ....*....|....*....|....*....|
gi 2104551491 374 LAAGIIALALEANKNLTWRDMQHLVVQTSK 403
Cdd:cd07492   193 HVTGMVALLLSEKPDIDANDLKRLLQRLAV 222
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 145-298 2.47e-05

Peptidase S8 family domain, uncharacterized subfamily 14; 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: 173821 [Multi-domain]  Cd Length: 311  Bit Score: 47.08  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 145 GKGIVVSILDDGIEKNHPDL--EANYDPGASFDvndqDP-------DPQPR-YTQMND-NRHGTRCAGEVAAVANNGICG 213
Cdd:cd07497     1 GEGVVIAIVDTGVDYSHPDLdiYGNFSWKLKFD----YKayllpgmDKWGGfYVIMYDfFSHGTSCASVAAGRGKMEYNL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 214 ---------VGVAYNARIGGVRMLDGEVTDAVEAHSLGLNPNH------------IHIYSASWGPEDDGKTVDGPARLAE 272
Cdd:cd07497    77 ygytgkfliRGIAPDAKIAAVKALWFGDVIYAWLWTAGFDPVDrklswiytggprVDVISNSWGISNFAYTGYAPGLDIS 156

                         170       180
                  ....*....|....*....|....*.
gi 2104551491 273 EAFFRGVSQGRgglGSIFVWASGNGG 298
Cdd:cd07497   157 SLVIDALVTYT---GVPIVSAAGNGG 179
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 366-436 6.87e-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: 45.36  E-value: 6.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2104551491 366 TGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSKPAHLNANDwvtngvgrkvsHSYGYGLLDAGAMV 436
Cdd:cd05562   214 FGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMGEPGYD-----------NASGSGLVDADRAV 273
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 587-623 8.43e-05

Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.


Pssm-ID: 464939 [Multi-domain]  Cd Length: 102  Bit Score: 42.42  E-value: 8.43e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2104551491 587 SSGCKTLTPSQTCVVCEEGYYLHQKSCLKRCPPGFAP 623
Cdd:pfam15913  59 AENCESCFSKDFCTKCKEGFYLHKGKCLDTCPEGTAA 95
VSP pfam03302
Giardia variant-specific surface protein;
597-667 1.15e-04

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 45.35  E-value: 1.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2104551491 597 QTCVVCEEGYYL--HQKSCLKRCPPGFApgvqnthynlensmepIAPQLCLPCHPSCATCTGPGPNQCLTCPA 667
Cdd:pfam03302  74 KICKECTVANCKtcEDQGQCQACNDGFY----------------KSGDACSPCHESCKTCSGGTASDCTECLT 130
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 139-162 1.05e-03

Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound subtilisin-kexin-isoenzyme) proteins are secretory Ca2+-dependent serine proteinases cleave at nonbasic residues: Thr, Leu, and Lys. SKI-1s play a critical role in the regulation of the synthesis and metabolism of cholesterol and fatty acid metabolism. 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: 173805 [Multi-domain]  Cd Length: 255  Bit Score: 41.67  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....
gi 2104551491 139 WEQGYTGKGIVVSILDDGIEKNHP 162
Cdd:cd07479     1 WQLGYTGAGVKVAVFDTGLAKDHP 24
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 237-389 2.68e-03

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: 40.15  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 237 EAHSLGLNPNHIHIYSASWGpedDGKTVDGPARL---AEEAFFRGVSQGRGGLgsIFVWASGNGGREH-DSCNCDGYTNS 312
Cdd:cd07488    75 ECLEAQQNGNNVKIINHSYG---EGLKRDPRAVLygyALLSLYLDWLSRNYEV--INVFSAGNQGKEKeKFGGISIPTLA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2104551491 313 IYTLSISSTTQYGNvPWySEACSSTLATTYSSGNQNEKQIVT-----TDLRQKcTESHTGTSASAPLAAGIIALALEANK 387
Cdd:cd07488   150 YNSIVVGSTDRNGD-RF-FASDVSNAGSEINSYGRRKVLIVApgsnyNLPDGK-DDFVSGTSFSAPLVTGIIALLLEFYD 226


                  ..
gi 2104551491 388 NL 389
Cdd:cd07488   227 RQ 228
 
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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