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Conserved domains on  [gi|2217321725|ref|XP_047294939|]
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proprotein convertase subtilisin/kexin type 4 isoform X13 [Homo sapiens]

Protein Classification

S8 family peptidase( domain architecture ID 10134558)

S8 family peptidase is a subtilisin-like serine protease containing a Asp/His/Ser catalytic triad that is not homologous to trypsin; similar to Candida albicans kexin that catalyzes the cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors

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 ...
 34-219 4.07e-101

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: 307.56  E-value: 4.07e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  34 PPAKRTGVRMLDGTITDVIEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGILTREAFRRGVTKGRGGLGTLFIWASGNG 113
Cdd:cd04059   109 PGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGPLAQRALENGVTNGRNGKGSIFVWAAGNG 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 114 GLHYDNCNCDGYTNSIHTLSVGSTTQQGRVPWYSEACASTLTTTYSSG-VATDPQIVTTDLH--HGCTDQHTGTSASAPL 190
Cdd:cd04059   189 GNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGsGNPEASIVTTDLGgnCNCTSSHNGTSAAAPL 268

                         170       180
                  ....*....|....*....|....*....
gi 2217321725 191 AAGMIALALEANPFLTWRDMQHLVVRASK 219
Cdd:cd04059   269 AAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 301-385 1.51e-29

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: 111.59  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 301 LEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYfNTGTL 380
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG-DTGTL 79


                  ....*
gi 2217321725 381 YRYTL 385
Cdd:pfam01483  80 NSWQL 84
FU smart00261
Furin-like repeats;
459-496 1.46e-05

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 42.50  E-value: 1.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217321725  459 RVCSSCHASCYTCRGGSPRDCTSCPPSSTLDqqQGSCM 496
Cdd:smart00261   2 GECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCV 37
 
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 ...
 34-219 4.07e-101

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: 307.56  E-value: 4.07e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  34 PPAKRTGVRMLDGTITDVIEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGILTREAFRRGVTKGRGGLGTLFIWASGNG 113
Cdd:cd04059   109 PGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGPLAQRALENGVTNGRNGKGSIFVWAAGNG 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 114 GLHYDNCNCDGYTNSIHTLSVGSTTQQGRVPWYSEACASTLTTTYSSG-VATDPQIVTTDLH--HGCTDQHTGTSASAPL 190
Cdd:cd04059   189 GNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGsGNPEASIVTTDLGgnCNCTSSHNGTSAAAPL 268

                         170       180
                  ....*....|....*....|....*....
gi 2217321725 191 AAGMIALALEANPFLTWRDMQHLVVRASK 219
Cdd:cd04059   269 AAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 301-385 1.51e-29

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: 111.59  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 301 LEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYfNTGTL 380
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG-DTGTL 79


                  ....*
gi 2217321725 381 YRYTL 385
Cdd:pfam01483  80 NSWQL 84
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 34-244 2.32e-29

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: 117.56  E-value: 2.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  34 PPAKRTGVRML-DGTITDVIEAQSLS-LQPQHIHIYSASWGPEddgRTVDGPGILTREAFRRGvtkGRGGLGTLFIWASG 111
Cdd:pfam00082  78 PGAKILGVRVFgDGGGTDAITAQAISwAIPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 112 NGGLHYDNCNCDGY-TNSIHTLSVGSTTQ---QGRVPW--YSEACASTL--------TTTYSSGVATDPQIVTTDLHHGC 177
Cdd:pfam00082 152 NGSPGGNNGSSVGYpAQYKNVIAVGAVDEaseGNLASFssYGPTLDGRLkpdivapgGNITGGNISSTLLTTTSDPPNQG 231

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217321725 178 TDQHTGTSASAPLAAGMIALALEANPFLTWRDMQHLVVRASKPAHLQAEDwrtngvgrqvsHHYGYG 244
Cdd:pfam00082 232 YDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD-----------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 40-255 6.55e-13

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 70.90  E-value: 6.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  40 GVRMLD----GTITDVIEAQSLSLQpQHIHIYSASWGpeddgrtvdGPGILTREAFRRGVTKGRGgLGTLFIWASGNGGl 115
Cdd:COG1404   179 PVRVLDdngsGTTSDIAAAIDWAAD-NGADVINLSLG---------GPADGYSDALAAAVDYAVD-KGVLVVAAAGNSG- 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 116 hyDNCNCDGYTNSI-HTLSVGSTTQQGRVPWYSeacastltttySSGVATD---P--QIVTTDLHHGcTDQHTGTSASAP 189
Cdd:COG1404   247 --SDDATVSYPAAYpNVIAVGAVDANGQLASFS-----------NYGPKVDvaaPgvDILSTYPGGG-YATLSGTSMAAP 312

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217321725 190 LAAGMIALALEANPFLTWRDMQHLVVRASKPAHLQaedwrtngvgrqvSHHYGYGLLDAGLLVDTA 255
Cdd:COG1404   313 HVAGAAALLLSANPDLTPAQVRAILLNTATPLGAP-------------GPYYGYGLLADGAAGATS 365
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 302-389 5.63e-07

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: 52.52  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 302 EHVQAQLTLSYSRRGDLEISLTSPMGTRSTLvaIRPLDVSTEGYnNWVFMSTHFWDENPQGVWTLGLENkGYYFNTGTLY 381
Cdd:COG4935   558 EDVTVTVDITHTYRGDLVITLISPDGTTVVL--KNRSGGSADNI-NATFDVANFSGESANGTWTLRVVD-TAGGDTGTLN 633


                  ....*...
gi 2217321725 382 RYTLLLYG 389
Cdd:COG4935   634 SWSLTFTG 641
FU smart00261
Furin-like repeats;
459-496 1.46e-05

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 42.50  E-value: 1.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217321725  459 RVCSSCHASCYTCRGGSPRDCTSCPPSSTLDqqQGSCM 496
Cdd:smart00261   2 GECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCV 37
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 464-496 1.37e-04

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: 39.81  E-value: 1.37e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217321725 464 CHASCYTCRGGSPRDCTSCPPSSTLDqqQGSCM 496
Cdd:cd00064     2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCV 32
VSP pfam03302
Giardia variant-specific surface protein;
461-495 6.57e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 39.18  E-value: 6.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217321725 461 CSSCHASCYTCRGGSPRDCTSCPPSSTL----DQQQGSC 495
Cdd:pfam03302 107 CSPCHESCKTCSGGTASDCTECLTGKALrygnDGTKGTC 145
 
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 ...
 34-219 4.07e-101

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: 307.56  E-value: 4.07e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  34 PPAKRTGVRMLDGTITDVIEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGILTREAFRRGVTKGRGGLGTLFIWASGNG 113
Cdd:cd04059   109 PGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGPLAQRALENGVTNGRNGKGSIFVWAAGNG 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 114 GLHYDNCNCDGYTNSIHTLSVGSTTQQGRVPWYSEACASTLTTTYSSG-VATDPQIVTTDLH--HGCTDQHTGTSASAPL 190
Cdd:cd04059   189 GNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGsGNPEASIVTTDLGgnCNCTSSHNGTSAAAPL 268

                         170       180
                  ....*....|....*....|....*....
gi 2217321725 191 AAGMIALALEANPFLTWRDMQHLVVRASK 219
Cdd:cd04059   269 AAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 301-385 1.51e-29

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: 111.59  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 301 LEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYfNTGTL 380
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAPG-DTGTL 79


                  ....*
gi 2217321725 381 YRYTL 385
Cdd:pfam01483  80 NSWQL 84
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 34-244 2.32e-29

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: 117.56  E-value: 2.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  34 PPAKRTGVRML-DGTITDVIEAQSLS-LQPQHIHIYSASWGPEddgRTVDGPGILTREAFRRGvtkGRGGLGTLFIWASG 111
Cdd:pfam00082  78 PGAKILGVRVFgDGGGTDAITAQAISwAIPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 112 NGGLHYDNCNCDGY-TNSIHTLSVGSTTQ---QGRVPW--YSEACASTL--------TTTYSSGVATDPQIVTTDLHHGC 177
Cdd:pfam00082 152 NGSPGGNNGSSVGYpAQYKNVIAVGAVDEaseGNLASFssYGPTLDGRLkpdivapgGNITGGNISSTLLTTTSDPPNQG 231

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217321725 178 TDQHTGTSASAPLAAGMIALALEANPFLTWRDMQHLVVRASKPAHLQAEDwrtngvgrqvsHHYGYG 244
Cdd:pfam00082 232 YDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD-----------RLFGYG 287
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 65-209 2.49e-13

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: 69.68  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  65 HIYSASWGPEDdgrtvdgPGILTREAFRRGVTKGRGGLGTLFIWASGNGGlhydNCNCDGYTNSIHTLSVGSTTQQGRVP 144
Cdd:cd07498    99 DVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLFAAGNSG----RSVSSGYAANPSVIAVAATDSNDARA 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217321725 145 WYSEACASTLTTTYSSGVATD--PQIVTTDLHHGCTDQHTGTSASAPLAAGMIALALEANPFLTWRD 209
Cdd:cd07498   168 SYSNYGNYVDLVAPGVGIWTTgtGRGSAGDYPGGGYGSFSGTSFASPVAAGVAALILSANPNLTPAE 234
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 40-255 6.55e-13

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 70.90  E-value: 6.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  40 GVRMLD----GTITDVIEAQSLSLQpQHIHIYSASWGpeddgrtvdGPGILTREAFRRGVTKGRGgLGTLFIWASGNGGl 115
Cdd:COG1404   179 PVRVLDdngsGTTSDIAAAIDWAAD-NGADVINLSLG---------GPADGYSDALAAAVDYAVD-KGVLVVAAAGNSG- 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 116 hyDNCNCDGYTNSI-HTLSVGSTTQQGRVPWYSeacastltttySSGVATD---P--QIVTTDLHHGcTDQHTGTSASAP 189
Cdd:COG1404   247 --SDDATVSYPAAYpNVIAVGAVDANGQLASFS-----------NYGPKVDvaaPgvDILSTYPGGG-YATLSGTSMAAP 312

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217321725 190 LAAGMIALALEANPFLTWRDMQHLVVRASKPAHLQaedwrtngvgrqvSHHYGYGLLDAGLLVDTA 255
Cdd:COG1404   313 HVAGAAALLLSANPDLTPAQVRAILLNTATPLGAP-------------GPYYGYGLLADGAAGATS 365
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 28-216 1.14e-12

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: 68.00  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  28 TPSPATPPAKRTGVRMLD----GTITDVIEAQSLSLQPQHIHIYSASWGPEDDGRTVDgpgilTREAFRRGVTKgrggLG 103
Cdd:cd00306    62 GGVGVAPGAKLIPVKVLDgdgsGSSSDIAAAIDYAAADQGADVINLSLGGPGSPPSSA-----LSEAIDYALAK----LG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 104 TLFIWASGNGGLHYDNcNCDGYTNSIHTLSVGSTTQQGRV-PWYSEACASTLTTTYSSGVATDPQIVTtdlhhGCTDQHT 182
Cdd:cd00306   133 VLVVAAAGNDGPDGGT-NIGYPAASPNVIAVGAVDRDGTPaSPSSNGGAGVDIAAPGGDILSSPTTGG-----GGYATLS 206

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217321725 183 GTSASAPLAAGMIALALEANPFLTWRDMQHLVVR 216
Cdd:cd00306   207 GTSMAAPIVAGVAALLLSANPDLTPAQVKAALLS 240
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 64-209 7.17e-10

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: 59.90  E-value: 7.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  64 IHIYSASWGPeddgrtvDGPGILTREAFRRGVTKGrgglgTLFIWASGNGGLhyDNCNCDGYTNSI---HTLSVGSTTQQ 140
Cdd:cd07473   121 AKIINNSWGG-------GGPSQALRDAIARAIDAG-----ILFVAAAGNDGT--NNDKTPTYPASYdldNIISVAATDSN 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217321725 141 GRVPWYSeacastltttySSGVAT-D---P--QIVTTDLhHGCTDQHTGTSASAPLAAGMIALALEANPFLTWRD 209
Cdd:cd07473   187 DALASFS-----------NYGKKTvDlaaPgvDILSTSP-GGGYGYMSGTSMATPHVAGAAALLLSLNPNLTAAQ 249
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 62-206 8.45e-09

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: 56.56  E-value: 8.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  62 QHIHIYSASWGPEDDGRTVDGPGIL--------TREAFRRGVTKGrgglgTLFIWASGNGGlhydncncdGYTNSI---- 129
Cdd:cd04848   102 SGVRIINNSWGGNPAIDTVSTTYKGsaatqgntLLAALARAANAG-----GLFVFAAGNDG---------QANPSLaaaa 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 130 ----------HTLSVGSTTQQGRVP--WYSEACastLTTTYSSGVATDPQIVTTDLHHGCT-DQHTGTSASAPLAAGMIA 196
Cdd:cd04848   168 lpylepelegGWIAVVAVDPNGTIAsySYSNRC---GVAANWCLAAPGENIYSTDPDGGNGyGRVSGTSFAAPHVSGAAA 244

                         170
                  ....*....|
gi 2217321725 197 LALEANPFLT 206
Cdd:cd04848   245 LLAQKFPWLT 254
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 302-389 5.63e-07

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: 52.52  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 302 EHVQAQLTLSYSRRGDLEISLTSPMGTRSTLvaIRPLDVSTEGYnNWVFMSTHFWDENPQGVWTLGLENkGYYFNTGTLY 381
Cdd:COG4935   558 EDVTVTVDITHTYRGDLVITLISPDGTTVVL--KNRSGGSADNI-NATFDVANFSGESANGTWTLRVVD-TAGGDTGTLN 633


                  ....*...
gi 2217321725 382 RYTLLLYG 389
Cdd:COG4935   634 SWSLTFTG 641
FU smart00261
Furin-like repeats;
459-496 1.46e-05

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 42.50  E-value: 1.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2217321725  459 RVCSSCHASCYTCRGGSPRDCTSCPPSSTLDqqQGSCM 496
Cdd:smart00261   2 GECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCV 37
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 102-206 1.16e-04

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: 44.21  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 102 LGTLFIWASGNGGLHYDN---CNCDGytnsihTLSVGSTTQQGRVPWYSE--------ACASTLTTTYSSGVATDPQIVT 170
Cdd:cd07496   165 RGVLVVVAAGNEGSSASVdapANCRG------VIAVGATDLRGQRASYSNygpavdvsAPGGDCASDVNGDGYPDSNTGT 238

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217321725 171 TDLHHGCTDQHTGTSASAPLAAGMIALALEANPFLT 206
Cdd:cd07496   239 TSPGGSTYGFLQGTSMAAPHVAGVAALMKSVNPSLT 274
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 464-496 1.37e-04

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: 39.81  E-value: 1.37e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217321725 464 CHASCYTCRGGSPRDCTSCPPSSTLDqqQGSCM 496
Cdd:cd00064     2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCV 32
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 77-227 2.47e-04

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: 43.09  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  77 GRTVDGPGILTREAFRRGVTkgrggLGTLFIWASGNGGlhyDNCNCDG-YTNSIHTLSVGSTTqqGRVPWYSEacasTLT 155
Cdd:cd07474   128 GSSVNGPDDPDAIAINNAVK-----AGVVVVAAAGNSG---PAPYTIGsPATAPSAITVGAST--VADVAEAD----TVG 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 156 TTYSSGVATDPQIVTTDL-------------HHGCTDQHTGTSASAPLAAGMIALALEANPFLTWRDMQHLVVRASKPAH 222
Cdd:cd07474   194 PSSSRGPPTSDSAIKPDIvapgvdimstapgSGTGYARMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLY 273


                  ....*
gi 2217321725 223 LQAED 227
Cdd:cd07474   274 DSDGV 278
Peptidases_S53 cd04056
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
 34-202 5.53e-04

Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.


Pssm-ID: 173788 [Multi-domain]  Cd Length: 361  Bit Score: 42.30  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  34 PPAK----RTGVRMLDGTITDVIEAqsLSLQPQHIHIYSASWG-PEDDgrtvDGPGILTR--EAFR----RGVTkgrggl 102
Cdd:cd04056    88 PGANitlyFAPGTVTNGPLLAFLAA--VLDNPNLPSVISISYGePEQS----LPPAYAQRvcNLFAqaaaQGIT------ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 103 gtlFIWASGNGGLHYDNCNCDGYTNSIHT-------LSVGSTT--QQGRVPWYSEACASTLTTTYSSG------------ 161
Cdd:cd04056   156 ---VLAASGDSGAGGCGGDGSGTGFSVSFpasspyvTAVGGTTlyTGGTGSSAESTVWSSEGGWGGSGggfsnyfprpsy 232

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217321725 162 ----VATDPQIVTT--------------DLHHG---CTDQHT----GTSASAPLAAGMIALALEAN 202
Cdd:cd04056   233 qsgaVLGLPPSGLYngsgrgvpdvaanaDPGTGylvVVNGQWylvgGTSAAAPLFAGLIALINQAR 298
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 182-254 6.00e-04

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: 41.89  E-value: 6.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217321725 182 TGTSASAPLAAGMIALALEANPFLTWRDMQhLVVRASkpahlqAEDWRTNGvgrqVSHHYGYGLLDAGLLVDT 254
Cdd:cd05562   214 FGTSAAAPHAAGVAALVLSANPGLTPADIR-DALRST------ALDMGEPG----YDNASGSGLVDADRAVAA 275
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 103-200 2.32e-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: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 103 GTLFIWASGNGGLHYDNC-NCDGYTNSIHTLSVGSTTQQGRvPWySEACASTLTTTYSSGVATDPQIVTT----DLHHGC 177
Cdd:cd07488   123 EVINVFSAGNQGKEKEKFgGISIPTLAYNSIVVGSTDRNGD-RF-FASDVSNAGSEINSYGRRKVLIVAPgsnyNLPDGK 200

                          90       100
                  ....*....|....*....|...
gi 2217321725 178 TDQHTGTSASAPLAAGMIALALE 200
Cdd:cd07488   201 DDFVSGTSFSAPLVTGIIALLLE 223
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
 132-207 2.69e-03

Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173818 [Multi-domain]  Cd Length: 261  Bit Score: 39.98  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725 132 LSVGSTTQQGRVpwyseacastltTTYSS-GVATDPQI----------VTTDLHHGCTDQHTGTSASAPLAAGMIALALE 200
Cdd:cd07493   175 LSVGAVDANGNK------------ASFSSiGPTADGRLkpdvmalgtgIYVINGDGNITYANGTSFSCPLIAGLIACLWQ 242


                  ....*..
gi 2217321725 201 ANPFLTW 207
Cdd:cd07493   243 AHPNWTN 249
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 65-203 5.59e-03

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: 38.90  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217321725  65 HIYSASWGpeddgrtvdGPGiLTREAFRRGVTKGRGGlGTLFIWASGNGGLHYDNCNcDGYTNSIHTLSVGSTTQQGRVP 144
Cdd:cd07481   121 DVINNSWG---------GPS-GDNEWLQPAVAAWRAA-GIFPVFAAGNDGPRCSTLN-APPANYPESFAVGATDRNDVLA 188

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217321725 145 WYSEACASTLTTTYSSGVATDPQIVTTdLHHGCTDQHTGTSASAPLAAGMIALALEANP 203
Cdd:cd07481   189 DFSSRGPSTYGRIKPDISAPGVNIRSA-VPGGGYGSSSGTSMAAPHVAGVAALLWSANP 246
VSP pfam03302
Giardia variant-specific surface protein;
461-495 6.57e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 39.18  E-value: 6.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217321725 461 CSSCHASCYTCRGGSPRDCTSCPPSSTL----DQQQGSC 495
Cdd:pfam03302 107 CSPCHESCKTCSGGTASDCTECLTGKALrygnDGTKGTC 145
 
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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