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Conserved domains on  [gi|1831506036|ref|NP_001367786|]
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Endoprotease bli-4 [Caenorhabditis elegans]

Protein Classification

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 ...
 160-448 1.30e-163

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: 476.28  E-value: 1.30e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 160 FPDPLYKDQWYLHG----GAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQN 235
Cdd:cd04059     1 PNDPLFPYQWYLKNtgqaGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 236 NGDNKHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGP 315
Cdd:cd04059    81 DDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 316 LAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDSCSADGYTTSVYTLSISSATYDNHRPWYLEECPSSIATTYSS-ADFR 394
Cdd:cd04059   161 LAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGgSGNP 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831506036 395 QPAIVTVDV--PGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTA 448
Cdd:cd04059   241 EASIVTTDLggNCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTA 296
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 536-621 8.09e-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: 110.05  E-value: 8.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 536 LEHVQVHATVRYLKRGDLKLTLFSPSGTRSVLLPPRPQDFNANGFHKWPFLSVQQWGEDPRGTWLLMVESvtTNPAATGT 615
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD--TAPGDTGT 78


                  ....*.
gi 1831506036 616 FHDWTL 621
Cdd:pfam01483  79 LNSWQL 84
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 41-116 2.18e-20

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: 85.73  E-value: 2.18e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831506036  41 HTVIRLaKRDDELARRIAADHDMHVKGDPF-LDTHYFLYHSET-TRTRRHKRAIVERLDSHPAVEWVEEQRPKKRVKR 116
Cdd:pfam16470   1 EWAVHL-EGGPEEADRIAEKHGFINLGQIGgLEDYYHFRHRRVsKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
Furin-like super family cl25784
Furin-like cysteine rich region;
675-773 4.50e-09

Furin-like cysteine rich region;


The actual alignment was detected with superfamily member pfam00757:

Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 55.91  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 675 CHDECNGGCTESSsATSCFACKHLtqtlRNKGgsgfKCVQKCDDTYYLDGDKCKmcsshchtctkaeVCETCPGSlllID 754
Cdd:pfam00757  49 CHEQCLGGCTGPN-DSDCLACRHF----NDEG----TCVDQCPPGTYQFGWRCV-------------TFKECPKS---HL 103

                          90       100
                  ....*....|....*....|
gi 1831506036 755 VDNMPHY-DHGKCVESCPPG 773
Cdd:pfam00757 104 PGYNPLViHNGECVRECPSG 123
 
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 ...
 160-448 1.30e-163

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: 476.28  E-value: 1.30e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 160 FPDPLYKDQWYLHG----GAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQN 235
Cdd:cd04059     1 PNDPLFPYQWYLKNtgqaGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 236 NGDNKHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGP 315
Cdd:cd04059    81 DDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 316 LAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDSCSADGYTTSVYTLSISSATYDNHRPWYLEECPSSIATTYSS-ADFR 394
Cdd:cd04059   161 LAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGgSGNP 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831506036 395 QPAIVTVDV--PGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTA 448
Cdd:cd04059   241 EASIVTTDLggNCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTA 296
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 193-475 1.12e-59

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: 204.23  E-value: 1.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 193 GRNVSVSILDDGIQRDHPDLAANY------DPLASTDINDHDDDPTPQNNGDNKHGTRCAGEVAALAGNNQCGVGVAFKA 266
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLdndpsdDPEASVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 267 KIGGVRML-DGAVSDSVEAASLSLN-QDHIDIYSASWGPEddgKTFDGPGPLAREAFYRGiknGRGGKGNIFVWASGNGG 344
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 345 SRQDSCSADGY-TTSVYTLSISS---------ATYDNHRP-WYLEECPSSIA---TTYSSADFRQPAIVTVDVPGGCTDK 410
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAvdeasegnlASFSSYGPtLDGRLKPDIVApggNITGGNISSTLLTTTSDPPNQGYDS 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831506036 411 HTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKPlennpgwsrngvGRMVSNKFGYG 475
Cdd:pfam00082 235 MSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLG------------DAGLDRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 91-482 8.03e-36

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 141.77  E-value: 8.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036  91 AIVERLDSHPAVEWVEEQRPKKRVKRDYILLDNDVHHSNPFRRSVLNRDGTRRAQRQQPQSPREIPSLPFPDPLYKDQWY 170
Cdd:COG1404     6 LALVAALVAAALAAAAAAAAALAAALLVVLAAGVAVAAAAAALVAAAAAAAVAAALAAPLAPAALAAPAPLPVPAAAPAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 171 LHGGAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYdpLASTDINDHDDDPTpqnnGDNKHGTRCAGEVA 250
Cdd:COG1404    86 VRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRV--VGGYDFVDGDGDPS----DDNGHGTHVAGIIA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 251 ALAGNNQCGVGVAFKAKIGGVRMLD----GAVSDSVEAASLSLNQdHIDIYSASWGpeddgktfdGPGPLAREAFYRGIK 326
Cdd:COG1404   160 ANGNNGGGVAGVAPGAKLLPVRVLDdngsGTTSDIAAAIDWAADN-GADVINLSLG---------GPADGYSDALAAAVD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 327 NGRGgKGNIFVWASGNGGSRQDS----CSADGyttsvyTLSISSATYDNHRPWYleecpSSIATTYS-SAdfrqP--AIV 399
Cdd:COG1404   230 YAVD-KGVLVVAAAGNSGSDDATvsypAAYPN------VIAVGAVDANGQLASF-----SNYGPKVDvAA----PgvDIL 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 400 TVdVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKPLENnpgwsrngvgrmvsNKFGYGLIDG 479
Cdd:COG1404   294 ST-YPGGGYATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPG--------------PYYGYGLLAD 358


                  ...
gi 1831506036 480 GAL 482
Cdd:COG1404   359 GAA 361
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 536-621 8.09e-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: 110.05  E-value: 8.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 536 LEHVQVHATVRYLKRGDLKLTLFSPSGTRSVLLPPRPQDFNANGFHKWPFLSVQQWGEDPRGTWLLMVESvtTNPAATGT 615
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD--TAPGDTGT 78


                  ....*.
gi 1831506036 616 FHDWTL 621
Cdd:pfam01483  79 LNSWQL 84
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 41-116 2.18e-20

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: 85.73  E-value: 2.18e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831506036  41 HTVIRLaKRDDELARRIAADHDMHVKGDPF-LDTHYFLYHSET-TRTRRHKRAIVERLDSHPAVEWVEEQRPKKRVKR 116
Cdd:pfam16470   1 EWAVHL-EGGPEEADRIAEKHGFINLGQIGgLEDYYHFRHRRVsKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 181-494 1.96e-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: 75.44  E-value: 1.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 181 MNVRQAWlQGYAGRNVSVSILDDGIQrDHPDLAANYDP----LASTD-INDHDddptpqnngdnKHGTRCAGEVAALAGN 255
Cdd:TIGR03921   1 LSLEQAW-KFSTGAGVTVAVIDTGVD-DHPRLPGLVLPggdfVGSGDgTDDCD-----------GHGTLVAGIIAGRPGE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 256 NQCGVGVAFKAKIGGVRMLDGAVSDSVEAAS--------------LSLNQDHIDIYSASWGPEDDGKTFDGPGPLAREAF 321
Cdd:TIGR03921  68 GDGFSGVAPDARILPIRQTSAAFEPDEGTSGvgdlgtlakairraADLGADVINISLVACLPAGSGADDPELGAAVRYAL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 322 yrgikngrgGKGNIFVWASGNGGsrqdscsADGYTTSV-------YTLSISS-------ATYDNHRPWYLEECPSSIatt 387
Cdd:TIGR03921 148 ---------DKGVVVVAAAGNTG-------GDGQKTTVvypawypGVLAVGSidrdgtpSSFSLPGPWVDLAAPGEN--- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 388 yssadfrqpaIVTVDVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTAnwkplennpgwsRNGVGRM 467
Cdd:TIGR03921 209 ----------IVSLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEATA------------DHPARGG 266

                         330       340
                  ....*....|....*....|....*..
gi 1831506036 468 VSNKFGYGLIDGGAlvnmAKTWKTVPE 494
Cdd:TIGR03921 267 RDDYVGYGVVDPVA----ALTGELPPE 289
Furin-like pfam00757
Furin-like cysteine rich region;
675-773 4.50e-09

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 55.91  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 675 CHDECNGGCTESSsATSCFACKHLtqtlRNKGgsgfKCVQKCDDTYYLDGDKCKmcsshchtctkaeVCETCPGSlllID 754
Cdd:pfam00757  49 CHEQCLGGCTGPN-DSDCLACRHF----NDEG----TCVDQCPPGTYQFGWRCV-------------TFKECPKS---HL 103

                          90       100
                  ....*....|....*....|
gi 1831506036 755 VDNMPHY-DHGKCVESCPPG 773
Cdd:pfam00757 104 PGYNPLViHNGECVRECPSG 123
FU smart00261
Furin-like repeats;
724-773 1.14e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.96  E-value: 1.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831506036  724 GDKCKMCSSHCHTCT--KAEVCETCPGSLLLidvdnmphyDHGKCVESCPPG 773
Cdd:smart00261   1 DGECKPCHPECATCTgpGPDDCTSCKHGFFL---------DGGKCVSECPPG 43
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 730-777 2.31e-05

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: 42.51  E-value: 2.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831506036 730 CSSHCHTCT--KAEVCETCPGSLLLidvdnmphyDHGKCVESCPPGLVAD 777
Cdd:cd00064     2 CHPSCATCTgpGPDQCTSCRHGFYL---------DGGTCVSECPEGTYAD 42
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 196-459 2.45e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 44.57  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 196 VSVSILDDGIQRDHPDLAANY---------------------DPLASTDINDHDDDPTpqnnGDNKHGTRCAGEVAALAG 254
Cdd:PTZ00262  318 TNICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM----DDNYHGTHVSGIISAIGN 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 255 NNQCGVGVAFKAKIGGVRMLD----GAVSDSVEAASLSLNQDhIDIYSASWGPEDDGKTFDGPGPLAREafyrgikngrg 330
Cdd:PTZ00262  394 NNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFNESVKYLEE----------- 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 331 gKGNIFVWASGNggsrqdsCSADGYTTSVYT---LSIS-------SATYDN-------------HRPWYLEECPSSI--- 384
Cdd:PTZ00262  462 -KGILFVVSASN-------CSHTKESKPDIPkcdLDVNkvyppilSKKLRNvitvsnlikdknnQYSLSPNSFYSAKycq 533

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 385 -----ATTYSSADFRQPAIVtvdvpggctdkhTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKP-LENNPG 458
Cdd:PTZ00262  534 laapgTNIYSTFPKNSYRKL------------NGTSMAAPHVAAIASLILSINPSLSYEEVIRILKESIVQLPsLKNKVK 601


                  .
gi 1831506036 459 W 459
Cdd:PTZ00262  602 W 602
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 678-793 3.79e-03

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 41.06  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 678 ECNGGCTESSSAT--SCFACKHLTQTLRNKGGSGFKCVQ--KCDDTYYLDGDKCKMCSS-HCHTCTKAEVCETCPGSlLL 752
Cdd:PTZ00214  578 ECDPTCLACTAPGpgRCTRCPSDKLLKRASGAATGSCVDpgACVDGYYADGDACLPCATpGCKTCGHASFCTECAGE-LF 656

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831506036 753 IDVDN-----------------------------MPHYDHGKCV--ESCPPGLvadyaenfDFCAKNNESGR 793
Cdd:PTZ00214  657 VSLDGqscleectgdkvvgevsggvrrcwcergfLPALDRSGCVlpTECPPDM--------PSCAACDESGR 720
 
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 ...
 160-448 1.30e-163

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: 476.28  E-value: 1.30e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 160 FPDPLYKDQWYLHG----GAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQN 235
Cdd:cd04059     1 PNDPLFPYQWYLKNtgqaGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 236 NGDNKHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGP 315
Cdd:cd04059    81 DDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 316 LAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDSCSADGYTTSVYTLSISSATYDNHRPWYLEECPSSIATTYSS-ADFR 394
Cdd:cd04059   161 LAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGgSGNP 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831506036 395 QPAIVTVDV--PGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTA 448
Cdd:cd04059   241 EASIVTTDLggNCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTA 296
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 193-475 1.12e-59

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: 204.23  E-value: 1.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 193 GRNVSVSILDDGIQRDHPDLAANY------DPLASTDINDHDDDPTPQNNGDNKHGTRCAGEVAALAGNNQCGVGVAFKA 266
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLdndpsdDPEASVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 267 KIGGVRML-DGAVSDSVEAASLSLN-QDHIDIYSASWGPEddgKTFDGPGPLAREAFYRGiknGRGGKGNIFVWASGNGG 344
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 345 SRQDSCSADGY-TTSVYTLSISS---------ATYDNHRP-WYLEECPSSIA---TTYSSADFRQPAIVTVDVPGGCTDK 410
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAvdeasegnlASFSSYGPtLDGRLKPDIVApggNITGGNISSTLLTTTSDPPNQGYDS 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831506036 411 HTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKPlennpgwsrngvGRMVSNKFGYG 475
Cdd:pfam00082 235 MSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLG------------DAGLDRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 91-482 8.03e-36

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 141.77  E-value: 8.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036  91 AIVERLDSHPAVEWVEEQRPKKRVKRDYILLDNDVHHSNPFRRSVLNRDGTRRAQRQQPQSPREIPSLPFPDPLYKDQWY 170
Cdd:COG1404     6 LALVAALVAAALAAAAAAAAALAAALLVVLAAGVAVAAAAAALVAAAAAAAVAAALAAPLAPAALAAPAPLPVPAAAPAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 171 LHGGAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYdpLASTDINDHDDDPTpqnnGDNKHGTRCAGEVA 250
Cdd:COG1404    86 VRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRV--VGGYDFVDGDGDPS----DDNGHGTHVAGIIA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 251 ALAGNNQCGVGVAFKAKIGGVRMLD----GAVSDSVEAASLSLNQdHIDIYSASWGpeddgktfdGPGPLAREAFYRGIK 326
Cdd:COG1404   160 ANGNNGGGVAGVAPGAKLLPVRVLDdngsGTTSDIAAAIDWAADN-GADVINLSLG---------GPADGYSDALAAAVD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 327 NGRGgKGNIFVWASGNGGSRQDS----CSADGyttsvyTLSISSATYDNHRPWYleecpSSIATTYS-SAdfrqP--AIV 399
Cdd:COG1404   230 YAVD-KGVLVVAAAGNSGSDDATvsypAAYPN------VIAVGAVDANGQLASF-----SNYGPKVDvAA----PgvDIL 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 400 TVdVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKPLENnpgwsrngvgrmvsNKFGYGLIDG 479
Cdd:COG1404   294 ST-YPGGGYATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPG--------------PYYGYGLLAD 358


                  ...
gi 1831506036 480 GAL 482
Cdd:COG1404   359 GAA 361
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 196-447 1.11e-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: 135.55  E-value: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 196 VSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQNNgdnkHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLD 275
Cdd:cd07498     1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPTSDIDG----HGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRIAD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 276 --GAVSDSVEAASLSLNQDH-IDIYSASWGPEDdgktfdgPGPLAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDSCSA 352
Cdd:cd07498    77 slGYAYWSDIAQAITWAADNgADVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLFAAGNSGRSVSSGYA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 353 DgyTTSVYTLSISS-----ATYDNHRPwYLEEC-PSS-IATTYSsadfrqPAIVTVDVPGGCTDKHTGTSASAPLAAGII 425
Cdd:cd07498   150 A--NPSVIAVAATDsndarASYSNYGN-YVDLVaPGVgIWTTGT------GRGSAGDYPGGGYGSFSGTSFASPVAAGVA 220

                         250       260
                  ....*....|....*....|..
gi 1831506036 426 ALALEANPELTWRDMQHLVLRT 447
Cdd:cd07498   221 ALILSANPNLTPAEVEDILTST 242
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 196-447 7.11e-32

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: 124.62  E-value: 7.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 196 VSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQNNGDNKHGTRCAGEVAAlAGNNQCGVGVAFKAKIGGVRMLD 275
Cdd:cd00306     1 VTVAVIDTGVDPDHPDLDGLFGGGDGGNDDDDNENGPTDPDDGNGHGTHVAGIIAA-SANNGGGVGVAPGAKLIPVKVLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 276 ----GAVSDSVEAASLSLNQDHIDIYSASWGpeddgktfdGPGPLAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDScS 351
Cdd:cd00306    80 gdgsGSSSDIAAAIDYAAADQGADVINLSLG---------GPGSPPSSALSEAIDYALAKLGVLVVAAAGNDGPDGGT-N 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 352 ADGYTTSVYTLSISSATYDNHRpwyleecpssiaTTYSSADFRQPAIV--------TVDVPGGCTDKHTGTSASAPLAAG 423
Cdd:cd00306   150 IGYPAASPNVIAVGAVDRDGTP------------ASPSSNGGAGVDIAapggdilsSPTTGGGGYATLSGTSMAAPIVAG 217

                         250       260
                  ....*....|....*....|....
gi 1831506036 424 IIALALEANPELTWRDMQHLVLRT 447
Cdd:cd00306   218 VAALLLSANPDLTPAQVKAALLST 241
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 536-621 8.09e-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: 110.05  E-value: 8.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 536 LEHVQVHATVRYLKRGDLKLTLFSPSGTRSVLLPPRPQDFNANGFHKWPFLSVQQWGEDPRGTWLLMVESvtTNPAATGT 615
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD--TAPGDTGT 78


                  ....*.
gi 1831506036 616 FHDWTL 621
Cdd:pfam01483  79 LNSWQL 84
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 194-448 1.18e-28

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


Pssm-ID: 173799 [Multi-domain]  Cd Length: 259  Bit Score: 115.75  E-value: 1.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 194 RNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDptpQNNG-------------------DNKHGTRCAGEVAALAG 254
Cdd:cd07473     2 GDVVVAVIDTGVDYNHPDLKDNMWVNPGEIPGNGIDD---DGNGyvddiygwnfvnndndpmdDNGHGTHVAGIIGAVGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 255 NNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLN--QDH-IDIYSASWGPeddgktfDGPGPLAREAFYRGIKngrgg 331
Cdd:cd07473    79 NGIGIAGVAWNVKIMPLKFLGADGSGTTSDAIKAIDyaVDMgAKIINNSWGG-------GGPSQALRDAIARAID----- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 332 KGNIFVWASGNGGSRQDScsaDGYTTSVYTLS--ISSATYDnhrpwyleecPSSIATTYSSADFRqpaivTVDV------ 403
Cdd:cd07473   147 AGILFVAAAGNDGTNNDK---TPTYPASYDLDniISVAATD----------SNDALASFSNYGKK-----TVDLaapgvd 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831506036 404 -----PGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTA 448
Cdd:cd07473   209 ilstsPGGGYGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSA 258
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 193-449 3.61e-23

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: 100.09  E-value: 3.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 193 GRNVSVSILDDGIQRDHPDLAANYDPlASTDINDHDDDPTPQNNGDNkHGTRCAGeVAALAGNNQCGVGVAFKAKIGGVR 272
Cdd:cd04848     2 GAGVKVGVIDSGIDLSHPEFAGRVSE-ASYYVAVNDAGYASNGDGDS-HGTHVAG-VIAAARDGGGMHGVAPDATLYSAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 273 MLDGAVSDSVEAASLSLNQDHID----IYSASWGPEDDGKTFDGPGPL---AREAFYRGIKNGRGGKGNIFVWASGNGGS 345
Cdd:cd04848    79 ASASAGSTFSDADIAAAYDFLAAsgvrIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVFAAGNDGQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 346 RQDSCSADGYTTSVYTL--------------SISSATYDNH----RPWYLeecpssiattysSAdfrqPA---IVTVDVP 404
Cdd:cd04848   159 ANPSLAAAALPYLEPELeggwiavvavdpngTIASYSYSNRcgvaANWCL------------AA----PGeniYSTDPDG 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1831506036 405 GGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTAN 449
Cdd:cd04848   223 GNGYGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTAT 267
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 185-433 5.75e-22

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: 96.79  E-value: 5.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 185 QAWLQGYAGRNVSVSILDDGIQRDHPDLAAN-----YDPLAS-TDINDHDDDPTPQNNGDNKHGTRCAGEVAAlAGNNQC 258
Cdd:cd07485     1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNgdgdgYDPAVNgYNFVPNVGDIDNDVSVGGGHGTHVAGTIAA-VNNNGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 259 GVG-------VAFKAKIGGVRMLDGA--VSDSVEAASLSLNQDH-IDIYSASWGpeddGKTFDGPGPLAREAFYRGIKNG 328
Cdd:cd07485    80 GVGgiagaggVAPGVKIMSIQIFAGRyyVGDDAVAAAIVYAADNgAVILQNSWG----GTGGGIYSPLLKDAFDYFIENA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 329 RGG--KGNIFVWASGNGGSRQdscsadgyttsvytlsissatydnhrPWYLEECPSSIATTYSSADFRQPAI------VT 400
Cdd:cd07485   156 GGSplDGGIVVFSAGNSYTDE--------------------------HRFPAAYPGVIAVAALDTNDNKASFsnygrwVD 209

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1831506036 401 VDVPGGCT----------------DKHTGTSASAPLAAGIIALALEANP 433
Cdd:cd07485   210 IAAPGVGTilstvpkldgdgggnyEYLSGTSMAAPHVSGVAALVLSKFP 258
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 41-116 2.18e-20

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: 85.73  E-value: 2.18e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831506036  41 HTVIRLaKRDDELARRIAADHDMHVKGDPF-LDTHYFLYHSET-TRTRRHKRAIVERLDSHPAVEWVEEQRPKKRVKR 116
Cdd:pfam16470   1 EWAVHL-EGGPEEADRIAEKHGFINLGQIGgLEDYYHFRHRRVsKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 195-436 8.19e-20

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: 89.13  E-value: 8.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 195 NVSVSILDDGIQRDHPDLAANYdpLASTDINDHDDDPTPQNNGdnkHGTRCAGEVAALaGNNQCGVGVAFKAKIGGVRML 274
Cdd:cd07477     1 GVKVAVIDTGIDSSHPDLKLNI--VGGANFTGDDNNDYQDGNG---HGTHVAGIIAAL-DNGVGVVGVAPEADLYAVKVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 275 D----GAVSDSVEAASLSLNQDhIDIYSASWGpeddgktfdgpGPLAREAFYRGIKNGRgGKGNIFVWASGNGGSRQDSC 350
Cdd:cd07477    75 NddgsGTYSDIIAGIEWAIENG-MDIINMSLG-----------GPSDSPALREAIKKAY-AAGILVVAAAGNSGNGDSSY 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 351 SADGYTTSVytLSISSATYDNHRpwyleecpssiaTTYSSADfRQPAIVT--VDV----PGGCTDKHTGTSASAPLAAGI 424
Cdd:cd07477   142 DYPAKYPSV--IAVGAVDSNNNR------------ASFSSTG-PEVELAApgVDIlstyPNNDYAYLSGTSMATPHVAGV 206

                         250
                  ....*....|..
gi 1831506036 425 IALALEANPELT 436
Cdd:cd07477   207 AALVWSKRPELT 218
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 162-433 2.20e-19

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: 88.86  E-value: 2.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 162 DPLYKDQWYLhggavggYDMNVRQAWLQGyAGRNVSVSILDDGIQRDHPDLAA-----NYDPLastdinDHDDDPTPqnn 236
Cdd:cd07484     4 DPYYSYQWNL-------DQIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLLKvkfvlGYDFV------DNDSDAMD--- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 237 gDNKHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLD----GAVSDSVE----AAslslnqDH-IDIYSASWGpeddg 307
Cdd:cd07484    67 -DNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANgiryAA------DKgAKVINLSLG----- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 308 ktfdgpGPLAREAFYRGIKNGRgGKGNIFVWASGNGGSRQDSCSAdgytTSVYTLSISSATYDNHRPWYleecpssiaTT 387
Cdd:cd07484   135 ------GGLGSTALQEAINYAW-NKGVVVVAAAGNEGVSSVSYPA----AYPGAIAVAATDQDDKRASF---------SN 194

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1831506036 388 YSSA-DFRQP--AIVTvDVPGGCTDKHTGTSASAPLAAGIIALALEANP 433
Cdd:cd07484   195 YGKWvDVSAPggGILS-TTPDGDYAYMSGTSMATPHVAGVAALLYSQGP 242
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 193-466 1.48e-16

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: 81.22  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 193 GRNVSVSILDDGIQRDHPDLAANYDP---------LASTDINDHDDDPTPQNNGDNK------HGTRCAGEVAALAGNNQ 257
Cdd:cd07474     1 GKGVKVAVIDTGIDYTHPDLGGPGFPndkvkggydFVDDDYDPMDTRPYPSPLGDASagdatgHGTHVAGIIAGNGVNVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 258 CGVGVAFKAKIGGVRMLD---GAVSDSVEAAslsLNQ---DHIDIYSASWGPEDDGKtfDGPGPLARE-AFYRGIkngrg 330
Cdd:cd07474    81 TIKGVAPKADLYAYKVLGpggSGTTDVIIAA---IEQavdDGMDVINLSLGSSVNGP--DDPDAIAINnAVKAGV----- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 331 gkgnIFVWASGNGGSrqdscsaDGYTT---SVYTLSISSATYDNHRPWyleecPSSIATTYSSADFRQ------PAIV-- 399
Cdd:cd07474   151 ----VVVAAAGNSGP-------APYTIgspATAPSAITVGASTVADVA-----EADTVGPSSSRGPPTsdsaikPDIVap 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831506036 400 TVDV----PGGCTD--KHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTAnwKPL----ENNPGWSRNGVGR 466
Cdd:cd07474   215 GVDImstaPGSGTGyaRMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTA--KPLydsdGVVYPVSRQGAGR 289
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 195-436 9.86e-16

Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173820 [Multi-domain]  Cd Length: 285  Bit Score: 78.49  E-value: 9.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 195 NVSVSILDDGIQRDHPDLA----ANYD----PLASTDINDHDDDPTPQNNGDNK------------------HGTRCAGE 248
Cdd:cd07496     1 GVVVAVLDTGVLFHHPDLAgvllPGYDfisdPAIANDGDGRDSDPTDPGDWVTGddvppggfcgsgvspsswHGTHVAGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 249 VAAlAGNNQCGV-GVAFKAKIGGVRML---DGAVSDSVE----AASLS-----LNQDHIDIYSASWGPeddgktfDGPGP 315
Cdd:cd07496    81 IAA-VTNNGVGVaGVAWGARILPVRVLgkcGGTLSDIVDgmrwAAGLPvpgvpVNPNPAKVINLSLGG-------DGACS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 316 lareAFYRGIKNGRGGKGNIFVWASGNGGSrqdscSADGYTTSVY--TLSISSATYDNHRPWYleecpssiATTYSSADF 393
Cdd:cd07496   153 ----ATMQNAINDVRARGVLVVVAAGNEGS-----SASVDAPANCrgVIAVGATDLRGQRASY--------SNYGPAVDV 215

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831506036 394 RQPAI---VTVDVPGGCTDKHT-------------GTSASAPLAAGIIALALEANPELT 436
Cdd:cd07496   216 SAPGGdcaSDVNGDGYPDSNTGttspggstygflqGTSMAAPHVAGVAALMKSVNPSLT 274
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 181-494 1.96e-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: 75.44  E-value: 1.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 181 MNVRQAWlQGYAGRNVSVSILDDGIQrDHPDLAANYDP----LASTD-INDHDddptpqnngdnKHGTRCAGEVAALAGN 255
Cdd:TIGR03921   1 LSLEQAW-KFSTGAGVTVAVIDTGVD-DHPRLPGLVLPggdfVGSGDgTDDCD-----------GHGTLVAGIIAGRPGE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 256 NQCGVGVAFKAKIGGVRMLDGAVSDSVEAAS--------------LSLNQDHIDIYSASWGPEDDGKTFDGPGPLAREAF 321
Cdd:TIGR03921  68 GDGFSGVAPDARILPIRQTSAAFEPDEGTSGvgdlgtlakairraADLGADVINISLVACLPAGSGADDPELGAAVRYAL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 322 yrgikngrgGKGNIFVWASGNGGsrqdscsADGYTTSV-------YTLSISS-------ATYDNHRPWYLEECPSSIatt 387
Cdd:TIGR03921 148 ---------DKGVVVVAAAGNTG-------GDGQKTTVvypawypGVLAVGSidrdgtpSSFSLPGPWVDLAAPGEN--- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 388 yssadfrqpaIVTVDVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTAnwkplennpgwsRNGVGRM 467
Cdd:TIGR03921 209 ----------IVSLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEATA------------DHPARGG 266

                         330       340
                  ....*....|....*....|....*..
gi 1831506036 468 VSNKFGYGLIDGGAlvnmAKTWKTVPE 494
Cdd:TIGR03921 267 RDDYVGYGVVDPVA----ALTGELPPE 289
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 191-450 9.43e-14

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: 72.16  E-value: 9.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 191 YAGRNVSVSILDDGIQRDHPDLAANydplASTDINDHDDDPTPQNNGdnkHGTRCAGEVaalAGNNqcgVGVAFKAKIGG 270
Cdd:cd04077    22 STGSGVDVYVLDTGIRTTHVEFGGR----AIWGADFVGGDPDSDCNG---HGTHVAGTV---GGKT---YGVAKKANLVA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 271 VRMLD----GAVSDSVEA----------------ASLSLNQDhidiYSASWgpeDDgktfdgpgpLAREAFYRGIkngrg 330
Cdd:cd04077    89 VKVLDcngsGTLSGIIAGlewvandatkrgkpavANMSLGGG----ASTAL---DA---------AVAAAVNAGV----- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 331 gkgnIFVWASGNggSRQDSC-----SADGyttsvyTLSISSATYDNHRPWYLE--EC-----P-SSIATTYSSADfrqpa 397
Cdd:cd04077   148 ----VVVVAAGN--SNQDACnyspaSAPE------AITVGATDSDDARASFSNygSCvdifaPgVDILSAWIGSD----- 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831506036 398 ivtvdvpgGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANW 450
Cdd:cd04077   211 --------TATATLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLATK 255
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 193-448 2.10e-13

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: 71.08  E-value: 2.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 193 GRNVSVSILDDGIQRDHPDLAANYDPLAsTDINDHDDDPTPqnNGDNKHGTRCAGEVAA-LAGNNQCGVGVAFKAKIGGV 271
Cdd:cd07487     1 GKGITVAVLDTGIDAPHPDFDGRIIRFA-DFVNTVNGRTTP--YDDNGHGTHVAGIIAGsGRASNGKYKGVAPGANLVGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 272 RMLDGAVSDSVEAASLSL-----NQDHIDI--------YSASWGPEDDgktfdgpgPLARE---AFYRGIkngrggkgnI 335
Cdd:cd07487    78 KVLDDSGSGSESDIIAGIdwvveNNEKYNIrvvnlslgAPPDPSYGED--------PLCQAverLWDAGI---------V 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 336 FVWASGNGGSRQDSCSADGYTTSVYTLsisSATYDNHRPWYleecpssIATTYSS----AD-FRQPAIVTVDV------P 404
Cdd:cd07487   141 VVVAAGNSGPGPGTITSPGNSPKVITV---GAVDDNGPHDD-------GISYFSSrgptGDgRIKPDVVAPGEnivscrS 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831506036 405 GGCTDKH---------TGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTA 448
Cdd:cd07487   211 PGGNPGAgvgsgyfemSGTSMATPHVSGAIALLLQANPILTPDEVKCILRDTA 263
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 193-435 7.57e-13

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: 69.33  E-value: 7.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 193 GRNVSVSILDDGIQRDHPDLAANYDPLASTDInDHDD---DP---TPQNNGDNKHGTRCAGevaALAGNN--QCGVGVAF 264
Cdd:cd07481     1 GTGIVVANIDTGVDWTHPALKNKYRGWGGGSA-DHDYnwfDPvgnTPLPYDDNGHGTHTMG---TMVGNDgdGQQIGVAP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 265 KAKIGGVRMLD---GAVSDSVEAASLSLNQDHI-----------DIYSASWGpeddgktfdGPGPLaREAFYRGIKNGRG 330
Cdd:cd07481    77 GARWIACRALDrngGNDADYLRCAQWMLAPTDSagnpadpdlapDVINNSWG---------GPSGD-NEWLQPAVAAWRA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 331 GkGNIFVWASGNGGSRQDSCSAdgyTTSVYTLSISSATYDNHRpwYLEECPSSIATTYSSadfRQPAIVT--VDV----P 404
Cdd:cd07481   147 A-GIFPVFAAGNDGPRCSTLNA---PPANYPESFAVGATDRND--VLADFSSRGPSTYGR---IKPDISApgVNIrsavP 217

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1831506036 405 GGCTDKHTGTSASAPLAAGIIALALEANPEL 435
Cdd:cd07481   218 GGGYGSSSGTSMAAPHVAGVAALLWSANPSL 248
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 196-436 1.59e-12

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: 68.34  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 196 VSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPqnNGDNKHGTRCAGEVAAlAGNNQCGVGVAFKAKiggvrMLD 275
Cdd:cd07490     2 VTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEV--FDAGGHGTHVSGTIGG-GGAKGVYIGVAPEAD-----LLH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 276 GAVSDSVEAASLSLnqdhidIYSASWGPEDD--------GKTFDGPGPLArEAFyRGIKNGRGGkgnIFVWASGNGGSRQ 347
Cdd:cd07490    74 GKVLDDGGGSLSQI------IAGMEWAVEKDadvvsmslGGTYYSEDPLE-EAV-EALSNQTGA---LFVVSAGNEGHGT 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 348 DSCSADGYTtsvyTLSISSATYDNHRPWyleecPSSIATTYSSADFRQP-----------AIVTVDV--------PGGCT 408
Cdd:cd07490   143 SGSPGSAYA----ALSVGAVDRDDEDAW-----FSSFGSSGASLVSAPDsppdeytkpdvAAPGVDVysarqganGDGQY 213

                         250       260
                  ....*....|....*....|....*...
gi 1831506036 409 DKHTGTSASAPLAAGIIALALEANPELT 436
Cdd:cd07490   214 TRLSGTSMAAPHVAGVAALLAAAHPDLS 241
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 181-448 2.01e-12

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: 68.66  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 181 MNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDplASTDINDHDDDPTPQNNGdnkHGTrcaGEVAALagnnqcgV 260
Cdd:cd07494     8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQ--VRVVLAPGATDPACDENG---HGT---GESANL-------F 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 261 GVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHiDIYSASWG-----PEDDGKTFDGPGPLARE-----AFYRGI----- 325
Cdd:cd07494    73 AIAPGAQFIGVKLGGPDLVNSVGAFKKAISLSP-DIISNSWGydlrsPGTSWSRSLPNALKALAatlqdAVARGIvvvfs 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 326 -KNGRGG----------KGNIFVwasGNGGSRQDSCSADGYTTSVY---TLS--ISSATYDNHRPWYLEECPSSIATTYS 389
Cdd:cd07494   152 aGNGGWSfpaqhpeviaAGGVFV---DEDGARRASSYASGFRSKIYpgrQVPdvCGLVGMLPHAAYLMLPVPPGSQLDRS 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831506036 390 SADFrqPAIVTVDVPGGCTdkhTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTA 448
Cdd:cd07494   229 CAAF--PDGTPPNDGWGVF---SGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTA 282
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 196-449 1.78e-11

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: 64.67  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 196 VSVSILDDGIQRDHPDLAanydPLASTDINDHDDDPTPQNNGD---NKHGTRCAGEVAALAGNNQCG-VGVAFKAKIGGV 271
Cdd:cd07492     2 VRVAVIDSGVDTDHPDLG----NLALDGEVTIDLEIIVVSAEGgdkDGHGTACAGIIKKYAPEAEIGsIKILGEDGRCNS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 272 RMLDGA----VSDSVEAASLSLnqdhidiysaswgpeddGKTFDGPGPLAREAFYRGIKNGRggkgnIFVwASGNGGSRQ 347
Cdd:cd07492    78 FVLEKAlracVENDIRIVNLSL-----------------GGPGDRDFPLLKELLEYAYKAGG-----IIV-AAAPNNNDI 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 348 DSCSADgyTTSVYTLSiSSATYDNHRPWYLEECpssiattyssadFRQPAI-VTVDVPGGCTDKHTGTSASAPLAAGIIA 426
Cdd:cd07492   135 GTPPAS--FPNVIGVK-SDTADDPKSFWYIYVE------------FSADGVdIIAPAPHGRYLTVSGNSFAAPHVTGMVA 199

                         250       260
                  ....*....|....*....|...
gi 1831506036 427 LALEANPELTWRDMQHLVLRTAN 449
Cdd:cd07492   200 LLLSEKPDIDANDLKRLLQRLAV 222
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 189-458 5.86e-11

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: 64.55  E-value: 5.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 189 QGYAGRNVSVSILDDGIQRDHPDL----------AANYDPLASTDINDH----DDDPTpQNNGdnkHGTRCAGEVAALaG 254
Cdd:cd07489     8 EGITGKGVKVAVVDTGIDYTHPALggcfgpgckvAGGYDFVGDDYDGTNppvpDDDPM-DCQG---HGTHVAGIIAAN-P 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 255 NNQCGVGVAFKAKIGGVRML---DGAVSDSVEAASLSLNQDHIDIYSASWGpEDDGKTFDgpgPLArEAFYRGIKngrgg 331
Cdd:cd07489    83 NAYGFTGVAPEATLGAYRVFgcsGSTTEDTIIAAFLRAYEDGADVITASLG-GPSGWSED---PWA-VVASRIVD----- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 332 KGNIFVWASGNGGSRqDSCSADGYTTSVYTLSISSAtydnhrpwyleecpSSIATTY-SSADFR-QPAIV--------TV 401
Cdd:cd07489   153 AGVVVTIAAGNDGER-GPFYASSPASGRGVIAVASV--------------DSYFSSWgPTNELYlKPDVAapggnilsTY 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1831506036 402 DVPGGCTDKHTGTSASAPLAAGIIALALEA-NPELTWRDMQHLVLRTAnwKPLENNPG 458
Cdd:cd07489   218 PLAGGGYAVLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTA--KPLPWSDG 273
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 167-625 7.89e-11

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: 65.61  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 167 DQWYLHGGAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQNNGDNKHGTRCA 246
Cdd:COG4935   206 GGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVV 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 247 GEVAALAGNNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGPLAREAFYRGIK 326
Cdd:COG4935   286 GAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAA 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 327 NGRGGKGNIFVWASGNGGSRQDSCSADGYTTSVYTLSISSATYDNHRPWYLEECPSSIATTYSSADFRQPAIVTVDVPGG 406
Cdd:COG4935   366 AGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGL 445

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 407 CTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWkpleNNPGWSRNGVGRMVSNKFGYGLIDGGAlvnma 486
Cdd:COG4935   446 GGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTTAAAAAAAAG----LATTAAVAAGAAGAAAAAATAASVGGA----- 516

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 487 kTWKTVPEQHICTYEyrlaNPNPRPI--VGRFQLNFTLDVNGcesGTPVlylEHVQVHATVRYLKRGDLKLTLFSPSGTR 564
Cdd:COG4935   517 -TGAAGTTNSTATFS----NTTDVAIpdNGPAGVTSTITVSG---GGAV---EDVTVTVDITHTYRGDLVITLISPDGTT 585

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831506036 565 SVLLPPRP---QDFNangfhkWPFLSVQQWGEDPRGTWLLMVesVTTNPAATGTFHDWTLLLYG 625
Cdd:COG4935   586 VVLKNRSGgsaDNIN------ATFDVANFSGESANGTWTLRV--VDTAGGDTGTLNSWSLTFTG 641
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 190-431 1.11e-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: 63.50  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 190 GYAGRNVSVSILDDGIQRDHPDLaanYDPLASTDINDH----DDDPTPQNNGD-NKHGTRCAGEVAALAGNNQCGV---G 261
Cdd:cd04842     3 GLTGKGQIVGVADTGLDTNHCFF---YDPNFNKTNLFHrkivRYDSLSDTKDDvDGHGTHVAGIIAGKGNDSSSISlykG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 262 VAFKAKIGGVRMLDGAVSDSVEAASLSL----NQDHIDIYSASWGPEDDG------KTFDgpgplaREAFyrgiKNgrgg 331
Cdd:cd04842    80 VAPKAKLYFQDIGDTSGNLSSPPDLNKLfspmYDAGARISSNSWGSPVNNgytllaRAYD------QFAY----NN---- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 332 KGNIFVWASGNGGsrqdscsaDGYTTSVYTLSIS------SATYDNhRPWYLEECPSSIATTYSSADF----------RQ 395
Cdd:cd04842   146 PDILFVFSAGNDG--------NDGSNTIGSPATAknvltvGASNNP-SVSNGEGGLGQSDNSDTVASFssrgptydgrIK 216

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831506036 396 PAIV-----------TVDVPGGCTDKH----TGTSASAPLAAGIIALALEA 431
Cdd:cd04842   217 PDLVapgtgilsarsGGGGIGDTSDSAytskSGTSMATPLVAGAAALLRQY 267
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 191-439 2.03e-09

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: 59.70  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 191 YAGRNVSVSILDDGIQRDHPDLAAnydplasTDINDHDDDPTPQNNGDNKHGTRCAGEVaalAGNNQCGV--GVAFKAKI 268
Cdd:cd07480     5 FTGAGVRVAVLDTGIDLTHPAFAG-------RDITTKSFVGGEDVQDGHGHGTHCAGTI---FGRDVPGPryGVARGAEI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 269 --GGVRMLDGAVSDS--VEAASLSLNQDhIDIYSASWGPEDDGKTFDG--PGPLAREAFYRGIKNGRGGKGNIFVWASGN 342
Cdd:cd07480    75 alIGKVLGDGGGGDGgiLAGIQWAVANG-ADVISMSLGADFPGLVDQGwpPGLAFSRALEAYRQRARLFDALMTLVAAQA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 343 GGSRQdscsadgyttsvyTLSISSATYDNHRPWY------LEECPS-----SIATTYSSADFRQPAIVT----------V 401
Cdd:cd07480   154 ALARG-------------TLIVAAAGNESQRPAGippvgnPAACPSamgvaAVGALGRTGNFSAVANFSngevdiaapgV 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1831506036 402 DV----PGGCTDKHTGTSASAPLAAGIIALALEANPELTWRD 439
Cdd:cd07480   221 DIvsaaPGGGYRSMSGTSMATPHVAGVAALWAEALPKAGGRA 262
Furin-like pfam00757
Furin-like cysteine rich region;
675-773 4.50e-09

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 55.91  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 675 CHDECNGGCTESSsATSCFACKHLtqtlRNKGgsgfKCVQKCDDTYYLDGDKCKmcsshchtctkaeVCETCPGSlllID 754
Cdd:pfam00757  49 CHEQCLGGCTGPN-DSDCLACRHF----NDEG----TCVDQCPPGTYQFGWRCV-------------TFKECPKS---HL 103

                          90       100
                  ....*....|....*....|
gi 1831506036 755 VDNMPHY-DHGKCVESCPPG 773
Cdd:pfam00757 104 PGYNPLViHNGECVRECPSG 123
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 195-436 1.45e-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: 56.99  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 195 NVSVSILDDGIQRDHPDLAA-------NYDPLASTDINDHDDDPTPQNNGD-NKHGTRCAGEVAAlagnNQCGVGVAFKA 266
Cdd:cd07482     1 KVTVAVIDSGIDPDHPDLKNsissyskNLVPKGGYDGKEAGETGDINDIVDkLGHGTAVAGQIAA----NGNIKGVAPGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 267 KIGGVRMLD---GAVSDSVEAASLSLNQDHIDIYSASWGPEDDGktfDGPGPLAREAF--YRGIKNGRGGKGNIFVWASG 341
Cdd:cd07482    77 GIVSYRVFGscgSAESSWIIKAIIDAADDGVDVINLSLGGYLII---GGEYEDDDVEYnaYKKAINYAKSKGSIVVAAAG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 342 NGG-SRQDSCSADGYTTSVYTLSISSATYDnhrpwYLEECPSSIA----------TTYSS------------ADFRQP-- 396
Cdd:cd07482   154 NDGlDVSNKQELLDFLSSGDDFSVNGEVYD-----VPASLPNVITvsatdnngnlSSFSNygnsridlaapgGDFLLLdq 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1831506036 397 ---------AIVTVDV-----PGGCTDKHTGTSASAPLAAGIIALALEANPELT 436
Cdd:cd07482   229 ygkekwvnnGLMTKEQilttaPEGGYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 399-483 8.24e-08

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: 54.61  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 399 VTVDVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTAnwkpLE-NNPGWsrngvgrmvSNKFGYGLI 477
Cdd:cd05562   201 GTVDGDGDGPPNFFGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTA----LDmGEPGY---------DNASGSGLV 267


                  ....*.
gi 1831506036 478 DGGALV 483
Cdd:cd05562   268 DADRAV 273
Peptidases_S8_9 cd07493
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
 196-449 8.76e-07

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


Pssm-ID: 173818 [Multi-domain]  Cd Length: 261  Bit Score: 51.15  E-value: 8.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 196 VSVSILDDGIQRDHPDLAANYDP-----LASTDINDHDDDPTPQnngDNKHGTRCageVAALAGNN-QCGVGVAFKAKIG 269
Cdd:cd07493     2 ITIAVIDAGFPKVHEAFAFKHLFknlriLGEYDFVDNSNNTNYT---DDDHGTAV---LSTMAGYTpGVMVGTAPNASYY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 270 GVRMLDGAV------SDSVEAA-----------SLSLNQDHIDIYSASWGPED-DGKTfdgpGPLARE---AFYRGIkng 328
Cdd:cd07493    76 LARTEDVASetpveeDNWVAAAewadslgvdiiSSSLGYTTFDNPTYSYTYADmDGKT----SFISRAaniAASKGM--- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 329 rggkgnIFVWASGNGGSRQD---SCSADGyttsVYTLSISSATYDNHRPWYleecpSSIATTyssADFR-QPAIV----- 399
Cdd:cd07493   149 ------LVVNSAGNEGSTQWkgiGAPADA----ENVLSVGAVDANGNKASF-----SSIGPT---ADGRlKPDVMalgtg 210

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831506036 400 -TVDVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTAN 449
Cdd:cd07493   211 iYVINGDGNITYANGTSFSCPLIAGLIACLWQAHPNWTNLQIKEAILKSAS 261
FU smart00261
Furin-like repeats;
724-773 1.14e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.96  E-value: 1.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831506036  724 GDKCKMCSSHCHTCT--KAEVCETCPGSLLLidvdnmphyDHGKCVESCPPG 773
Cdd:smart00261   1 DGECKPCHPECATCTgpGPDDCTSCKHGFFL---------DGGKCVSECPPG 43
VSP pfam03302
Giardia variant-specific surface protein;
668-773 3.41e-06

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 50.35  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 668 DLTSAGNCHDECNG-----GCTESSSATSCFAC---KHLTQTlrNKGgsgfkCVQKCDDTYYLDGDKCKMCSSHCHTCT- 738
Cdd:pfam03302  47 YLTPTSQCIDDCAKignyyYTTNANNKKICKECtvaNCKTCE--DQG-----QCQACNDGFYKSGDACSPCHESCKTCSg 119

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1831506036 739 -KAEVCETCP-GSLLLIDVDNMPHYDHGKCVESCPPG 773
Cdd:pfam03302 120 gTASDCTECLtGKALRYGNDGTKGTCGEGCTTGTGAG 156
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 193-431 9.51e-06

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: 48.62  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 193 GRNVSVSILDDGIQRDHPDLAA--NYDPLASTDIN-------DHDDDPTPQNNGDNKHGTRCAgEVAALAGN-------- 255
Cdd:cd07497     1 GEGVVIAIVDTGVDYSHPDLDIygNFSWKLKFDYKayllpgmDKWGGFYVIMYDFFSHGTSCA-SVAAGRGKmeynlygy 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 256 --NQCGVGVAFKAKIGGVRML------------DGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGPLAREAF 321
Cdd:cd07497    80 tgKFLIRGIAPDAKIAAVKALwfgdviyawlwtAGFDPVDRKLSWIYTGGPRVDVISNSWGISNFAYTGYAPGLDISSLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 322 YRGIKNgrgGKGNIFVWASGNGGSRQDSCSADGytTSVYTLSISSATYDNHRPWYLeecpsSIATTYSSADF-----RQP 396
Cdd:cd07497   160 IDALVT---YTGVPIVSAAGNGGPGYGTITAPG--AASLAISVGAATNFDYRPFYL-----FGYLPGGSGDVvswssRGP 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831506036 397 AIVTVDVPG-----------GCTDKHT-------------GTSASAPLAAGIIALALEA 431
Cdd:cd07497   230 SIAGDPKPDlaaigafawapGRVLDSGgaldgneafdlfgGTSMATPMTAGSAALVISA 288
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 681-777 1.09e-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: 44.73  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 681 GGCTESSSATSCFACKH-LTQTLRNKGGSGF-KCVQKCDDTYY----LDGDKCKMC-SSHCHTCTKAEVCETCPGSLLLi 753
Cdd:pfam15913   2 SGCVLCSEENGCLTCQPrLFLLLERNGIRQYgVCLHSCPPGYFgirgQEVNRCTKCkAENCESCFSKDFCTKCKEGFYL- 80

                          90       100
                  ....*....|....*....|....
gi 1831506036 754 dvdnmpHydHGKCVESCPPGLVAD 777
Cdd:pfam15913  81 ------H--KGKCLDTCPEGTAAQ 96
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 730-777 2.31e-05

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: 42.51  E-value: 2.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831506036 730 CSSHCHTCT--KAEVCETCPGSLLLidvdnmphyDHGKCVESCPPGLVAD 777
Cdd:cd00064     2 CHPSCATCTgpGPDQCTSCRHGFYL---------DGGTCVSECPEGTYAD 42
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 181-429 3.48e-05

Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173792  Cd Length: 277  Bit Score: 46.54  E-value: 3.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 181 MNVRQAW-LQGYAGRNVSVSILDDGIQRDHPDLAANYDPLAStdindhddDPTPQNNGDnkHGTRCAGEVAAlAGNNQCG 259
Cdd:cd04843     2 INARYAWtKPGGSGQGVTFVDIEQGWNLNHEDLVGNGITLIS--------GLTDQADSD--HGTAVLGIIVA-KDNGIGV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 260 VGVAFKAKIGGVRMldGAVSDSVEA---ASLSLNQDHIDIYSASWGPEDDGKTfdgpgPLARE---AFYRGIKNGRgGKG 333
Cdd:cd04843    71 TGIAHGAQAAVVSS--TRVSNTADAildAADYLSPGDVILLEMQTGGPNNGYP-----PLPVEyeqANFDAIRTAT-DLG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 334 NIFVWASGNGGSRQDSCSadgyTTSVYTLSISSATY--------------DNHRPWYLEECPS---------SIATTYSS 390
Cdd:cd04843   143 IIVVEAAGNGGQDLDAPV----YNRGPILNRFSPDFrdsgaimvgagsstTGHTRLAFSNYGSrvdvygwgeNVTTTGYG 218

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1831506036 391 ADFRQPAIVTvdvpgGCTDKHTGTSASAPLAAGiiALAL 429
Cdd:cd04843   219 DLQDLGGENQ-----DYTDSFSGTSSASPIVAG--AAAS 250
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 332-448 1.08e-04

Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173813  Cd Length: 247  Bit Score: 44.77  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 332 KGNIFVWASGNGGsrqDSCSADGYTtSVYTLSISS----ATYDNHRPWYLEEcPSSIATTYSSADFRQPAIVT----VDV 403
Cdd:cd07488   122 YEVINVFSAGNQG---KEKEKFGGI-SIPTLAYNSivvgSTDRNGDRFFASD-VSNAGSEINSYGRRKVLIVApgsnYNL 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1831506036 404 PGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTA 448
Cdd:cd07488   197 PDGKDDFVSGTSFSAPLVTGIIALLLEFYDRQYKKGNNNLIALRA 241
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 675-728 1.28e-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: 40.19  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831506036 675 CHDECNgGCTeSSSATSCFACKHltqtlrNKGGSGFKCVQKCDDTYYLD--GDKCK 728
Cdd:cd00064     2 CHPSCA-TCT-GPGPDQCTSCRH------GFYLDGGTCVSECPEGTYADteGGVCL 49
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 196-459 2.45e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 44.57  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 196 VSVSILDDGIQRDHPDLAANY---------------------DPLASTDINDHDDDPTpqnnGDNKHGTRCAGEVAALAG 254
Cdd:PTZ00262  318 TNICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM----DDNYHGTHVSGIISAIGN 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 255 NNQCGVGVAFKAKIGGVRMLD----GAVSDSVEAASLSLNQDhIDIYSASWGPEDDGKTFDGPGPLAREafyrgikngrg 330
Cdd:PTZ00262  394 NNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFNESVKYLEE----------- 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 331 gKGNIFVWASGNggsrqdsCSADGYTTSVYT---LSIS-------SATYDN-------------HRPWYLEECPSSI--- 384
Cdd:PTZ00262  462 -KGILFVVSASN-------CSHTKESKPDIPkcdLDVNkvyppilSKKLRNvitvsnlikdknnQYSLSPNSFYSAKycq 533

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 385 -----ATTYSSADFRQPAIVtvdvpggctdkhTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKP-LENNPG 458
Cdd:PTZ00262  534 laapgTNIYSTFPKNSYRKL------------NGTSMAAPHVAAIASLILSINPSLSYEEVIRILKESIVQLPsLKNKVK 601


                  .
gi 1831506036 459 W 459
Cdd:PTZ00262  602 W 602
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 675-785 4.59e-04

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: 40.82  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 675 CHDECNGGCTESSSATSCFACKHLtqtlrNKGGSgfkCVQKCDDTY-----YLDGDKCKMCSSHCHTCTKAEVCeTCPGS 749
Cdd:pfam14843   2 CDPLCSSEGCWGPGPDQCLSCRNF-----SRGGT---CVESCNILQgepreYVVNSTCVPCHPECLPQNGTATC-SGPGA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831506036 750 lllIDVDNMPHYDHGK-CVESCP------PGLVADYAENFDFC 785
Cdd:pfam14843  73 ---DNCTKCAHFRDGPhCVSSCPsgvlgeNDLIWKYADANGVC 112
FU smart00261
Furin-like repeats;
675-721 1.60e-03

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 37.10  E-value: 1.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1831506036  675 CHDECNGgCTeSSSATSCFACKHLTQTLRNkggsgfKCVQKCDDTYY 721
Cdd:smart00261   7 CHPECAT-CT-GPGPDDCTSCKHGFFLDGG------KCVSECPPGTY 45
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 364-475 3.08e-03

Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173804 [Multi-domain]  Cd Length: 455  Bit Score: 41.06  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 364 ISSATYDNHRpwyleecpSSIATtYSSADF-R----QPAIVT--VDV----PGGCTDKHTGTSASAPLAAGIIALALEAN 432
Cdd:cd07478   347 ITVGAYNQNN--------NSIAI-FSGRGPtRdgriKPDIAApgVNIltasPGGGYTTRSGTSVAAAIVAGACALLLQWG 417

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1831506036 433 ------PELTWRDMQHLVLRTAnwKPLENNPGWSRngvgrmvsnKFGYG 475
Cdd:cd07478   418 ivrgndPYLYGEKIKTYLIRGA--RRRPGDEYPNP---------EWGYG 455
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 678-793 3.79e-03

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 41.06  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831506036 678 ECNGGCTESSSAT--SCFACKHLTQTLRNKGGSGFKCVQ--KCDDTYYLDGDKCKMCSS-HCHTCTKAEVCETCPGSlLL 752
Cdd:PTZ00214  578 ECDPTCLACTAPGpgRCTRCPSDKLLKRASGAATGSCVDpgACVDGYYADGDACLPCATpGCKTCGHASFCTECAGE-LF 656

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831506036 753 IDVDN-----------------------------MPHYDHGKCV--ESCPPGLvadyaenfDFCAKNNESGR 793
Cdd:PTZ00214  657 VSLDGqscleectgdkvvgevsggvrrcwcergfLPALDRSGCVlpTECPPDM--------PSCAACDESGR 720
VSP pfam03302
Giardia variant-specific surface protein;
679-746 4.78e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 40.34  E-value: 4.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831506036 679 CNGGCTESSSATSCfackhltqtlrnkggsgfkcvQKCDDTYYLDGDKCKMCSSHCHTCT-KAEVCETC 746
Cdd:pfam03302 259 CSPGCKTCTSNTVC---------------------TTCMDGYVKTSDSCTKCDSSCETCTgATTTCKTC 306
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 730-773 4.98e-03

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: 37.41  E-value: 4.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1831506036 730 CSShCHTCTKAEVCETC-PGSLLLIDVDNMPHYdhGKCVESCPPG 773
Cdd:pfam15913   1 CSG-CVLCSEENGCLTCqPRLFLLLERNGIRQY--GVCLHSCPPG 42
 
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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