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Conserved domains on  [gi|4505577|ref|NP_002561|]
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proprotein convertase subtilisin/kexin type 6 isoform PACE4-AI preproprotein [Homo sapiens]

Protein Classification

Peptidases_S8_Protein_convertases_Kexins_Furin-lik and P_proprotein domain-containing protein( domain architecture ID 13872809)

protein containing domains S8_pro-domain, Peptidases_S8_Protein_convertases_Kexins_Furin-lik, P_proprotein, and FU

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 ...
 160-454 3.10e-172

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: 503.25  E-value: 3.10e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  160 FNDPIWSNMWYLH-CGDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRY 238
Cdd:cd04059   1 PNDPLFPYQWYLKnTGQAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  239 DasNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGP 318
Cdd:cd04059  81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  319 GRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDYCSCDGYTNSIYTISVSSATENGYKPWYLEECASTLATTYSSGA- 397
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4505577  398 FYERKIVTTDLR--QRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSR 454
Cdd:cd04059 239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 539-629 3.29e-39

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: 140.10  E-value: 3.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    539 LEHVVVRTSISHPRRGDLQIYLVSPSGTKSQLLAKRLLDLSNEGFTNWEFMTVHCWGEKAEGQWTLEIQDlpsqvRNPEK 618
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD-----TAPGD 75

                          90
                  ....*....|.
gi 4505577    619 QGKLKEWSLIL 629
Cdd:pfam01483  76 TGTLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 73-149 1.62e-37

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: 135.04  E-value: 1.62e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505577     73 HWAVQVLGGPAEADRVAAAHGYLNLGQIGNLEDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKR 149
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
GF_recep_IV super family cl37890
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 694-804 1.72e-17

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


The actual alignment was detected with superfamily member pfam14843:

Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 79.73  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    694 VCHPECGDKGCDGPNADQCLNCVHFSLGsvktsRKCVSVCPLGYFGD---TAARRCRRCHKGCE------TCSSRAATQC 764
Cdd:pfam14843   1 VCDPLCSSEGCWGPGPDQCLSCRNFSRG-----GTCVESCNILQGEPreyVVNSTCVPCHPECLpqngtaTCSGPGADNC 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 4505577    765 LSCRrgfyHHQEMNTCVTLCPAG---------FYADEsQKNCLKCHPSC 804
Cdd:pfam14843  76 TKCA----HFRDGPHCVSSCPSGvlgendliwKYADA-NGVCQPCHPNC 119
FU smart00261
Furin-like repeats;
844-886 6.50e-10

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 55.21  E-value: 6.50e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 4505577     844 RCGECHHTCGTCVGPGREECIHCAKNFHFHDWKCVPACGEGFY 886
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 799-845 6.82e-09

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


:

Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 52.52  E-value: 6.82e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 4505577  799 KCHPSCKKCVDE-PEKCTVCKEGFSLARGSCIPDCEPGTYFDSELIRC 845
Cdd:cd00064   1 PCHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVC 48
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 942-965 4.15e-04

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


:

Pssm-ID: 462560  Cd Length: 31  Bit Score: 38.29  E-value: 4.15e-04
                          10        20
                  ....*....|....*....|....
gi 4505577    942 FCEMVKSNRLCERKLFIQFCCRTC 965
Cdd:pfam08686   7 NCSLVVQARLCSHKYYRQFCCRSC 30
FU smart00261
Furin-like repeats;
896-930 4.56e-03

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 35.95  E-value: 4.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 4505577     896 KVCRRCDENCLSCAGS-SRNCSRCKTGFTQLGTSCI 930
Cdd:smart00261   2 GECKPCHPECATCTGPgPDDCTSCKHGFFLDGGKCV 37
 
Name Accession Description Interval E-value
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 160-454 3.10e-172

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: 503.25  E-value: 3.10e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  160 FNDPIWSNMWYLH-CGDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRY 238
Cdd:cd04059   1 PNDPLFPYQWYLKnTGQAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  239 DasNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGP 318
Cdd:cd04059  81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  319 GRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDYCSCDGYTNSIYTISVSSATENGYKPWYLEECASTLATTYSSGA- 397
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4505577  398 FYERKIVTTDLR--QRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSR 454
Cdd:cd04059 239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 196-479 2.31e-66

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: 224.26  E-value: 2.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    196 GKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDY----DPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNA 271
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDfnneWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    272 KIGGIRML-DGDVTDVVEAKSLG-IRPNYIDIYSASWGPDddgKTVDGPGRLAKQAFEYGikkGRQGLGSIFVWASGNGG 349
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISwAIPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    350 REGDYCSCDGY-TNSIYTISVSSATengykpwyleECASTLATTYSSG------------AFY-----------ERKIVT 405
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVD----------EASEGNLASFSSYgptldgrlkpdiVAPggnitggnissTLLTTT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505577    406 TDLRQRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAHLKASDwkvngaghkvsHFYGFG 479
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD-----------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 193-490 9.28e-41

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 156.80  E-value: 9.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  193 GYTGKNVVVTILDDGIERNHPDLAPNYDsyASYDVNGNDYDPSprydasNENKHGTRCAGEVAASANNSYCIVGIAYNAK 272
Cdd:COG1404 105 GLTGAGVTVAVIDTGVDADHPDLAGRVV--GGYDFVDGDGDPS------DDNGHGTHVAGIIAANGNNGGGVAGVAPGAK 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  273 IGGIRMLD----GDVTDVVE----AKSLGIrpnyiDIYSASWGPDDDGKTvdgpgRLAKQAFEYGIKKGrqglgSIFVWA 344
Cdd:COG1404 177 LLPVRVLDdngsGTTSDIAAaidwAADNGA-----DVINLSLGGPADGYS-----DALAAAVDYAVDKG-----VLVVAA 241

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  345 SGNggrEGDYCSCDGYTNSIY-TISVSSATENGYKPWYleecaStlattySSGAFYE-----RKIVTTDLRQRcTDGHTG 418
Cdd:COG1404 242 AGN---SGSDDATVSYPAAYPnVIAVGAVDANGQLASF-----S------NYGPKVDvaapgVDILSTYPGGG-YATLSG 306

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505577  419 TSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAHLKasdwkvngaghkvSHFYGFGLVDAEALVVEA 490
Cdd:COG1404 307 TSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAP-------------GPYYGYGLLADGAAGATS 365
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 539-629 3.29e-39

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: 140.10  E-value: 3.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    539 LEHVVVRTSISHPRRGDLQIYLVSPSGTKSQLLAKRLLDLSNEGFTNWEFMTVHCWGEKAEGQWTLEIQDlpsqvRNPEK 618
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD-----TAPGD 75

                          90
                  ....*....|.
gi 4505577    619 QGKLKEWSLIL 629
Cdd:pfam01483  76 TGTLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 73-149 1.62e-37

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: 135.04  E-value: 1.62e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505577     73 HWAVQVLGGPAEADRVAAAHGYLNLGQIGNLEDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKR 149
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 694-804 1.72e-17

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: 79.73  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    694 VCHPECGDKGCDGPNADQCLNCVHFSLGsvktsRKCVSVCPLGYFGD---TAARRCRRCHKGCE------TCSSRAATQC 764
Cdd:pfam14843   1 VCDPLCSSEGCWGPGPDQCLSCRNFSRG-----GTCVESCNILQGEPreyVVNSTCVPCHPECLpqngtaTCSGPGADNC 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 4505577    765 LSCRrgfyHHQEMNTCVTLCPAG---------FYADEsQKNCLKCHPSC 804
Cdd:pfam14843  76 TKCA----HFRDGPHCVSSCPSGvlgendliwKYADA-NGVCQPCHPNC 119
FU smart00261
Furin-like repeats;
743-789 4.18e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 55.98  E-value: 4.18e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 4505577     743 ARRCRRCHKGCETCSSRAATQCLSCRRGFYHHQemNTCVTLCPAGFY 789
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDG--GKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
844-886 6.50e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 55.21  E-value: 6.50e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 4505577     844 RCGECHHTCGTCVGPGREECIHCAKNFHFHDWKCVPACGEGFY 886
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 749-798 8.73e-10

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: 55.22  E-value: 8.73e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4505577  749 CHKGCETCSSRAATQCLSCRRGFYHHQemNTCVTLCPAGFYADESQKNCL 798
Cdd:cd00064   2 CHPSCATCTGPGPDQCTSCRHGFYLDG--GTCVSECPEGTYADTEGGVCL 49
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 847-889 4.93e-09

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 52.91  E-value: 4.93e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4505577  847 ECHHTCGTCVGPGREECIHCAKNFHFHDWKCVPACGEGFYPEE 889
Cdd:cd00064   1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADT 43
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 799-845 6.82e-09

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 52.52  E-value: 6.82e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 4505577  799 KCHPSCKKCVDE-PEKCTVCKEGFSLARGSCIPDCEPGTYFDSELIRC 845
Cdd:cd00064   1 PCHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVC 48
FU smart00261
Furin-like repeats;
795-837 4.42e-08

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 50.20  E-value: 4.42e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505577     795 KNCLKCHPSCKKCVD-EPEKCTVCKEGFSLARGSCIPDCEPGTY 837
Cdd:smart00261   2 GECKPCHPECATCTGpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 201-449 9.46e-08

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 56.13  E-value: 9.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577   201 VTILDDGIERNHPDLAPNY----------------------DSYASYDVNGNDydpspryDASNENKHGTRCAGEVAASA 258
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvdDEYGANFVNNDG-------GPMDDNYHGTHVSGIISAIG 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577   259 NNSYCIVGIAYNAKIGGIRMLD----GDVTDVVEAKSLGIRPNyIDIYSASWGPDDDGKTVDgpgrlakQAFEYgikkgR 334
Cdd:PTZ00262 393 NNNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFN-------ESVKY-----L 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577   335 QGLGSIFVWASGN----GGREGDYCSCDGYTNSIY----------TISVSSATENGYKPWYLeECASTLATTYSSGAFYE 400
Cdd:PTZ00262 460 EEKGILFVVSASNcshtKESKPDIPKCDLDVNKVYppilskklrnVITVSNLIKDKNNQYSL-SPNSFYSAKYCQLAAPG 538

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 4505577   401 RKIVTTDLRQRCTDGhTGTSVSAPMVAGIIALALEANSQLTWRDVQHLL 449
Cdd:PTZ00262 539 TNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEVIRIL 586
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 826-885 5.25e-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: 43.19  E-value: 5.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505577    826 GSCIPDCEPGtYF---DSELIRCGECH-HTCGTCVGpgREECIHCAKNFHFHDWKCVPACGEGF 885
Cdd:pfam15913  33 GVCLHSCPPG-YFgirGQEVNRCTKCKaENCESCFS--KDFCTKCKEGFYLHKGKCLDTCPEGT 93
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 942-965 4.15e-04

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 38.29  E-value: 4.15e-04
                          10        20
                  ....*....|....*....|....
gi 4505577    942 FCEMVKSNRLCERKLFIQFCCRTC 965
Cdd:pfam08686   7 NCSLVVQARLCSHKYYRQFCCRSC 30
FU smart00261
Furin-like repeats;
896-930 4.56e-03

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 35.95  E-value: 4.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 4505577     896 KVCRRCDENCLSCAGS-SRNCSRCKTGFTQLGTSCI 930
Cdd:smart00261   2 GECKPCHPECATCTGPgPDDCTSCKHGFFLDGGKCV 37
 
Name Accession Description Interval E-value
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 160-454 3.10e-172

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: 503.25  E-value: 3.10e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  160 FNDPIWSNMWYLH-CGDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRY 238
Cdd:cd04059   1 PNDPLFPYQWYLKnTGQAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  239 DasNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGP 318
Cdd:cd04059  81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  319 GRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDYCSCDGYTNSIYTISVSSATENGYKPWYLEECASTLATTYSSGA- 397
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4505577  398 FYERKIVTTDLR--QRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSR 454
Cdd:cd04059 239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 196-479 2.31e-66

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: 224.26  E-value: 2.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    196 GKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDY----DPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNA 271
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDfnneWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    272 KIGGIRML-DGDVTDVVEAKSLG-IRPNYIDIYSASWGPDddgKTVDGPGRLAKQAFEYGikkGRQGLGSIFVWASGNGG 349
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISwAIPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    350 REGDYCSCDGY-TNSIYTISVSSATengykpwyleECASTLATTYSSG------------AFY-----------ERKIVT 405
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVD----------EASEGNLASFSSYgptldgrlkpdiVAPggnitggnissTLLTTT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505577    406 TDLRQRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAHLKASDwkvngaghkvsHFYGFG 479
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD-----------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 193-490 9.28e-41

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 156.80  E-value: 9.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  193 GYTGKNVVVTILDDGIERNHPDLAPNYDsyASYDVNGNDYDPSprydasNENKHGTRCAGEVAASANNSYCIVGIAYNAK 272
Cdd:COG1404 105 GLTGAGVTVAVIDTGVDADHPDLAGRVV--GGYDFVDGDGDPS------DDNGHGTHVAGIIAANGNNGGGVAGVAPGAK 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  273 IGGIRMLD----GDVTDVVE----AKSLGIrpnyiDIYSASWGPDDDGKTvdgpgRLAKQAFEYGIKKGrqglgSIFVWA 344
Cdd:COG1404 177 LLPVRVLDdngsGTTSDIAAaidwAADNGA-----DVINLSLGGPADGYS-----DALAAAVDYAVDKG-----VLVVAA 241

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  345 SGNggrEGDYCSCDGYTNSIY-TISVSSATENGYKPWYleecaStlattySSGAFYE-----RKIVTTDLRQRcTDGHTG 418
Cdd:COG1404 242 AGN---SGSDDATVSYPAAYPnVIAVGAVDANGQLASF-----S------NYGPKVDvaapgVDILSTYPGGG-YATLSG 306

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505577  419 TSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAHLKasdwkvngaghkvSHFYGFGLVDAEALVVEA 490
Cdd:COG1404 307 TSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAP-------------GPYYGYGLLADGAAGATS 365
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 539-629 3.29e-39

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: 140.10  E-value: 3.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    539 LEHVVVRTSISHPRRGDLQIYLVSPSGTKSQLLAKRLLDLSNEGFTNWEFMTVHCWGEKAEGQWTLEIQDlpsqvRNPEK 618
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD-----TAPGD 75

                          90
                  ....*....|.
gi 4505577    619 QGKLKEWSLIL 629
Cdd:pfam01483  76 TGTLNSWQLTL 86
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 199-452 1.37e-37

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: 141.33  E-value: 1.37e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  199 VVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSprydasNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRM 278
Cdd:cd07498   1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPTS------DIDGHGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  279 LDGDVTDVVEAKSLGIR---PNYIDIYSASWGpdddGKTVDGPGRLakqAFEYGIKKGRQGLGSIFVWASGNGGREGDYc 355
Cdd:cd07498  75 ADSLGYAYWSDIAQAITwaaDNGADVISNSWG----GSDSTESISS---AIDNAATYGRNGKGGVVLFAAGNSGRSVSS- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  356 scdGYTNSIYTISVSSATENGYK-PW-----YLEECA--STLATTYSSGafyerkIVTTDLRQRCTDGHTGTSVSAPMVA 427
Cdd:cd07498 147 ---GYAANPSVIAVAATDSNDARaSYsnygnYVDLVApgVGIWTTGTGR------GSAGDYPGGGYGSFSGTSFASPVAA 217

                       250       260
                ....*....|....*....|....*
gi 4505577  428 GIIALALEANSQLTWRDVQHLLVKT 452
Cdd:cd07498 218 GVAALILSANPNLTPAEVEDILTST 242
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 73-149 1.62e-37

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: 135.04  E-value: 1.62e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505577     73 HWAVQVLGGPAEADRVAAAHGYLNLGQIGNLEDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKR 149
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 199-452 4.22e-34

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: 131.17  E-value: 4.22e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  199 VVVTILDDGIERNHPDLapnyDSYASYDVNGNDYDPSPRY--DASNENKHGTRCAGEVAASANNSYCiVGIAYNAKIGGI 276
Cdd:cd00306   1 VTVAVIDTGVDPDHPDL----DGLFGGGDGGNDDDDNENGptDPDDGNGHGTHVAGIIAASANNGGG-VGVAPGAKLIPV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  277 RMLDGDVTDVVEAKSLGIR----PNYIDIYSASWGPDDDGktvdgPGRLAKQAFEYGIKKgrqgLGSIFVWASGNGGREG 352
Cdd:cd00306  76 KVLDGDGSGSSSDIAAAIDyaaaDQGADVINLSLGGPGSP-----PSSALSEAIDYALAK----LGVLVVAAAGNDGPDG 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  353 DYCScDGYTNSIYTISVSSATENGykpwyleecasTLATTYSSG-------AFYERKIVTTDLRQRCTDGHTGTSVSAPM 425
Cdd:cd00306 147 GTNI-GYPAASPNVIAVGAVDRDG-----------TPASPSSNGgagvdiaAPGGDILSSPTTGGGGYATLSGTSMAAPI 214

                       250       260
                ....*....|....*....|....*..
gi 4505577  426 VAGIIALALEANSQLTWRDVQHLLVKT 452
Cdd:cd00306 215 VAGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 197-454 3.32e-33

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: 129.24  E-value: 3.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  197 KNVVVTILDDGIERNHPDLAPN-------------------Y-DSYASYDVNGNDYDPSPrydasnENKHGTRCAGEVAA 256
Cdd:cd07473   2 GDVVVAVIDTGVDYNHPDLKDNmwvnpgeipgngidddgngYvDDIYGWNFVNNDNDPMD------DNGHGTHVAGIIGA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  257 SANNSYCIVGIAYNAKIGGIRMLD----GDVTDVVEAkslgIrpNY-----IDIYSASWGPdddgktvDGPGRLAKQAFE 327
Cdd:cd07473  76 VGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKA----I--DYavdmgAKIINNSWGG-------GGPSQALRDAIA 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  328 YGIKKgrqglGSIFVWASGNGGREGDY-----CScdgYTNSiYTISVSSATENGYKPWYLEECAST--LA-------TTY 393
Cdd:cd07473 143 RAIDA-----GILFVAAAGNDGTNNDKtptypAS---YDLD-NIISVAATDSNDALASFSNYGKKTvdLAapgvdilSTS 213

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505577  394 SSGAfYERKivttdlrqrctdghTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSR 454
Cdd:cd07473 214 PGGG-YGYM--------------SGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 161-455 1.56e-26

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: 109.66  E-value: 1.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  161 NDPIWSNMWYLHcgdknsrcrsEMNVQAAWKRGyTGKNVVVTILDDGIERNHPDLApNYDSYASYDVNGNDYDPSpryda 240
Cdd:cd07484   3 NDPYYSYQWNLD----------QIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLL-KVKFVLGYDFVDNDSDAM----- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  241 sNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLD----GDVTDVVEakslGIRpnyidiysasWGPDDDGKTV- 315
Cdd:cd07484  66 -DDNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIAN----GIR----------YAADKGAKVIn 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  316 -----DGPGRLAKQAFEYGIKKgrqglGSIFVWASGNGGREgdycSCDgYTNSI-YTISVSSATENGYKPWYleecaSTL 389
Cdd:cd07484 131 lslggGLGSTALQEAINYAWNK-----GVVVVAAAGNEGVS----SVS-YPAAYpGAIAVAATDQDDKRASF-----SNY 195

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505577  390 ATTYSSGAFYErKIVTTDLRQRcTDGHTGTSVSAPMVAGIIALaLEANSQLTWRDVQHLLVKTSRP 455
Cdd:cd07484 196 GKWVDVSAPGG-GILSTTPDGD-YAYMSGTSMATPHVAGVAAL-LYSQGPLSASEVRDALKKTADD 258
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 188-439 1.20e-25

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: 107.57  E-value: 1.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  188 AAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYA-SYDVNGNDYDPSPRYDA---SNENKHGTRCAGEVAASANNSYC 263
Cdd:cd07485   1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGyDPAVNGYNFVPNVGDIDndvSVGGGHGTHVAGTIAAVNNNGGG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  264 IVGIAYN------AKIGGIRMLDGD--VTDVVEAKSLG-IRPNYIDIYSASWGpdddGKTVDGPGRLAKQAFEYGIKKGR 334
Cdd:cd07485  81 VGGIAGAggvapgVKIMSIQIFAGRyyVGDDAVAAAIVyAADNGAVILQNSWG----GTGGGIYSPLLKDAFDYFIENAG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  335 QGL--GSIFVWASGNGGREGDY--CSCDGytnsiyTISVSSATENGYKPWYleecaSTLATTYSSGAFYERKIVTTDLRQ 410
Cdd:cd07485 157 GSPldGGIVVFSAGNSYTDEHRfpAAYPG------VIAVAALDTNDNKASF-----SNYGRWVDIAAPGVGTILSTVPKL 225

                       250       260       270
                ....*....|....*....|....*....|....
gi 4505577  411 RCTDGHT-----GTSVSAPMVAGIIALALEANSQ 439
Cdd:cd07485 226 DGDGGGNyeylsGTSMAAPHVSGVAALVLSKFPD 259
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 198-452 5.51e-24

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: 101.45  E-value: 5.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  198 NVVVTILDDGIERNHPDLAPNYdsyasydVNGNDYDPSPRYDASNENKHGTRCAGEVAAsANNSYCIVGIAYNAKIGGIR 277
Cdd:cd07477   1 GVKVAVIDTGIDSSHPDLKLNI-------VGGANFTGDDNNDYQDGNGHGTHVAGIIAA-LDNGVGVVGVAPEADLYAVK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  278 MLD----GDVTDVVEAKSLGIRpNYIDIYSASWGPDDDGKTVdgpgrlaKQAFEYGIKKGrqglgsIF-VWASGNggreg 352
Cdd:cd07477  73 VLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLGGPSDSPAL-------REAIKKAYAAG------ILvVAAAGN----- 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  353 dycscDGYTNSIYT--------ISVSSATENGykpwyleecasTLATTYSSGAFYE-----RKIVTTDLRQRCTDGhTGT 419
Cdd:cd07477 134 -----SGNGDSSYDypakypsvIAVGAVDSNN-----------NRASFSSTGPEVElaapgVDILSTYPNNDYAYL-SGT 196

                       250       260       270
                ....*....|....*....|....*....|...
gi 4505577  420 SVSAPMVAGIIALALEANSQLTWRDVQHLLVKT 452
Cdd:cd07477 197 SMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 195-454 5.62e-24

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: 102.40  E-value: 5.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  195 TGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRydasNENKHGTRCAGEVAASANNSYcIVGIAYNAKIG 274
Cdd:cd04848   1 TGAGVKVGVIDSGIDLSHPEFAGRVSEASYYVAVNDAGYASNG----DGDSHGTHVAGVIAAARDGGG-MHGVAPDATLY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  275 GIRMLDGDVTDVVEAkslGIRPNY-------IDIYSASWGPDDDGKTVDGPGRL---AKQAFEYGIKKGRQGLGSIFVWA 344
Cdd:cd04848  76 SARASASAGSTFSDA---DIAAAYdflaasgVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVFA 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  345 SGNGGREGDYCSCDGYT-------NSIytISVSSATENG-------------YKPWYLeecastlattyssGAFYERKIV 404
Cdd:cd04848 153 AGNDGQANPSLAAAALPylepeleGGW--IAVVAVDPNGtiasysysnrcgvAANWCL-------------AAPGENIYS 217

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 4505577  405 TTDLRQRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSR 454
Cdd:cd04848 218 TDPDGGNGYGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTAT 267
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 198-449 7.39e-24

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: 102.76  E-value: 7.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  198 NVVVTILDDGIERNHPDLA----PNYD----SYASYDVNGNDYDPS----------------PRYDASNENKHGTRCAGE 253
Cdd:cd07496   1 GVVVAVLDTGVLFHHPDLAgvllPGYDfisdPAIANDGDGRDSDPTdpgdwvtgddvppggfCGSGVSPSSWHGTHVAGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  254 VAASANNSYCIVGIAYNAKIGGIRML---DGDVTDVVEakslGIRpnyidiYSAswgpdddGKTVDG---PGRLAK---- 323
Cdd:cd07496  81 IAAVTNNGVGVAGVAWGARILPVRVLgkcGGTLSDIVD----GMR------WAA-------GLPVPGvpvNPNPAKvinl 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  324 ---------QAFEYGIKKGRQgLGSIFVWASGNGGR--EGDY-CSCDGytnsiyTISVSSATENGYKPWYLE-------- 383
Cdd:cd07496 144 slggdgacsATMQNAINDVRA-RGVLVVVAAGNEGSsaSVDApANCRG------VIAVGATDLRGQRASYSNygpavdvs 216

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505577  384 ----ECASTL---------ATTYSSGAFYERkivttdlrqrctdGHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLL 449
Cdd:cd07496 217 apggDCASDVngdgypdsnTGTTSPGGSTYG-------------FLQGTSMAAPHVAGVAALMKSVNPSLTPAQIESLL 282
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 196-457 8.69e-21

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: 93.93  E-value: 8.69e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  196 GKNVVVTILDDGIERNHPDLA----PNYDSYASYDVNGNDYDPSPR---------YDASNENKHGTRCAGEVAASANNSY 262
Cdd:cd07474   1 GKGVKVAVIDTGIDYTHPDLGgpgfPNDKVKGGYDFVDDDYDPMDTrpypsplgdASAGDATGHGTHVAGIIAGNGVNVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  263 CIVGIAYNAKIGGIRMLDGD---VTDVVEAK--------------SLGIRPNYIDiysaswgpDDDGKTVDgpgRLAKqa 325
Cdd:cd07474  81 TIKGVAPKADLYAYKVLGPGgsgTTDVIIAAieqavddgmdvinlSLGSSVNGPD--------DPDAIAIN---NAVK-- 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  326 feygikkgrqgLGSIFVWASGNGGrEGDYCScDGYTNSIYTISVSSATenGYKPWYleecASTLATTYSSGAFYERKIVT 405
Cdd:cd07474 148 -----------AGVVVVAAAGNSG-PAPYTI-GSPATAPSAITVGAST--VADVAE----ADTVGPSSSRGPPTSDSAIK 208

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505577  406 TDL----------RQRCTDG---HTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAH 457
Cdd:cd07474 209 PDIvapgvdimstAPGSGTGyarMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLY 273
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 186-631 2.87e-19

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: 92.96  E-value: 2.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  186 VQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIV 265
Cdd:COG4935 198 VAGGAAGGGGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAA 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  266 GIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGPGRLAKQAFEYGIKKGRQGLGSIFVWAS 345
Cdd:COG4935 278 GGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASG 357

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  346 GNGGREGDYCSCDGYTNSIYTISVSSATENGYKPWYLEECASTLATTYSSGAFYERKIVTTDLRQRCTDGHTGTSVSAPM 425
Cdd:COG4935 358 GGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTG 437

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  426 VAGIIALALEANSQLTWRDVQHLLV--------------KTSRPAHLKASDWKVNGAGHKVSHFYGFGLVDAEALVVEAK 491
Cdd:COG4935 438 TTATATGLGGGADAGSTSTGTGSAAgaaggtttatsglaSSTTAAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGAT 517

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  492 KWTAVPSQHMCVAASDkrPRSIP---LVQVLRTTALTSACAehsdqrvvyLEHVVVRTSISHPRRGDLQIYLVSPSGTKS 568
Cdd:COG4935 518 GAAGTTNSTATFSNTT--DVAIPdngPAGVTSTITVSGGGA---------VEDVTVTVDITHTYRGDLVITLISPDGTTV 586

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505577  569 QLLAKRLLDLSNEgftNWEFMTVHCWGEKAEGQWTLEIQDlpsqvRNPEKQGKLKEWSLILYG 631
Cdd:COG4935 587 VLKNRSGGSADNI---NATFDVANFSGESANGTWTLRVVD-----TAGGDTGTLNSWSLTFTG 641
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 196-452 7.56e-19

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: 87.64  E-value: 7.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  196 GKNVVVTILDDGIERNHPDLAPNYDSYAsYDVNGNDYDPSPrYDasnENKHGTRCAGEVA---ASANNSYCivGIAYNAK 272
Cdd:cd07487   1 GKGITVAVLDTGIDAPHPDFDGRIIRFA-DFVNTVNGRTTP-YD---DNGHGTHVAGIIAgsgRASNGKYK--GVAPGAN 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  273 IGGIRMLD----GDVTDVVEA--------KSLGIRpnyidIYSASWGPDDDGKTVDGPGRLA-KQAFEYGIkkgrqglgs 339
Cdd:cd07487  74 LVGVKVLDdsgsGSESDIIAGidwvvennEKYNIR-----VVNLSLGAPPDPSYGEDPLCQAvERLWDAGI--------- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  340 IFVWASGNGGREGDYCSCDGytNSIYTISVSSATENGYKPWYLeecastlaTTYSSG---AFYERK--IVT--------- 405
Cdd:cd07487 140 VVVVAAGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGI--------SYFSSRgptGDGRIKpdVVApgenivscr 209

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 4505577  406 -TDLRQRCTDGH-----TGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKT 452
Cdd:cd07487 210 sPGGNPGAGVGSgyfemSGTSMATPHVSGAIALLLQANPILTPDEVKCILRDT 262
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 191-460 7.95e-19

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: 88.16  E-value: 7.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  191 KRGYTGKNVVVTILDDGIERNHPDLapnydsyasYDVNGNDYDPSPR----YDASNENK-----HGTRCAGEVAASANNS 261
Cdd:cd04842   1 GLGLTGKGQIVGVADTGLDTNHCFF---------YDPNFNKTNLFHRkivrYDSLSDTKddvdgHGTHVAGIIAGKGNDS 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  262 YCIV---GIAYNAKIGGIRMLDG--------DVTDVVE-AKSLGIRpnyidIYSASWGPDDDG------KTVDgpgrlaK 323
Cdd:cd04842  72 SSISlykGVAPKAKLYFQDIGDTsgnlssppDLNKLFSpMYDAGAR-----ISSNSWGSPVNNgytllaRAYD------Q 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  324 QAFEYgikkgrQGLgsIFVWASGNGGREGdycscdgyTNSIYT-------ISVSSAT----ENGYKPWYLEECASTLATT 392
Cdd:cd04842 141 FAYNN------PDI--LFVFSAGNDGNDG--------SNTIGSpataknvLTVGASNnpsvSNGEGGLGQSDNSDTVASF 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  393 YSSGAFYERKI----------VTTDLRQRCTDGHT---------GTSVSAPMVAGIIALALEAnsqltWRDVQHLLVKTS 453
Cdd:cd04842 205 SSRGPTYDGRIkpdlvapgtgILSARSGGGGIGDTsdsaytsksGTSMATPLVAGAAALLRQY-----FVDGYYPTKFNP 279


                ....*..
gi 4505577  454 RPAHLKA 460
Cdd:cd04842 280 SAALLKA 286
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 694-804 1.72e-17

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: 79.73  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    694 VCHPECGDKGCDGPNADQCLNCVHFSLGsvktsRKCVSVCPLGYFGD---TAARRCRRCHKGCE------TCSSRAATQC 764
Cdd:pfam14843   1 VCDPLCSSEGCWGPGPDQCLSCRNFSRG-----GTCVESCNILQGEPreyVVNSTCVPCHPECLpqngtaTCSGPGADNC 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 4505577    765 LSCRrgfyHHQEMNTCVTLCPAG---------FYADEsQKNCLKCHPSC 804
Cdd:pfam14843  76 TKCA----HFRDGPHCVSSCPSGvlgendliwKYADA-NGVCQPCHPNC 119
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 192-483 8.08e-16

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: 79.57  E-value: 8.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  192 RGYTGKNVVVTILDDGIERNHPDLA----PNYDSYASYDVNGNDYDPS----PRYDASNENKHGTRCAGEVAASaNNSYC 263
Cdd:cd07489   8 EGITGKGVKVAVVDTGIDYTHPALGgcfgPGCKVAGGYDFVGDDYDGTnppvPDDDPMDCQGHGTHVAGIIAAN-PNAYG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  264 IVGIAYNAKIGGIRMLD--GDVTDVVEAKSL------GirpnyIDIYSASWGpdDDGKTVDGPG-----RLAKQafeygi 330
Cdd:cd07489  87 FTGVAPEATLGAYRVFGcsGSTTEDTIIAAFlrayedG-----ADVITASLG--GPSGWSEDPWavvasRIVDA------ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  331 kkgrqglGSIFVWASGNGGREGDYCSCDGyTNSIYTISVSSAtENGYKPWyleecastlattyssGAFYE---------- 400
Cdd:cd07489 154 -------GVVVTIAAGNDGERGPFYASSP-ASGRGVIAVASV-DSYFSSW---------------GPTNElylkpdvaap 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  401 -RKIVTTDLRQrcTDGH---TGTSVSAPMVAGIIALALEANS-QLTWRDVQHLLVKTSRPahLKASDWKVNGAGHKVSHF 475
Cdd:cd07489 210 gGNILSTYPLA--GGGYavlSGTSMATPYVAGAAALLIQARHgKLSPAELRDLLASTAKP--LPWSDGTSALPDLAPVAQ 285


                ....*...
gi 4505577  476 YGFGLVDA 483
Cdd:cd07489 286 QGAGLVNA 293
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 198-452 2.43e-14

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: 74.71  E-value: 2.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  198 NVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPS-PRYDASNENK-----HGTRCAGEVAASANnsycIVGIAYNA 271
Cdd:cd07482   1 KVTVAVIDSGIDPDHPDLKNSISSYSKNLVPKGGYDGKeAGETGDINDIvdklgHGTAVAGQIAANGN----IKGVAPGI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  272 KIGGIRMLD------------------GDVTDVVEAkSLGirpNYIDIYSASWgpDDDGKTvdgpgRLAKQAFEYGIKKg 333
Cdd:cd07482  77 GIVSYRVFGscgsaesswiikaiidaaDDGVDVINL-SLG---GYLIIGGEYE--DDDVEY-----NAYKKAINYAKSK- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  334 rqglGSIFVWASGNGG-------------REGDYCSCDGYTNSIY-----TISVSSATENGYKPWY---------LEECA 386
Cdd:cd07482 145 ----GSIVVAAAGNDGldvsnkqelldflSSGDDFSVNGEVYDVPaslpnVITVSATDNNGNLSSFsnygnsridLAAPG 220

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505577  387 STLATT--YSSGAFYERKIVTTDLR-----QRCTDGHTGTSVSAPMVAGIIALALEANSQLTWRD-VQHLLVKT 452
Cdd:cd07482 221 GDFLLLdqYGKEKWVNNGLMTKEQIlttapEGGYAYMYGTSLAAPKVSGALALIIDKNPLKKPPDeAIRILYNT 294
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
 197-453 1.09e-13

Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of alkaline proteinases originating from different strains of Bacillus subtilis. Novo is one of the strains that produced enzymes belonging to this group. The enzymes obtained from the Novo and BPN' strains are identical. The Carlsburg and Novo subtilisins are thought to have arisen from a common ancestral protein. They have similar peptidase and esterase activities, pH profiles, catalyze transesterification reactions, and are both inhibited by diispropyl fluorophosphate, though they differ in 85 positions in the amino acid sequence. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin.. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173809 [Multi-domain]  Cd Length: 291  Bit Score: 72.78  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  197 KNVVVTILDDGIERNHPDLAP----NYDSYAS---------Y--DVNG----NDYDPSP-----RYDASNEN-------- 244
Cdd:cd07483   1 KTVIVAVLDSGVDIDHEDLKGklwiNKKEIPGngidddnngYidDVNGwnflGQYDPRRivgddPYDLTEKGygnndvng 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  245 -----KHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRM------LDGDVtdvveakSLGIR---PNYIDIYSASWgpdd 310
Cdd:cd07483  81 pisdaDHGTHVAGIIAAVRDNGIGIDGVADNVKIMPLRIvpngdeRDKDI-------ANAIRyavDNGAKVINMSF---- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  311 dGKTVDGPGRLAKQAFEYGIKKgrqglGSIFVWASGNGGREGDycSCDGYTNSIYTIS---VSSATENGYKPWYLEEcas 387
Cdd:cd07483 150 -GKSFSPNKEWVDDAIKYAESK-----GVLIVHAAGNDGLDLD--ITPNFPNDYDKNGgepANNFITVGASSKKYEN--- 218

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505577  388 TLATTYSS-G-------AFYERKIVTTDLRQRCTDGhtGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTS 453
Cdd:cd07483 219 NLVANFSNyGkknvdvfAPGERIYSTTPDNEYETDS--GTSMAAPVVSGVAALIWSYYPNLTAKEVKQIILESG 290
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 194-469 1.34e-12

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: 69.71  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  194 YTGKNVVVTILDDGIERNHPDLApnydsyasyDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIvGIAYNAKI 273
Cdd:cd07480   5 FTGAGVRVAVLDTGIDLTHPAFA---------GRDITTKSFVGGEDVQDGHGHGTHCAGTIFGRDVPGPRY-GVARGAEI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  274 GGIRML----DGDVTDVVEAKSLGIRpNYIDIYSASWGPDDDGKTVDG--PGRLAKQAFE--------------YGIKKG 333
Cdd:cd07480  75 ALIGKVlgdgGGGDGGILAGIQWAVA-NGADVISMSLGADFPGLVDQGwpPGLAFSRALEayrqrarlfdalmtLVAAQA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  334 RQGLGSIFVWASGN-GGREGdycscdgytNSIYTISVSSatengykpwyleeCASTLA----------TTYSSGAFYERK 402
Cdd:cd07480 154 ALARGTLIVAAAGNeSQRPA---------GIPPVGNPAA-------------CPSAMGvaavgalgrtGNFSAVANFSNG 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  403 IVT-----TDLRQRCTDGHT----GTSVSAPMVAGIIAL----ALEANSQLTWRDVQHLLVKTSRPAHLKASDWKVNGAG 469
Cdd:cd07480 212 EVDiaapgVDIVSAAPGGGYrsmsGTSMATPHVAGVAALwaeaLPKAGGRALAALLQARLTAARTTQFAPGLDLPDRGVG 291
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 184-461 2.13e-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: 69.04  E-value: 2.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  184 MNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDydpsPRYDasnENKHGTrcaGEvaaSANnsyc 263
Cdd:cd07494   8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQVRVVLAPGATD----PACD---ENGHGT---GE---SAN---- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  264 IVGIAYNAKIGGIRMLDGDVTDVVEA--KSLGIRPnyiDIYSASWGPDDDGKTVDGPGRL--AKQAFEYGIKKG-RQGLg 338
Cdd:cd07494  71 LFAIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSP---DIISNSWGYDLRSPGTSWSRSLpnALKALAATLQDAvARGI- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  339 sIFVWASGNGG------------------------REGDYCScdGYTNSIY---TIS-----VSSATENGYkpwyleeca 386
Cdd:cd07494 147 -VVVFSAGNGGwsfpaqhpeviaaggvfvdedgarRASSYAS--GFRSKIYpgrQVPdvcglVGMLPHAAY--------- 214

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505577  387 stLATTYSSGAFYERKIVTTDLRQRCTDG---HTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAHLKAS 461
Cdd:cd07494 215 --LMLPVPPGSQLDRSCAAFPDGTPPNDGwgvFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTARDVTKGAS 290
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 199-454 2.26e-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: 2.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  199 VVVTILDDGIERNHPDLAPNydsyASYDVNGNDYDPSPRYD-ASNENKHGTRCAGEVAASAnnSYCIVGIAynakigGIR 277
Cdd:cd07492   2 VRVAVIDSGVDTDHPDLGNL----ALDGEVTIDLEIIVVSAeGGDKDGHGTACAGIIKKYA--PEAEIGSI------KIL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  278 MLDGDVTDVVEAKSLG-IRPNYIDIYSASWGPDDDGKTVdgpgrLAKQAFEYGIKKGRqglgsIFVWASGNGGREGDYCS 356
Cdd:cd07492  70 GEDGRCNSFVLEKALRaCVENDIRIVNLSLGGPGDRDFP-----LLKELLEYAYKAGG-----IIVAAAPNNNDIGTPPA 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  357 cdGYTNsiyTISVSSATENGYKP-WYLEECASTLATTYSSGAFYERKIVTtdlrqrctdghTGTSVSAPMVAGIIALALE 435
Cdd:cd07492 140 --SFPN---VIGVKSDTADDPKSfWYIYVEFSADGVDIIAPAPHGRYLTV-----------SGNSFAAPHVTGMVALLLS 203

                       250
                ....*....|....*....
gi 4505577  436 ANSQLTWRDVQHLLVKTSR 454
Cdd:cd07492 204 EKPDIDANDLKRLLQRLAV 222
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 199-454 3.25e-10

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: 61.80  E-value: 3.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  199 VVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPrydaSNENKHGTRCAGEVAASANNSYCIvGIAYNAKIGGIRM 278
Cdd:cd07490   2 VTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEV----FDAGGHGTHVSGTIGGGGAKGVYI-GVAPEADLLHGKV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  279 LDGD---VTDVVEAKSLGIRPNyIDIYSASWGPDD--DGKTVDGPGRLAKQAfeygikkgrqglGSIFVWASGNGGreGD 353
Cdd:cd07490  77 LDDGggsLSQIIAGMEWAVEKD-ADVVSMSLGGTYysEDPLEEAVEALSNQT------------GALFVVSAGNEG--HG 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  354 YCSCDGYTNSIYTISVSSATENGYKPwylEECASTLATTYSSGAFYERKIVTTDL-----------RQRCTDGH----TG 418
Cdd:cd07490 142 TSGSPGSAYAALSVGAVDRDDEDAWF---SSFGSSGASLVSAPDSPPDEYTKPDVaapgvdvysarQGANGDGQytrlSG 218

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 4505577  419 TSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSR 454
Cdd:cd07490 219 TSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 196-452 4.12e-10

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: 62.10  E-value: 4.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  196 GKNVVVTILDDGIERNHPDLAP--NYDSYASYDVNGNDY---DPSPRYDA--SNENKHGTRCAGEVAASANNSY------ 262
Cdd:cd07497   1 GEGVVIAIVDTGVDYSHPDLDIygNFSWKLKFDYKAYLLpgmDKWGGFYVimYDFFSHGTSCASVAAGRGKMEYnlygyt 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  263 ---CIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNY------------IDIYSASWGPDDDGKTVDGPGRLAKQAFE 327
Cdd:cd07497  81 gkfLIRGIAPDAKIAAVKALWFGDVIYAWLWTAGFDPVDrklswiytggprVDVISNSWGISNFAYTGYAPGLDISSLVI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  328 YGIKKGRqglGSIFVWASGNGGRegDYCSCDGYTNSIYTISVSSATENGYKPWYLeecasTLATTYSSG---AFYER--- 401
Cdd:cd07497 161 DALVTYT---GVPIVSAAGNGGP--GYGTITAPGAASLAISVGAATNFDYRPFYL-----FGYLPGGSGdvvSWSSRgps 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505577  402 --KIVTTDLRQ---------RCTDGHT------------GTSVSAPMVAGIIALALEANSQLTWRD-VQHLLVKT 452
Cdd:cd07497 231 iaGDPKPDLAAigafawapgRVLDSGGaldgneafdlfgGTSMATPMTAGSAALVISALKEKEGVGeYDPFLVRT 305
FU smart00261
Furin-like repeats;
743-789 4.18e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 55.98  E-value: 4.18e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 4505577     743 ARRCRRCHKGCETCSSRAATQCLSCRRGFYHHQemNTCVTLCPAGFY 789
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDG--GKCVSECPPGTY 45
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 188-485 5.93e-10

Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173801 [Multi-domain]  Cd Length: 346  Bit Score: 61.90  E-value: 5.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  188 AAW-KRGYTGKNVVVTILDDGIERNHPDLA---------------------PNYDSYAS------YDVNGNDYDPSPRYD 239
Cdd:cd07475   1 PLWdKGGYKGEGMVVAVIDSGVDPTHDAFRldddskakyseefeakkkkagIGYGKYYNekvpfaYNYADNNDDILDEDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  240 ASNenkHGTRCAGEVAASANNSYC---IVGIAYNAKIGGIRMLD-----GDVTDVV-----EAKSLGirpnyIDIYSASW 306
Cdd:cd07475  81 GSS---HGMHVAGIVAGNGDEEDNgegIKGVAPEAQLLAMKVFSnpeggSTYDDAYakaieDAVKLG-----ADVINMSL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  307 GPDDDGKTVDGPGrlaKQAFEYGIKKGrqglgsIFVWAS-GNGGREGDYCSCDGYTN----------SIY--TISVSSAT 373
Cdd:cd07475 153 GSTAGFVDLDDPE---QQAIKRAREAG------VVVVVAaGNDGNSGSGTSKPLATNnpdtgtvgspATAddVLTVASAN 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  374 ENGYKPwyleeCASTLATTYSSGafyerkiVTTDLRQR-------------CTDGH----TGTSVSAPMVAGIIALALEA 436
Cdd:cd07475 224 KKVPNP-----NGGQMSGFSSWG-------PTPDLDLKpditapggniystVNDNTygymSGTSMASPHVAGASALVKQR 291

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505577  437 ----NSQLTWRD----VQHLLVKTSRPAHlkasDWKVNGAghkvshFY-----GFGLVDAEA 485
Cdd:cd07475 292 lkekYPKLSGEElvdlVKNLLMNTATPPL----DSEDTKT------YYsprrqGAGLIDVAK 343
FU smart00261
Furin-like repeats;
844-886 6.50e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 55.21  E-value: 6.50e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 4505577     844 RCGECHHTCGTCVGPGREECIHCAKNFHFHDWKCVPACGEGFY 886
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 749-798 8.73e-10

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: 55.22  E-value: 8.73e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4505577  749 CHKGCETCSSRAATQCLSCRRGFYHHQemNTCVTLCPAGFYADESQKNCL 798
Cdd:cd00064   2 CHPSCATCTGPGPDQCTSCRHGFYLDG--GTCVSECPEGTYADTEGGVCL 49
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 728-797 3.39e-09

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: 55.13  E-value: 3.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505577    728 KCVSVCPLGYFG--DTAARRCRRCH-KGCETCSSRaaTQCLSCRRGFYHHqeMNTCVTLCPAGFYADESQKNC 797
Cdd:pfam15913  34 VCLHSCPPGYFGirGQEVNRCTKCKaENCESCFSK--DFCTKCKEGFYLH--KGKCLDTCPEGTAAQNSTMEC 102
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 847-889 4.93e-09

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 52.91  E-value: 4.93e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4505577  847 ECHHTCGTCVGPGREECIHCAKNFHFHDWKCVPACGEGFYPEE 889
Cdd:cd00064   1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADT 43
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 799-845 6.82e-09

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 52.52  E-value: 6.82e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 4505577  799 KCHPSCKKCVDE-PEKCTVCKEGFSLARGSCIPDCEPGTYFDSELIRC 845
Cdd:cd00064   1 PCHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVC 48
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 184-434 1.64e-08

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


Pssm-ID: 173792  Cd Length: 277  Bit Score: 56.94  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  184 MNVQAAWKR-GYTGKNVVVTILDDGIERNHPDLAPNYDSyasydvngndydPSPRYDASNENKHGTRCAGEVAAsANNSY 262
Cdd:cd04843   2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGNGIT------------LISGLTDQADSDHGTAVLGIIVA-KDNGI 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  263 CIVGIAYNAKIG--GIRMLDGDVTDVVEAKSLgIRPNYIDIYSASWGPDDDGkTVDGPGRLAKQAFEyGIKKGRQgLGSI 340
Cdd:cd04843  69 GVTGIAHGAQAAvvSSTRVSNTADAILDAADY-LSPGDVILLEMQTGGPNNG-YPPLPVEYEQANFD-AIRTATD-LGII 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  341 FVWASGNGGREGDYCS-CDGYTNSIYTISVS---------SATENGYKPWYLE------ECAS---TLATTYSSGAFYER 401
Cdd:cd04843 145 VVEAAGNGGQDLDAPVyNRGPILNRFSPDFRdsgaimvgaGSSTTGHTRLAFSnygsrvDVYGwgeNVTTTGYGDLQDLG 224

                       250       260       270
                ....*....|....*....|....*....|...
gi 4505577  402 kivttDLRQRCTDGHTGTSVSAPMVAGiiALAL 434
Cdd:cd04843 225 -----GENQDYTDSFSGTSSASPIVAG--AAAS 250
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 194-455 2.02e-08

Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.


Pssm-ID: 173790 [Multi-domain]  Cd Length: 255  Bit Score: 56.37  E-value: 2.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  194 YTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPsprydasneNKHGTRCAGEVAASannsycIVGIAYNAKI 273
Cdd:cd04077  22 STGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDC---------NGHGTHVAGTVGGK------TYGVAKKANL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  274 GGIRMLD----GDVTDVVEAkslgirpnyIDiYSASWGPDDDGKTV-----DGPG-----RLAKQAFEYGIkkgrqglgs 339
Cdd:cd04077  87 VAVKVLDcngsGTLSGIIAG---------LE-WVANDATKRGKPAVanmslGGGAstaldAAVAAAVNAGV--------- 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  340 IFVWASGNGGRegDYCscdGYT--NSIYTISVSSATENGYKPWYLE--ECASTLAttysSGAfyerKIVTTDLRQ-RCTD 414
Cdd:cd04077 148 VVVVAAGNSNQ--DAC---NYSpaSAPEAITVGATDSDDARASFSNygSCVDIFA----PGV----DILSAWIGSdTATA 214

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 4505577  415 GHTGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRP 455
Cdd:cd04077 215 TLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLATK 255
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 695-747 2.16e-08

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: 50.98  E-value: 2.16e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 4505577  695 CHPECgdKGCDGPNADQCLNCVHfslGSVKTSRKCVSVCPLGYFGDTAARRCR 747
Cdd:cd00064   2 CHPSC--ATCTGPGPDQCTSCRH---GFYLDGGTCVSECPEGTYADTEGGVCL 49
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 751-836 2.33e-08

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: 52.82  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    751 KGCETCSSRAAtqCLSCRRGFYHHQEMN------TCVTLCPAGFYADESQK--NCLKCH-PSCKKCVDEpEKCTVCKEGF 821
Cdd:pfam15913   2 SGCVLCSEENG--CLTCQPRLFLLLERNgirqygVCLHSCPPGYFGIRGQEvnRCTKCKaENCESCFSK-DFCTKCKEGF 78

                          90
                  ....*....|....*
gi 4505577    822 SLARGSCIPDCEPGT 836
Cdd:pfam15913  79 YLHKGKCLDTCPEGT 93
VSP pfam03302
Giardia variant-specific surface protein;
649-937 3.22e-08

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 56.90  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    649 MLELSAPELEPPKAALSPS---QVEVPEDEEDYTAqsTPGSANILQTSVCHPECGDKGC--DGPNADQCLNCVHFSLGSV 723
Cdd:pfam03302   7 GYELSADKTKCTSSAPCKTencKACSNDKREVCEE--CNSNNYLTPTSQCIDDCAKIGNyyYTTNANNKKICKECTVANC 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    724 KTSRK--CVSVCPLGYFGDTAArrCRRCHKGCETCSSRAATQCLSCRRG----FYHHQEMNTCVTLCPAGFYADESQ--- 794
Cdd:pfam03302  85 KTCEDqgQCQACNDGFYKSGDA--CSPCHESCKTCSGGTASDCTECLTGkalrYGNDGTKGTCGEGCTTGTGAGACKtcg 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    795 ------KNCLKCH-------------------PSCKKCVDEPEKCTVCKEGFSLARGSCIPDCE-PGTYFDSELIRCGEC 848
Cdd:pfam03302 163 ltidgtSYCSECAteteypqngvctstaaratATCKASSVANGMCSSCANGYFRMNGGCYETTKfPGKSVCEEANSGGTC 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    849 ------HHTCGTCVGPGREECIHCAKNfhfhdwKCVPACGEGFYPEEmpglphKVCRRCDENCLSCAGSSRNCSRCKTGF 922
Cdd:pfam03302 243 qkeapgYKLNNGDLVTCSPGCKTCTSN------TVCTTCMDGYVKTS------DSCTKCDSSCETCTGATTTCKTCATGY 310

                         330
                  ....*....|....*
gi 4505577    923 TQLGTSCITNHTCSN 937
Cdd:pfam03302 311 YKSGTGCVSCTSSES 325
FU smart00261
Furin-like repeats;
795-837 4.42e-08

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 50.20  E-value: 4.42e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505577     795 KNCLKCHPSCKKCVD-EPEKCTVCKEGFSLARGSCIPDCEPGTY 837
Cdd:smart00261   2 GECKPCHPECATCTGpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 201-449 9.46e-08

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 56.13  E-value: 9.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577   201 VTILDDGIERNHPDLAPNY----------------------DSYASYDVNGNDydpspryDASNENKHGTRCAGEVAASA 258
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvdDEYGANFVNNDG-------GPMDDNYHGTHVSGIISAIG 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577   259 NNSYCIVGIAYNAKIGGIRMLD----GDVTDVVEAKSLGIRPNyIDIYSASWGPDDDGKTVDgpgrlakQAFEYgikkgR 334
Cdd:PTZ00262 393 NNNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFN-------ESVKY-----L 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577   335 QGLGSIFVWASGN----GGREGDYCSCDGYTNSIY----------TISVSSATENGYKPWYLeECASTLATTYSSGAFYE 400
Cdd:PTZ00262 460 EEKGILFVVSASNcshtKESKPDIPKCDLDVNKVYppilskklrnVITVSNLIKDKNNQYSL-SPNSFYSAKYCQLAAPG 538

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 4505577   401 RKIVTTDLRQRCTDGhTGTSVSAPMVAGIIALALEANSQLTWRDVQHLL 449
Cdd:PTZ00262 539 TNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEVIRIL 586
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 193-487 1.53e-07

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: 53.84  E-value: 1.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  193 GYTGKNVVVTILDDGIERnhpdLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAG---EVAASANNSYCIVGIAY 269
Cdd:cd05562   1 GVDGTGIKIGVISDGFDG----LGDAADDQASGDLPGNVNVLGDLDGGSGGGDEGRAMLEiihDIAPGAELAFHTAGGGE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  270 NAKIGGIRML-DGDVTDVVEakslgirpnyiDIYSASWGPDDDGKTVDGPGRLAKQAfeygikkgrqglGSIFVWASGNG 348
Cdd:cd05562  77 LDFAAAIRALaAAGADIIVD-----------DIGYLNEPFFQDGPIAQAVDEVVASP------------GVLYFSSAGND 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  349 GREGdycSCDGYTNSIYTISVSSAtenGYKPWYLEECASTLATTYSSGAFYERKIVTTDLRQR---------------CT 413
Cdd:cd05562 134 GQSG---SIFGHAAAPGAIAVGAV---DYGNTPAFGSDPAPGGTPSSFDPVGIRLPTPEVRQKpdvtapdgvngtvdgDG 207

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505577  414 DGH---TGTSVSAPMVAGIIALALEANSQLTWRDVQHLLVKTSRPAHlkasdwkvngaGHKVSHFYGFGLVDAEALV 487
Cdd:cd05562 208 DGPpnfFGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMG-----------EPGYDNASGSGLVDADRAV 273
Furin-like pfam00757
Furin-like cysteine rich region;
695-806 1.57e-07

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 51.67  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577    695 CHPEC-GdkGCDGPNADQCLNCVHFSLGSVktsrkCVSVCPLGYFgdTAARRCrrchkgcetcssRAATQCLSCRRGFYH 773
Cdd:pfam00757  49 CHEQClG--GCTGPNDSDCLACRHFNDEGT-----CVDQCPPGTY--QFGWRC------------VTFKECPKSHLPGYN 107

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 4505577    774 H--QEMNTCVTLCPAGFYADESQKN-CLKCHPSCKK 806
Cdd:pfam00757 108 PlvIHNGECVRECPSGYTEVENNSRkCEPCEGLCPK 143
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 695-754 1.58e-07

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: 51.22  E-value: 1.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505577    695 CHPEC----GDKGCDGPNADQCLNCVHFslgsvKTSRKCVSVCPLGYFGD--------TAARRCRRCHKGCE 754
Cdd:pfam14843  54 CHPEClpqnGTATCSGPGADNCTKCAHF-----RDGPHCVSSCPSGVLGEndliwkyaDANGVCQPCHPNCT 120
FU smart00261
Furin-like repeats;
695-738 3.18e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 44.81  E-value: 3.18e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505577     695 CHPECgdKGCDGPNADQCLNCVHfslGSVKTSRKCVSVCPLGYF 738
Cdd:smart00261   7 CHPEC--ATCTGPGPDDCTSCKH---GFFLDGGKCVSECPPGTY 45
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 218-440 9.96e-06

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: 48.23  E-value: 9.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  218 NYD----SYASYDVNGNDYDPSPRYDASN-ENKHGTRCAGeVAASANNSYCIVGIaYNAKIG-----GIRMldgdvtdvv 287
Cdd:cd07488   6 LWDkndsKNAPNTLAAVFIRNNPRFGRNNtFDDHATLVAS-IMGGRDGGLPAVNL-YSSAFGiksnnGQWQ--------- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  288 EAKSLGIRPNYIDIYSASWGpddDGKTVDGPGRLAKQAFE-YGIKKGRQGLGSIFVWASGNGGREG-DYCSCDGYTNSIY 365
Cdd:cd07488  75 ECLEAQQNGNNVKIINHSYG---EGLKRDPRAVLYGYALLsLYLDWLSRNYEVINVFSAGNQGKEKeKFGGISIPTLAYN 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  366 TISVSSATENGyKPWYleecASTLATTYSSGAFYERKIVT-------TDLRQRCTDGHTGTSVSAPMVAGIIALALEANS 438
Cdd:cd07488 152 SIVVGSTDRNG-DRFF----ASDVSNAGSEINSYGRRKVLivapgsnYNLPDGKDDFVSGTSFSAPLVTGIIALLLEFYD 226


                ..
gi 4505577  439 QL 440
Cdd:cd07488 227 RQ 228
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 826-885 5.25e-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: 43.19  E-value: 5.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505577    826 GSCIPDCEPGtYF---DSELIRCGECH-HTCGTCVGpgREECIHCAKNFHFHDWKCVPACGEGF 885
Cdd:pfam15913  33 GVCLHSCPPG-YFgirGQEVNRCTKCKaENCESCFS--KDFCTKCKEGFYLHKGKCLDTCPEGT 93
Peptidases_S8_7 cd07491
Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the ...
 195-434 5.65e-05

Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173816  Cd Length: 247  Bit Score: 45.79  E-value: 5.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  195 TGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYD-PSPRYDASneNKHGT---RCAGEVaasanNSYCIVGIA-- 268
Cdd:cd07491   1 LLKRIKVALIDDGVDILDSDLQGKIIGGKSFSPYEGDGNkVSPYYVSA--DGHGTamaRMICRI-----CPSAKLYVIkl 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  269 --YNAKIGGIRMLD-GDVTDVVEAkslGIRPNyIDIYSASWGPDDDGKTVDGPGRLAKqAFEYGIKKGRQGLGSifvwAS 345
Cdd:cd07491  74 edRPSPDSNKRSITpQSAAKAIEA---AVEKK-VDIISMSWTIKKPEDNDNDINELEN-AIKEALDRGILLFCS----AS 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  346 GNGGREGD-YCSCDGYTNsIYTISVSSATENGYKPWYLEEcastlATTY--------SSGAFYERKIVTTdlrqrctdgH 416
Cdd:cd07491 145 DQGAFTGDtYPPPAARDR-IFRIGAADEDGGADAPVGDED-----RVDYilpgenveARDRPPLSNSFVT---------H 209

                       250
                ....*....|....*...
gi 4505577  417 TGTSVSAPMVAGIIALAL 434
Cdd:cd07491 210 TGSSVATALAAGLAALIL 227
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 194-273 7.37e-05

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: 46.46  E-value: 7.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  194 YTGKNVVVTILDDGIERNHPD---------------------LAPNYDSYASYDV---------NGNDYDPSPRYDasnE 243
Cdd:cd07478   1 LTGKGVLVGIIDTGIDYLHPEfrnedgttrilyiwdqtipggPPPGGYYGGGEYTeeiinaalaSDNPYDIVPSRD---E 77

                        90       100       110
                ....*....|....*....|....*....|
gi 4505577  244 NKHGTRCAGEVAASANNSYCIVGIAYNAKI 273
Cdd:cd07478  78 NGHGTHVAGIAAGNGDNNPDFKGVAPEAEL 107
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 942-965 4.15e-04

PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short six-cysteine region that is usually found at the C terminal of proteins. It is found in a range of proteins including PACE4 (paired basic amino acid cleaving enzyme 4) and the extracellular matrix protein lacunin.


Pssm-ID: 462560  Cd Length: 31  Bit Score: 38.29  E-value: 4.15e-04
                          10        20
                  ....*....|....*....|....
gi 4505577    942 FCEMVKSNRLCERKLFIQFCCRTC 965
Cdd:pfam08686   7 NCSLVVQARLCSHKYYRQFCCRSC 30
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 721-841 6.04e-04

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 41.52  E-value: 6.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  721 GSVKTSRKCVSVCPLGyFGdtAARRCRRCHKGCETC-------SSRAAT-QCLSCRRGFYHHQEMNTC------VTLCPA 786
Cdd:cd13416   6 GQYTSSGECCEQCPPG-EG--VARPCGDNQTVCEPCldgvtfsDVVSHTePCQPCTRCPGLMSMRAPCtathdtVCECAY 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505577  787 GFYADESQKNClkchpsckkcvdepEKCTVCKEGFSLARgSCIPD-------CEPGTYFDSE 841
Cdd:cd13416  83 GYYLDEDSGTC--------------EPCTVCPPGQGVVQ-SCGPNqdtvceaCPEGTYSDED 129
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 190-434 9.48e-04

Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound subtilisin-kexin-isoenzyme) proteins are secretory Ca2+-dependent serine proteinases cleave at nonbasic residues: Thr, Leu, and Lys. SKI-1s play a critical role in the regulation of the synthesis and metabolism of cholesterol and fatty acid metabolism. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173805 [Multi-domain]  Cd Length: 255  Bit Score: 42.06  E-value: 9.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  190 WKRGYTGKNVVVTILDDGIERNHPDLAPNYDsyasydvngndydpspRYDASNENK------HGTRCAGEVAASanNSYC 263
Cdd:cd07479   1 WQLGYTGAGVKVAVFDTGLAKDHPHFRNVKE----------------RTNWTNEKTlddglgHGTFVAGVIASS--REQC 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  264 iVGIAYNAKIGGIRMLDGDVTD----VVEAKSLGIRPNyIDIYSAS-WGPDddgkTVDGPgrLAKQAFEYGIKkgrqglG 338
Cdd:cd07479  63 -LGFAPDAEIYIFRVFTNNQVSytswFLDAFNYAILTK-IDVLNLSiGGPD----FMDKP--FVDKVWELTAN------N 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505577  339 SIFVWASGNGG-------REGDYCSCDGYTNSIYTISVSSATENGYKPWYLEECASTLA---TTYSSGafyerkIVTTDL 408
Cdd:cd07479 129 IIMVSAIGNDGplygtlnNPADQMDVIGVGGIDFDDNIARFSSRGMTTWELPGGYGRVKpdiVTYGSG------VYGSKL 202

                       250       260
                ....*....|....*....|....*.
gi 4505577  409 RQRCTdGHTGTSVSAPMVAGIIALAL 434
Cdd:cd07479 203 KGGCR-ALSGTSVASPVVAGAVALLL 227
FU smart00261
Furin-like repeats;
896-930 4.56e-03

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 35.95  E-value: 4.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 4505577     896 KVCRRCDENCLSCAGS-SRNCSRCKTGFTQLGTSCI 930
Cdd:smart00261   2 GECKPCHPECATCTGPgPDDCTSCKHGFFLDGGKCV 37
 
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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