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Conserved domains on  [gi|599044042|ref|NP_001278113|]
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proprotein convertase subtilisin/kexin type 6 isoform 1 isoform 2 [Mus musculus]

Protein Classification

S8 family peptidase( domain architecture ID 13872968)

S8 family peptidase is a subtilisin-like serine protease containing a Asp/His/Ser catalytic triad that is not homologous to trypsin; similar to human neuroendocrine convertase 2 that is involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 150-444 7.18e-173

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: 504.02  E-value: 7.18e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 150 FNDPIWSNMWYMHCTDKNS-RCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRY 228
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAGgTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 229 DasNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGP 308
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 309 GRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDHCSCDGYTNSIYTISVSSTTENGHKPWYLEECASTLATTYSSGA- 387
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 599044042 388 FYERKIVTTDLR--QRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSR 444
Cdd:cd04059  239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 529-619 6.91e-41

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: 144.72  E-value: 6.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  529 LEHVVVRISISHPRRGDLQIHLISPSGTKSQLLAKRLLDFSNEGFTNWEFMTVHCWGEKAEGEWTLEVQDipsqvRNPEK 608
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD-----TAPGD 75

                          90
                  ....*....|.
gi 599044042  609 QGKLKEWSLIL 619
Cdd:pfam01483  76 TGTLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 65-141 8.89e-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: 132.73  E-value: 8.89e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 599044042   65 HWAVQVLGGPGAADRVAAAHGYLNLGQIGNLDDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKR 141
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 ...
 671-781 9.27e-20

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: 86.27  E-value: 9.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  671 VCHPECGDKGCDGPNADQCLNCVHFSLGNSktnrkCVSECPLGYFGD---AAARRCRRCHKGCE------TCTGRSPAQC 741
Cdd:pfam14843   1 VCDPLCSSEGCWGPGPDQCLSCRNFSRGGT-----CVESCNILQGEPreyVVNSTCVPCHPECLpqngtaTCSGPGADNC 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 599044042  742 LSCRrgfyHHQETNTCVTLCPAGL---------YADEsQRLCLRCHPSC 781
Cdd:pfam14843  76 TKCA----HFRDGPHCVSSCPSGVlgendliwkYADA-NGVCQPCHPNC 119
FU smart00261
Furin-like repeats;
821-863 6.03e-09

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 52.51  E-value: 6.03e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 599044042   821 KCGECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFY 863
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
774-814 1.59e-07

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 48.66  E-value: 1.59e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 599044042   774 CLRCHPSCQKCVD-EPEKCTVCKEGFSLARGSCIPDCEPGTY 814
Cdd:smart00261   4 CKPCHPECATCTGpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 919-942 3.71e-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: 38.67  E-value: 3.71e-04
                          10        20
                  ....*....|....*....|....
gi 599044042  919 FCEMVKSNRLCERKLFIQFCCRTC 942
Cdd:pfam08686   7 NCSLVVQARLCSHKYYRQFCCRSC 30
 
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 ...
 150-444 7.18e-173

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: 504.02  E-value: 7.18e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 150 FNDPIWSNMWYMHCTDKNS-RCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRY 228
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAGgTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 229 DasNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGP 308
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 309 GRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDHCSCDGYTNSIYTISVSSTTENGHKPWYLEECASTLATTYSSGA- 387
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 599044042 388 FYERKIVTTDLR--QRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSR 444
Cdd:cd04059  239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 186-469 4.20e-67

Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.


Pssm-ID: 395035 [Multi-domain]  Cd Length: 287  Bit Score: 226.19  E-value: 4.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  186 GKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDY----DPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNA 261
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDfnneWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  262 KIGGIRML-DGDVTDVVEAKSLG-IRPNYIDIYSASWGPDddgKTVDGPGRLAKQAFEYGikkGRQGLGSIFVWASGNGG 339
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISwAIPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  340 REGDHCSCDGY-TNSIYTISVSSTTEnghkpwyleeCASTLATTYSSG------------AFY-----------ERKIVT 395
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVDE----------ASEGNLASFSSYgptldgrlkpdiVAPggnitggnissTLLTTT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599044042  396 TDLRQRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAHLKASDwkvngaghkvsHLYGFG 469
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD-----------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 183-476 3.73e-41

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 157.95  E-value: 3.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 183 GYTGKNVVVTILDDGIERNHPDLAPNYDsyASYDVNGNDYDPSprydasNENKHGTRCAGEVAASANNSYCIVGIAYNAK 262
Cdd:COG1404  105 GLTGAGVTVAVIDTGVDADHPDLAGRVV--GGYDFVDGDGDPS------DDNGHGTHVAGIIAANGNNGGGVAGVAPGAK 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 263 IGGIRMLD----GDVTDVVE----AKSLGIrpnyiDIYSASWGPDDDGKTvdgpgRLAKQAFEYGIKKGrqglgSIFVWA 334
Cdd:COG1404  177 LLPVRVLDdngsGTTSDIAAaidwAADNGA-----DVINLSLGGPADGYS-----DALAAAVDYAVDKG-----VLVVAA 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 335 SGNggrEGDHCSCDGYTNSIY-TISVSSTTENGHKPWYleecaStlattySSGAFYE-----RKIVTTDLRQRcTDGHTG 408
Cdd:COG1404  242 AGN---SGSDDATVSYPAAYPnVIAVGAVDANGQLASF-----S------NYGPKVDvaapgVDILSTYPGGG-YATLSG 306

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 599044042 409 TSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAHLKASDwkvngaghkvshlYGFGLVDAEAL 476
Cdd:COG1404  307 TSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGPY-------------YGYGLLADGAA 361
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 529-619 6.91e-41

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: 144.72  E-value: 6.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  529 LEHVVVRISISHPRRGDLQIHLISPSGTKSQLLAKRLLDFSNEGFTNWEFMTVHCWGEKAEGEWTLEVQDipsqvRNPEK 608
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD-----TAPGD 75

                          90
                  ....*....|.
gi 599044042  609 QGKLKEWSLIL 619
Cdd:pfam01483  76 TGTLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 65-141 8.89e-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: 132.73  E-value: 8.89e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 599044042   65 HWAVQVLGGPGAADRVAAAHGYLNLGQIGNLDDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKR 141
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 671-781 9.27e-20

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: 86.27  E-value: 9.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  671 VCHPECGDKGCDGPNADQCLNCVHFSLGNSktnrkCVSECPLGYFGD---AAARRCRRCHKGCE------TCTGRSPAQC 741
Cdd:pfam14843   1 VCDPLCSSEGCWGPGPDQCLSCRNFSRGGT-----CVESCNILQGEPreyVVNSTCVPCHPECLpqngtaTCSGPGADNC 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 599044042  742 LSCRrgfyHHQETNTCVTLCPAGL---------YADEsQRLCLRCHPSC 781
Cdd:pfam14843  76 TKCA----HFRDGPHCVSSCPSGVlgendliwkYADA-NGVCQPCHPNC 119
FU smart00261
Furin-like repeats;
720-766 1.18e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 54.44  E-value: 1.18e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 599044042   720 ARRCRRCHKGCETCTGRSPAQCLSCRRGFYHHQetNTCVTLCPAGLY 766
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDG--GKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 672-724 2.73e-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: 53.68  E-value: 2.73e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 599044042 672 CHPECgdKGCDGPNADQCLNCVHFSLGNsktNRKCVSECPLGYFGDAAARRCR 724
Cdd:cd00064    2 CHPSC--ATCTGPGPDQCTSCRHGFYLD---GGTCVSECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
821-863 6.03e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 52.51  E-value: 6.03e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 599044042   821 KCGECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFY 863
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 824-866 8.33e-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: 49.44  E-value: 8.33e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 599044042 824 ECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFYPEE 866
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADT 43
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 191-439 8.64e-08

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 56.13  E-value: 8.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 191 VTILDDGIERNHPDLAPNY----------------------DSYASYDVNGNDydpspryDASNENKHGTRCAGEVAASA 248
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvdDEYGANFVNNDG-------GPMDDNYHGTHVSGIISAIG 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 249 NNSYCIVGIAYNAKIGGIRMLD----GDVTDVVEAKSLGIRPNyIDIYSASWGPDDDGKTVDgpgrlakQAFEYgikkgR 324
Cdd:PTZ00262 393 NNNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFN-------ESVKY-----L 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 325 QGLGSIFVWASGN----GGREGDHCSCDGYTNSIY----------TISVSSTTE--NGHKPWYLEECASTLattYSSGAF 388
Cdd:PTZ00262 460 EEKGILFVVSASNcshtKESKPDIPKCDLDVNKVYppilskklrnVITVSNLIKdkNNQYSLSPNSFYSAK---YCQLAA 536

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 599044042 389 YERKIVTTDLRQRCTDGhTGTSVSAPMVAGIIALALEANNQLTWRDVQHLL 439
Cdd:PTZ00262 537 PGTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEVIRIL 586
FU smart00261
Furin-like repeats;
774-814 1.59e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 48.66  E-value: 1.59e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 599044042   774 CLRCHPSCQKCVD-EPEKCTVCKEGFSLARGSCIPDCEPGTY 814
Cdd:smart00261   4 CKPCHPECATCTGpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 777-822 2.89e-07

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: 47.90  E-value: 2.89e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 599044042 777 CHPSCQKCVDE-PEKCTVCKEGFSLARGSCIPDCEPGTYFDSELVKC 822
Cdd:cd00064    2 CHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVC 48
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 803-862 9.45e-05

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


Pssm-ID: 464939 [Multi-domain]  Cd Length: 102  Bit Score: 42.42  E-value: 9.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599044042  803 GSCIPDCEPGtYF---DSELVKCGECH-HTCRTCVgpSREECIHCAKSFHFQDWKCVPACGEGF 862
Cdd:pfam15913  33 GVCLHSCPPG-YFgirGQEVNRCTKCKaENCESCF--SKDFCTKCKEGFYLHKGKCLDTCPEGT 93
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 919-942 3.71e-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: 38.67  E-value: 3.71e-04
                          10        20
                  ....*....|....*....|....
gi 599044042  919 FCEMVKSNRLCERKLFIQFCCRTC 942
Cdd:pfam08686   7 NCSLVVQARLCSHKYYRQFCCRSC 30
 
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 ...
 150-444 7.18e-173

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: 504.02  E-value: 7.18e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 150 FNDPIWSNMWYMHCTDKNS-RCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRY 228
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAGgTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 229 DasNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGP 308
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 309 GRLAKQAFEYGIKKGRQGLGSIFVWASGNGGREGDHCSCDGYTNSIYTISVSSTTENGHKPWYLEECASTLATTYSSGA- 387
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 599044042 388 FYERKIVTTDLR--QRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSR 444
Cdd:cd04059  239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 186-469 4.20e-67

Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.


Pssm-ID: 395035 [Multi-domain]  Cd Length: 287  Bit Score: 226.19  E-value: 4.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  186 GKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDY----DPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNA 261
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEASVDfnneWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  262 KIGGIRML-DGDVTDVVEAKSLG-IRPNYIDIYSASWGPDddgKTVDGPGRLAKQAFEYGikkGRQGLGSIFVWASGNGG 339
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISwAIPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  340 REGDHCSCDGY-TNSIYTISVSSTTEnghkpwyleeCASTLATTYSSG------------AFY-----------ERKIVT 395
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVDE----------ASEGNLASFSSYgptldgrlkpdiVAPggnitggnissTLLTTT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599044042  396 TDLRQRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAHLKASDwkvngaghkvsHLYGFG 469
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD-----------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 183-476 3.73e-41

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 157.95  E-value: 3.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 183 GYTGKNVVVTILDDGIERNHPDLAPNYDsyASYDVNGNDYDPSprydasNENKHGTRCAGEVAASANNSYCIVGIAYNAK 262
Cdd:COG1404  105 GLTGAGVTVAVIDTGVDADHPDLAGRVV--GGYDFVDGDGDPS------DDNGHGTHVAGIIAANGNNGGGVAGVAPGAK 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 263 IGGIRMLD----GDVTDVVE----AKSLGIrpnyiDIYSASWGPDDDGKTvdgpgRLAKQAFEYGIKKGrqglgSIFVWA 334
Cdd:COG1404  177 LLPVRVLDdngsGTTSDIAAaidwAADNGA-----DVINLSLGGPADGYS-----DALAAAVDYAVDKG-----VLVVAA 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 335 SGNggrEGDHCSCDGYTNSIY-TISVSSTTENGHKPWYleecaStlattySSGAFYE-----RKIVTTDLRQRcTDGHTG 408
Cdd:COG1404  242 AGN---SGSDDATVSYPAAYPnVIAVGAVDANGQLASF-----S------NYGPKVDvaapgVDILSTYPGGG-YATLSG 306

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 599044042 409 TSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAHLKASDwkvngaghkvshlYGFGLVDAEAL 476
Cdd:COG1404  307 TSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGAPGPY-------------YGYGLLADGAA 361
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 529-619 6.91e-41

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: 144.72  E-value: 6.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  529 LEHVVVRISISHPRRGDLQIHLISPSGTKSQLLAKRLLDFSNEGFTNWEFMTVHCWGEKAEGEWTLEVQDipsqvRNPEK 608
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTD-----TAPGD 75

                          90
                  ....*....|.
gi 599044042  609 QGKLKEWSLIL 619
Cdd:pfam01483  76 TGTLNSWQLTL 86
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 189-442 1.32e-38

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: 144.02  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 189 VVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSprydasNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRM 268
Cdd:cd07498    1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPTS------DIDGHGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 269 LDGDVTDVVEAKSLGIR---PNYIDIYSASWGpdddGKTVDGPGRLakqAFEYGIKKGRQGLGSIFVWASGNGGREGDhc 345
Cdd:cd07498   75 ADSLGYAYWSDIAQAITwaaDNGADVISNSWG----GSDSTESISS---AIDNAATYGRNGKGGVVLFAAGNSGRSVS-- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 346 scDGYTNSIYTISVSSTTENGHK-PW-----YLEECA--STLATTYSSGafyerkIVTTDLRQRCTDGHTGTSVSAPMVA 417
Cdd:cd07498  146 --SGYAANPSVIAVAATDSNDARaSYsnygnYVDLVApgVGIWTTGTGR------GSAGDYPGGGYGSFSGTSFASPVAA 217

                        250       260
                 ....*....|....*....|....*
gi 599044042 418 GIIALALEANNQLTWRDVQHLLVKT 442
Cdd:cd07498  218 GVAALILSANPNLTPAEVEDILTST 242
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 65-141 8.89e-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: 132.73  E-value: 8.89e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 599044042   65 HWAVQVLGGPGAADRVAAAHGYLNLGQIGNLDDYYHFYHSKTFKRSTLSSRGPHTFLRMDPQVKWLQQQEVKRRVKR 141
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 189-442 2.34e-35

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: 134.63  E-value: 2.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 189 VVVTILDDGIERNHPDLapnyDSYASYDVNGNDYDPSPRY--DASNENKHGTRCAGEVAASANNSYCiVGIAYNAKIGGI 266
Cdd:cd00306    1 VTVAVIDTGVDPDHPDL----DGLFGGGDGGNDDDDNENGptDPDDGNGHGTHVAGIIAASANNGGG-VGVAPGAKLIPV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 267 RMLDGDVTDVVEAKSLGIR----PNYIDIYSASWGPDDDGktvdgPGRLAKQAFEYGIKKgrqgLGSIFVWASGNGGREG 342
Cdd:cd00306   76 KVLDGDGSGSSSDIAAAIDyaaaDQGADVINLSLGGPGSP-----PSSALSEAIDYALAK----LGVLVVAAAGNDGPDG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 343 DHCScDGYTNSIYTISVSSTTENGHKPWYleecASTLATTYSSGAFYERKIVTTDLRQRCTDGHTGTSVSAPMVAGIIAL 422
Cdd:cd00306  147 GTNI-GYPAASPNVIAVGAVDRDGTPASP----SSNGGAGVDIAAPGGDILSSPTTGGGGYATLSGTSMAAPIVAGVAAL 221

                        250       260
                 ....*....|....*....|
gi 599044042 423 ALEANNQLTWRDVQHLLVKT 442
Cdd:cd00306  222 LLSANPDLTPAQVKAALLST 241
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 187-444 1.07e-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: 130.39  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 187 KNVVVTILDDGIERNHPDLAPN-------------------Y-DSYASYDVNGNDYDPSPrydasnENKHGTRCAGEVAA 246
Cdd:cd07473    2 GDVVVAVIDTGVDYNHPDLKDNmwvnpgeipgngidddgngYvDDIYGWNFVNNDNDPMD------DNGHGTHVAGIIGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 247 SANNSYCIVGIAYNAKIGGIRMLD----GDVTDVVEAkslgIrpNY-----IDIYSASWGPdddgktvDGPGRLAKQAFE 317
Cdd:cd07473   76 VGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKA----I--DYavdmgAKIINNSWGG-------GGPSQALRDAIA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 318 YGIKKgrqglGSIFVWASGNGGREGDH-----CScdgYTNSiYTISVSSTTENGHKPWYLEECAST--LA-------TTY 383
Cdd:cd07473  143 RAIDA-----GILFVAAAGNDGTNNDKtptypAS---YDLD-NIISVAATDSNDALASFSNYGKKTvdLAapgvdilSTS 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599044042 384 SSGAfYERKivttdlrqrctdghTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSR 444
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, ...
 151-445 1.61e-28

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: 115.44  E-value: 1.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 151 NDPIWSNMWYMHCTDKNSrcrsemnvqaAWKRGyTGKNVVVTILDDGIERNHPDLApNYDSYASYDVNGNDYDPSpryda 230
Cdd:cd07484    3 NDPYYSYQWNLDQIGAPK----------AWDIT-GGSGVTVAVVDTGVDPTHPDLL-KVKFVLGYDFVDNDSDAM----- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 231 sNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLD----GDVTDVVEakslGIRpnyidiysasWGPDDDGKTV- 305
Cdd:cd07484   66 -DDNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIAN----GIR----------YAADKGAKVIn 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 306 -----DGPGRLAKQAFEYGIKKgrqglGSIFVWASGNGGREgdhcSCDgYTNSI-YTISVSSTTENGHKPWYleecaSTL 379
Cdd:cd07484  131 lslggGLGSTALQEAINYAWNK-----GVVVVAAAGNEGVS----SVS-YPAAYpGAIAVAATDQDDKRASF-----SNY 195

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 599044042 380 ATTYSSGAFYErKIVTTDLRQRcTDGHTGTSVSAPMVAGIIALaLEANNQLTWRDVQHLLVKTSRP 445
Cdd:cd07484  196 GKWVDVSAPGG-GILSTTPDGD-YAYMSGTSMATPHVAGVAAL-LYSQGPLSASEVRDALKKTADD 258
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 178-426 1.22e-26

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: 110.65  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 178 AAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYA-SYDVNGNDYDPSPRYDA---SNENKHGTRCAGEVAASANNSYC 253
Cdd:cd07485    1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGyDPAVNGYNFVPNVGDIDndvSVGGGHGTHVAGTIAAVNNNGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 254 IVGIAYN------AKIGGIRMLDGD--VTDVVEAKSLG-IRPNYIDIYSASWGpdddGKTVDGPGRLAKQAFEYGIKKGR 324
Cdd:cd07485   81 VGGIAGAggvapgVKIMSIQIFAGRyyVGDDAVAAAIVyAADNGAVILQNSWG----GTGGGIYSPLLKDAFDYFIENAG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 325 QGL--GSIFVWASGNGGREGDH--CSCDGytnsiyTISVSSTTENGHKPWYleecaSTLATTYSSGAFYERKIVTTDLRQ 400
Cdd:cd07485  157 GSPldGGIVVFSAGNSYTDEHRfpAAYPG------VIAVAALDTNDNKASF-----SNYGRWVDIAAPGVGTILSTVPKL 225

                        250       260       270
                 ....*....|....*....|....*....|.
gi 599044042 401 RCTDGHT-----GTSVSAPMVAGIIALALEA 426
Cdd:cd07485  226 DGDGGGNyeylsGTSMAAPHVSGVAALVLSK 256
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 188-442 9.93e-25

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: 103.77  E-value: 9.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 188 NVVVTILDDGIERNHPDLAPNYdsyasydVNGNDYDPSPRYDASNENKHGTRCAGEVAAsANNSYCIVGIAYNAKIGGIR 267
Cdd:cd07477    1 GVKVAVIDTGIDSSHPDLKLNI-------VGGANFTGDDNNDYQDGNGHGTHVAGIIAA-LDNGVGVVGVAPEADLYAVK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 268 MLD----GDVTDVVEAKSLGIRpNYIDIYSASWGPDDDGKTVdgpgrlaKQAFEYGIKKGrqglgsIF-VWASGNggreg 342
Cdd:cd07477   73 VLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLGGPSDSPAL-------REAIKKAYAAG------ILvVAAAGN----- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 343 dhcscDGYTNSIYT--------ISVSSTTENGhkpwyleecasTLATTYSSGAFYE-----RKIVTTDLRQRCTDGhTGT 409
Cdd:cd07477  134 -----SGNGDSSYDypakypsvIAVGAVDSNN-----------NRASFSSTGPEVElaapgVDILSTYPNNDYAYL-SGT 196

                        250       260       270
                 ....*....|....*....|....*....|...
gi 599044042 410 SVSAPMVAGIIALALEANNQLTWRDVQHLLVKT 442
Cdd:cd07477  197 SMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 188-439 1.40e-23

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: 101.99  E-value: 1.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 188 NVVVTILDDGIERNHPDLA----PNYD----SYASYDVNGNDYDPS----------------PRYDASNENKHGTRCAGE 243
Cdd:cd07496    1 GVVVAVLDTGVLFHHPDLAgvllPGYDfisdPAIANDGDGRDSDPTdpgdwvtgddvppggfCGSGVSPSSWHGTHVAGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 244 VAASANNSYCIVGIAYNAKIGGIRML---DGDVTDVVEakslGIRpnyidiYSAswgpdddGKTVDG---PGRLAK---- 313
Cdd:cd07496   81 IAAVTNNGVGVAGVAWGARILPVRVLgkcGGTLSDIVD----GMR------WAA-------GLPVPGvpvNPNPAKvinl 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 314 ---------QAFEYGIKKGRQgLGSIFVWASGNGGREGDH---CSCDGytnsiyTISVSSTTENGHKPWYLE-------- 373
Cdd:cd07496  144 slggdgacsATMQNAINDVRA-RGVLVVVAAGNEGSSASVdapANCRG------VIAVGATDLRGQRASYSNygpavdvs 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 599044042 374 ----ECASTL---------ATTYSSGAFYERkivttdlrqrctdGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLL 439
Cdd:cd07496  217 apggDCASDVngdgypdsnTGTTSPGGSTYG-------------FLQGTSMAAPHVAGVAALMKSVNPSLTPAQIESLL 282
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 185-444 1.54e-23

Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.


Pssm-ID: 173794 [Multi-domain]  Cd Length: 267  Bit Score: 101.25  E-value: 1.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 185 TGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRydasNENKHGTRCAGEVAASANNSYcIVGIAYNAKIG 264
Cdd:cd04848    1 TGAGVKVGVIDSGIDLSHPEFAGRVSEASYYVAVNDAGYASNG----DGDSHGTHVAGVIAAARDGGG-MHGVAPDATLY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 265 GIRMLDGDVTDVVEAkslGIRPNY-------IDIYSASWGPDDDGKTVDGPGRL---AKQAFEYGIKKGRQGLGSIFVWA 334
Cdd:cd04848   76 SARASASAGSTFSDA---DIAAAYdflaasgVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVFA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 335 SGNggregdhcscDGYTNSIYT---------------ISVSSTTENGHKP--WYLEECAST----LAttyssgAFYERKI 393
Cdd:cd04848  153 AGN----------DGQANPSLAaaalpylepeleggwIAVVAVDPNGTIAsySYSNRCGVAanwcLA------APGENIY 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 599044042 394 VTTDLRQRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSR 444
Cdd:cd04848  217 STDPDGGNGYGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTAT 267
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 186-447 1.42e-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: 96.25  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 186 GKNVVVTILDDGIERNHPDLA----PNYDSYASYDVNGNDYDPSPR---------YDASNENKHGTRCAGEVAASANNSY 252
Cdd:cd07474    1 GKGVKVAVIDTGIDYTHPDLGgpgfPNDKVKGGYDFVDDDYDPMDTrpypsplgdASAGDATGHGTHVAGIIAGNGVNVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 253 CIVGIAYNAKIGGIRMLDGD---VTDVVEAK--------------SLGIRPNYIDiysaswgpDDDGKTVDgpgRLAKqa 315
Cdd:cd07474   81 TIKGVAPKADLYAYKVLGPGgsgTTDVIIAAieqavddgmdvinlSLGSSVNGPD--------DPDAIAIN---NAVK-- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 316 feygikkgrqgLGSIFVWASGNGGreGDHCSCDGYTNSIYTISVSSTTenGHKPWYleecASTLATTYSSGAFYERKIVT 395
Cdd:cd07474  148 -----------AGVVVVAAAGNSG--PAPYTIGSPATAPSAITVGAST--VADVAE----ADTVGPSSSRGPPTSDSAIK 208

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 599044042 396 TDL----------RQRCTDG---HTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAH 447
Cdd:cd07474  209 PDIvapgvdimstAPGSGTGyarMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLY 273
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 176-621 7.37e-20

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: 94.89  E-value: 7.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 176 VQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIV 255
Cdd:COG4935  198 VAGGAAGGGGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAA 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 256 GIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNYIDIYSASWGPDDDGKTVDGPGRLAKQAFEYGIKKGRQGLGSIFVWAS 335
Cdd:COG4935  278 GGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASG 357

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 336 GNGGREGDHCSCDGYTNSIYTISVSSTTENGHKPWYLEECASTLATTYSSGAFYERKIVTTDLRQRCTDGHTGTSVSAPM 415
Cdd:COG4935  358 GGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTG 437

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 416 VAGIIALALEANNQLTWRDVQHLLV--------------KTSRPAHLKASDWKVNGAGHKVSHlYGFGLVDAEALVLEAR 481
Cdd:COG4935  438 TTATATGLGGGADAGSTSTGTGSAAgaaggtttatsglaSSTTAAAAAAAAGLATTAAVAAGA-AGAAAAAATAASVGGA 516

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 482 KWTAVPSQHVCVATADkRPRSIP---IVQVLRTTALTNACAdhsdqrvvyLEHVVVRISISHPRRGDLQIHLISPSGTKS 558
Cdd:COG4935  517 TGAAGTTNSTATFSNT-TDVAIPdngPAGVTSTITVSGGGA---------VEDVTVTVDITHTYRGDLVITLISPDGTTV 586

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 599044042 559 QLLAKRLLDFSNEgftNWEFMTVHCWGEKAEGEWTLEVQDipsqvRNPEKQGKLKEWSLILYG 621
Cdd:COG4935  587 VLKNRSGGSADNI---NATFDVANFSGESANGTWTLRVVD-----TAGGDTGTLNSWSLTFTG 641
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 671-781 9.27e-20

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: 86.27  E-value: 9.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  671 VCHPECGDKGCDGPNADQCLNCVHFSLGNSktnrkCVSECPLGYFGD---AAARRCRRCHKGCE------TCTGRSPAQC 741
Cdd:pfam14843   1 VCDPLCSSEGCWGPGPDQCLSCRNFSRGGT-----CVESCNILQGEPreyVVNSTCVPCHPECLpqngtaTCSGPGADNC 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 599044042  742 LSCRrgfyHHQETNTCVTLCPAGL---------YADEsQRLCLRCHPSC 781
Cdd:pfam14843  76 TKCA----HFRDGPHCVSSCPSGVlgendliwkYADA-NGVCQPCHPNC 119
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 181-450 4.15e-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: 88.93  E-value: 4.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 181 KRGYTGKNVVVTILDDGIERNHPDLapnydsyasYDVNGNDYDPSPR----YDASNENK-----HGTRCAGEVAASANNS 251
Cdd:cd04842    1 GLGLTGKGQIVGVADTGLDTNHCFF---------YDPNFNKTNLFHRkivrYDSLSDTKddvdgHGTHVAGIIAGKGNDS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 252 YCIV---GIAYNAKIGGIRMLDG--------DVTDVVE-AKSLGIRpnyidIYSASWGPDDDG------KTVDgpgrlaK 313
Cdd:cd04842   72 SSISlykGVAPKAKLYFQDIGDTsgnlssppDLNKLFSpMYDAGAR-----ISSNSWGSPVNNgytllaRAYD------Q 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 314 QAFEYgikkgrQGLgsIFVWASGNGGREGdhcscdgyTNSIYT-------ISVSSTT----ENGHKPWYLEECASTLATT 382
Cdd:cd04842  141 FAYNN------PDI--LFVFSAGNDGNDG--------SNTIGSpataknvLTVGASNnpsvSNGEGGLGQSDNSDTVASF 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 383 YSSGAFYERKI----------VTTDLRQRCTDGHT---------GTSVSAPMVAGIIALALEAnnqltWRDVQHLLVKTS 443
Cdd:cd04842  205 SSRGPTYDGRIkpdlvapgtgILSARSGGGGIGDTsdsaytsksGTSMATPLVAGAAALLRQY-----FVDGYYPTKFNP 279


                 ....*..
gi 599044042 444 RPAHLKA 450
Cdd:cd04842  280 SAALLKA 286
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 186-442 7.34e-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: 7.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 186 GKNVVVTILDDGIERNHPDLAPNYDSYAsYDVNGNDYDPSPrYDasnENKHGTRCAGEVA---ASANNSYCivGIAYNAK 262
Cdd:cd07487    1 GKGITVAVLDTGIDAPHPDFDGRIIRFA-DFVNTVNGRTTP-YD---DNGHGTHVAGIIAgsgRASNGKYK--GVAPGAN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 263 IGGIRMLD----GDVTDVVEA--------KSLGIRpnyidIYSASWGPDDDGKTVDGPGRLA-KQAFEYGIkkgrqglgs 329
Cdd:cd07487   74 LVGVKVLDdsgsGSESDIIAGidwvvennEKYNIR-----VVNLSLGAPPDPSYGEDPLCQAvERLWDAGI--------- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 330 IFVWASGNGGREGDHCSCDGytNSIYTISVSSTTENGHKPWYLeecastlaTTYSSG---AFYERK--IVT--------- 395
Cdd:cd07487  140 VVVVAAGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGI--------SYFSSRgptGDGRIKpdVVApgenivscr 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 599044042 396 -TDLRQRCTDGH-----TGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKT 442
Cdd:cd07487  210 sPGGNPGAGVGSgyfemSGTSMATPHVSGAIALLLQANPILTPDEVKCILRDT 262
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 182-473 2.96e-15

Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173814 [Multi-domain]  Cd Length: 312  Bit Score: 77.64  E-value: 2.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 182 RGYTGKNVVVTILDDGIERNHPDLA----PNYDSYASYDVNGNDYDPS----PRYDASNENKHGTRCAGEVAASaNNSYC 253
Cdd:cd07489    8 EGITGKGVKVAVVDTGIDYTHPALGgcfgPGCKVAGGYDFVGDDYDGTnppvPDDDPMDCQGHGTHVAGIIAAN-PNAYG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 254 IVGIAYNAKIGGIRMLD--GDVTDVVEAKSL------GirpnyIDIYSASWGpdDDGKTVDGPG-----RLAKQafeygi 320
Cdd:cd07489   87 FTGVAPEATLGAYRVFGcsGSTTEDTIIAAFlrayedG-----ADVITASLG--GPSGWSEDPWavvasRIVDA------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 321 kkgrqglGSIFVWASGNGGREGDHCSCDGyTNSIYTISVSSttenghkpwyleecastLATTYSS-GAFYE--------- 390
Cdd:cd07489  154 -------GVVVTIAAGNDGERGPFYASSP-ASGRGVIAVAS-----------------VDSYFSSwGPTNElylkpdvaa 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 391 --RKIVTTDLRQrcTDGH---TGTSVSAPMVAGIIALALEA-NNQLTWRDVQHLLVKTSRPahLKASDWKVNGAGHKVSH 464
Cdd:cd07489  209 pgGNILSTYPLA--GGGYavlSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKP--LPWSDGTSALPDLAPVA 284


                 ....*....
gi 599044042 465 LYGFGLVDA 473
Cdd:cd07489  285 QQGAGLVNA 293
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 188-442 5.57e-15

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: 76.64  E-value: 5.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 188 NVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPS-PRYDASNENK-----HGTRCAGEVAASANnsycIVGIAYNA 261
Cdd:cd07482    1 KVTVAVIDSGIDPDHPDLKNSISSYSKNLVPKGGYDGKeAGETGDINDIvdklgHGTAVAGQIAANGN----IKGVAPGI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 262 KIGGIRMLD------------------GDVTDVVEAkSLGirpNYIDIYSASWgpDDDGKTvdgpgRLAKQAFEYGIKKg 323
Cdd:cd07482   77 GIVSYRVFGscgsaesswiikaiidaaDDGVDVINL-SLG---GYLIIGGEYE--DDDVEY-----NAYKKAINYAKSK- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 324 rqglGSIFVWASGNGGREG-------DHCSCDGY--TNSIY---------TISVSSTTENGhkpwYLEECAS------TL 379
Cdd:cd07482  145 ----GSIVVAAAGNDGLDVsnkqellDFLSSGDDfsVNGEVydvpaslpnVITVSATDNNG----NLSSFSNygnsriDL 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 599044042 380 ATT---------YSSGAFYERKIVTTDLR-----QRCTDGHTGTSVSAPMVAGIIALALEANNQLTWRD-VQHLLVKT 442
Cdd:cd07482  217 AAPggdfllldqYGKEKWVNNGLMTKEQIlttapEGGYAYMYGTSLAAPKVSGALALIIDKNPLKKPPDeAIRILYNT 294
Peptidases_S8_Subtilisin_Novo-like cd07483
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ...
 187-443 3.23e-14

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: 74.32  E-value: 3.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 187 KNVVVTILDDGIERNHPDLAP----NYDSYAS---------Y--DVNG----NDYDPSP-----RYDASNEN-------- 234
Cdd:cd07483    1 KTVIVAVLDSGVDIDHEDLKGklwiNKKEIPGngidddnngYidDVNGwnflGQYDPRRivgddPYDLTEKGygnndvng 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 235 -----KHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRM------LDGDVtdvveakSLGIR---PNYIDIYSASWgpdd 300
Cdd:cd07483   81 pisdaDHGTHVAGIIAAVRDNGIGIDGVADNVKIMPLRIvpngdeRDKDI-------ANAIRyavDNGAKVINMSF---- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 301 dGKTVDGPGRLAKQAFEYGIKKgrqglGSIFVWASGNggregDHCSCDGYTNSIYTIS------VSSTTENGHKPWYLEE 374
Cdd:cd07483  150 -GKSFSPNKEWVDDAIKYAESK-----GVLIVHAAGN-----DGLDLDITPNFPNDYDknggepANNFITVGASSKKYEN 218

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 599044042 375 casTLATTYSS-G-------AFYERKIVTTDLRQRCTDGhtGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTS 443
Cdd:cd07483  219 ---NLVANFSNyGkknvdvfAPGERIYSTTPDNEYETDS--GTSMAAPVVSGVAALIWSYYPNLTAKEVKQIILESG 290
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 184-459 3.84e-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: 68.17  E-value: 3.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 184 YTGKNVVVTILDDGIERNHPDLApnydsyasyDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIvGIAYNAKI 263
Cdd:cd07480    5 FTGAGVRVAVLDTGIDLTHPAFA---------GRDITTKSFVGGEDVQDGHGHGTHCAGTIFGRDVPGPRY-GVARGAEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 264 GGIRML----DGDVTDVVEAKSLGIRpNYIDIYSASWGPDDDGKTVDG--PGRLAKQAFE--------------YGIKKG 323
Cdd:cd07480   75 ALIGKVlgdgGGGDGGILAGIQWAVA-NGADVISMSLGADFPGLVDQGwpPGLAFSRALEayrqrarlfdalmtLVAAQA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 324 RQGLGSIFVWASGN-GGREGdhcscdgytNSIYTISVSSttenghkpwyleeCASTLA----------TTYSSGAFYERK 392
Cdd:cd07480  154 ALARGTLIVAAAGNeSQRPA---------GIPPVGNPAA-------------CPSAMGvaavgalgrtGNFSAVANFSNG 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 393 IVT-----TDLRQRCTDGHT----GTSVSAPMVAGIIALALEANNQLTWRD----VQHLLVKTSRPAHLKASDWKVNGAG 459
Cdd:cd07480  212 EVDiaapgVDIVSAAPGGGYrsmsGTSMATPHVAGVAALWAEALPKAGGRAlaalLQARLTAARTTQFAPGLDLPDRGVG 291
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 174-451 6.28e-11

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: 64.42  E-value: 6.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 174 MNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDydpsPRYDasnENKHGTrcaGEvaaSANnsyc 253
Cdd:cd07494    8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQVRVVLAPGATD----PACD---ENGHGT---GE---SAN---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 254 IVGIAYNAKIGGIRMLDGDVTDVVEA--KSLGIRPnyiDIYSASWGPDDDGKTVDGPGRL--AKQAFEYGIKKG-RQGLg 328
Cdd:cd07494   71 LFAIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSP---DIISNSWGYDLRSPGTSWSRSLpnALKALAATLQDAvARGI- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 329 sIFVWASGNGG------------------------REGDHCScdGYTNSIYTisvSSTTEN-----GHKPWyleecASTL 379
Cdd:cd07494  147 -VVVFSAGNGGwsfpaqhpeviaaggvfvdedgarRASSYAS--GFRSKIYP---GRQVPDvcglvGMLPH-----AAYL 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 599044042 380 ATTYSSGAFYERKIVTTDLRQRCTDG---HTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAHLKAS 451
Cdd:cd07494  216 MLPVPPGSQLDRSCAAFPDGTPPNDGwgvFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTARDVTKGAS 290
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 189-444 1.37e-10

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: 62.36  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 189 VVVTILDDGIERNHPDLAPNydsyASYDVNGNDYDPSPRYD-ASNENKHGTRCAGEVAASAnnSYCIVGIAynakigGIR 267
Cdd:cd07492    2 VRVAVIDSGVDTDHPDLGNL----ALDGEVTIDLEIIVVSAeGGDKDGHGTACAGIIKKYA--PEAEIGSI------KIL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 268 MLDGDVTDVVEAKSLG-IRPNYIDIYSASWGPDDDGKTVdgpgrLAKQAFEYGIKKGRqglgsIFVWASGNGGREGdhcS 346
Cdd:cd07492   70 GEDGRCNSFVLEKALRaCVENDIRIVNLSLGGPGDRDFP-----LLKELLEYAYKAGG-----IIVAAAPNNNDIG---T 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 347 CDGYTNSIytISVSSTTENGHKP-WYLEECASTLATTYSSGAFYERKIVTtdlrqrctdghTGTSVSAPMVAGIIALALE 425
Cdd:cd07492  137 PPASFPNV--IGVKSDTADDPKSfWYIYVEFSADGVDIIAPAPHGRYLTV-----------SGNSFAAPHVTGMVALLLS 203

                        250
                 ....*....|....*....
gi 599044042 426 ANNQLTWRDVQHLLVKTSR 444
Cdd:cd07492  204 EKPDIDANDLKRLLQRLAV 222
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 174-424 1.47e-10

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: 63.10  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 174 MNVQAAWKR-GYTGKNVVVTILDDGIERNHPDLAPNYDSyasydvngndydPSPRYDASNENKHGTRCAGEVAAsANNSY 252
Cdd:cd04843    2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGNGIT------------LISGLTDQADSDHGTAVLGIIVA-KDNGI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 253 CIVGIAYNAKIG--GIRMLDGDVTDVVEAKSLgIRPNYIDIYSASWGPDDDGkTVDGPGRLAKQAFEyGIKKGRQgLGSI 330
Cdd:cd04843   69 GVTGIAHGAQAAvvSSTRVSNTADAILDAADY-LSPGDVILLEMQTGGPNNG-YPPLPVEYEQANFD-AIRTATD-LGII 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 331 FVWASGNGGREGDHCS-CDGYTNSIYTISVS---------STTENGHKPWYLE------ECAS---TLATTYSSGAFYER 391
Cdd:cd04843  145 VVEAAGNGGQDLDAPVyNRGPILNRFSPDFRdsgaimvgaGSSTTGHTRLAFSnygsrvDVYGwgeNVTTTGYGDLQDLG 224

                        250       260       270
                 ....*....|....*....|....*....|...
gi 599044042 392 kivttDLRQRCTDGHTGTSVSAPMVAGiiALAL 424
Cdd:cd04843  225 -----GENQDYTDSFSGTSSASPIVAG--AAAS 250
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 189-444 2.93e-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: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 189 VVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPrydaSNENKHGTRCAGEVAASANNSYCIvGIAYNAKIGGIRM 268
Cdd:cd07490    2 VTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEV----FDAGGHGTHVSGTIGGGGAKGVYI-GVAPEADLLHGKV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 269 LDGD---VTDVVEAKSLGIRPNyIDIYSASWGPDD--DGKTVDGPGRLAKQAfeygikkgrqglGSIFVWASGNGGreGD 343
Cdd:cd07490   77 LDDGggsLSQIIAGMEWAVEKD-ADVVSMSLGGTYysEDPLEEAVEALSNQT------------GALFVVSAGNEG--HG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 344 HCSCDGYTNSiyTISVSSTTENGHKPWYlEECASTLATTYSSGAFYERKIVTTDL-----------RQRCTDGH----TG 408
Cdd:cd07490  142 TSGSPGSAYA--ALSVGAVDRDDEDAWF-SSFGSSGASLVSAPDSPPDEYTKPDVaapgvdvysarQGANGDGQytrlSG 218

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 599044042 409 TSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSR 444
Cdd:cd07490  219 TSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 184-445 4.08e-10

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: 61.38  E-value: 4.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 184 YTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPsprydasneNKHGTRCAGEVAASannsycIVGIAYNAKI 263
Cdd:cd04077   22 STGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDC---------NGHGTHVAGTVGGK------TYGVAKKANL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 264 GGIRMLD----GDVTDVVEAkslgirpnyIDiYSASWGPDDDGKTV-----DGPG-----RLAKQAFEYGIkkgrqglgs 329
Cdd:cd04077   87 VAVKVLDcngsGTLSGIIAG---------LE-WVANDATKRGKPAVanmslGGGAstaldAAVAAAVNAGV--------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 330 IFVWASGNGGRegDHCscdGYT--NSIYTISVSSTTENGHKPWYLE--ECASTLAttysSGAfyerKIVTTDLRQ-RCTD 404
Cdd:cd04077  148 VVVVAAGNSNQ--DAC---NYSpaSAPEAITVGATDSDDARASFSNygSCVDIFA----PGV----DILSAWIGSdTATA 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 599044042 405 GHTGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRP 445
Cdd:cd04077  215 TLSGTSMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLATK 255
FU smart00261
Furin-like repeats;
720-766 1.18e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 54.44  E-value: 1.18e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 599044042   720 ARRCRRCHKGCETCTGRSPAQCLSCRRGFYHHQetNTCVTLCPAGLY 766
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDG--GKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 672-724 2.73e-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: 53.68  E-value: 2.73e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 599044042 672 CHPECgdKGCDGPNADQCLNCVHFSLGNsktNRKCVSECPLGYFGDAAARRCR 724
Cdd:cd00064    2 CHPSC--ATCTGPGPDQCTSCRHGFYLD---GGTCVSECPEGTYADTEGGVCL 49
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 726-775 3.85e-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: 53.29  E-value: 3.85e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 599044042 726 CHKGCETCTGRSPAQCLSCRRGFYHHQetNTCVTLCPAGLYADESQRLCL 775
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLDG--GTCVSECPEGTYADTEGGVCL 49
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 186-442 4.75e-09

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: 59.02  E-value: 4.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 186 GKNVVVTILDDGIERNHPDLAP--NYDSYASYDVNGNDY---DPSPRYDA--SNENKHGTRCAGEVAASANNSY------ 252
Cdd:cd07497    1 GEGVVIAIVDTGVDYSHPDLDIygNFSWKLKFDYKAYLLpgmDKWGGFYVimYDFFSHGTSCASVAAGRGKMEYnlygyt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 253 ---CIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRPNY------------IDIYSASWGPDDDGKTVDGPGRLAKQAFE 317
Cdd:cd07497   81 gkfLIRGIAPDAKIAAVKALWFGDVIYAWLWTAGFDPVDrklswiytggprVDVISNSWGISNFAYTGYAPGLDISSLVI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 318 YGIKKGRqglGSIFVWASGNGGRegdhcscdGYTN------SIYTISVSSTTENGHKPWYLeecasTLATTYSSG---AF 388
Cdd:cd07497  161 DALVTYT---GVPIVSAAGNGGP--------GYGTitapgaASLAISVGAATNFDYRPFYL-----FGYLPGGSGdvvSW 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 389 YER-----KIVTTDLRQ---------RCTDGHT------------GTSVSAPMVAGIIALALEANNQLTWRD-VQHLLVK 441
Cdd:cd07497  225 SSRgpsiaGDPKPDLAAigafawapgRVLDSGGaldgneafdlfgGTSMATPMTAGSAALVISALKEKEGVGeYDPFLVR 304


                 .
gi 599044042 442 T 442
Cdd:cd07497  305 T 305
FU smart00261
Furin-like repeats;
821-863 6.03e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 52.51  E-value: 6.03e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 599044042   821 KCGECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFY 863
Cdd:smart00261   3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 672-742 2.49e-08

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: 53.53  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  672 CHPEC----GDKGCDGPNADQCLNCVHFslgnsKTNRKCVSECPLGYFGDA--------AARRCRRCHKGC-ETCTGRSP 738
Cdd:pfam14843  54 CHPEClpqnGTATCSGPGADNCTKCAHF-----RDGPHCVSSCPSGVLGENdliwkyadANGVCQPCHPNCtQGCTGPGL 128


                  ....
gi 599044042  739 AQCL 742
Cdd:pfam14843 129 TGCP 132
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 178-447 3.45e-08

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: 56.51  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 178 AAW-KRGYTGKNVVVTILDDGIERNHPDLA---------------------PNYDSYAS------YDVNGNDYDPSPRYD 229
Cdd:cd07475    1 PLWdKGGYKGEGMVVAVIDSGVDPTHDAFRldddskakyseefeakkkkagIGYGKYYNekvpfaYNYADNNDDILDEDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 230 ASNenkHGTRCAGEVAASANNSYC---IVGIAYNAKIGGIRMLD-----GDVTDVV-----EAKSLGirpnyIDIYSASW 296
Cdd:cd07475   81 GSS---HGMHVAGIVAGNGDEEDNgegIKGVAPEAQLLAMKVFSnpeggSTYDDAYakaieDAVKLG-----ADVINMSL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 297 GPDDDGKTVDGPGrlaKQAFEYGIKKGrqglgsIFVWAS-GNGGREG-DHCSCDGYTNSIY-----------TISVSSTT 363
Cdd:cd07475  153 GSTAGFVDLDDPE---QQAIKRAREAG------VVVVVAaGNDGNSGsGTSKPLATNNPDTgtvgspataddVLTVASAN 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 364 ENGHKPwyleeCASTLATTYSSGafyerkiVTTDLRQR-------------CTDGH----TGTSVSAPMVAGIIALALEA 426
Cdd:cd07475  224 KKVPNP-----NGGQMSGFSSWG-------PTPDLDLKpditapggniystVNDNTygymSGTSMASPHVAGASALVKQR 291

                        330       340
                 ....*....|....*....|....*....
gi 599044042 427 ----NNQLTWRD----VQHLLVKTSRPAH 447
Cdd:cd07475  292 lkekYPKLSGEElvdlVKNLLMNTATPPL 320
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 824-866 8.33e-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: 49.44  E-value: 8.33e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 599044042 824 ECHHTCRTCVGPSREECIHCAKSFHFQDWKCVPACGEGFYPEE 866
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADT 43
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 191-439 8.64e-08

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 56.13  E-value: 8.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 191 VTILDDGIERNHPDLAPNY----------------------DSYASYDVNGNDydpspryDASNENKHGTRCAGEVAASA 248
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvdDEYGANFVNNDG-------GPMDDNYHGTHVSGIISAIG 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 249 NNSYCIVGIAYNAKIGGIRMLD----GDVTDVVEAKSLGIRPNyIDIYSASWGPDDDGKTVDgpgrlakQAFEYgikkgR 324
Cdd:PTZ00262 393 NNNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFN-------ESVKY-----L 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 325 QGLGSIFVWASGN----GGREGDHCSCDGYTNSIY----------TISVSSTTE--NGHKPWYLEECASTLattYSSGAF 388
Cdd:PTZ00262 460 EEKGILFVVSASNcshtKESKPDIPKCDLDVNKVYppilskklrnVITVSNLIKdkNNQYSLSPNSFYSAK---YCQLAA 536

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 599044042 389 YERKIVTTDLRQRCTDGhTGTSVSAPMVAGIIALALEANNQLTWRDVQHLL 439
Cdd:PTZ00262 537 PGTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEVIRIL 586
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 705-774 1.42e-07

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: 50.51  E-value: 1.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 599044042  705 KCVSECPLGYFG--DAAARRCRRCH-KGCETCTGRSpaQCLSCRRGFYHHQetNTCVTLCPAGLYADESQRLC 774
Cdd:pfam15913  34 VCLHSCPPGYFGirGQEVNRCTKCKaENCESCFSKD--FCTKCKEGFYLHK--GKCLDTCPEGTAAQNSTMEC 102
FU smart00261
Furin-like repeats;
774-814 1.59e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 48.66  E-value: 1.59e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 599044042   774 CLRCHPSCQKCVD-EPEKCTVCKEGFSLARGSCIPDCEPGTY 814
Cdd:smart00261   4 CKPCHPECATCTGpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
Furin-like pfam00757
Furin-like cysteine rich region;
672-783 1.87e-07

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 51.28  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  672 CHPEC-GdkGCDGPNADQCLNCVHFSLGNSktnrkCVSECPLGYFgdAAARRCrrchkgcetctgRSPAQCLSCRRGFYH 750
Cdd:pfam00757  49 CHEQClG--GCTGPNDSDCLACRHFNDEGT-----CVDQCPPGTY--QFGWRC------------VTFKECPKSHLPGYN 107

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 599044042  751 H--QETNTCVTLCPAGLYADESQ-RLCLRCHPSCQK 783
Cdd:pfam00757 108 PlvIHNGECVRECPSGYTEVENNsRKCEPCEGLCPK 143
Peptidases_S53 cd04056
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
 183-429 2.09e-07

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


Pssm-ID: 173788 [Multi-domain]  Cd Length: 361  Bit Score: 54.24  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 183 GYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSprYDASNENKHGTRCAGEvaASANNSYcIVGIAYNAK 262
Cdd:cd04056   17 GYTGSGQTIGIIEFGGGYYNPSDLQTFFQLFGLPAPTVFIVVV--IGGGNAPGTSSGWGGE--ASLDVEY-AGAIAPGAN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 263 I----GGIRMLDGDVTDVVEAksLGIRPNYIDIYSASWG------PDDDGKTVDgpgRLAKQAfeygikkGRQGLgSIFV 332
Cdd:cd04056   92 ItlyfAPGTVTNGPLLAFLAA--VLDNPNLPSVISISYGepeqslPPAYAQRVC---NLFAQA-------AAQGI-TVLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 333 wASGNGGREGDHCSCDGYTNSI-------YTISVSSTT---ENGHKPWYLEECASTLATTYSSGAF--------YERKIV 394
Cdd:cd04056  159 -ASGDSGAGGCGGDGSGTGFSVsfpasspYVTAVGGTTlytGGTGSSAESTVWSSEGGWGGSGGGFsnyfprpsYQSGAV 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 599044042 395 TTDLRQ-------RCT-------DGHT--------------GTSVSAPMVAGIIALALEANNQ 429
Cdd:cd04056  238 LGLPPSglyngsgRGVpdvaanaDPGTgylvvvngqwylvgGTSAAAPLFAGLIALINQARLA 300
FU smart00261
Furin-like repeats;
672-715 2.83e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 47.89  E-value: 2.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 599044042   672 CHPECgdKGCDGPNADQCLNCVHfslGNSKTNRKCVSECPLGYF 715
Cdd:smart00261   7 CHPEC--ATCTGPGPDDCTSCKH---GFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 777-822 2.89e-07

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: 47.90  E-value: 2.89e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 599044042 777 CHPSCQKCVDE-PEKCTVCKEGFSLARGSCIPDCEPGTYFDSELVKC 822
Cdd:cd00064    2 CHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVC 48
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 728-822 4.97e-07

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: 48.97  E-value: 4.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  728 KGCETCTGRSpaQCLSCRRGFYHHQETN------TCVTLCPAGLYADESQRL--CLRCH-PSCQKCVDEpEKCTVCKEGF 798
Cdd:pfam15913   2 SGCVLCSEEN--GCLTCQPRLFLLLERNgirqygVCLHSCPPGYFGIRGQEVnrCTKCKaENCESCFSK-DFCTKCKEGF 78

                          90       100
                  ....*....|....*....|....
gi 599044042  799 SLARGSCIPDCEPGTYFDSELVKC 822
Cdd:pfam15913  79 YLHKGKCLDTCPEGTAAQNSTMEC 102
Peptidases_S8_2 cd07488
Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the ...
 208-425 8.87e-07

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: 51.32  E-value: 8.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 208 NYD----SYASYDVNGNDYDPSPRYDASN-ENKHGTRCAGeVAASANNSYCIVGIaYNAKIG-----GIRMldgdvtdvv 277
Cdd:cd07488    6 LWDkndsKNAPNTLAAVFIRNNPRFGRNNtFDDHATLVAS-IMGGRDGGLPAVNL-YSSAFGiksnnGQWQ--------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 278 EAKSLGIRPNYIDIYSASWGpddDGKTVDGPGRLAKQAFE-YGIKKGRQGLGSIFVWASGNGGREG-DHCSCDGYTNSIY 355
Cdd:cd07488   75 ECLEAQQNGNNVKIINHSYG---EGLKRDPRAVLYGYALLsLYLDWLSRNYEVINVFSAGNQGKEKeKFGGISIPTLAYN 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 599044042 356 TISVSSTTENGHkPWYleecASTLATTYSSGAFYERKIVT-------TDLRQRCTDGHTGTSVSAPMVAGIIALALE 425
Cdd:cd07488  152 SIVVGSTDRNGD-RFF----ASDVSNAGSEINSYGRRKVLivapgsnYNLPDGKDDFVSGTSFSAPLVTGIIALLLE 223
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 183-479 5.24e-06

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: 49.21  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 183 GYTGKNVVVTILDDGIERnhpdLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAG---EVAASANNSYCIVGIAY 259
Cdd:cd05562    1 GVDGTGIKIGVISDGFDG----LGDAADDQASGDLPGNVNVLGDLDGGSGGGDEGRAMLEiihDIAPGAELAFHTAGGGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 260 NAKIGGIRML-DGDVTDVVEakslgirpnyiDIYSASWGPDDDGKTVDGPGRLAKQAfeygikkgrqglGSIFVWASGNG 338
Cdd:cd05562   77 LDFAAAIRALaAAGADIIVD-----------DIGYLNEPFFQDGPIAQAVDEVVASP------------GVLYFSSAGND 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 339 GREGdhcSCDGYTNSIYTISVSSTtenGHKPWYLEECASTLATTYSSGAFYERKIVTTDLRQR---------------CT 403
Cdd:cd05562  134 GQSG---SIFGHAAAPGAIAVGAV---DYGNTPAFGSDPAPGGTPSSFDPVGIRLPTPEVRQKpdvtapdgvngtvdgDG 207

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 599044042 404 DGH---TGTSVSAPMVAGIIALALEANNQLTWRDVQHLLVKTSRPAHlkasdwkvngaGHKVSHLYGFGLVDAEALVLE 479
Cdd:cd05562  208 DGPpnfFGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMG-----------EPGYDNASGSGLVDADRAVAA 275
VSP pfam03302
Giardia variant-specific surface protein;
708-896 4.69e-05

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 46.89  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  708 SECPLGYFGDAAARRCRRCHK----GCETCTGRSPAQCLSCRRGFYHhQETNTCVTLC---PAGLYADESQ--RLCLRCH 778
Cdd:pfam03302   2 DECKPGYELSADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYL-TPTSQCIDDCakiGNYYYTTNANnkKICKECT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042  779 PSCQKCVDEPEKCTVCKEGFSLARGSCIPdcepgtyfdselvkcgeCHHTCRTCVGPSREECIHC--AKSFHFQDWKCVP 856
Cdd:pfam03302  81 VANCKTCEDQGQCQACNDGFYKSGDACSP-----------------CHESCKTCSGGTASDCTECltGKALRYGNDGTKG 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 599044042  857 ACGEGFYPEEMPGlphkvcrRCEENCLSCEGSSRnCSRCK 896
Cdd:pfam03302 144 TCGEGCTTGTGAG-------ACKTCGLTIDGTSY-CSECA 175
Peptidases_S8_7 cd07491
Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the ...
 185-424 5.07e-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: 5.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 185 TGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYD-PSPRYDASneNKHGT---RCAGEVaasanNSYCIVGIA-- 258
Cdd:cd07491    1 LLKRIKVALIDDGVDILDSDLQGKIIGGKSFSPYEGDGNkVSPYYVSA--DGHGTamaRMICRI-----CPSAKLYVIkl 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 259 --YNAKIGGIRMLD-GDVTDVVEAkslGIRPNyIDIYSASWGPDDDGKTVDGPGRLAKqAFEYGIKKGRQGLGSifvwAS 335
Cdd:cd07491   74 edRPSPDSNKRSITpQSAAKAIEA---AVEKK-VDIISMSWTIKKPEDNDNDINELEN-AIKEALDRGILLFCS----AS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 336 GNGGREGDHCSCDGYTNSIYTISVSSTTENGHKPWYLEEcastlATTY--------SSGAFYERKIVTTdlrqrctdgHT 407
Cdd:cd07491  145 DQGAFTGDTYPPPAARDRIFRIGAADEDGGADAPVGDED-----RVDYilpgenveARDRPPLSNSFVT---------HT 210

                        250
                 ....*....|....*..
gi 599044042 408 GTSVSAPMVAGIIALAL 424
Cdd:cd07491  211 GSSVATALAAGLAALIL 227
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 184-263 7.16e-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: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 184 YTGKNVVVTILDDGIERNHPD---------------------LAPNYDSYASYDV---------NGNDYDPSPRYDasnE 233
Cdd:cd07478    1 LTGKGVLVGIIDTGIDYLHPEfrnedgttrilyiwdqtipggPPPGGYYGGGEYTeeiinaalaSDNPYDIVPSRD---E 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 599044042 234 NKHGTRCAGEVAASANNSYCIVGIAYNAKI 263
Cdd:cd07478   78 NGHGTHVAGIAAGNGDNNPDFKGVAPEAEL 107
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 803-862 9.45e-05

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


Pssm-ID: 464939 [Multi-domain]  Cd Length: 102  Bit Score: 42.42  E-value: 9.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 599044042  803 GSCIPDCEPGtYF---DSELVKCGECH-HTCRTCVgpSREECIHCAKSFHFQDWKCVPACGEGF 862
Cdd:pfam15913  33 GVCLHSCPPG-YFgirGQEVNRCTKCKaENCESCF--SKDFCTKCKEGFYLHKGKCLDTCPEGT 93
PLAC pfam08686
PLAC (protease and lacunin) domain; The PLAC (protease and lacunin) domain is a short ...
 919-942 3.71e-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: 38.67  E-value: 3.71e-04
                          10        20
                  ....*....|....*....|....
gi 599044042  919 FCEMVKSNRLCERKLFIQFCCRTC 942
Cdd:pfam08686   7 NCSLVVQARLCSHKYYRQFCCRSC 30
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 180-424 5.68e-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: 42.83  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 180 WKRGYTGKNVVVTILDDGIERNHPDLAPNYDsyasydvngndydpspRYDASNENK------HGTRCAGEVAASanNSYC 253
Cdd:cd07479    1 WQLGYTGAGVKVAVFDTGLAKDHPHFRNVKE----------------RTNWTNEKTlddglgHGTFVAGVIASS--REQC 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 254 iVGIAYNAKIGGIRMLDGDVTD----VVEAKSLGIRPNyIDIYSAS-WGPDddgkTVDGPgrLAKQAFEYGIKkgrqglG 328
Cdd:cd07479   63 -LGFAPDAEIYIFRVFTNNQVSytswFLDAFNYAILTK-IDVLNLSiGGPD----FMDKP--FVDKVWELTAN------N 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599044042 329 SIFVWASGNGG-------REGDHCSCDGYTNSIYTISVSSTTENGHKPWYLEECASTLA---TTYSSGafyerkIVTTDL 398
Cdd:cd07479  129 IIMVSAIGNDGplygtlnNPADQMDVIGVGGIDFDDNIARFSSRGMTTWELPGGYGRVKpdiVTYGSG------VYGSKL 202

                        250       260
                 ....*....|....*....|....*.
gi 599044042 399 RQRCTdGHTGTSVSAPMVAGIIALAL 424
Cdd:cd07479  203 KGGCR-ALSGTSVASPVVAGAVALLL 227
 
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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