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Conserved domains on  [gi|24642494|ref|NP_727967|]
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furin 2, isoform F [Drosophila melanogaster]

Protein Classification

S8 family peptidase( domain architecture ID 13872880)

S8 family peptidase is a subtilisin-like serine protease containing an Asp/His/Ser catalytic triad that is not homologous to trypsin; similar to Homo sapiens furin, a ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif

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 ...
 375-671 1.00e-169

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: 514.03  E-value: 1.00e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  375 FPDPLFKEQWYLNG----GAKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQD 450
Cdd:cd04059    1 PNDPLFPYQWYLKNtgqaGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  451 NGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGPGP 530
Cdd:cd04059   81 DDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  531 LARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGTPGH 610
Cdd:cd04059  161 LAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSGNP 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24642494  611 DKSVATVDMDGSlrpdHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 671
Cdd:cd04059  241 EASIVTTDLGGN----CNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 758-846 4.26e-35

Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.


:

Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 128.93  E-value: 4.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    758 LEHVQCRITLRFFPRGNLRILLTSPMGTTSTLLFERPRDIVKSNFDDWPFLSVHFWGEKAEGRWTLQVINGGRrrvNQPG 837
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAP---GDTG 77


                   ....*....
gi 24642494    838 ILSKWQLIF 846
Cdd:pfam01483   78 TLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 242-318 7.53e-34

Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to family S8.


:

Pssm-ID: 465126  Cd Length: 77  Bit Score: 125.03  E-value: 7.53e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642494    242 EFAVNIPAGKQMADVIATKHGFINRGQIGSLDNYYLFQHHHVSKRSLRSSRKHQGALKSENEVKWMQQQHEKVRRKR 318
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 ...
 967-1070 2.61e-17

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


The actual alignment was detected with superfamily member pfam14843:

Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 80.11  E-value: 2.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    967 CDAECDSSGCYGRGPTQCVACSHYRLDNTCVSRCP-----PRSFPNQvGICWPCHDTCE------TCAGAGPDSCLTCAp 1035
Cdd:pfam14843    2 CDPLCSSEGCWGPGPDQCLSCRNFSRGGTCVESCNilqgePREYVVN-STCVPCHPECLpqngtaTCSGPGADNCTKCA- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24642494   1036 ahlHVIDLAVCLQFCPDG--------YFENSRNRTCVPCEPNC 1070
Cdd:pfam14843   80 ---HFRDGPHCVSSCPSGvlgendliWKYADANGVCQPCHPNC 119
VSP super family cl31427
Giardia variant-specific surface protein;
1017-1376 7.54e-17

Giardia variant-specific surface protein;


The actual alignment was detected with superfamily member pfam03302:

Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 84.64  E-value: 7.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1017 DTCETCAGAGPDSCLTCAPAHlHVIDLAVCLQFCPD----GYFENSRNR-TCVPCEP-NCASCQDHpeyctscdhhlvmh 1090
Cdd:pfam03302   26 ENCKACSNDKREVCEECNSNN-YLTPTSQCIDDCAKignyYYTTNANNKkICKECTVaNCKTCEDQ-------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1091 ehKCYSACPLDTYETEDnKCAFCHSTCATCNGPTDQDCITCRSSryawqnKCLISCPDGfyadKKRLECMPCQEG----- 1165
Cdd:pfam03302   91 --GQCQACNDGFYKSGD-ACSPCHESCKTCSGGTASDCTECLTG------KALRYGNDG----TKGTCGEGCTTGtgaga 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1166 CKTC--TSNGV--CSECLQNWTLNKRDKCIVSGSEGCSESEFYSQVEGQCRPCHASCGSCNG--------PADTSCTSCP 1233
Cdd:pfam03302  158 CKTCglTIDGTsyCSECATETEYPQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGgcyettkfPGKSVCEEAN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1234 PNRLLEQSrcvsgcREGFFVEAGSLCSpCLHTCSQCVSRTNCsncskglelqngecrTTCADGYYSDRGICAKCYLSCHT 1313
Cdd:pfam03302  238 SGGTCQKE------APGYKLNNGDLVT-CSPGCKTCTSNTVC---------------TTCMDGYVKTSDSCTKCDSSCET 295

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642494   1314 CSGprrnQCVQCPAgwqlaagechpeCPEGFYKSDFGCQKCHHYCKTCNDAGPLACTSCPPHS 1376
Cdd:pfam03302  296 CTG----ATTTCKT------------CATGYYKSGTGCVSCTSSESDNGITGVKGCLNCAPPS 342
FU smart00261
Furin-like repeats;
1398-1441 8.00e-06

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 44.42  E-value: 8.00e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24642494    1398 TCKTCHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQT 1441
Cdd:smart00261    3 ECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPGT 44
 
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 ...
 375-671 1.00e-169

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: 514.03  E-value: 1.00e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  375 FPDPLFKEQWYLNG----GAKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQD 450
Cdd:cd04059    1 PNDPLFPYQWYLKNtgqaGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  451 NGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGPGP 530
Cdd:cd04059   81 DDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  531 LARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGTPGH 610
Cdd:cd04059  161 LAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSGNP 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24642494  611 DKSVATVDMDGSlrpdHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 671
Cdd:cd04059  241 EASIVTTDLGGN----CNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 408-697 1.97e-57

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: 200.76  E-value: 1.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    408 GKGVVVSILDDGIQTNHPDLAQNY------DPEASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNA 481
Cdd:pfam00082    1 GKGVVVAVLDTGIDPNHPDLSGNLdndpsdDPEASVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    482 SIGGVRML-DGKVNDVVEAQALSLN-PSHIDIYSASWGPEddgSTVDGPGPLARRAFIYGvtsGRQGKGSIFVWASGNGG 559
Cdd:pfam00082   81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    560 RYTDSCNCDGY-TNSIFTLSISSATqagfkpwyleECSSTLATTYSSGTPGHDKS-----VA------------TVDMDG 621
Cdd:pfam00082  155 PGGNNGSSVGYpAQYKNVIAVGAVD----------EASEGNLASFSSYGPTLDGRlkpdiVApggnitggnissTLLTTT 224

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642494    622 SlRPDHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLEKENgwtlngvkrkysHKFGYG 697
Cdd:pfam00082  225 S-DPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD------------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 376-703 4.45e-37

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 146.78  E-value: 4.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  376 PDPLFKEQWYLNGGAKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDingnDSDPTPQDngDNK 455
Cdd:COG1404   76 LPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDFV----DGDGDPSD--DNG 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  456 HGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLD----GKVNDVVEA--QALSLNpshIDIYSASWgpeddGSTVDGPG 529
Cdd:COG1404  150 HGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDdngsGTTSDIAAAidWAADNG---ADVINLSL-----GGPADGYS 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  530 PLARRAFIYGVtsgrqGKGSIFVWASGNGGRYTDS----CNCDGytnsifTLSISSATQAGFKPWYleecSSTlattyss 605
Cdd:COG1404  222 DALAAAVDYAV-----DKGVLVVAAAGNSGSDDATvsypAAYPN------VIAVGAVDANGQLASF----SNY------- 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  606 GT------PGHDksVATVDMDGSlrpdhicTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLeken 679
Cdd:COG1404  280 GPkvdvaaPGVD--ILSTYPGGG-------YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGA---- 346

                        330       340
                 ....*....|....*....|....
gi 24642494  680 gwtlngvkrkYSHKFGYGLMDAGA 703
Cdd:COG1404  347 ----------PGPYYGYGLLADGA 360
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 758-846 4.26e-35

Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.


Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 128.93  E-value: 4.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    758 LEHVQCRITLRFFPRGNLRILLTSPMGTTSTLLFERPRDIVKSNFDDWPFLSVHFWGEKAEGRWTLQVINGGRrrvNQPG 837
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAP---GDTG 77


                   ....*....
gi 24642494    838 ILSKWQLIF 846
Cdd:pfam01483   78 TLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 242-318 7.53e-34

Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to family S8.


Pssm-ID: 465126  Cd Length: 77  Bit Score: 125.03  E-value: 7.53e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642494    242 EFAVNIPAGKQMADVIATKHGFINRGQIGSLDNYYLFQHHHVSKRSLRSSRKHQGALKSENEVKWMQQQHEKVRRKR 318
Cdd:pfam16470    1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 967-1070 2.61e-17

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


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 80.11  E-value: 2.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    967 CDAECDSSGCYGRGPTQCVACSHYRLDNTCVSRCP-----PRSFPNQvGICWPCHDTCE------TCAGAGPDSCLTCAp 1035
Cdd:pfam14843    2 CDPLCSSEGCWGPGPDQCLSCRNFSRGGTCVESCNilqgePREYVVN-STCVPCHPECLpqngtaTCSGPGADNCTKCA- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24642494   1036 ahlHVIDLAVCLQFCPDG--------YFENSRNRTCVPCEPNC 1070
Cdd:pfam14843   80 ---HFRDGPHCVSSCPSGvlgendliWKYADANGVCQPCHPNC 119
VSP pfam03302
Giardia variant-specific surface protein;
1017-1376 7.54e-17

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 84.64  E-value: 7.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1017 DTCETCAGAGPDSCLTCAPAHlHVIDLAVCLQFCPD----GYFENSRNR-TCVPCEP-NCASCQDHpeyctscdhhlvmh 1090
Cdd:pfam03302   26 ENCKACSNDKREVCEECNSNN-YLTPTSQCIDDCAKignyYYTTNANNKkICKECTVaNCKTCEDQ-------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1091 ehKCYSACPLDTYETEDnKCAFCHSTCATCNGPTDQDCITCRSSryawqnKCLISCPDGfyadKKRLECMPCQEG----- 1165
Cdd:pfam03302   91 --GQCQACNDGFYKSGD-ACSPCHESCKTCSGGTASDCTECLTG------KALRYGNDG----TKGTCGEGCTTGtgaga 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1166 CKTC--TSNGV--CSECLQNWTLNKRDKCIVSGSEGCSESEFYSQVEGQCRPCHASCGSCNG--------PADTSCTSCP 1233
Cdd:pfam03302  158 CKTCglTIDGTsyCSECATETEYPQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGgcyettkfPGKSVCEEAN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1234 PNRLLEQSrcvsgcREGFFVEAGSLCSpCLHTCSQCVSRTNCsncskglelqngecrTTCADGYYSDRGICAKCYLSCHT 1313
Cdd:pfam03302  238 SGGTCQKE------APGYKLNNGDLVT-CSPGCKTCTSNTVC---------------TTCMDGYVKTSDSCTKCDSSCET 295

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642494   1314 CSGprrnQCVQCPAgwqlaagechpeCPEGFYKSDFGCQKCHHYCKTCNDAGPLACTSCPPHS 1376
Cdd:pfam03302  296 CTG----ATTTCKT------------CATGYYKSGTGCVSCTSSESDNGITGVKGCLNCAPPS 342
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1113-1160 4.61e-11

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: 59.45  E-value: 4.61e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 24642494 1113 CHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFYADKKRLECM 1160
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
1107-1151 1.72e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.52  E-value: 1.72e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642494    1107 DNKCAFCHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFY 1151
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 1162-1479 5.14e-10

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 64.55  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1162 CQEGCKTCTsNGVCSEclqnwtlnkrdkcIVSGSEGCSES-------EFYSQvEGQCRPCHASCGSCNGPADTSCTSCPP 1234
Cdd:PTZ00214  391 CSESCSGDT-RGVCTK-------------VAEGSESTEVScrcvckpTFYNS-SGTCTPCTDSCAVCKDGTPTGCQQCSP 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1235 NRLLEQS-------RCVSGCRE-------GFFVEAGSLCSPCLHTC---------------SQCVSRTN--CSNCSKGLE 1283
Cdd:PTZ00214  456 GKILEFSivssesaDCVDQCSVgsecaecGITIDGSRYCTRCKDAStypfngvcipntqrdAYCTSTANgaCTTCSGAAF 535

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1284 LQNGECRT-------------------TCADGYY-SDRGICAKCYLSCHTCSGPRRNQCVQCPAGWQL------AAGEC- 1336
Cdd:PTZ00214  536 LMNGGCYTtehypgsticdkqsngkctTTKKGYGiSPDGKLLECDPTCLACTAPGPGRCTRCPSDKLLkrasgaATGSCv 615

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1337 -HPECPEGFYKSDFGCQKCHHY-CKTCNDAGplACTSCPPHSM--LDGGLCM-ECLSSQYYDTTSATCKTCHdsCRSCFG 1411
Cdd:PTZ00214  616 dPGACVDGYYADGDACLPCATPgCKTCGHAS--FCTECAGELFvsLDGQSCLeECTGDKVVGEVSGGVRRCW--CERGFL 691

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1412 PGqFSCKGCVPPLHLDQLNSQCVSC----------------------CQNQTLAEKTSSAACCNCDGET----GECKATS 1465
Cdd:PTZ00214  692 PA-LDRSGCVLPTECPPDMPSCAACdesgrcllcvtsghnvqvdqrtCAEGCGARASSNQGVCMCELDAvltkGVCVPAK 770

                         410
                  ....*....|....
gi 24642494  1466 TGGKRRTVVGSGSA 1479
Cdd:PTZ00214  771 ELAKKRTAAIAGGT 784
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1014-1064 3.58e-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: 48.28  E-value: 3.58e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24642494 1014 PCHDTCETCAGAGPDSCLTCapAHLHVIDLAVCLQFCPDGYFENSRNRTCV 1064
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSC--RHGFYLDGGTCVSECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
1010-1055 4.79e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 47.89  E-value: 4.79e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24642494    1010 GICWPCHDTCETCAGAGPDSCLTCAPAHLHviDLAVCLQFCPDGYF 1055
Cdd:smart00261    2 GECKPCHPECATCTGPGPDDCTSCKHGFFL--DGGKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
1398-1441 8.00e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 44.42  E-value: 8.00e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24642494    1398 TCKTCHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQT 1441
Cdd:smart00261    3 ECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPGT 44
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1402-1448 4.56e-04

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 39.42  E-value: 4.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 24642494 1402 CHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQTLAEKTSS 1448
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCVSECPEGTYADTEGG 46
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 413-496 7.88e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 44.19  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   413 VSILDDGIQTNHPDLAQNYDPEASF---------DINGN----------DSDPTPQDngDNKHGTRCAGEVAAVAFNNFC 473
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIDVNVKElhgrkgiddDNNGNvddeyganfvNNDGGPMD--DNYHGTHVSGIISAIGNNNIG 397

                          90       100
                  ....*....|....*....|....*..
gi 24642494   474 GVGVAYNASIGGVRMLD----GKVNDV 496
Cdd:PTZ00262  398 IVGVDKRSKLIICKALDshklGRLGDM 424
 
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 ...
 375-671 1.00e-169

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: 514.03  E-value: 1.00e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  375 FPDPLFKEQWYLNG----GAKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQD 450
Cdd:cd04059    1 PNDPLFPYQWYLKNtgqaGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  451 NGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGPGP 530
Cdd:cd04059   81 DDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGPGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  531 LARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGTPGH 610
Cdd:cd04059  161 LAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSGNP 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24642494  611 DKSVATVDMDGSlrpdHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 671
Cdd:cd04059  241 EASIVTTDLGGN----CNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 408-697 1.97e-57

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: 200.76  E-value: 1.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    408 GKGVVVSILDDGIQTNHPDLAQNY------DPEASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNA 481
Cdd:pfam00082    1 GKGVVVAVLDTGIDPNHPDLSGNLdndpsdDPEASVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    482 SIGGVRML-DGKVNDVVEAQALSLN-PSHIDIYSASWGPEddgSTVDGPGPLARRAFIYGvtsGRQGKGSIFVWASGNGG 559
Cdd:pfam00082   81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    560 RYTDSCNCDGY-TNSIFTLSISSATqagfkpwyleECSSTLATTYSSGTPGHDKS-----VA------------TVDMDG 621
Cdd:pfam00082  155 PGGNNGSSVGYpAQYKNVIAVGAVD----------EASEGNLASFSSYGPTLDGRlkpdiVApggnitggnissTLLTTT 224

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642494    622 SlRPDHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLEKENgwtlngvkrkysHKFGYG 697
Cdd:pfam00082  225 S-DPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD------------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 376-703 4.45e-37

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 146.78  E-value: 4.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  376 PDPLFKEQWYLNGGAKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDingnDSDPTPQDngDNK 455
Cdd:COG1404   76 LPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDFV----DGDGDPSD--DNG 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  456 HGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLD----GKVNDVVEA--QALSLNpshIDIYSASWgpeddGSTVDGPG 529
Cdd:COG1404  150 HGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDdngsGTTSDIAAAidWAADNG---ADVINLSL-----GGPADGYS 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  530 PLARRAFIYGVtsgrqGKGSIFVWASGNGGRYTDS----CNCDGytnsifTLSISSATQAGFKPWYleecSSTlattyss 605
Cdd:COG1404  222 DALAAAVDYAV-----DKGVLVVAAAGNSGSDDATvsypAAYPN------VIAVGAVDANGQLASF----SNY------- 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  606 GT------PGHDksVATVDMDGSlrpdhicTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLeken 679
Cdd:COG1404  280 GPkvdvaaPGVD--ILSTYPGGG-------YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGA---- 346

                        330       340
                 ....*....|....*....|....
gi 24642494  680 gwtlngvkrkYSHKFGYGLMDAGA 703
Cdd:COG1404  347 ----------PGPYYGYGLLADGA 360
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 758-846 4.26e-35

Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.


Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 128.93  E-value: 4.26e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    758 LEHVQCRITLRFFPRGNLRILLTSPMGTTSTLLFERPRDIVKSNFDDWPFLSVHFWGEKAEGRWTLQVINGGRrrvNQPG 837
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAP---GDTG 77


                   ....*....
gi 24642494    838 ILSKWQLIF 846
Cdd:pfam01483   78 TLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 242-318 7.53e-34

Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to family S8.


Pssm-ID: 465126  Cd Length: 77  Bit Score: 125.03  E-value: 7.53e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642494    242 EFAVNIPAGKQMADVIATKHGFINRGQIGSLDNYYLFQHHHVSKRSLRSSRKHQGALKSENEVKWMQQQHEKVRRKR 318
Cdd:pfam16470    1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 411-661 2.00e-32

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: 127.07  E-value: 2.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  411 VVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNgdnkHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLD 490
Cdd:cd07498    1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPTSDIDG----HGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRIAD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  491 --GKVNDVVEAQALSLNPSH-IDIYSASWGPEDDGSTVdgpgplaRRAFIYGVTSGRQGKGSIFVWASGNGGRYTDScnc 567
Cdd:cd07498   77 slGYAYWSDIAQAITWAADNgADVISNSWGGSDSTESI-------SSAIDNAATYGRNGKGGVVLFAAGNSGRSVSS--- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  568 dGYTNSIFTLSISSATQAGFKPWY--------LEECSSTLATTYSSGTPGHDksvatvDMDGSlrpdhicTVEHTGTSAS 639
Cdd:cd07498  147 -GYAANPSVIAVAATDSNDARASYsnygnyvdLVAPGVGIWTTGTGRGSAGD------YPGGG-------YGSFSGTSFA 212

                        250       260
                 ....*....|....*....|..
gi 24642494  640 APLAAGICALALEANPELTWRD 661
Cdd:cd07498  213 SPVAAGVAALILSANPNLTPAE 234
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 411-669 2.89e-32

Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.


Pssm-ID: 173787 [Multi-domain]  Cd Length: 241  Bit Score: 126.55  E-value: 2.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  411 VVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAfNNFCGVGVAYNASIGGVRMLD 490
Cdd:cd00306    1 VTVAVIDTGVDPDHPDLDGLFGGGDGGNDDDDNENGPTDPDDGNGHGTHVAGIIAASA-NNGGGVGVAPGAKLIPVKVLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  491 GKVN----DVVEAQALSLNPSHIDIYSASWgpeddGSTVDGPGPLARRAFIYGVTSgrqgKGSIFVWASGNGGRYTDScN 566
Cdd:cd00306   80 GDGSgsssDIAAAIDYAAADQGADVINLSL-----GGPGSPPSSALSEAIDYALAK----LGVLVVAAAGNDGPDGGT-N 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  567 CDGYTNSIFTLSISSATQAGfkpwyleecssTLATTYSSGTPGHDKSVATVDMDGSLRPDHICTVEHTGTSASAPLAAGI 646
Cdd:cd00306  150 IGYPAASPNVIAVGAVDRDG-----------TPASPSSNGGAGVDIAAPGGDILSSPTTGGGGYATLSGTSMAAPIVAGV 218

                        250       260
                 ....*....|....*....|...
gi 24642494  647 CALALEANPELTWRDMQYLVVYT 669
Cdd:cd00306  219 AALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 409-671 5.34e-26

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: 109.20  E-value: 5.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  409 KGVVVSILDDGIQTNHPDLAQN------YDPEASFDINGN------------DSDPTPQDngDNKHGTRCAGEVAAVAFN 470
Cdd:cd07473    2 GDVVVAVIDTGVDYNHPDLKDNmwvnpgEIPGNGIDDDGNgyvddiygwnfvNNDNDPMD--DNGHGTHVAGIIGAVGNN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  471 NFCGVGVAYNASIGGVRMLD----GKVNDVVEA--QALSLNpshIDIYSASWGPeddgstvDGPGPLARRAFIYGvtsgr 544
Cdd:cd07473   80 GIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAidYAVDMG---AKIINNSWGG-------GGPSQALRDAIARA----- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  545 QGKGSIFVWASGNGGRYTDS-----CNCDgYTNSIftlSISSATQAGFKPWYleecSSTLATTYSSGTPGHDkSVATVDM 619
Cdd:cd07473  145 IDAGILFVAAAGNDGTNNDKtptypASYD-LDNII---SVAATDSNDALASF----SNYGKKTVDLAAPGVD-ILSTSPG 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24642494  620 DGslrpdhicTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 671
Cdd:cd07473  216 GG--------YGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 407-658 7.44e-25

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: 105.87  E-value: 7.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  407 TGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNGDnkHGTRCAGeVAAVAFNNFCGVGVAYNASIGGV 486
Cdd:cd04848    1 TGAGVKVGVIDSGIDLSHPEFAGRVSEASYYVAVNDAGYASNGDGDS--HGTHVAG-VIAAARDGGGMHGVAPDATLYSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  487 RMLDGKVNDVVEAQALS----LNPSHIDIYSASWGPEDDGSTVDGPGPL---ARRAFIYGVTSGRQGKGSIFVWASGNGG 559
Cdd:cd04848   78 RASASAGSTFSDADIAAaydfLAASGVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVFAAGNDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  560 RYTDSCNCDGYT--------NSIFTLSI-SSATQAGFKpwYLEEC----SSTLAttyssgTPGHDKSVATVDMDGSLRPd 626
Cdd:cd04848  158 QANPSLAAAALPylepelegGWIAVVAVdPNGTIASYS--YSNRCgvaaNWCLA------APGENIYSTDPDGGNGYGR- 228

                        250       260       270
                 ....*....|....*....|....*....|..
gi 24642494  627 hictveHTGTSASAPLAAGICALALEANPELT 658
Cdd:cd04848  229 ------VSGTSFAAPHVSGAAALLAQKFPWLT 254
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 377-655 7.43e-23

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: 100.03  E-value: 7.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  377 DPLFKEQWYLNggakdglDMNVGPAWQKGyTGKGVVVSILDDGIQTNHPDLAQ-NYDPeaSFDINGNDSDPTPqdngDNK 455
Cdd:cd07484    4 DPYYSYQWNLD-------QIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLLKvKFVL--GYDFVDNDSDAMD----DNG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  456 HGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLD----GKVNDVVEAqalslnpshIdIYSAswgpeDDGSTV-----D 526
Cdd:cd07484   70 HGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANG---------I-RYAA-----DKGAKVinlslG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  527 GPGP--LARRAFIYGvtsgrQGKGSIFVWASGNGGRYTDScncdgYTNSIF-TLSISSATQAGFKPWyleecsstlattY 603
Cdd:cd07484  135 GGLGstALQEAINYA-----WNKGVVVVAAAGNEGVSSVS-----YPAAYPgAIAVAATDQDDKRAS------------F 192

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24642494  604 SSGTPGHDKSVATVDMDgSLRPDHICTVeHTGTSASAPLAAGICALALEANP 655
Cdd:cd07484  193 SNYGKWVDVSAPGGGIL-STTPDGDYAY-MSGTSMATPHVAGVAALLYSQGP 242
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 410-658 7.99e-22

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: 97.36  E-value: 7.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  410 GVVVSILDDGIQTNHPDLA----QNYD----PEASFDINGNDSDPTPQDNGDNK------------------HGTRCAGE 463
Cdd:cd07496    1 GVVVAVLDTGVLFHHPDLAgvllPGYDfisdPAIANDGDGRDSDPTDPGDWVTGddvppggfcgsgvspsswHGTHVAGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  464 VAAVAfNNFCGV-GVAYNASIGGVRML---DGKVNDVVEAqalslnpshidIYSASwgpeddGSTVDGPGPLARRAFIYG 539
Cdd:cd07496   81 IAAVT-NNGVGVaGVAWGARILPVRVLgkcGGTLSDIVDG-----------MRWAA------GLPVPGVPVNPNPAKVIN 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  540 VTSGRQG---------------KGSIFVWASGNGGRYTDS---CNCDGytnsifTLSISSATQAGFKPWYleecsSTLAT 601
Cdd:cd07496  143 LSLGGDGacsatmqnaindvraRGVLVVVAAGNEGSSASVdapANCRG------VIAVGATDLRGQRASY-----SNYGP 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642494  602 TYSSGTPGHDksvATVDMDGSLRPDHICT---------VEHTGTSASAPLAAGICALALEANPELT 658
Cdd:cd07496  212 AVDVSAPGGD---CASDVNGDGYPDSNTGttspggstyGFLQGTSMAAPHVAGVAALMKSVNPSLT 274
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 408-672 5.71e-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: 95.47  E-value: 5.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  408 GKGVVVSILDDGIQTNHPDLAQNYDPEASF----DINGNDSDP-----TPQDNGDNK------HGTRCAGEVAAVAFNNF 472
Cdd:cd07474    1 GKGVKVAVIDTGIDYTHPDLGGPGFPNDKVkggyDFVDDDYDPmdtrpYPSPLGDASagdatgHGTHVAGIIAGNGVNVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  473 CGVGVAYNASIGGVRMLD--GKVNDVVEAQAL--SLNPsHIDIYSASWGPEDDGStvDGPGPLA-RRAFIYGVtsgrqgk 547
Cdd:cd07474   81 TIKGVAPKADLYAYKVLGpgGSGTTDVIIAAIeqAVDD-GMDVINLSLGSSVNGP--DDPDAIAiNNAVKAGV------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  548 gsIFVWASGNGGrytDSCNCDGyTNSIFTLSISSATQAGFKPWYleecSSTLATTYSSGTPGHD--------------KS 613
Cdd:cd07474  151 --VVVAAAGNSG---PAPYTIG-SPATAPSAITVGASTVADVAE----ADTVGPSSSRGPPTSDsaikpdivapgvdiMS 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24642494  614 VATVDMDGSLRpdhictveHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRP 672
Cdd:cd07474  221 TAPGSGTGYAR--------MSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKP 271
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 400-655 1.62e-19

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: 90.62  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  400 PAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEA------SFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAfNNFC 473
Cdd:cd07485    1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGydpavnGYNFVPNVGDIDNDVSVGGGHGTHVAGTIAAVN-NNGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  474 GVG-------VAYNASIGGVRMLDGK--VNDVVEAQALSLNPSH-IDIYSASWGpeddGSTVDGPGPLARRAFIYGVTSG 543
Cdd:cd07485   80 GVGgiagaggVAPGVKIMSIQIFAGRyyVGDDAVAAAIVYAADNgAVILQNSWG----GTGGGIYSPLLKDAFDYFIENA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  544 RQG--KGSIFVWASGNggrytDSCNCDGYTNSIFTLSISSATQAGFKPWYLeecsSTLATTYSSGTPGHDKSVATV---D 618
Cdd:cd07485  156 GGSplDGGIVVFSAGN-----SYTDEHRFPAAYPGVIAVAALDTNDNKASF----SNYGRWVDIAAPGVGTILSTVpklD 226

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 24642494  619 MDGSLRPDHIctvehTGTSASAPLAAGICALALEANP 655
Cdd:cd07485  227 GDGGGNYEYL-----SGTSMAAPHVSGVAALVLSKFP 258
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 967-1070 2.61e-17

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


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 80.11  E-value: 2.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    967 CDAECDSSGCYGRGPTQCVACSHYRLDNTCVSRCP-----PRSFPNQvGICWPCHDTCE------TCAGAGPDSCLTCAp 1035
Cdd:pfam14843    2 CDPLCSSEGCWGPGPDQCLSCRNFSRGGTCVESCNilqgePREYVVN-STCVPCHPECLpqngtaTCSGPGADNCTKCA- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24642494   1036 ahlHVIDLAVCLQFCPDG--------YFENSRNRTCVPCEPNC 1070
Cdd:pfam14843   80 ---HFRDGPHCVSSCPSGvlgendliWKYADANGVCQPCHPNC 119
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 410-658 5.56e-17

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: 81.81  E-value: 5.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  410 GVVVSILDDGIQTNHPDLAQNYDPEASFdINGNDSDPTPqDNGdnkHGTRCAGEVAAVAfNNFCGVGVAYNASIGGVRML 489
Cdd:cd07477    1 GVKVAVIDTGIDSSHPDLKLNIVGGANF-TGDDNNDYQD-GNG---HGTHVAGIIAALD-NGVGVVGVAPEADLYAVKVL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  490 D----GKVNDVVEAQALSLNpSHIDIYSASWGPEDDGSTVdgpgplaRRAFIYGVtsgrqGKGSIFVWASGNGGRYTDSC 565
Cdd:cd07477   75 NddgsGTYSDIIAGIEWAIE-NGMDIINMSLGGPSDSPAL-------REAIKKAY-----AAGILVVAAAGNSGNGDSSY 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  566 NCDGYTNSifTLSISSATQAGfkpwyleecssTLATTYSSGT------PGHDkSVATVDMDGslrpdhicTVEHTGTSAS 639
Cdd:cd07477  142 DYPAKYPS--VIAVGAVDSNN-----------NRASFSSTGPevelaaPGVD-ILSTYPNND--------YAYLSGTSMA 199

                        250
                 ....*....|....*....
gi 24642494  640 APLAAGICALALEANPELT 658
Cdd:cd07477  200 TPHVAGVAALVWSKRPELT 218
VSP pfam03302
Giardia variant-specific surface protein;
1017-1376 7.54e-17

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 84.64  E-value: 7.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1017 DTCETCAGAGPDSCLTCAPAHlHVIDLAVCLQFCPD----GYFENSRNR-TCVPCEP-NCASCQDHpeyctscdhhlvmh 1090
Cdd:pfam03302   26 ENCKACSNDKREVCEECNSNN-YLTPTSQCIDDCAKignyYYTTNANNKkICKECTVaNCKTCEDQ-------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1091 ehKCYSACPLDTYETEDnKCAFCHSTCATCNGPTDQDCITCRSSryawqnKCLISCPDGfyadKKRLECMPCQEG----- 1165
Cdd:pfam03302   91 --GQCQACNDGFYKSGD-ACSPCHESCKTCSGGTASDCTECLTG------KALRYGNDG----TKGTCGEGCTTGtgaga 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1166 CKTC--TSNGV--CSECLQNWTLNKRDKCIVSGSEGCSESEFYSQVEGQCRPCHASCGSCNG--------PADTSCTSCP 1233
Cdd:pfam03302  158 CKTCglTIDGTsyCSECATETEYPQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGgcyettkfPGKSVCEEAN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1234 PNRLLEQSrcvsgcREGFFVEAGSLCSpCLHTCSQCVSRTNCsncskglelqngecrTTCADGYYSDRGICAKCYLSCHT 1313
Cdd:pfam03302  238 SGGTCQKE------APGYKLNNGDLVT-CSPGCKTCTSNTVC---------------TTCMDGYVKTSDSCTKCDSSCET 295

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642494   1314 CSGprrnQCVQCPAgwqlaagechpeCPEGFYKSDFGCQKCHHYCKTCNDAGPLACTSCPPHS 1376
Cdd:pfam03302  296 CTG----ATTTCKT------------CATGYYKSGTGCVSCTSSESDNGITGVKGCLNCAPPS 342
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 408-658 5.58e-16

Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173812 [Multi-domain]  Cd Length: 264  Bit Score: 79.94  E-value: 5.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  408 GKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNGdnkHGTRCAGEVAA-VAFNNFCGVGVAYNASIGGV 486
Cdd:cd07487    1 GKGITVAVLDTGIDAPHPDFDGRIIRFADFVNTVNGRTTPYDDNG---HGTHVAGIIAGsGRASNGKYKGVAPGANLVGV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  487 RMLD----GKVNDVVEA------QALSLNpshIDIYSASWGPEDDGStvDGPGPL---ARRAFIYGVTsgrqgkgsiFVW 553
Cdd:cd07487   78 KVLDdsgsGSESDIIAGidwvveNNEKYN---IRVVNLSLGAPPDPS--YGEDPLcqaVERLWDAGIV---------VVV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  554 ASGNGGRYTDSCNCDGytNSIFTLSISSATQAGFKPWYLEECSStlattySSGTP-GHDK-----------SVATVDMDG 621
Cdd:cd07487  144 AAGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSS------RGPTGdGRIKpdvvapgenivSCRSPGGNP 215

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 24642494  622 SLRPDHIcTVEHTGTSASAPLAAGICALALEANPELT 658
Cdd:cd07487  216 GAGVGSG-YFEMSGTSMATPHVSGAIALLLQANPILT 251
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 404-674 4.17e-14

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


Pssm-ID: 173814 [Multi-domain]  Cd Length: 312  Bit Score: 75.33  E-value: 4.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  404 KGYTGKGVVVSILDDGIQTNHPDLAQNYDP----EASFDINGNDSDP--TPQDNGD----NKHGTRCAGEVAAVAfNNFC 473
Cdd:cd07489    8 EGITGKGVKVAVVDTGIDYTHPALGGCFGPgckvAGGYDFVGDDYDGtnPPVPDDDpmdcQGHGTHVAGIIAANP-NAYG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  474 GVGVAYNASIGGVRMLD--GKVNDVVEAQALSLNPSH-IDIYSASWG-----PEDDGSTVdgPGPLARRAFIYGVTSGRQ 545
Cdd:cd07489   87 FTGVAPEATLGAYRVFGcsGSTTEDTIIAAFLRAYEDgADVITASLGgpsgwSEDPWAVV--ASRIVDAGVVVTIAAGND 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  546 GKGSIFVWASGNGGRYTDSCncdGYTNSIFTlSISSATQAGFKPwyleecsSTLATTYS--SGTPGHDKSVATVdmdgsl 623
Cdd:cd07489  165 GERGPFYASSPASGRGVIAV---ASVDSYFS-SWGPTNELYLKP-------DVAAPGGNilSTYPLAGGGYAVL------ 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24642494  624 rpdhictvehTGTSASAPLAAGICALALEA-NPELTWRDMQYLVVYTSRPAP 674
Cdd:cd07489  228 ----------SGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKPLP 269
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 410-658 7.20e-14

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: 73.35  E-value: 7.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  410 GVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNgdNKHGTRCAGEVaAVAFNNFCGVGVAynasiGGVRML 489
Cdd:cd07490    1 GVTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEVFDA--GGHGTHVSGTI-GGGGAKGVYIGVA-----PEADLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  490 DGKVNDVVEAQALSLnpshidIYSASWGPEDD--------GSTVDGPGPLARRafiygVTSGRQGKGSIFVWASGNGGRY 561
Cdd:cd07490   73 HGKVLDDGGGSLSQI------IAGMEWAVEKDadvvsmslGGTYYSEDPLEEA-----VEALSNQTGALFVVSAGNEGHG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  562 TDSCNCDGYTnsifTLSISSATQAGFKPWYLEECSSTLATTYSSGTPGHDKSVATVDMDG----SLRPDHICTVEHT--- 634
Cdd:cd07490  142 TSGSPGSAYA----ALSVGAVDRDDEDAWFSSFGSSGASLVSAPDSPPDEYTKPDVAAPGvdvySARQGANGDGQYTrls 217

                        250       260
                 ....*....|....*....|....
gi 24642494  635 GTSASAPLAAGICALALEANPELT 658
Cdd:cd07490  218 GTSMAAPHVAGVAALLAAAHPDLS 241
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 435-848 1.48e-13

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: 75.63  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  435 ASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSA 514
Cdd:COG4935  248 GAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAA 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  515 SWGPEDDGSTVDGPGPLARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEE 594
Cdd:COG4935  328 AGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGGVASAAGA 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  595 CSSTLATTYSSGTPGHDKSVATVDMDGSLRPDHicTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAP 674
Cdd:COG4935  408 VGAGTAAGASATAAVSTGAASGSSTTSSTGTTA--TATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTTAAAAA 485

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  675 lekenGWTLNGVKRKYSHKFGYGLMDAGAMVSLAEQWTSVPPQHICKSRENNEDRKIDGAYGSTLSTHMDVNGcAGTINE 754
Cdd:COG4935  486 -----AAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVAIPDNGPAGVTSTITVSG-GGAVED 559

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  755 VRylehVQCRITLRFfpRGNLRILLTSPMGTTSTLLfeRPRDIVKSNFDdWPFLSVHFWGEKAEGRWTLQVINGGRRRVn 834
Cdd:COG4935  560 VT----VTVDITHTY--RGDLVITLISPDGTTVVLK--NRSGGSADNIN-ATFDVANFSGESANGTWTLRVVDTAGGDT- 629

                        410
                 ....*....|....
gi 24642494  835 qpGILSKWQLIFYG 848
Cdd:COG4935  630 --GTLNSWSLTFTG 641
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 396-671 4.80e-13

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: 71.74  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  396 MNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYdpEASFDINGNDSDPTPQDNGdnkHGTrcaGEVAAVafnnfcgV 475
Cdd:cd07494    8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGY--QVRVVLAPGATDPACDENG---HGT---GESANL-------F 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  476 GVAYNASIGGVRMLDGKVNDVVEA--QALSLNPshiDIYSASWG-----PEDDGSTVDGPGPLARRAFIYGVTSgrqgKG 548
Cdd:cd07494   73 AIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSP---DIISNSWGydlrsPGTSWSRSLPNALKALAATLQDAVA----RG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  549 SIFVWASGNGGrytdscncdgytnSIFTLSISSATQAGfkPWYLEECSSTLATTYSSG---------------------- 606
Cdd:cd07494  146 IVVVFSAGNGG-------------WSFPAQHPEVIAAG--GVFVDEDGARRASSYASGfrskiypgrqvpdvcglvgmlp 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642494  607 ---------TPGH--DKSVATVDmDGSLRPDHICTVehTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 671
Cdd:cd07494  211 haaylmlpvPPGSqlDRSCAAFP-DGTPPNDGWGVF--SGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTAR 283
Furin-like pfam00757
Furin-like cysteine rich region;
949-1070 4.69e-12

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 65.15  E-value: 4.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    949 QLVAAPETRDGDKKILHSCDAECdSSGCYGRGPTQCVACSHYRLDNTCVSRCPPRSFpnQVGicWPCHdTCETCAGAGPD 1028
Cdd:pfam00757   31 QKVCPEQCKKRCTKPGECCHEQC-LGGCTGPNDSDCLACRHFNDEGTCVDQCPPGTY--QFG--WRCV-TFKECPKSHLP 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24642494   1029 SCltcapaHLHVIDLAVCLQFCPDGYFEN-SRNRTCVPCEPNC 1070
Cdd:pfam00757  105 GY------NPLVIHNGECVRECPSGYTEVeNNSRKCEPCEGLC 141
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 406-658 7.74e-12

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: 67.54  E-value: 7.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  406 YTGKGVVVSILDDGIQTNHPDLAQNydpeASFDINGNDSDPTPQDNGdnkHGTRCAGEVAAVAFnnfcgvGVAYNASIGG 485
Cdd:cd04077   22 STGSGVDVYVLDTGIRTTHVEFGGR----AIWGADFVGGDPDSDCNG---HGTHVAGTVGGKTY------GVAKKANLVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  486 VRMLDGK-----------VNDVVEAQALSLNPSHIdiySASWGpEDDGSTVDGpgpLARRAFIYGVTsgrqgkgsiFVWA 554
Cdd:cd04077   89 VKVLDCNgsgtlsgiiagLEWVANDATKRGKPAVA---NMSLG-GGASTALDA---AVAAAVNAGVV---------VVVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  555 SGNGGryTDSCNcdgYTNSiftlSISSATQAGfkpwyleecSSTLATTYSSGT----------PGHDKSVATVDMDGslr 624
Cdd:cd04077  153 AGNSN--QDACN---YSPA----SAPEAITVG---------ATDSDDARASFSnygscvdifaPGVDILSAWIGSDT--- 211

                        250       260       270
                 ....*....|....*....|....*....|....
gi 24642494  625 pdhiCTVEHTGTSASAPLAAGICALALEANPELT 658
Cdd:cd04077  212 ----ATATLSGTSMAAPHVAGLAAYLLSLGPDLS 241
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 403-653 1.57e-11

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: 66.97  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  403 QKGYTGKGVVVSILDDGIQTNHPDLaqnYDPEASFDINGN----DSDPTPQDNGD-NKHGTRCAGEVAAVAFNNFCGV-- 475
Cdd:cd04842    1 GLGLTGKGQIVGVADTGLDTNHCFF---YDPNFNKTNLFHrkivRYDSLSDTKDDvDGHGTHVAGIIAGKGNDSSSISly 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  476 -GVAYNASIGGVRMLDGKVN-------DVVEAQALSLNpshIDIYSASWGPEDDGSTVDgpgpLARR--AFIYgvtsgrQ 545
Cdd:cd04842   78 kGVAPKAKLYFQDIGDTSGNlssppdlNKLFSPMYDAG---ARISSNSWGSPVNNGYTL----LARAydQFAY------N 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  546 GKGSIFVWASGNGGrytdscncDGYTNSIFT-------LSISSATQA----GFKPWYLEECSSTLAtTYSSGTPGHD--- 611
Cdd:cd04842  145 NPDILFVFSAGNDG--------NDGSNTIGSpataknvLTVGASNNPsvsnGEGGLGQSDNSDTVA-SFSSRGPTYDgri 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24642494  612 -----------KSVATVDMDGSLRPDHIcTVEHTGTSASAPLAAGICALALEA 653
Cdd:cd04842  216 kpdlvapgtgiLSARSGGGGIGDTSDSA-YTSKSGTSMATPLVAGAAALLRQY 267
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1113-1160 4.61e-11

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: 59.45  E-value: 4.61e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 24642494 1113 CHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFYADKKRLECM 1160
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 408-657 1.29e-10

Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F, encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity.


Pssm-ID: 173807 [Multi-domain]  Cd Length: 264  Bit Score: 63.93  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  408 GKGVVVSILDDGIQTNHPDLAQNYDPE--ASFDINGNDSDP---TPQDNGDNKHGTRCAGevAAVAFN-NFCGVGVAYNA 481
Cdd:cd07481    1 GTGIVVANIDTGVDWTHPALKNKYRGWggGSADHDYNWFDPvgnTPLPYDDNGHGTHTMG--TMVGNDgDGQQIGVAPGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  482 SIGGVRMLD---GKVNDVVEAQALSLNPSHI-----------DIYSASWGPEDDGSTVDGPGPLARRAfiygvtsgrqgK 547
Cdd:cd07481   79 RWIACRALDrngGNDADYLRCAQWMLAPTDSagnpadpdlapDVINNSWGGPSGDNEWLQPAVAAWRA-----------A 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  548 GSIFVWASGNGGRYTDSCNCD--GYTNSIFTLSISSATQ-AGFkpwyleecSSTLATTYSS-----GTPGHD-KSVATVD 618
Cdd:cd07481  148 GIFPVFAAGNDGPRCSTLNAPpaNYPESFAVGATDRNDVlADF--------SSRGPSTYGRikpdiSAPGVNiRSAVPGG 219

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 24642494  619 MDGSLrpdhictvehTGTSASAPLAAGICALALEANPEL 657
Cdd:cd07481  220 GYGSS----------SGTSMAAPHVAGVAALLWSANPSL 248
FU smart00261
Furin-like repeats;
1107-1151 1.72e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.52  E-value: 1.72e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642494    1107 DNKCAFCHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFY 1151
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
1208-1252 2.07e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.52  E-value: 2.07e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642494    1208 EGQCRPCHASCGSCNGPADTSCTSCPPNRLLEQSRCVSGCREGFF 1252
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 1162-1479 5.14e-10

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 64.55  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1162 CQEGCKTCTsNGVCSEclqnwtlnkrdkcIVSGSEGCSES-------EFYSQvEGQCRPCHASCGSCNGPADTSCTSCPP 1234
Cdd:PTZ00214  391 CSESCSGDT-RGVCTK-------------VAEGSESTEVScrcvckpTFYNS-SGTCTPCTDSCAVCKDGTPTGCQQCSP 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1235 NRLLEQS-------RCVSGCRE-------GFFVEAGSLCSPCLHTC---------------SQCVSRTN--CSNCSKGLE 1283
Cdd:PTZ00214  456 GKILEFSivssesaDCVDQCSVgsecaecGITIDGSRYCTRCKDAStypfngvcipntqrdAYCTSTANgaCTTCSGAAF 535

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1284 LQNGECRT-------------------TCADGYY-SDRGICAKCYLSCHTCSGPRRNQCVQCPAGWQL------AAGEC- 1336
Cdd:PTZ00214  536 LMNGGCYTtehypgsticdkqsngkctTTKKGYGiSPDGKLLECDPTCLACTAPGPGRCTRCPSDKLLkrasgaATGSCv 615

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1337 -HPECPEGFYKSDFGCQKCHHY-CKTCNDAGplACTSCPPHSM--LDGGLCM-ECLSSQYYDTTSATCKTCHdsCRSCFG 1411
Cdd:PTZ00214  616 dPGACVDGYYADGDACLPCATPgCKTCGHAS--FCTECAGELFvsLDGQSCLeECTGDKVVGEVSGGVRRCW--CERGFL 691

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1412 PGqFSCKGCVPPLHLDQLNSQCVSC----------------------CQNQTLAEKTSSAACCNCDGET----GECKATS 1465
Cdd:PTZ00214  692 PA-LDRSGCVLPTECPPDMPSCAACdesgrcllcvtsghnvqvdqrtCAEGCGARASSNQGVCMCELDAvltkGVCVPAK 770

                         410
                  ....*....|....
gi 24642494  1466 TGGKRRTVVGSGSA 1479
Cdd:PTZ00214  771 ELAKKRTAAIAGGT 784
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 406-661 2.37e-09

Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173806 [Multi-domain]  Cd Length: 297  Bit Score: 60.47  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  406 YTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDptpqdngDNKHGTRCAGEVAAvAFNNFCGVGVAYNASIgg 485
Cdd:cd07480    5 FTGAGVRVAVLDTGIDLTHPAFAGRDITTKSFVGGEDVQD-------GHGHGTHCAGTIFG-RDVPGPRYGVARGAEI-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  486 vrMLDGKVND--------VVEAQALSLNpSHIDIYSASWGPEDDGSTVDG--PGPLARRA----------FIYGVT---- 541
Cdd:cd07480   75 --ALIGKVLGdggggdggILAGIQWAVA-NGADVISMSLGADFPGLVDQGwpPGLAFSRAleayrqrarlFDALMTlvaa 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  542 SGRQGKGSIFVWASGNggrytDScNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGT------PGHDksVA 615
Cdd:cd07480  152 QAALARGTLIVAAAGN-----ES-QRPAGIPPVGNPAACPSAMGVAAVGALGRTGNFSAVANFSNGevdiaaPGVD--IV 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 24642494  616 TVDMDGSLRPdhictveHTGTSASAPLAAGICALALEANPELTWRD 661
Cdd:cd07480  224 SAAPGGGYRS-------MSGTSMATPHVAGVAALWAEALPKAGGRA 262
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 411-658 2.38e-09

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: 60.46  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  411 VVVSILDDGIQTNHPDLA-------QNYDPEASFDINGNDSDPTPQDNGD-NKHGTRCAGEVAAVAFNNfcgvGVAYNAS 482
Cdd:cd07482    2 VTVAVIDSGIDPDHPDLKnsissysKNLVPKGGYDGKEAGETGDINDIVDkLGHGTAVAGQIAANGNIK----GVAPGIG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  483 IGGVRMLD----GKVNDVVEAQALSLNpSHIDIYSASWGP---EDDGSTVDGPGPLA-RRAFIYGvtsgrQGKGSIFVWA 554
Cdd:cd07482   78 IVSYRVFGscgsAESSWIIKAIIDAAD-DGVDVINLSLGGyliIGGEYEDDDVEYNAyKKAINYA-----KSKGSIVVAA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  555 SGNGGRytDSCNCDGYTNsiFTLSISSATQAG---FKPWYLEE---CSST-----LATTYSSG-------TPGHD----K 612
Cdd:cd07482  152 AGNDGL--DVSNKQELLD--FLSSGDDFSVNGevyDVPASLPNvitVSATdnngnLSSFSNYGnsridlaAPGGDflllD 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24642494  613 SVATVDM--DGSLRPDHICTVE-------HTGTSASAPLAAGICALALEANPELT 658
Cdd:cd07482  228 QYGKEKWvnNGLMTKEQILTTApeggyayMYGTSLAAPKVSGALALIIDKNPLKK 282
FU smart00261
Furin-like repeats;
1301-1345 2.91e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 54.05  E-value: 2.91e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642494    1301 RGICAKCYLSCHTCSGPRRNQCVQCPAGWQLAAGECHPECPEGFY 1345
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
VSP pfam03302
Giardia variant-specific surface protein;
1218-1467 2.98e-09

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 61.14  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1218 CGSCNGPADTSCTSC-PPNRLLEQSRCVSGCREGFFVEAGSlCSPCLHTCSQCvSRTNCSNCSKGLELQngecrtTCADG 1296
Cdd:pfam03302   28 CKACSNDKREVCEECnSNNYLTPTSQCIDDCAKIGNYYYTT-NANNKKICKEC-TVANCKTCEDQGQCQ------ACNDG 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1297 YYSDRGICAKCYLSCHTCSGPRRNQCVQCPAGWQL------AAGECHPECPEGfyKSDFGCQKC------HHYCKTCNDA 1364
Cdd:pfam03302  100 FYKSGDACSPCHESCKTCSGGTASDCTECLTGKALrygndgTKGTCGEGCTTG--TGAGACKTCgltidgTSYCSECATE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1365 GPL----ACTS--------CPPHSMLDgGLCMECLSSQY------YDTTSATCKTCHDScrscfGPGQFSCKGCVPPLHL 1426
Cdd:pfam03302  178 TEYpqngVCTStaaratatCKASSVAN-GMCSSCANGYFrmnggcYETTKFPGKSVCEE-----ANSGGTCQKEAPGYKL 251

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24642494   1427 DQ--------------LNSQCVSCCQNQTLAEKTSS---AACCNCDGETGECKATSTG 1467
Cdd:pfam03302  252 NNgdlvtcspgcktctSNTVCTTCMDGYVKTSDSCTkcdSSCETCTGATTTCKTCATG 309
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 400-703 3.00e-09

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


Pssm-ID: 173801 [Multi-domain]  Cd Length: 346  Bit Score: 60.74  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  400 PAWQKG-YTGKGVVVSILDDGIQTNHPDLAQNYDPEA---------------------------SFDINGNDSDPTPQDN 451
Cdd:cd07475    1 PLWDKGgYKGEGMVVAVIDSGVDPTHDAFRLDDDSKAkyseefeakkkkagigygkyynekvpfAYNYADNNDDILDEDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  452 GDNkHGTRCAGEVAAVAFNNFCG---VGVAYNASIGGVRMLDGKV------NDVVEA--QALSLNPshiDIYSASWGped 520
Cdd:cd07475   81 GSS-HGMHVAGIVAGNGDEEDNGegiKGVAPEAQLLAMKVFSNPEggstydDAYAKAieDAVKLGA---DVINMSLG--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  521 DGSTVDGPGPLARRAFIYGVTsgrqgKGSIFVWASGNggrytdscncDGYTNSIFTLSISSATQagfkpwyleecsstla 600
Cdd:cd07475  154 STAGFVDLDDPEQQAIKRARE-----AGVVVVVAAGN----------DGNSGSGTSKPLATNNP---------------- 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  601 TTYSSGTPGHDKSVATV-------------DM----------DGSLRPD------HI-CTVEH------TGTSASAPLAA 644
Cdd:cd07475  203 DTGTVGSPATADDVLTVasankkvpnpnggQMsgfsswgptpDLDLKPDitapggNIySTVNDntygymSGTSMASPHVA 282

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642494  645 GICALALEA----NPELTWRDMQYLVVY----TSRPAPLEKENGwTLNGVKRKyshkfGYGLMDAGA 703
Cdd:cd07475  283 GASALVKQRlkekYPKLSGEELVDLVKNllmnTATPPLDSEDTK-TYYSPRRQ-----GAGLIDVAK 343
Furin-like pfam00757
Furin-like cysteine rich region;
963-1123 6.31e-09

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 56.29  E-value: 6.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    963 ILHSCDAECDSSGCYGRGPTQCVacshyrldntCVSRCPPRSFPNqvGICwpCHDTC-ETCAGAGPDSCLTCapahLHVI 1041
Cdd:pfam00757   11 TMEKCHSCCNNGYCWGPGHCQKV----------CPEQCKKRCTKP--GEC--CHEQClGGCTGPNDSDCLAC----RHFN 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1042 DLAVCLQFCPDGYFENSRnrTCVPCEpncaSCqdhPEYCTSCDHHLVMHEHKCYSACPLDTYETEDNKcafchSTCATCN 1121
Cdd:pfam00757   73 DEGTCVDQCPPGTYQFGW--RCVTFK----EC---PKSHLPGYNPLVIHNGECVRECPSGYTEVENNS-----RKCEPCE 138


                   ..
gi 24642494   1122 GP 1123
Cdd:pfam00757  139 GL 140
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 966-1031 8.35e-09

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: 55.46  E-value: 8.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494    966 SCDAEC----DSSGCYGRGPTQCVACSHYRLDNTCVSRCP---------PRSFPNQVGICWPCHDTC-ETCAGAGPDSCL 1031
Cdd:pfam14843   53 PCHPEClpqnGTATCSGPGADNCTKCAHFRDGPHCVSSCPsgvlgendlIWKYADANGVCQPCHPNCtQGCTGPGLTGCP 132
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1306-1350 9.08e-09

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 52.91  E-value: 9.08e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 24642494 1306 KCYLSCHTCSGPRRNQCVQCPAGWQLAAGECHPECPEGFYKSDFG 1350
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEG 45
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 968-1254 1.87e-08

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 59.54  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   968 DAECDSSGCYG--RGPTQCVACSHYRLDNTCVSRCPPrSFPNQVGICWPCHDTCETCAGAGPDSCLTCAPAhlHVIDLAV 1045
Cdd:PTZ00214  387 DGKSCSESCSGdtRGVCTKVAEGSESTEVSCRCVCKP-TFYNSSGTCTPCTDSCAVCKDGTPTGCQQCSPG--KILEFSI 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1046 CLQFCPDGYFENSRNRTCVPC------EPNCASCQDHPEY-----------------------CTSCDHHLVMHEHKCYS 1096
Cdd:PTZ00214  464 VSSESADCVDQCSVGSECAECgitidgSRYCTRCKDASTYpfngvcipntqrdayctstangaCTTCSGAAFLMNGGCYT 543

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1097 AC--PLDT-----------------YETEDNKCAFCHSTCATCNGPTDQDCITCRSSRY------AWQNKCLI--SCPDG 1149
Cdd:PTZ00214  544 TEhyPGSTicdkqsngkctttkkgyGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKLlkrasgAATGSCVDpgACVDG 623

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1150 FYADKKrlECMPCQE-GCKTCTSNGVCSECLQNWTLNKRDKcivSGSEGCSESEFYSQVEGQCRPCHASCGSCNGPADTS 1228
Cdd:PTZ00214  624 YYADGD--ACLPCATpGCKTCGHASFCTECAGELFVSLDGQ---SCLEECTGDKVVGEVSGGVRRCWCERGFLPALDRSG 698

                         330       340       350
                  ....*....|....*....|....*....|....
gi 24642494  1229 C---TSCPPNRLL-----EQSRCVSGCREGFFVE 1254
Cdd:PTZ00214  699 CvlpTECPPDMPScaacdESGRCLLCVTSGHNVQ 732
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1213-1257 2.49e-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: 51.75  E-value: 2.49e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 24642494 1213 PCHASCGSCNGPADTSCTSCPPNRLLEQSRCVSGCREGFFVEAGS 1257
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEG 45
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 410-658 2.72e-08

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: 56.19  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  410 GVVVSILDDGIQTNHPDLAQN-YDPEASfdINGNDSDPTPQDNGDNKHGTRCAGEVAAvafnnfcgvgVAYNASIGGVRM 488
Cdd:cd07492    1 GVRVAVIDSGVDTDHPDLGNLaLDGEVT--IDLEIIVVSAEGGDKDGHGTACAGIIKK----------YAPEAEIGSIKI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  489 L--DGKVNDVVEAQALS-LNPSHIDIYSASWgpeddGSTVDGPGPLARRAFIYGVTSGRqgkgsIFVWASGNGGRYtdsc 565
Cdd:cd07492   69 LgeDGRCNSFVLEKALRaCVENDIRIVNLSL-----GGPGDRDFPLLKELLEYAYKAGG-----IIVAAAPNNNDI---- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  566 ncdGYTNSIFTLSIssatqaGFKpwyleecSSTLATTYSSGTPGHDKSVATVDMDGSLRpdHICTVEHTGTSASAPLAAG 645
Cdd:cd07492  135 ---GTPPASFPNVI------GVK-------SDTADDPKSFWYIYVEFSADGVDIIAPAP--HGRYLTVSGNSFAAPHVTG 196

                        250
                 ....*....|...
gi 24642494  646 ICALALEANPELT 658
Cdd:cd07492  197 MVALLLSEKPDID 209
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 405-705 3.03e-08

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


Pssm-ID: 173798 [Multi-domain]  Cd Length: 275  Bit Score: 56.92  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  405 GYTGKGVVVSILDDGIQTnhpdLAQNYDPEASFDI--NGNDSDPTPQDNGDNKHGTRCAGEV------AAVAFNNFCGVG 476
Cdd:cd05562    1 GVDGTGIKIGVISDGFDG----LGDAADDQASGDLpgNVNVLGDLDGGSGGGDEGRAMLEIIhdiapgAELAFHTAGGGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  477 VAYNASIG-----GVRMLdgkVNDV-----------VEAQALSLNPSHIDI-YSASWGPEDDGSTVDGPGplarrafiyg 539
Cdd:cd05562   77 LDFAAAIRalaaaGADII---VDDIgylnepffqdgPIAQAVDEVVASPGVlYFSSAGNDGQSGSIFGHA---------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  540 vtsgrQGKGSIFVWASGNGGRYTDSCNCD--GYTNSIFTLSISSATQAGfkpwyleecssTLATTYSsgtpGHDKSVATV 617
Cdd:cd05562  144 -----AAPGAIAVGAVDYGNTPAFGSDPApgGTPSSFDPVGIRLPTPEV-----------RQKPDVT----APDGVNGTV 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  618 DMDGSLRPDHictvehTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPlekENGWTlngvkrkysHKFGYG 697
Cdd:cd05562  204 DGDGDGPPNF------FGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMG---EPGYD---------NASGSG 265


                 ....*...
gi 24642494  698 LMDAGAMV 705
Cdd:cd05562  266 LVDADRAV 273
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1353-1400 3.47e-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: 51.37  E-value: 3.47e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 24642494 1353 KCHHYCKTCNDAGPLACTSCPPHSMLDGGLCM-ECLSSQYYDTTSATCK 1400
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVsECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
1351-1392 4.13e-08

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 50.97  E-value: 4.13e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 24642494    1351 CQKCHHYCKTCNDAGPLACTSCPPHSMLDGGLCMECLSSQYY 1392
Cdd:smart00261    4 CKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 396-565 2.68e-07

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: 53.86  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  396 MNVGPAWQK-GYTGKGVVVSILDDGIQTNHPDLAQNydpeaSFDINgndSDPTPQDNGDnkHGTRCAGEVAAVAfNNFCG 474
Cdd:cd04843    2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGN-----GITLI---SGLTDQADSD--HGTAVLGIIVAKD-NGIGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  475 VGVAYNASIG--GVRMLDGKVNDVVEAqALSLNPSHIDIYSASWGPEDDGSTvdgPGPLARRAFIYGVTSGRQGKGSIFV 552
Cdd:cd04843   71 TGIAHGAQAAvvSSTRVSNTADAILDA-ADYLSPGDVILLEMQTGGPNNGYP---PLPVEYEQANFDAIRTATDLGIIVV 146

                        170
                 ....*....|...
gi 24642494  553 WASGNGGRYTDSC 565
Cdd:cd04843  147 EAAGNGGQDLDAP 159
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1014-1064 3.58e-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: 48.28  E-value: 3.58e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24642494 1014 PCHDTCETCAGAGPDSCLTCapAHLHVIDLAVCLQFCPDGYFENSRNRTCV 1064
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSC--RHGFYLDGGTCVSECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
1010-1055 4.79e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 47.89  E-value: 4.79e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24642494    1010 GICWPCHDTCETCAGAGPDSCLTCAPAHLHviDLAVCLQFCPDGYF 1055
Cdd:smart00261    2 GECKPCHPECATCTGPGPDDCTSCKHGFFL--DGGKCVSECPPGTY 45
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 1266-1344 1.33e-06

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: 48.20  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1266 CSQCVSRTNCSNCSKGLEL--------QNGECRTTCADGYYSDRGI----CAKC-YLSCHTCSGprRNQCVQCPAGWQLA 1332
Cdd:pfam15913    4 CVLCSEENGCLTCQPRLFLllerngirQYGVCLHSCPPGYFGIRGQevnrCTKCkAENCESCFS--KDFCTKCKEGFYLH 81

                           90
                   ....*....|..
gi 24642494   1333 AGECHPECPEGF 1344
Cdd:pfam15913   82 KGKCLDTCPEGT 93
FU smart00261
Furin-like repeats;
1060-1103 1.48e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 46.35  E-value: 1.48e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642494    1060 NRTCVPCEPNCASCQDH-PEYCTSCDHHLVMHEHKCYSACPLDTY 1103
Cdd:smart00261    1 DGECKPCHPECATCTGPgPDDCTSCKHGFFLDGGKCVSECPPGTY 45
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 1019-1102 2.74e-06

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: 47.43  E-value: 2.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1019 CETCAGAgpDSCLTCAPAHLHVI------DLAVCLQFCPDGYF--ENSRNRTCVPCE-PNCASCQDHpEYCTSCDHHLVM 1089
Cdd:pfam15913    4 CVLCSEE--NGCLTCQPRLFLLLerngirQYGVCLHSCPPGYFgiRGQEVNRCTKCKaENCESCFSK-DFCTKCKEGFYL 80

                           90
                   ....*....|...
gi 24642494   1090 HEHKCYSACPLDT 1102
Cdd:pfam15913   81 HKGKCLDTCPEGT 93
FU smart00261
Furin-like repeats;
1398-1441 8.00e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 44.42  E-value: 8.00e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24642494    1398 TCKTCHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQT 1441
Cdd:smart00261    3 ECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPGT 44
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 408-653 9.09e-06

Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173821 [Multi-domain]  Cd Length: 311  Bit Score: 49.78  E-value: 9.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  408 GKGVVVSILDDGIQTNHPDLAQ--NYDPEASFDINGN---DSDPTPQ----DNGDNKHGTRCAGEVAAVAFNNFCG---- 474
Cdd:cd07497    1 GEGVVIAIVDTGVDYSHPDLDIygNFSWKLKFDYKAYllpGMDKWGGfyviMYDFFSHGTSCASVAAGRGKMEYNLygyt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  475 -----VGVAYNASIGGVRML------------DGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGPGPLARRAFI 537
Cdd:cd07497   81 gkfliRGIAPDAKIAAVKALwfgdviyawlwtAGFDPVDRKLSWIYTGGPRVDVISNSWGISNFAYTGYAPGLDISSLVI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  538 YGVTSgrqGKGSIFVWASGNGGRYTDSCNCDGytNSIFTLSISSATQAGFKPWYLeecssTLATT--------YSSGTPG 609
Cdd:cd07497  161 DALVT---YTGVPIVSAAGNGGPGYGTITAPG--AASLAISVGAATNFDYRPFYL-----FGYLPggsgdvvsWSSRGPS 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24642494  610 HdKSVATVDM--------------------DGSLRPDHIctvehTGTSASAPLAAGICALALEA 653
Cdd:cd07497  231 I-AGDPKPDLaaigafawapgrvldsggalDGNEAFDLF-----GGTSMATPMTAGSAALVISA 288
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 1070-1159 1.58e-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: 45.50  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1070 CASCQDHpEYCTSCDHHL--------VMHEHKCYSACPLDTY---ETEDNKCAFCHS-TCATCngpTDQD-CITCRSSRY 1136
Cdd:pfam15913    4 CVLCSEE-NGCLTCQPRLflllerngIRQYGVCLHSCPPGYFgirGQEVNRCTKCKAeNCESC---FSKDfCTKCKEGFY 79

                           90       100
                   ....*....|....*....|...
gi 24642494   1137 AWQNKCLISCPDGFYADKKRLEC 1159
Cdd:pfam15913   80 LHKGKCLDTCPEGTAAQNSTMEC 102
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 1065-1229 1.59e-05

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: 46.21  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1065 PCEPNCASCQ---DHPEYCTSCDHHLVMHEhkCYSACPLDTYE----TEDNKCAFCHSTC------ATCNGPTDQDCITC 1131
Cdd:pfam14843    1 VCDPLCSSEGcwgPGPDQCLSCRNFSRGGT--CVESCNILQGEpreyVVNSTCVPCHPEClpqngtATCSGPGADNCTKC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1132 RSsrYAWQNKCLISCPDGFYADKkrlecmpcqegcktctsngvcseclqnwtlnkrdkcivsgsegcSESEFYSQVEGQC 1211
Cdd:pfam14843   79 AH--FRDGPHCVSSCPSGVLGEN--------------------------------------------DLIWKYADANGVC 112

                          170
                   ....*....|....*....
gi 24642494   1212 RPCHASC-GSCNGPADTSC 1229
Cdd:pfam14843  113 QPCHPNCtQGCTGPGLTGC 131
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 967-1010 1.68e-05

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 43.66  E-value: 1.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 24642494  967 CDAECDssGCYGRGPTQCVACSHYRL--DNTCVSRCPPRSFPNQVG 1010
Cdd:cd00064    2 CHPSCA--TCTGPGPDQCTSCRHGFYldGGTCVSECPEGTYADTEG 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1065-1109 1.96e-05

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 43.28  E-value: 1.96e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 24642494 1065 PCEPNCASCQDH-PEYCTSCDHHLVMHEHKCYSACPLDTYETEDNK 1109
Cdd:cd00064    1 PCHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGG 46
FU smart00261
Furin-like repeats;
965-1005 5.88e-05

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 42.11  E-value: 5.88e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 24642494     965 HSCDAECdsSGCYGRGPTQCVACSHYR--LDNTCVSRCPPRSF 1005
Cdd:smart00261    5 KPCHPEC--ATCTGPGPDDCTSCKHGFflDGGKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
1256-1298 1.25e-04

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 40.96  E-value: 1.25e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642494    1256 GSLCSPCLHTCSQCVSR--TNCSNCSKGLELQNGECRTTCADGYY 1298
Cdd:smart00261    1 DGECKPCHPECATCTGPgpDDCTSCKHGFFLDGGKCVSECPPGTY 45
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 1286-1456 2.16e-04

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 46.06  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1286 NGECRTTCADGYYSDRGICAKC---YL-----SC-HTCSGPRRNQCVQCPAGWQLAAGECHPECPEGFYKSDFGCQKCHH 1356
Cdd:PTZ00214  358 NGGVSGCATCGYNSGAVTCTRCsagYLgvdgkSCsESCSGDTRGVCTKVAEGSESTEVSCRCVCKPTFYNSSGTCTPCTD 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  1357 YCKTCNDAGPLACTSCPPHSMLDGGLC----MECLSSQYYDTTSATCKTCHDSCRSCfgpgqFSCKGCvpplHLDQLNSQ 1432
Cdd:PTZ00214  438 SCAVCKDGTPTGCQQCSPGKILEFSIVssesADCVDQCSVGSECAECGITIDGSRYC-----TRCKDA----STYPFNGV 508

                         170       180
                  ....*....|....*....|....
gi 24642494  1433 CVSCCQNQTLAEKTSSAACCNCDG 1456
Cdd:PTZ00214  509 CIPNTQRDAYCTSTANGACTTCSG 532
Furin-like pfam00757
Furin-like cysteine rich region;
1060-1151 2.31e-04

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 43.19  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1060 NRTCVPCEPN----CASCQdHPEYCTSCDHHLVMHEHKCYSACpldtyeTEDNKCafCHSTCA-TCNGPTDQDCITCRSS 1134
Cdd:pfam00757    1 NRECGDVCPGtmekCHSCC-NNGYCWGPGHCQKVCPEQCKKRC------TKPGEC--CHEQCLgGCTGPNDSDCLACRHF 71

                           90
                   ....*....|....*..
gi 24642494   1135 RYawQNKCLISCPDGFY 1151
Cdd:pfam00757   72 ND--EGTCVDQCPPGTY 86
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 1211-1302 3.70e-04

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: 41.26  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1211 CRPChASCGSCNGpadtsCTSCPP--------NRLLEQSRCVSGCREGFFVEAG---SLCSPC-LHTCSQCVSRTNCSNC 1278
Cdd:pfam15913    1 CSGC-VLCSEENG-----CLTCQPrlflllerNGIRQYGVCLHSCPPGYFGIRGqevNRCTKCkAENCESCFSKDFCTKC 74

                           90       100
                   ....*....|....*....|....
gi 24642494   1279 SKGLELQNGECRTTCADGYYSDRG 1302
Cdd:pfam15913   75 KEGFYLHKGKCLDTCPEGTAAQNS 98
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1402-1448 4.56e-04

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 39.42  E-value: 4.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 24642494 1402 CHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQTLAEKTSS 1448
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCVSECPEGTYADTEGG 46
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 1314-1413 5.38e-04

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


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 41.59  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   1314 CSGPRRNQCVQCpAGWQLaAGECHPECP-----EGFYKSDFGCQKCHHYCK------TCNDAGPLACTSCpPHSMlDGGL 1382
Cdd:pfam14843   11 CWGPGPDQCLSC-RNFSR-GGTCVESCNilqgePREYVVNSTCVPCHPECLpqngtaTCSGPGADNCTKC-AHFR-DGPH 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 24642494   1383 CME-CLSSQY--------YDTTSATCKTCHDSC-RSCFGPG 1413
Cdd:pfam14843   87 CVSsCPSGVLgendliwkYADANGVCQPCHPNCtQGCTGPG 127
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 406-559 6.37e-04

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: 44.15  E-value: 6.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  406 YTGKGVVVSILDDGIQTNHP---------------DLAQNYDPEASFDING-----------------NDSDPTPQDNGd 453
Cdd:cd07478    1 LTGKGVLVGIIDTGIDYLHPefrnedgttrilyiwDQTIPGGPPPGGYYGGgeyteeiinaalasdnpYDIVPSRDENG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  454 nkHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGK--------------VNDVVEA------QALSLN-PSHIDIy 512
Cdd:cd07478   80 --HGTHVAGIAAGNGDNNPDFKGVAPEAELIVVKLKQAKkylrefyedvpfyqETDIMLAikylydKALELNkPLVINI- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24642494  513 saSWGpEDDGSTvDGPGPLARraFIYGVTSGRqgkGSIFVWASGNGG 559
Cdd:cd07478  157 --SLG-TNFGSH-DGTSLLER--YIDAISRLR---GIAVVVGAGNEG 194
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 413-496 7.88e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 44.19  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494   413 VSILDDGIQTNHPDLAQNYDPEASF---------DINGN----------DSDPTPQDngDNKHGTRCAGEVAAVAFNNFC 473
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIDVNVKElhgrkgiddDNNGNvddeyganfvNNDGGPMD--DNYHGTHVSGIISAIGNNNIG 397

                          90       100
                  ....*....|....*....|....*..
gi 24642494   474 GVGVAYNASIGGVRMLD----GKVNDV 496
Cdd:PTZ00262  398 IVGVDKRSKLIICKALDshklGRLGDM 424
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 402-483 3.57e-03

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


Pssm-ID: 173805 [Multi-domain]  Cd Length: 255  Bit Score: 41.29  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642494  402 WQKGYTGKGVVVSILDDGIQTNHPDLAQNYDpeasfdingnDSDPTPQDNGDNK--HGTRCAGEVAAVafNNFCgVGVAY 479
Cdd:cd07479    1 WQLGYTGAGVKVAVFDTGLAKDHPHFRNVKE----------RTNWTNEKTLDDGlgHGTFVAGVIASS--REQC-LGFAP 67


                 ....
gi 24642494  480 NASI 483
Cdd:cd07479   68 DAEI 71
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1261-1300 4.44e-03

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: 36.73  E-value: 4.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 24642494 1261 PCLHTCSQCVSR--TNCSNCSKGLELQNGECRTTCADGYYSD 1300
Cdd:cd00064    1 PCHPSCATCTGPgpDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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