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Conserved domains on  [gi|24642484|ref|NP_727963|]
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furin 2, isoform A [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 ...
 375-674 3.53e-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: 512.49  E-value: 3.53e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  375 FPDPLFKEQWYLvsKNGG---AKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTP 451
Cdd:cd04059    1 PNDPLFPYQWYL--KNTGqagGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  452 QDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGP 531
Cdd:cd04059   79 RYDDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  532 GPLARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGTP 611
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642484  612 GHDKSVATVDMDGSlrpdHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 674
Cdd:cd04059  239 NPEASIVTTDLGGN----CNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 761-849 4.27e-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: 4.27e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    761 LEHVQCRITLRFFPRGNLRILLTSPMGTTSTLLFERPRDIVKSNFDDWPFLSVHFWGEKAEGRWTLQVINGGRrrvNQPG 840
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAP---GDTG 77


                   ....*....
gi 24642484    841 ILSKWQLIF 849
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 7.54e-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: 7.54e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642484    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 ...
 970-1073 2.20e-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: 2.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    970 CDAECDSSGCYGRGPTQCVACSHYRLDNTCVSRCP-----PRSFPNQvGICWPCHDTCE------TCAGAGPDSCLTCAp 1038
Cdd:pfam14843    2 CDPLCSSEGCWGPGPDQCLSCRNFSRGGTCVESCNilqgePREYVVN-STCVPCHPECLpqngtaTCSGPGADNCTKCA- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24642484   1039 ahlHVIDLAVCLQFCPDG--------YFENSRNRTCVPCEPNC 1073
Cdd:pfam14843   80 ---HFRDGPHCVSSCPSGvlgendliWKYADANGVCQPCHPNC 119
VSP super family cl31427
Giardia variant-specific surface protein;
1020-1379 7.42e-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: 7.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1020 DTCETCAGAGPDSCLTCAPAHlHVIDLAVCLQFCPD----GYFENSRNR-TCVPCEP-NCASCQDHpeyctscdhhlvmh 1093
Cdd:pfam03302   26 ENCKACSNDKREVCEECNSNN-YLTPTSQCIDDCAKignyYYTTNANNKkICKECTVaNCKTCEDQ-------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1094 ehKCYSACPLDTYETEDnKCAFCHSTCATCNGPTDQDCITCRSSryawqnKCLISCPDGfyadKKRLECMPCQEG----- 1168
Cdd:pfam03302   91 --GQCQACNDGFYKSGD-ACSPCHESCKTCSGGTASDCTECLTG------KALRYGNDG----TKGTCGEGCTTGtgaga 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1169 CKTC--TSNGV--CSECLQNWTLNKRDKCIVSGSEGCSESEFYSQVEGQCRPCHASCGSCNG--------PADTSCTSCP 1236
Cdd:pfam03302  158 CKTCglTIDGTsyCSECATETEYPQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGgcyettkfPGKSVCEEAN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1237 PNRLLEQSrcvsgcREGFFVEAGSLCSpCLHTCSQCVSRTNCsncskglelqngecrTTCADGYYSDRGICAKCYLSCHT 1316
Cdd:pfam03302  238 SGGTCQKE------APGYKLNNGDLVT-CSPGCKTCTSNTVC---------------TTCMDGYVKTSDSCTKCDSSCET 295

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642484   1317 CSGprrnQCVQCPAgwqlaagechpeCPEGFYKSDFGCQKCHHYCKTCNDAGPLACTSCPPHS 1379
Cdd:pfam03302  296 CTG----ATTTCKT------------CATGYYKSGTGCVSCTSSESDNGITGVKGCLNCAPPS 342
FU smart00261
Furin-like repeats;
1401-1444 7.94e-06

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 44.42  E-value: 7.94e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24642484    1401 TCKTCHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQT 1444
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 ...
 375-674 3.53e-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: 512.49  E-value: 3.53e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  375 FPDPLFKEQWYLvsKNGG---AKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTP 451
Cdd:cd04059    1 PNDPLFPYQWYL--KNTGqagGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  452 QDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGP 531
Cdd:cd04059   79 RYDDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  532 GPLARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGTP 611
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642484  612 GHDKSVATVDMDGSlrpdHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 674
Cdd:cd04059  239 NPEASIVTTDLGGN----CNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 411-700 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 24642484    411 GKGVVVSILDDGIQTNHPDLAQNY------DPEASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNA 484
Cdd:pfam00082    1 GKGVVVAVLDTGIDPNHPDLSGNLdndpsdDPEASVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    485 SIGGVRML-DGKVNDVVEAQALSLN-PSHIDIYSASWGPEddgSTVDGPGPLARRAFIYGvtsGRQGKGSIFVWASGNGG 562
Cdd:pfam00082   81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    563 RYTDSCNCDGY-TNSIFTLSISSATqagfkpwyleECSSTLATTYSSGTPGHDKS-----VA------------TVDMDG 624
Cdd:pfam00082  155 PGGNNGSSVGYpAQYKNVIAVGAVD----------EASEGNLASFSSYGPTLDGRlkpdiVApggnitggnissTLLTTT 224

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642484    625 SlRPDHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLEKENgwtlngvkrkysHKFGYG 700
Cdd:pfam00082  225 S-DPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD------------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 403-706 1.20e-36

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 145.63  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  403 PAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDingnDSDPTPQDngDNKHGTRCAGEVAAVAFNNFCGVGVAY 482
Cdd:COG1404  100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDFV----DGDGDPSD--DNGHGTHVAGIIAANGNNGGGVAGVAP 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  483 NASIGGVRMLD----GKVNDVVEA--QALSLNpshIDIYSASWgpeddGSTVDGPGPLARRAFIYGVtsgrqGKGSIFVW 556
Cdd:COG1404  174 GAKLLPVRVLDdngsGTTSDIAAAidWAADNG---ADVINLSL-----GGPADGYSDALAAAVDYAV-----DKGVLVVA 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  557 ASGNGGRYTDS----CNCDGytnsifTLSISSATQAGFKPWYleecSSTlattyssGT------PGHDksVATVDMDGSl 626
Cdd:COG1404  241 AAGNSGSDDATvsypAAYPN------VIAVGAVDANGQLASF----SNY-------GPkvdvaaPGVD--ILSTYPGGG- 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  627 rpdhicTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLekengwtlngvkrkYSHKFGYGLMDAGA 706
Cdd:COG1404  301 ------YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGA--------------PGPYYGYGLLADGA 360
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 761-849 4.27e-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: 4.27e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    761 LEHVQCRITLRFFPRGNLRILLTSPMGTTSTLLFERPRDIVKSNFDDWPFLSVHFWGEKAEGRWTLQVINGGRrrvNQPG 840
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAP---GDTG 77


                   ....*....
gi 24642484    841 ILSKWQLIF 849
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 7.54e-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: 7.54e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642484    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 ...
 970-1073 2.20e-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: 2.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    970 CDAECDSSGCYGRGPTQCVACSHYRLDNTCVSRCP-----PRSFPNQvGICWPCHDTCE------TCAGAGPDSCLTCAp 1038
Cdd:pfam14843    2 CDPLCSSEGCWGPGPDQCLSCRNFSRGGTCVESCNilqgePREYVVN-STCVPCHPECLpqngtaTCSGPGADNCTKCA- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24642484   1039 ahlHVIDLAVCLQFCPDG--------YFENSRNRTCVPCEPNC 1073
Cdd:pfam14843   80 ---HFRDGPHCVSSCPSGvlgendliWKYADANGVCQPCHPNC 119
VSP pfam03302
Giardia variant-specific surface protein;
1020-1379 7.42e-17

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 84.64  E-value: 7.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1020 DTCETCAGAGPDSCLTCAPAHlHVIDLAVCLQFCPD----GYFENSRNR-TCVPCEP-NCASCQDHpeyctscdhhlvmh 1093
Cdd:pfam03302   26 ENCKACSNDKREVCEECNSNN-YLTPTSQCIDDCAKignyYYTTNANNKkICKECTVaNCKTCEDQ-------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1094 ehKCYSACPLDTYETEDnKCAFCHSTCATCNGPTDQDCITCRSSryawqnKCLISCPDGfyadKKRLECMPCQEG----- 1168
Cdd:pfam03302   91 --GQCQACNDGFYKSGD-ACSPCHESCKTCSGGTASDCTECLTG------KALRYGNDG----TKGTCGEGCTTGtgaga 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1169 CKTC--TSNGV--CSECLQNWTLNKRDKCIVSGSEGCSESEFYSQVEGQCRPCHASCGSCNG--------PADTSCTSCP 1236
Cdd:pfam03302  158 CKTCglTIDGTsyCSECATETEYPQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGgcyettkfPGKSVCEEAN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1237 PNRLLEQSrcvsgcREGFFVEAGSLCSpCLHTCSQCVSRTNCsncskglelqngecrTTCADGYYSDRGICAKCYLSCHT 1316
Cdd:pfam03302  238 SGGTCQKE------APGYKLNNGDLVT-CSPGCKTCTSNTVC---------------TTCMDGYVKTSDSCTKCDSSCET 295

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642484   1317 CSGprrnQCVQCPAgwqlaagechpeCPEGFYKSDFGCQKCHHYCKTCNDAGPLACTSCPPHS 1379
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 ...
 1116-1163 4.57e-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: 4.57e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 24642484 1116 CHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFYADKKRLECM 1163
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
1110-1154 1.69e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.52  E-value: 1.69e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642484    1110 DNKCAFCHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFY 1154
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 1165-1482 4.94e-10

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 64.55  E-value: 4.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1165 CQEGCKTCTsNGVCSEclqnwtlnkrdkcIVSGSEGCSES-------EFYSQvEGQCRPCHASCGSCNGPADTSCTSCPP 1237
Cdd:PTZ00214  391 CSESCSGDT-RGVCTK-------------VAEGSESTEVScrcvckpTFYNS-SGTCTPCTDSCAVCKDGTPTGCQQCSP 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1238 NRLLEQS-------RCVSGCRE-------GFFVEAGSLCSPCLHTC---------------SQCVSRTN--CSNCSKGLE 1286
Cdd:PTZ00214  456 GKILEFSivssesaDCVDQCSVgsecaecGITIDGSRYCTRCKDAStypfngvcipntqrdAYCTSTANgaCTTCSGAAF 535

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1287 LQNGECRT-------------------TCADGYY-SDRGICAKCYLSCHTCSGPRRNQCVQCPAGWQL------AAGEC- 1339
Cdd:PTZ00214  536 LMNGGCYTtehypgsticdkqsngkctTTKKGYGiSPDGKLLECDPTCLACTAPGPGRCTRCPSDKLLkrasgaATGSCv 615

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1340 -HPECPEGFYKSDFGCQKCHHY-CKTCNDAGplACTSCPPHSM--LDGGLCM-ECLSSQYYDTTSATCKTCHdsCRSCFG 1414
Cdd:PTZ00214  616 dPGACVDGYYADGDACLPCATPgCKTCGHAS--FCTECAGELFvsLDGQSCLeECTGDKVVGEVSGGVRRCW--CERGFL 691

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1415 PGqFSCKGCVPPLHLDQLNSQCVSC----------------------CQNQTLAEKTSSAACCNCDGET----GECKATS 1468
Cdd:PTZ00214  692 PA-LDRSGCVLPTECPPDMPSCAACdesgrcllcvtsghnvqvdqrtCAEGCGARASSNQGVCMCELDAvltkGVCVPAK 770

                         410
                  ....*....|....
gi 24642484  1469 TGGKRRTVVGSGSA 1482
Cdd:PTZ00214  771 ELAKKRTAAIAGGT 784
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1017-1067 3.52e-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: 3.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24642484 1017 PCHDTCETCAGAGPDSCLTCapAHLHVIDLAVCLQFCPDGYFENSRNRTCV 1067
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSC--RHGFYLDGGTCVSECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
1013-1058 4.70e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 47.89  E-value: 4.70e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24642484    1013 GICWPCHDTCETCAGAGPDSCLTCAPAHLHviDLAVCLQFCPDGYF 1058
Cdd:smart00261    2 GECKPCHPECATCTGPGPDDCTSCKHGFFL--DGGKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
1401-1444 7.94e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 44.42  E-value: 7.94e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24642484    1401 TCKTCHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQT 1444
Cdd:smart00261    3 ECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPGT 44
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1405-1451 4.44e-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: 4.44e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 24642484 1405 CHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQTLAEKTSS 1451
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCVSECPEGTYADTEGG 46
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 416-499 8.03e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 44.19  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   416 VSILDDGIQTNHPDLAQNYDPEASF---------DINGN----------DSDPTPQDngDNKHGTRCAGEVAAVAFNNFC 476
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIDVNVKElhgrkgiddDNNGNvddeyganfvNNDGGPMD--DNYHGTHVSGIISAIGNNNIG 397

                          90       100
                  ....*....|....*....|....*..
gi 24642484   477 GVGVAYNASIGGVRMLD----GKVNDV 499
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 ...
 375-674 3.53e-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: 512.49  E-value: 3.53e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  375 FPDPLFKEQWYLvsKNGG---AKDGLDMNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTP 451
Cdd:cd04059    1 PNDPLFPYQWYL--KNTGqagGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  452 QDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGP 531
Cdd:cd04059   79 RYDDDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  532 GPLARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGTP 611
Cdd:cd04059  159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642484  612 GHDKSVATVDMDGSlrpdHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 674
Cdd:cd04059  239 NPEASIVTTDLGGN----CNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 411-700 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 24642484    411 GKGVVVSILDDGIQTNHPDLAQNY------DPEASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNA 484
Cdd:pfam00082    1 GKGVVVAVLDTGIDPNHPDLSGNLdndpsdDPEASVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    485 SIGGVRML-DGKVNDVVEAQALSLN-PSHIDIYSASWGPEddgSTVDGPGPLARRAFIYGvtsGRQGKGSIFVWASGNGG 562
Cdd:pfam00082   81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    563 RYTDSCNCDGY-TNSIFTLSISSATqagfkpwyleECSSTLATTYSSGTPGHDKS-----VA------------TVDMDG 624
Cdd:pfam00082  155 PGGNNGSSVGYpAQYKNVIAVGAVD----------EASEGNLASFSSYGPTLDGRlkpdiVApggnitggnissTLLTTT 224

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642484    625 SlRPDHICTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLEKENgwtlngvkrkysHKFGYG 700
Cdd:pfam00082  225 S-DPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAGLD------------RLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 403-706 1.20e-36

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 145.63  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  403 PAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDingnDSDPTPQDngDNKHGTRCAGEVAAVAFNNFCGVGVAY 482
Cdd:COG1404  100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDFV----DGDGDPSD--DNGHGTHVAGIIAANGNNGGGVAGVAP 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  483 NASIGGVRMLD----GKVNDVVEA--QALSLNpshIDIYSASWgpeddGSTVDGPGPLARRAFIYGVtsgrqGKGSIFVW 556
Cdd:COG1404  174 GAKLLPVRVLDdngsGTTSDIAAAidWAADNG---ADVINLSL-----GGPADGYSDALAAAVDYAV-----DKGVLVVA 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  557 ASGNGGRYTDS----CNCDGytnsifTLSISSATQAGFKPWYleecSSTlattyssGT------PGHDksVATVDMDGSl 626
Cdd:COG1404  241 AAGNSGSDDATvsypAAYPN------VIAVGAVDANGQLASF----SNY-------GPkvdvaaPGVD--ILSTYPGGG- 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  627 rpdhicTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPLekengwtlngvkrkYSHKFGYGLMDAGA 706
Cdd:COG1404  301 ------YATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTATPLGA--------------PGPYYGYGLLADGA 360
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 761-849 4.27e-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: 4.27e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    761 LEHVQCRITLRFFPRGNLRILLTSPMGTTSTLLFERPRDIVKSNFDDWPFLSVHFWGEKAEGRWTLQVINGGRrrvNQPG 840
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDTAP---GDTG 77


                   ....*....
gi 24642484    841 ILSKWQLIF 849
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 7.54e-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: 7.54e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642484    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 ...
 414-664 1.96e-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: 1.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  414 VVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNgdnkHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLD 493
Cdd:cd07498    1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPTSDIDG----HGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRIAD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  494 --GKVNDVVEAQALSLNPSH-IDIYSASWGPEDDGSTVdgpgplaRRAFIYGVTSGRQGKGSIFVWASGNGGRYTDScnc 570
Cdd:cd07498   77 slGYAYWSDIAQAITWAADNgADVISNSWGGSDSTESI-------SSAIDNAATYGRNGKGGVVLFAAGNSGRSVSS--- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  571 dGYTNSIFTLSISSATQAGFKPWY--------LEECSSTLATTYSSGTPGHDksvatvDMDGSlrpdhicTVEHTGTSAS 642
Cdd:cd07498  147 -GYAANPSVIAVAATDSNDARASYsnygnyvdLVAPGVGIWTTGTGRGSAGD------YPGGG-------YGSFSGTSFA 212

                        250       260
                 ....*....|....*....|..
gi 24642484  643 APLAAGICALALEANPELTWRD 664
Cdd:cd07498  213 SPVAAGVAALILSANPNLTPAE 234
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 414-672 2.90e-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: 2.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  414 VVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAfNNFCGVGVAYNASIGGVRMLD 493
Cdd:cd00306    1 VTVAVIDTGVDPDHPDLDGLFGGGDGGNDDDDNENGPTDPDDGNGHGTHVAGIIAASA-NNGGGVGVAPGAKLIPVKVLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  494 GKVN----DVVEAQALSLNPSHIDIYSASWgpeddGSTVDGPGPLARRAFIYGVTSgrqgKGSIFVWASGNGGRYTDScN 569
Cdd:cd00306   80 GDGSgsssDIAAAIDYAAADQGADVINLSL-----GGPGSPPSSALSEAIDYALAK----LGVLVVAAAGNDGPDGGT-N 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  570 CDGYTNSIFTLSISSATQAGfkpwyleecssTLATTYSSGTPGHDKSVATVDMDGSLRPDHICTVEHTGTSASAPLAAGI 649
Cdd:cd00306  150 IGYPAASPNVIAVGAVDRDG-----------TPASPSSNGGAGVDIAAPGGDILSSPTTGGGGYATLSGTSMAAPIVAGV 218

                        250       260
                 ....*....|....*....|...
gi 24642484  650 CALALEANPELTWRDMQYLVVYT 672
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 ...
 412-674 5.35e-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: 5.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  412 KGVVVSILDDGIQTNHPDLAQN------YDPEASFDINGN------------DSDPTPQDngDNKHGTRCAGEVAAVAFN 473
Cdd:cd07473    2 GDVVVAVIDTGVDYNHPDLKDNmwvnpgEIPGNGIDDDGNgyvddiygwnfvNNDNDPMD--DNGHGTHVAGIIGAVGNN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  474 NFCGVGVAYNASIGGVRMLD----GKVNDVVEA--QALSLNpshIDIYSASWGPeddgstvDGPGPLARRAFIYGvtsgr 547
Cdd:cd07473   80 GIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAidYAVDMG---AKIINNSWGG-------GGPSQALRDAIARA----- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  548 QGKGSIFVWASGNGGRYTDS-----CNCDgYTNSIftlSISSATQAGFKPWYleecSSTLATTYSSGTPGHDkSVATVDM 622
Cdd:cd07473  145 IDAGILFVAAAGNDGTNNDKtptypASYD-LDNII---SVAATDSNDALASF----SNYGKKTVDLAAPGVD-ILSTSPG 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24642484  623 DGslrpdhicTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 674
Cdd:cd07473  216 GG--------YGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 410-661 7.46e-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: 7.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  410 TGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNGDnkHGTRCAGeVAAVAFNNFCGVGVAYNASIGGV 489
Cdd:cd04848    1 TGAGVKVGVIDSGIDLSHPEFAGRVSEASYYVAVNDAGYASNGDGDS--HGTHVAG-VIAAARDGGGMHGVAPDATLYSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  490 RMLDGKVNDVVEAQALS----LNPSHIDIYSASWGPEDDGSTVDGPGPL---ARRAFIYGVTSGRQGKGSIFVWASGNGG 562
Cdd:cd04848   78 RASASAGSTFSDADIAAaydfLAASGVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVFAAGNDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  563 RYTDSCNCDGYT--------NSIFTLSI-SSATQAGFKpwYLEEC----SSTLAttyssgTPGHDKSVATVDMDGSLRPd 629
Cdd:cd04848  158 QANPSLAAAALPylepelegGWIAVVAVdPNGTIASYS--YSNRCgvaaNWCLA------APGENIYSTDPDGGNGYGR- 228

                        250       260       270
                 ....*....|....*....|....*....|..
gi 24642484  630 hictveHTGTSASAPLAAGICALALEANPELT 661
Cdd:cd04848  229 ------VSGTSFAAPHVSGAAALLAQKFPWLT 254
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 377-658 5.12e-22

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: 97.33  E-value: 5.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  377 DPLFKEQWylvsknggakdGLDMNVGP-AWQKGyTGKGVVVSILDDGIQTNHPDLAQ-NYDPeaSFDINGNDSDPTPqdn 454
Cdd:cd07484    4 DPYYSYQW-----------NLDQIGAPkAWDIT-GGSGVTVAVVDTGVDPTHPDLLKvKFVL--GYDFVDNDSDAMD--- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  455 gDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLD----GKVNDVVEAqalslnpshIdIYSAswgpeDDGSTV-- 528
Cdd:cd07484   67 -DNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANG---------I-RYAA-----DKGAKVin 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  529 ---DGPGP--LARRAFIYGvtsgrQGKGSIFVWASGNGGRYTDScncdgYTNSIF-TLSISSATQAGFKPWyleecsstl 602
Cdd:cd07484  131 lslGGGLGstALQEAINYA-----WNKGVVVVAAAGNEGVSSVS-----YPAAYPgAIAVAATDQDDKRAS--------- 191

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24642484  603 attYSSGTPGHDKSVATVDMDgSLRPDHICTVeHTGTSASAPLAAGICALALEANP 658
Cdd:cd07484  192 ---FSNYGKWVDVSAPGGGIL-STTPDGDYAY-MSGTSMATPHVAGVAALLYSQGP 242
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 413-661 7.79e-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: 97.75  E-value: 7.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  413 GVVVSILDDGIQTNHPDLA----QNYD----PEASFDINGNDSDPTPQDNGDNK------------------HGTRCAGE 466
Cdd:cd07496    1 GVVVAVLDTGVLFHHPDLAgvllPGYDfisdPAIANDGDGRDSDPTDPGDWVTGddvppggfcgsgvspsswHGTHVAGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  467 VAAVAfNNFCGV-GVAYNASIGGVRML---DGKVNDVVEAqalslnpshidIYSASwgpeddGSTVDGPGPLARRAFIYG 542
Cdd:cd07496   81 IAAVT-NNGVGVaGVAWGARILPVRVLgkcGGTLSDIVDG-----------MRWAA------GLPVPGVPVNPNPAKVIN 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  543 VTSGRQG---------------KGSIFVWASGNGGRYTDS---CNCDGytnsifTLSISSATQAGFKPWYleecsSTLAT 604
Cdd:cd07496  143 LSLGGDGacsatmqnaindvraRGVLVVVAAGNEGSSASVdapANCRG------VIAVGATDLRGQRASY-----SNYGP 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642484  605 TYSSGTPGHDksvATVDMDGSLRPDHICT---------VEHTGTSASAPLAAGICALALEANPELT 661
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 ...
 411-675 5.72e-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: 5.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  411 GKGVVVSILDDGIQTNHPDLAQNYDPEASF----DINGNDSDP-----TPQDNGDNK------HGTRCAGEVAAVAFNNF 475
Cdd:cd07474    1 GKGVKVAVIDTGIDYTHPDLGGPGFPNDKVkggyDFVDDDYDPmdtrpYPSPLGDASagdatgHGTHVAGIIAGNGVNVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  476 CGVGVAYNASIGGVRMLD--GKVNDVVEAQAL--SLNPsHIDIYSASWGPEDDGStvDGPGPLA-RRAFIYGVtsgrqgk 550
Cdd:cd07474   81 TIKGVAPKADLYAYKVLGpgGSGTTDVIIAAIeqAVDD-GMDVINLSLGSSVNGP--DDPDAIAiNNAVKAGV------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  551 gsIFVWASGNGGrytDSCNCDGyTNSIFTLSISSATQAGFKPWYleecSSTLATTYSSGTPGHD--------------KS 616
Cdd:cd07474  151 --VVVAAAGNSG---PAPYTIG-SPATAPSAITVGASTVADVAE----ADTVGPSSSRGPPTSDsaikpdivapgvdiMS 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24642484  617 VATVDMDGSLRpdhictveHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRP 675
Cdd:cd07474  221 TAPGSGTGYAR--------MSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKP 271
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 403-658 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 24642484  403 PAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYDPEA------SFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAfNNFC 476
Cdd:cd07485    1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGydpavnGYNFVPNVGDIDNDVSVGGGHGTHVAGTIAAVN-NNGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  477 GVG-------VAYNASIGGVRMLDGK--VNDVVEAQALSLNPSH-IDIYSASWGpeddGSTVDGPGPLARRAFIYGVTSG 546
Cdd:cd07485   80 GVGgiagaggVAPGVKIMSIQIFAGRyyVGDDAVAAAIVYAADNgAVILQNSWG----GTGGGIYSPLLKDAFDYFIENA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  547 RQG--KGSIFVWASGNggrytDSCNCDGYTNSIFTLSISSATQAGFKPWYLeecsSTLATTYSSGTPGHDKSVATV---D 621
Cdd:cd07485  156 GGSplDGGIVVFSAGN-----SYTDEHRFPAAYPGVIAVAALDTNDNKASF----SNYGRWVDIAAPGVGTILSTVpklD 226

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 24642484  622 MDGSLRPDHIctvehTGTSASAPLAAGICALALEANP 658
Cdd:cd07485  227 GDGGGNYEYL-----SGTSMAAPHVSGVAALVLSKFP 258
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 970-1073 2.20e-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: 2.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    970 CDAECDSSGCYGRGPTQCVACSHYRLDNTCVSRCP-----PRSFPNQvGICWPCHDTCE------TCAGAGPDSCLTCAp 1038
Cdd:pfam14843    2 CDPLCSSEGCWGPGPDQCLSCRNFSRGGTCVESCNilqgePREYVVN-STCVPCHPECLpqngtaTCSGPGADNCTKCA- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24642484   1039 ahlHVIDLAVCLQFCPDG--------YFENSRNRTCVPCEPNC 1073
Cdd:pfam14843   80 ---HFRDGPHCVSSCPSGvlgendliWKYADANGVCQPCHPNC 119
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 413-661 5.57e-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: 5.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  413 GVVVSILDDGIQTNHPDLAQNYDPEASFdINGNDSDPTPqDNGdnkHGTRCAGEVAAVAfNNFCGVGVAYNASIGGVRML 492
Cdd:cd07477    1 GVKVAVIDTGIDSSHPDLKLNIVGGANF-TGDDNNDYQD-GNG---HGTHVAGIIAALD-NGVGVVGVAPEADLYAVKVL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  493 D----GKVNDVVEAQALSLNpSHIDIYSASWGPEDDGSTVdgpgplaRRAFIYGVtsgrqGKGSIFVWASGNGGRYTDSC 568
Cdd:cd07477   75 NddgsGTYSDIIAGIEWAIE-NGMDIINMSLGGPSDSPAL-------REAIKKAY-----AAGILVVAAAGNSGNGDSSY 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  569 NCDGYTNSifTLSISSATQAGfkpwyleecssTLATTYSSGT------PGHDkSVATVDMDGslrpdhicTVEHTGTSAS 642
Cdd:cd07477  142 DYPAKYPS--VIAVGAVDSNN-----------NRASFSSTGPevelaaPGVD-ILSTYPNND--------YAYLSGTSMA 199

                        250
                 ....*....|....*....
gi 24642484  643 APLAAGICALALEANPELT 661
Cdd:cd07477  200 TPHVAGVAALVWSKRPELT 218
VSP pfam03302
Giardia variant-specific surface protein;
1020-1379 7.42e-17

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 84.64  E-value: 7.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1020 DTCETCAGAGPDSCLTCAPAHlHVIDLAVCLQFCPD----GYFENSRNR-TCVPCEP-NCASCQDHpeyctscdhhlvmh 1093
Cdd:pfam03302   26 ENCKACSNDKREVCEECNSNN-YLTPTSQCIDDCAKignyYYTTNANNKkICKECTVaNCKTCEDQ-------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1094 ehKCYSACPLDTYETEDnKCAFCHSTCATCNGPTDQDCITCRSSryawqnKCLISCPDGfyadKKRLECMPCQEG----- 1168
Cdd:pfam03302   91 --GQCQACNDGFYKSGD-ACSPCHESCKTCSGGTASDCTECLTG------KALRYGNDG----TKGTCGEGCTTGtgaga 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1169 CKTC--TSNGV--CSECLQNWTLNKRDKCIVSGSEGCSESEFYSQVEGQCRPCHASCGSCNG--------PADTSCTSCP 1236
Cdd:pfam03302  158 CKTCglTIDGTsyCSECATETEYPQNGVCTSTAARATATCKASSVANGMCSSCANGYFRMNGgcyettkfPGKSVCEEAN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1237 PNRLLEQSrcvsgcREGFFVEAGSLCSpCLHTCSQCVSRTNCsncskglelqngecrTTCADGYYSDRGICAKCYLSCHT 1316
Cdd:pfam03302  238 SGGTCQKE------APGYKLNNGDLVT-CSPGCKTCTSNTVC---------------TTCMDGYVKTSDSCTKCDSSCET 295

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24642484   1317 CSGprrnQCVQCPAgwqlaagechpeCPEGFYKSDFGCQKCHHYCKTCNDAGPLACTSCPPHS 1379
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 ...
 411-661 5.65e-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: 5.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  411 GKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNGdnkHGTRCAGEVAA-VAFNNFCGVGVAYNASIGGV 489
Cdd:cd07487    1 GKGITVAVLDTGIDAPHPDFDGRIIRFADFVNTVNGRTTPYDDNG---HGTHVAGIIAGsGRASNGKYKGVAPGANLVGV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  490 RMLD----GKVNDVVEA------QALSLNpshIDIYSASWGPEDDGStvDGPGPL---ARRAFIYGVTsgrqgkgsiFVW 556
Cdd:cd07487   78 KVLDdsgsGSESDIIAGidwvveNNEKYN---IRVVNLSLGAPPDPS--YGEDPLcqaVERLWDAGIV---------VVV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  557 ASGNGGRYTDSCNCDGytNSIFTLSISSATQAGFKPWYLEECSStlattySSGTP-GHDK-----------SVATVDMDG 624
Cdd:cd07487  144 AAGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSS------RGPTGdGRIKpdvvapgenivSCRSPGGNP 215

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 24642484  625 SLRPDHIcTVEHTGTSASAPLAAGICALALEANPELT 661
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 ...
 407-677 4.18e-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: 4.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  407 KGYTGKGVVVSILDDGIQTNHPDLAQNYDP----EASFDINGNDSDP--TPQDNGD----NKHGTRCAGEVAAVAfNNFC 476
Cdd:cd07489    8 EGITGKGVKVAVVDTGIDYTHPALGGCFGPgckvAGGYDFVGDDYDGtnPPVPDDDpmdcQGHGTHVAGIIAANP-NAYG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  477 GVGVAYNASIGGVRMLD--GKVNDVVEAQALSLNPSH-IDIYSASWG-----PEDDGSTVdgPGPLARRAFIYGVTSGRQ 548
Cdd:cd07489   87 FTGVAPEATLGAYRVFGcsGSTTEDTIIAAFLRAYEDgADVITASLGgpsgwSEDPWAVV--ASRIVDAGVVVTIAAGND 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  549 GKGSIFVWASGNGGRYTDSCncdGYTNSIFTlSISSATQAGFKPwyleecsSTLATTYS--SGTPGHDKSVATVdmdgsl 626
Cdd:cd07489  165 GERGPFYASSPASGRGVIAV---ASVDSYFS-SWGPTNELYLKP-------DVAAPGGNilSTYPLAGGGYAVL------ 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24642484  627 rpdhictvehTGTSASAPLAAGICALALEA-NPELTWRDMQYLVVYTSRPAP 677
Cdd:cd07489  228 ----------SGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKPLP 269
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 413-661 7.22e-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: 7.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  413 GVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDPTPQDNgdNKHGTRCAGEVaAVAFNNFCGVGVAynasiGGVRML 492
Cdd:cd07490    1 GVTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEVFDA--GGHGTHVSGTI-GGGGAKGVYIGVA-----PEADLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  493 DGKVNDVVEAQALSLnpshidIYSASWGPEDD--------GSTVDGPGPLARRafiygVTSGRQGKGSIFVWASGNGGRY 564
Cdd:cd07490   73 HGKVLDDGGGSLSQI------IAGMEWAVEKDadvvsmslGGTYYSEDPLEEA-----VEALSNQTGALFVVSAGNEGHG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  565 TDSCNCDGYTnsifTLSISSATQAGFKPWYLEECSSTLATTYSSGTPGHDKSVATVDMDG----SLRPDHICTVEHT--- 637
Cdd:cd07490  142 TSGSPGSAYA----ALSVGAVDRDDEDAWFSSFGSSGASLVSAPDSPPDEYTKPDVAAPGvdvySARQGANGDGQYTrls 217

                        250       260
                 ....*....|....*....|....
gi 24642484  638 GTSASAPLAAGICALALEANPELT 661
Cdd:cd07490  218 GTSMAAPHVAGVAALLAAAHPDLS 241
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 438-851 1.47e-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: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  438 ASFDINGNDSDPTPQDNGDNKHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGKVNDVVEAQALSLNPSHIDIYSA 517
Cdd:COG4935  248 GAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAA 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  518 SWGPEDDGSTVDGPGPLARRAFIYGVTSGRQGKGSIFVWASGNGGRYTDSCNCDGYTNSIFTLSISSATQAGFKPWYLEE 597
Cdd:COG4935  328 AGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAGAAAGAAAGAAAGAAAAGGVASAAGA 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  598 CSSTLATTYSSGTPGHDKSVATVDMDGSLRPDHicTVEHTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAP 677
Cdd:COG4935  408 VGAGTAAGASATAAVSTGAASGSSTTSSTGTTA--TATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTTAAAAA 485

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  678 lekenGWTLNGVKRKYSHKFGYGLMDAGAMVSLAEQWTSVPPQHICKSRENNEDRKIDGAYGSTLSTHMDVNGcAGTINE 757
Cdd:COG4935  486 -----AAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVAIPDNGPAGVTSTITVSG-GGAVED 559

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  758 VRylehVQCRITLRFfpRGNLRILLTSPMGTTSTLLfeRPRDIVKSNFDdWPFLSVHFWGEKAEGRWTLQVINGGRRRVn 837
Cdd:COG4935  560 VT----VTVDITHTY--RGDLVITLISPDGTTVVLK--NRSGGSADNIN-ATFDVANFSGESANGTWTLRVVDTAGGDT- 629

                        410
                 ....*....|....
gi 24642484  838 qpGILSKWQLIFYG 851
Cdd:COG4935  630 --GTLNSWSLTFTG 641
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 399-674 4.99e-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: 4.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  399 MNVGPAWQKGYTGKGVVVSILDDGIQTNHPDLAQNYdpEASFDINGNDSDPTPQDNGdnkHGTrcaGEVAAVafnnfcgV 478
Cdd:cd07494    8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGY--QVRVVLAPGATDPACDENG---HGT---GESANL-------F 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  479 GVAYNASIGGVRMLDGKVNDVVEA--QALSLNPshiDIYSASWG-----PEDDGSTVDGPGPLARRAFIYGVTSgrqgKG 551
Cdd:cd07494   73 AIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSP---DIISNSWGydlrsPGTSWSRSLPNALKALAATLQDAVA----RG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  552 SIFVWASGNGGrytdscncdgytnSIFTLSISSATQAGfkPWYLEECSSTLATTYSSG---------------------- 609
Cdd:cd07494  146 IVVVFSAGNGG-------------WSFPAQHPEVIAAG--GVFVDEDGARRASSYASGfrskiypgrqvpdvcglvgmlp 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24642484  610 ---------TPGH--DKSVATVDmDGSLRPDHICTVehTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSR 674
Cdd:cd07494  211 haaylmlpvPPGSqlDRSCAAFP-DGTPPNDGWGVF--SGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTAR 283
Furin-like pfam00757
Furin-like cysteine rich region;
952-1073 4.65e-12

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 65.15  E-value: 4.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    952 QLVAAPETRDGDKKILHSCDAECdSSGCYGRGPTQCVACSHYRLDNTCVSRCPPRSFpnQVGicWPCHdTCETCAGAGPD 1031
Cdd:pfam00757   31 QKVCPEQCKKRCTKPGECCHEQC-LGGCTGPNDSDCLACRHFNDEGTCVDQCPPGTY--QFG--WRCV-TFKECPKSHLP 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24642484   1032 SCltcapaHLHVIDLAVCLQFCPDGYFEN-SRNRTCVPCEPNC 1073
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 ...
 409-661 7.83e-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: 7.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  409 YTGKGVVVSILDDGIQTNHPDLAQNydpeASFDINGNDSDPTPQDNGdnkHGTRCAGEVAAVAFnnfcgvGVAYNASIGG 488
Cdd:cd04077   22 STGSGVDVYVLDTGIRTTHVEFGGR----AIWGADFVGGDPDSDCNG---HGTHVAGTVGGKTY------GVAKKANLVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  489 VRMLDGK-----------VNDVVEAQALSLNPSHIdiySASWGpEDDGSTVDGpgpLARRAFIYGVTsgrqgkgsiFVWA 557
Cdd:cd04077   89 VKVLDCNgsgtlsgiiagLEWVANDATKRGKPAVA---NMSLG-GGASTALDA---AVAAAVNAGVV---------VVVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  558 SGNGGryTDSCNcdgYTNSiftlSISSATQAGfkpwyleecSSTLATTYSSGT----------PGHDKSVATVDMDGslr 627
Cdd:cd04077  153 AGNSN--QDACN---YSPA----SAPEAITVG---------ATDSDDARASFSnygscvdifaPGVDILSAWIGSDT--- 211

                        250       260       270
                 ....*....|....*....|....*....|....
gi 24642484  628 pdhiCTVEHTGTSASAPLAAGICALALEANPELT 661
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 ...
 406-656 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 24642484  406 QKGYTGKGVVVSILDDGIQTNHPDLaqnYDPEASFDINGN----DSDPTPQDNGD-NKHGTRCAGEVAAVAFNNFCGV-- 478
Cdd:cd04842    1 GLGLTGKGQIVGVADTGLDTNHCFF---YDPNFNKTNLFHrkivRYDSLSDTKDDvDGHGTHVAGIIAGKGNDSSSISly 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  479 -GVAYNASIGGVRMLDGKVN-------DVVEAQALSLNpshIDIYSASWGPEDDGSTVDgpgpLARR--AFIYgvtsgrQ 548
Cdd:cd04842   78 kGVAPKAKLYFQDIGDTSGNlssppdlNKLFSPMYDAG---ARISSNSWGSPVNNGYTL----LARAydQFAY------N 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  549 GKGSIFVWASGNGGrytdscncDGYTNSIFT-------LSISSATQA----GFKPWYLEECSSTLAtTYSSGTPGHD--- 614
Cdd:cd04842  145 NPDILFVFSAGNDG--------NDGSNTIGSpataknvLTVGASNNPsvsnGEGGLGQSDNSDTVA-SFSSRGPTYDgri 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24642484  615 -----------KSVATVDMDGSLRPDHIcTVEHTGTSASAPLAAGICALALEA 656
Cdd:cd04842  216 kpdlvapgtgiLSARSGGGGIGDTSDSA-YTSKSGTSMATPLVAGAAALLRQY 267
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1116-1163 4.57e-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: 4.57e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 24642484 1116 CHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFYADKKRLECM 1163
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 411-660 1.26e-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: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  411 GKGVVVSILDDGIQTNHPDLAQNYDPE--ASFDINGNDSDP---TPQDNGDNKHGTRCAGevAAVAFN-NFCGVGVAYNA 484
Cdd:cd07481    1 GTGIVVANIDTGVDWTHPALKNKYRGWggGSADHDYNWFDPvgnTPLPYDDNGHGTHTMG--TMVGNDgDGQQIGVAPGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  485 SIGGVRMLD---GKVNDVVEAQALSLNPSHI-----------DIYSASWGPEDDGSTVDGPGPLARRAfiygvtsgrqgK 550
Cdd:cd07481   79 RWIACRALDrngGNDADYLRCAQWMLAPTDSagnpadpdlapDVINNSWGGPSGDNEWLQPAVAAWRA-----------A 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  551 GSIFVWASGNGGRYTDSCNCD--GYTNSIFTLSISSATQ-AGFkpwyleecSSTLATTYSS-----GTPGHD-KSVATVD 621
Cdd:cd07481  148 GIFPVFAAGNDGPRCSTLNAPpaNYPESFAVGATDRNDVlADF--------SSRGPSTYGRikpdiSAPGVNiRSAVPGG 219

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 24642484  622 MDGSLrpdhictvehTGTSASAPLAAGICALALEANPEL 660
Cdd:cd07481  220 GYGSS----------SGTSMAAPHVAGVAALLWSANPSL 248
FU smart00261
Furin-like repeats;
1110-1154 1.69e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.52  E-value: 1.69e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642484    1110 DNKCAFCHSTCATCNGPTDQDCITCRSSRYAWQNKCLISCPDGFY 1154
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
1211-1255 2.06e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 57.52  E-value: 2.06e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642484    1211 EGQCRPCHASCGSCNGPADTSCTSCPPNRLLEQSRCVSGCREGFF 1255
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 1165-1482 4.94e-10

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 64.55  E-value: 4.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1165 CQEGCKTCTsNGVCSEclqnwtlnkrdkcIVSGSEGCSES-------EFYSQvEGQCRPCHASCGSCNGPADTSCTSCPP 1237
Cdd:PTZ00214  391 CSESCSGDT-RGVCTK-------------VAEGSESTEVScrcvckpTFYNS-SGTCTPCTDSCAVCKDGTPTGCQQCSP 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1238 NRLLEQS-------RCVSGCRE-------GFFVEAGSLCSPCLHTC---------------SQCVSRTN--CSNCSKGLE 1286
Cdd:PTZ00214  456 GKILEFSivssesaDCVDQCSVgsecaecGITIDGSRYCTRCKDAStypfngvcipntqrdAYCTSTANgaCTTCSGAAF 535

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1287 LQNGECRT-------------------TCADGYY-SDRGICAKCYLSCHTCSGPRRNQCVQCPAGWQL------AAGEC- 1339
Cdd:PTZ00214  536 LMNGGCYTtehypgsticdkqsngkctTTKKGYGiSPDGKLLECDPTCLACTAPGPGRCTRCPSDKLLkrasgaATGSCv 615

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1340 -HPECPEGFYKSDFGCQKCHHY-CKTCNDAGplACTSCPPHSM--LDGGLCM-ECLSSQYYDTTSATCKTCHdsCRSCFG 1414
Cdd:PTZ00214  616 dPGACVDGYYADGDACLPCATPgCKTCGHAS--FCTECAGELFvsLDGQSCLeECTGDKVVGEVSGGVRRCW--CERGFL 691

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1415 PGqFSCKGCVPPLHLDQLNSQCVSC----------------------CQNQTLAEKTSSAACCNCDGET----GECKATS 1468
Cdd:PTZ00214  692 PA-LDRSGCVLPTECPPDMPSCAACdesgrcllcvtsghnvqvdqrtCAEGCGARASSNQGVCMCELDAvltkGVCVPAK 770

                         410
                  ....*....|....
gi 24642484  1469 TGGKRRTVVGSGSA 1482
Cdd:PTZ00214  771 ELAKKRTAAIAGGT 784
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 409-664 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 24642484  409 YTGKGVVVSILDDGIQTNHPDLAQNYDPEASFDINGNDSDptpqdngDNKHGTRCAGEVAAvAFNNFCGVGVAYNASIgg 488
Cdd:cd07480    5 FTGAGVRVAVLDTGIDLTHPAFAGRDITTKSFVGGEDVQD-------GHGHGTHCAGTIFG-RDVPGPRYGVARGAEI-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  489 vrMLDGKVND--------VVEAQALSLNpSHIDIYSASWGPEDDGSTVDG--PGPLARRA----------FIYGVT---- 544
Cdd:cd07480   75 --ALIGKVLGdggggdggILAGIQWAVA-NGADVISMSLGADFPGLVDQGwpPGLAFSRAleayrqrarlFDALMTlvaa 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  545 SGRQGKGSIFVWASGNggrytDScNCDGYTNSIFTLSISSATQAGFKPWYLEECSSTLATTYSSGT------PGHDksVA 618
Cdd:cd07480  152 QAALARGTLIVAAAGN-----ES-QRPAGIPPVGNPAACPSAMGVAAVGALGRTGNFSAVANFSNGevdiaaPGVD--IV 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 24642484  619 TVDMDGSLRPdhictveHTGTSASAPLAAGICALALEANPELTWRD 664
Cdd:cd07480  224 SAAPGGGYRS-------MSGTSMATPHVAGVAALWAEALPKAGGRA 262
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 414-661 2.39e-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: 2.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  414 VVVSILDDGIQTNHPDLA-------QNYDPEASFDINGNDSDPTPQDNGD-NKHGTRCAGEVAAVAFNNfcgvGVAYNAS 485
Cdd:cd07482    2 VTVAVIDSGIDPDHPDLKnsissysKNLVPKGGYDGKEAGETGDINDIVDkLGHGTAVAGQIAANGNIK----GVAPGIG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  486 IGGVRMLD----GKVNDVVEAQALSLNpSHIDIYSASWGP---EDDGSTVDGPGPLA-RRAFIYGvtsgrQGKGSIFVWA 557
Cdd:cd07482   78 IVSYRVFGscgsAESSWIIKAIIDAAD-DGVDVINLSLGGyliIGGEYEDDDVEYNAyKKAINYA-----KSKGSIVVAA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  558 SGNGGRytDSCNCDGYTNsiFTLSISSATQAG---FKPWYLEE---CSST-----LATTYSSG-------TPGHD----K 615
Cdd:cd07482  152 AGNDGL--DVSNKQELLD--FLSSGDDFSVNGevyDVPASLPNvitVSATdnngnLSSFSNYGnsridlaAPGGDflllD 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24642484  616 SVATVDM--DGSLRPDHICTVE-------HTGTSASAPLAAGICALALEANPELT 661
Cdd:cd07482  228 QYGKEKWvnNGLMTKEQILTTApeggyayMYGTSLAAPKVSGALALIIDKNPLKK 282
FU smart00261
Furin-like repeats;
1304-1348 2.83e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 54.05  E-value: 2.83e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642484    1304 RGICAKCYLSCHTCSGPRRNQCVQCPAGWQLAAGECHPECPEGFY 1348
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
VSP pfam03302
Giardia variant-specific surface protein;
1221-1470 2.96e-09

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 61.14  E-value: 2.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1221 CGSCNGPADTSCTSC-PPNRLLEQSRCVSGCREGFFVEAGSlCSPCLHTCSQCvSRTNCSNCSKGLELQngecrtTCADG 1299
Cdd:pfam03302   28 CKACSNDKREVCEECnSNNYLTPTSQCIDDCAKIGNYYYTT-NANNKKICKEC-TVANCKTCEDQGQCQ------ACNDG 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1300 YYSDRGICAKCYLSCHTCSGPRRNQCVQCPAGWQL------AAGECHPECPEGfyKSDFGCQKC------HHYCKTCNDA 1367
Cdd:pfam03302  100 FYKSGDACSPCHESCKTCSGGTASDCTECLTGKALrygndgTKGTCGEGCTTG--TGAGACKTCgltidgTSYCSECATE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1368 GPL----ACTS--------CPPHSMLDgGLCMECLSSQY------YDTTSATCKTCHDScrscfGPGQFSCKGCVPPLHL 1429
Cdd:pfam03302  178 TEYpqngVCTStaaratatCKASSVAN-GMCSSCANGYFrmnggcYETTKFPGKSVCEE-----ANSGGTCQKEAPGYKL 251

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24642484   1430 DQ--------------LNSQCVSCCQNQTLAEKTSS---AACCNCDGETGECKATSTG 1470
Cdd:pfam03302  252 NNgdlvtcspgcktctSNTVCTTCMDGYVKTSDSCTkcdSSCETCTGATTTCKTCATG 309
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 403-706 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 24642484  403 PAWQKG-YTGKGVVVSILDDGIQTNHPDLAQNYDPEA---------------------------SFDINGNDSDPTPQDN 454
Cdd:cd07475    1 PLWDKGgYKGEGMVVAVIDSGVDPTHDAFRLDDDSKAkyseefeakkkkagigygkyynekvpfAYNYADNNDDILDEDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  455 GDNkHGTRCAGEVAAVAFNNFCG---VGVAYNASIGGVRMLDGKV------NDVVEA--QALSLNPshiDIYSASWGped 523
Cdd:cd07475   81 GSS-HGMHVAGIVAGNGDEEDNGegiKGVAPEAQLLAMKVFSNPEggstydDAYAKAieDAVKLGA---DVINMSLG--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  524 DGSTVDGPGPLARRAFIYGVTsgrqgKGSIFVWASGNggrytdscncDGYTNSIFTLSISSATQagfkpwyleecsstla 603
Cdd:cd07475  154 STAGFVDLDDPEQQAIKRARE-----AGVVVVVAAGN----------DGNSGSGTSKPLATNNP---------------- 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  604 TTYSSGTPGHDKSVATV-------------DM----------DGSLRPD------HI-CTVEH------TGTSASAPLAA 647
Cdd:cd07475  203 DTGTVGSPATADDVLTVasankkvpnpnggQMsgfsswgptpDLDLKPDitapggNIySTVNDntygymSGTSMASPHVA 282

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642484  648 GICALALEA----NPELTWRDMQYLVVY----TSRPAPLEKENGwTLNGVKRKyshkfGYGLMDAGA 706
Cdd:cd07475  283 GASALVKQRlkekYPKLSGEELVDLVKNllmnTATPPLDSEDTK-TYYSPRRQ-----GAGLIDVAK 343
Furin-like pfam00757
Furin-like cysteine rich region;
966-1126 6.20e-09

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 56.29  E-value: 6.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    966 ILHSCDAECDSSGCYGRGPTQCVacshyrldntCVSRCPPRSFPNqvGICwpCHDTC-ETCAGAGPDSCLTCapahLHVI 1044
Cdd:pfam00757   11 TMEKCHSCCNNGYCWGPGHCQKV----------CPEQCKKRCTKP--GEC--CHEQClGGCTGPNDSDCLAC----RHFN 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1045 DLAVCLQFCPDGYFENSRnrTCVPCEpncaSCqdhPEYCTSCDHHLVMHEHKCYSACPLDTYETEDNKcafchSTCATCN 1124
Cdd:pfam00757   73 DEGTCVDQCPPGTYQFGW--RCVTFK----EC---PKSHLPGYNPLVIHNGECVRECPSGYTEVENNS-----RKCEPCE 138


                   ..
gi 24642484   1125 GP 1126
Cdd:pfam00757  139 GL 140
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 969-1034 7.67e-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: 55.84  E-value: 7.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484    969 SCDAEC----DSSGCYGRGPTQCVACSHYRLDNTCVSRCP---------PRSFPNQVGICWPCHDTC-ETCAGAGPDSCL 1034
Cdd:pfam14843   53 PCHPEClpqnGTATCSGPGADNCTKCAHFRDGPHCVSSCPsgvlgendlIWKYADANGVCQPCHPNCtQGCTGPGLTGCP 132
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1309-1353 8.83e-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: 8.83e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 24642484 1309 KCYLSCHTCSGPRRNQCVQCPAGWQLAAGECHPECPEGFYKSDFG 1353
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEG 45
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 971-1257 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 24642484   971 DAECDSSGCYG--RGPTQCVACSHYRLDNTCVSRCPPrSFPNQVGICWPCHDTCETCAGAGPDSCLTCAPAhlHVIDLAV 1048
Cdd:PTZ00214  387 DGKSCSESCSGdtRGVCTKVAEGSESTEVSCRCVCKP-TFYNSSGTCTPCTDSCAVCKDGTPTGCQQCSPG--KILEFSI 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1049 CLQFCPDGYFENSRNRTCVPC------EPNCASCQDHPEY-----------------------CTSCDHHLVMHEHKCYS 1099
Cdd:PTZ00214  464 VSSESADCVDQCSVGSECAECgitidgSRYCTRCKDASTYpfngvcipntqrdayctstangaCTTCSGAAFLMNGGCYT 543

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1100 AC--PLDT-----------------YETEDNKCAFCHSTCATCNGPTDQDCITCRSSRY------AWQNKCLI--SCPDG 1152
Cdd:PTZ00214  544 TEhyPGSTicdkqsngkctttkkgyGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKLlkrasgAATGSCVDpgACVDG 623

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1153 FYADKKrlECMPCQE-GCKTCTSNGVCSECLQNWTLNKRDKcivSGSEGCSESEFYSQVEGQCRPCHASCGSCNGPADTS 1231
Cdd:PTZ00214  624 YYADGD--ACLPCATpGCKTCGHASFCTECAGELFVSLDGQ---SCLEECTGDKVVGEVSGGVRRCWCERGFLPALDRSG 698

                         330       340       350
                  ....*....|....*....|....*....|....
gi 24642484  1232 C---TSCPPNRLL-----EQSRCVSGCREGFFVE 1257
Cdd:PTZ00214  699 CvlpTECPPDMPScaacdESGRCLLCVTSGHNVQ 732
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1216-1260 2.45e-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: 2.45e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 24642484 1216 PCHASCGSCNGPADTSCTSCPPNRLLEQSRCVSGCREGFFVEAGS 1260
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEG 45
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 413-661 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 24642484  413 GVVVSILDDGIQTNHPDLAQN-YDPEASfdINGNDSDPTPQDNGDNKHGTRCAGEVAAvafnnfcgvgVAYNASIGGVRM 491
Cdd:cd07492    1 GVRVAVIDSGVDTDHPDLGNLaLDGEVT--IDLEIIVVSAEGGDKDGHGTACAGIIKK----------YAPEAEIGSIKI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  492 L--DGKVNDVVEAQALS-LNPSHIDIYSASWgpeddGSTVDGPGPLARRAFIYGVTSGRqgkgsIFVWASGNGGRYtdsc 568
Cdd:cd07492   69 LgeDGRCNSFVLEKALRaCVENDIRIVNLSL-----GGPGDRDFPLLKELLEYAYKAGG-----IIVAAAPNNNDI---- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  569 ncdGYTNSIFTLSIssatqaGFKpwyleecSSTLATTYSSGTPGHDKSVATVDMDGSLRpdHICTVEHTGTSASAPLAAG 648
Cdd:cd07492  135 ---GTPPASFPNVI------GVK-------SDTADDPKSFWYIYVEFSADGVDIIAPAP--HGRYLTVSGNSFAAPHVTG 196

                        250
                 ....*....|...
gi 24642484  649 ICALALEANPELT 661
Cdd:cd07492  197 MVALLLSEKPDID 209
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 408-708 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 24642484  408 GYTGKGVVVSILDDGIQTnhpdLAQNYDPEASFDI--NGNDSDPTPQDNGDNKHGTRCAGEV------AAVAFNNFCGVG 479
Cdd:cd05562    1 GVDGTGIKIGVISDGFDG----LGDAADDQASGDLpgNVNVLGDLDGGSGGGDEGRAMLEIIhdiapgAELAFHTAGGGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  480 VAYNASIG-----GVRMLdgkVNDV-----------VEAQALSLNPSHIDI-YSASWGPEDDGSTVDGPGplarrafiyg 542
Cdd:cd05562   77 LDFAAAIRalaaaGADII---VDDIgylnepffqdgPIAQAVDEVVASPGVlYFSSAGNDGQSGSIFGHA---------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  543 vtsgrQGKGSIFVWASGNGGRYTDSCNCD--GYTNSIFTLSISSATQAGfkpwyleecssTLATTYSsgtpGHDKSVATV 620
Cdd:cd05562  144 -----AAPGAIAVGAVDYGNTPAFGSDPApgGTPSSFDPVGIRLPTPEV-----------RQKPDVT----APDGVNGTV 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  621 DMDGSLRPDHictvehTGTSASAPLAAGICALALEANPELTWRDMQYLVVYTSRPAPlekENGWTlngvkrkysHKFGYG 700
Cdd:cd05562  204 DGDGDGPPNF------FGTSAAAPHAAGVAALVLSANPGLTPADIRDALRSTALDMG---EPGYD---------NASGSG 265


                 ....*...
gi 24642484  701 LMDAGAMV 708
Cdd:cd05562  266 LVDADRAV 273
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1356-1403 3.41e-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: 3.41e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 24642484 1356 KCHHYCKTCNDAGPLACTSCPPHSMLDGGLCM-ECLSSQYYDTTSATCK 1403
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVsECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
1354-1395 4.02e-08

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 50.97  E-value: 4.02e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 24642484    1354 CQKCHHYCKTCNDAGPLACTSCPPHSMLDGGLCMECLSSQYY 1395
Cdd:smart00261    4 CKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 399-568 2.62e-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: 54.24  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  399 MNVGPAWQK-GYTGKGVVVSILDDGIQTNHPDLAQNydpeaSFDINgndSDPTPQDNGDnkHGTRCAGEVAAVAfNNFCG 477
Cdd:cd04843    2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGN-----GITLI---SGLTDQADSD--HGTAVLGIIVAKD-NGIGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  478 VGVAYNASIG--GVRMLDGKVNDVVEAqALSLNPSHIDIYSASWGPEDDGSTvdgPGPLARRAFIYGVTSGRQGKGSIFV 555
Cdd:cd04843   71 TGIAHGAQAAvvSSTRVSNTADAILDA-ADYLSPGDVILLEMQTGGPNNGYP---PLPVEYEQANFDAIRTATDLGIIVV 146

                        170
                 ....*....|...
gi 24642484  556 WASGNGGRYTDSC 568
Cdd:cd04843  147 EAAGNGGQDLDAP 159
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1017-1067 3.52e-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: 3.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24642484 1017 PCHDTCETCAGAGPDSCLTCapAHLHVIDLAVCLQFCPDGYFENSRNRTCV 1067
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSC--RHGFYLDGGTCVSECPEGTYADTEGGVCL 49
FU smart00261
Furin-like repeats;
1013-1058 4.70e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 47.89  E-value: 4.70e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24642484    1013 GICWPCHDTCETCAGAGPDSCLTCAPAHLHviDLAVCLQFCPDGYF 1058
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 ...
 1269-1347 1.32e-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: 48.58  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1269 CSQCVSRTNCSNCSKGLEL--------QNGECRTTCADGYYSDRGI----CAKC-YLSCHTCSGprRNQCVQCPAGWQLA 1335
Cdd:pfam15913    4 CVLCSEENGCLTCQPRLFLllerngirQYGVCLHSCPPGYFGIRGQevnrCTKCkAENCESCFS--KDFCTKCKEGFYLH 81

                           90
                   ....*....|..
gi 24642484   1336 AGECHPECPEGF 1347
Cdd:pfam15913   82 KGKCLDTCPEGT 93
FU smart00261
Furin-like repeats;
1063-1106 1.47e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 46.35  E-value: 1.47e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642484    1063 NRTCVPCEPNCASCQDH-PEYCTSCDHHLVMHEHKCYSACPLDTY 1106
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 ...
 1022-1105 2.75e-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: 2.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1022 CETCAGAgpDSCLTCAPAHLHVI------DLAVCLQFCPDGYF--ENSRNRTCVPCE-PNCASCQDHpEYCTSCDHHLVM 1092
Cdd:pfam15913    4 CVLCSEE--NGCLTCQPRLFLLLerngirQYGVCLHSCPPGYFgiRGQEVNRCTKCKaENCESCFSK-DFCTKCKEGFYL 80

                           90
                   ....*....|...
gi 24642484   1093 HEHKCYSACPLDT 1105
Cdd:pfam15913   81 HKGKCLDTCPEGT 93
FU smart00261
Furin-like repeats;
1401-1444 7.94e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 44.42  E-value: 7.94e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24642484    1401 TCKTCHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQT 1444
Cdd:smart00261    3 ECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPGT 44
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 411-656 9.11e-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: 9.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  411 GKGVVVSILDDGIQTNHPDLAQ--NYDPEASFDINGN---DSDPTPQ----DNGDNKHGTRCAGEVAAVAFNNFCG---- 477
Cdd:cd07497    1 GEGVVIAIVDTGVDYSHPDLDIygNFSWKLKFDYKAYllpGMDKWGGfyviMYDFFSHGTSCASVAAGRGKMEYNLygyt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  478 -----VGVAYNASIGGVRML------------DGKVNDVVEAQALSLNPSHIDIYSASWGPEDDGSTVDGPGPLARRAFI 540
Cdd:cd07497   81 gkfliRGIAPDAKIAAVKALwfgdviyawlwtAGFDPVDRKLSWIYTGGPRVDVISNSWGISNFAYTGYAPGLDISSLVI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  541 YGVTSgrqGKGSIFVWASGNGGRYTDSCNCDGytNSIFTLSISSATQAGFKPWYLeecssTLATT--------YSSGTPG 612
Cdd:cd07497  161 DALVT---YTGVPIVSAAGNGGPGYGTITAPG--AASLAISVGAATNFDYRPFYL-----FGYLPggsgdvvsWSSRGPS 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24642484  613 HdKSVATVDM--------------------DGSLRPDHIctvehTGTSASAPLAAGICALALEA 656
Cdd:cd07497  231 I-AGDPKPDLaaigafawapgrvldsggalDGNEAFDLF-----GGTSMATPMTAGSAALVISA 288
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 1068-1232 1.37e-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: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1068 PCEPNCASCQ---DHPEYCTSCDHHLVMHEhkCYSACPLDTYE----TEDNKCAFCHSTC------ATCNGPTDQDCITC 1134
Cdd:pfam14843    1 VCDPLCSSEGcwgPGPDQCLSCRNFSRGGT--CVESCNILQGEpreyVVNSTCVPCHPEClpqngtATCSGPGADNCTKC 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1135 RSsrYAWQNKCLISCPDGFYADKkrlecmpcqegcktctsngvcseclqnwtlnkrdkcivsgsegcSESEFYSQVEGQC 1214
Cdd:pfam14843   79 AH--FRDGPHCVSSCPSGVLGEN--------------------------------------------DLIWKYADANGVC 112

                          170
                   ....*....|....*....
gi 24642484   1215 RPCHASC-GSCNGPADTSC 1232
Cdd:pfam14843  113 QPCHPNCtQGCTGPGLTGC 131
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 1073-1162 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 24642484   1073 CASCQDHpEYCTSCDHHL--------VMHEHKCYSACPLDTY---ETEDNKCAFCHS-TCATCngpTDQD-CITCRSSRY 1139
Cdd:pfam15913    4 CVLCSEE-NGCLTCQPRLflllerngIRQYGVCLHSCPPGYFgirGQEVNRCTKCKAeNCESC---FSKDfCTKCKEGFY 79

                           90       100
                   ....*....|....*....|...
gi 24642484   1140 AWQNKCLISCPDGFYADKKRLEC 1162
Cdd:pfam15913   80 LHKGKCLDTCPEGTAAQNSTMEC 102
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 970-1013 1.65e-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: 1.65e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 24642484  970 CDAECDssGCYGRGPTQCVACSHYRL--DNTCVSRCPPRSFPNQVG 1013
Cdd:cd00064    2 CHPSCA--TCTGPGPDQCTSCRHGFYldGGTCVSECPEGTYADTEG 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1068-1112 1.95e-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: 1.95e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 24642484 1068 PCEPNCASCQDH-PEYCTSCDHHLVMHEHKCYSACPLDTYETEDNK 1112
Cdd:cd00064    1 PCHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGG 46
FU smart00261
Furin-like repeats;
968-1008 5.83e-05

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 42.11  E-value: 5.83e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 24642484     968 HSCDAECdsSGCYGRGPTQCVACSHYR--LDNTCVSRCPPRSF 1008
Cdd:smart00261    5 KPCHPEC--ATCTGPGPDDCTSCKHGFflDGGKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
1259-1301 1.24e-04

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 40.96  E-value: 1.24e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 24642484    1259 GSLCSPCLHTCSQCVSR--TNCSNCSKGLELQNGECRTTCADGYY 1301
Cdd:smart00261    1 DGECKPCHPECATCTGPgpDDCTSCKHGFFLDGGKCVSECPPGTY 45
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 1289-1459 2.15e-04

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 46.06  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1289 NGECRTTCADGYYSDRGICAKC---YL-----SC-HTCSGPRRNQCVQCPAGWQLAAGECHPECPEGFYKSDFGCQKCHH 1359
Cdd:PTZ00214  358 NGGVSGCATCGYNSGAVTCTRCsagYLgvdgkSCsESCSGDTRGVCTKVAEGSESTEVSCRCVCKPTFYNSSGTCTPCTD 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  1360 YCKTCNDAGPLACTSCPPHSMLDGGLC----MECLSSQYYDTTSATCKTCHDSCRSCfgpgqFSCKGCvpplHLDQLNSQ 1435
Cdd:PTZ00214  438 SCAVCKDGTPTGCQQCSPGKILEFSIVssesADCVDQCSVGSECAECGITIDGSRYC-----TRCKDA----STYPFNGV 508

                         170       180
                  ....*....|....*....|....
gi 24642484  1436 CVSCCQNQTLAEKTSSAACCNCDG 1459
Cdd:PTZ00214  509 CIPNTQRDAYCTSTANGACTTCSG 532
Furin-like pfam00757
Furin-like cysteine rich region;
1063-1154 2.34e-04

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 43.19  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1063 NRTCVPCEPN----CASCQdHPEYCTSCDHHLVMHEHKCYSACpldtyeTEDNKCafCHSTCA-TCNGPTDQDCITCRSS 1137
Cdd:pfam00757    1 NRECGDVCPGtmekCHSCC-NNGYCWGPGHCQKVCPEQCKKRC------TKPGEC--CHEQCLgGCTGPNDSDCLACRHF 71

                           90
                   ....*....|....*..
gi 24642484   1138 RYawQNKCLISCPDGFY 1154
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 ...
 1214-1305 3.71e-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: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1214 CRPChASCGSCNGpadtsCTSCPP--------NRLLEQSRCVSGCREGFFVEAG---SLCSPC-LHTCSQCVSRTNCSNC 1281
Cdd:pfam15913    1 CSGC-VLCSEENG-----CLTCQPrlflllerNGIRQYGVCLHSCPPGYFGIRGqevNRCTKCkAENCESCFSKDFCTKC 74

                           90       100
                   ....*....|....*....|....
gi 24642484   1282 SKGLELQNGECRTTCADGYYSDRG 1305
Cdd:pfam15913   75 KEGFYLHKGKCLDTCPEGTAAQNS 98
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1405-1451 4.44e-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: 4.44e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 24642484 1405 CHDSCRSCFGPGQFSCKGCVPPLHLDqlNSQCVSCCQNQTLAEKTSS 1451
Cdd:cd00064    2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCVSECPEGTYADTEGG 46
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 1317-1416 4.67e-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: 41.98  E-value: 4.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   1317 CSGPRRNQCVQCpAGWQLaAGECHPECP-----EGFYKSDFGCQKCHHYCK------TCNDAGPLACTSCpPHSMlDGGL 1385
Cdd:pfam14843   11 CWGPGPDQCLSC-RNFSR-GGTCVESCNilqgePREYVVNSTCVPCHPECLpqngtaTCSGPGADNCTKC-AHFR-DGPH 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 24642484   1386 CME-CLSSQY--------YDTTSATCKTCHDSC-RSCFGPG 1416
Cdd:pfam14843   87 CVSsCPSGVLgendliwkYADANGVCQPCHPNCtQGCTGPG 127
Peptidases_S8_CspA-like cd07478
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
 409-562 6.38e-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: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  409 YTGKGVVVSILDDGIQTNHP---------------DLAQNYDPEASFDING-----------------NDSDPTPQDNGd 456
Cdd:cd07478    1 LTGKGVLVGIIDTGIDYLHPefrnedgttrilyiwDQTIPGGPPPGGYYGGgeyteeiinaalasdnpYDIVPSRDENG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  457 nkHGTRCAGEVAAVAFNNFCGVGVAYNASIGGVRMLDGK--------------VNDVVEA------QALSLN-PSHIDIy 515
Cdd:cd07478   80 --HGTHVAGIAAGNGDNNPDFKGVAPEAELIVVKLKQAKkylrefyedvpfyqETDIMLAikylydKALELNkPLVINI- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24642484  516 saSWGpEDDGSTvDGPGPLARraFIYGVTSGRqgkGSIFVWASGNGG 562
Cdd:cd07478  157 --SLG-TNFGSH-DGTSLLER--YIDAISRLR---GIAVVVGAGNEG 194
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 416-499 8.03e-04

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 44.19  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484   416 VSILDDGIQTNHPDLAQNYDPEASF---------DINGN----------DSDPTPQDngDNKHGTRCAGEVAAVAFNNFC 476
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIDVNVKElhgrkgiddDNNGNvddeyganfvNNDGGPMD--DNYHGTHVSGIISAIGNNNIG 397

                          90       100
                  ....*....|....*....|....*..
gi 24642484   477 GVGVAYNASIGGVRMLD----GKVNDV 499
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 ...
 405-486 3.58e-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: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642484  405 WQKGYTGKGVVVSILDDGIQTNHPDLAQNYDpeasfdingnDSDPTPQDNGDNK--HGTRCAGEVAAVafNNFCgVGVAY 482
Cdd:cd07479    1 WQLGYTGAGVKVAVFDTGLAKDHPHFRNVKE----------RTNWTNEKTLDDGlgHGTFVAGVIASS--REQC-LGFAP 67


                 ....
gi 24642484  483 NASI 486
Cdd:cd07479   68 DAEI 71
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 1264-1303 4.40e-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: 4.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 24642484 1264 PCLHTCSQCVSR--TNCSNCSKGLELQNGECRTTCADGYYSD 1303
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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