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Conserved domains on  [gi|569006570|ref|XP_006526824|]
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proprotein convertase subtilisin/kexin type 5 isoform X5 [Mus musculus]

Protein Classification

S8 family peptidase( domain architecture ID 13872813)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
 128-422 1.75e-165

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: 488.22  E-value: 1.75e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  128 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 206
Cdd:cd04059     1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  207 DasNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGP 286
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  287 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 365
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569006570  366 SYDKKIITTDLR--QRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd04059   239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 507-597 5.44e-39

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


:

Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 139.33  E-value: 5.44e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   507 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 586
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75

                           90
                   ....*....|.
gi 569006570   587 PGKLKEWSLVL 597
Cdd:pfam01483   76 TGTLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 40-116 3.61e-37

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


:

Pssm-ID: 465126  Cd Length: 77  Bit Score: 133.88  E-value: 3.61e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006570    40 HWAVKIAGGFAEADRIASKYGFINVGQIGALKDYYHFYHSRTIKRSVLSSRGTHSFISMEPKVEWIQQQVVKKRTKR 116
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 ...
 637-746 1.64e-12

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: 65.47  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   637 PCDPECSEVGCDGPGPDHCSDCLHYyyklkNNTRICVSSCP-----PGHYhADKKRCRKCAPNCE------SCFGSHGNQ 705
Cdd:pfam14843    1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNilqgePREY-VVNSTCVPCHPECLpqngtaTCSGPGADN 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 569006570   706 CLSCKYgyflNEETSSCVTQCPDGSYEDI--------KKNVCGKCSENC 746
Cdd:pfam14843   75 CTKCAH----FRDGPHCVSSCPSGVLGENdliwkyadANGVCQPCHPNC 119
VSP super family cl31427
Giardia variant-specific surface protein;
674-959 8.88e-11

Giardia variant-specific surface protein;


The actual alignment was detected with superfamily member pfam03302:

Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 64.99  E-value: 8.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   674 SSCPPGH-YHADKKRCRKCAP----NCESCFGSHGNQCLSCKYGYFLNEeTSSCVTQCpdgsyEDIKKNVCGKCSENCKA 748
Cdd:pfam03302    2 DECKPGYeLSADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYLTP-TSQCIDDC-----AKIGNYYYTTNANNKKI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   749 CIGFH--NCTECKGGLSLQgsrcsvTCEDGQFFNGHDCQPCHRFCATCSGAGADGCINCTEGYVME------EGRCVQSC 820
Cdd:pfam03302   76 CKECTvaNCKTCEDQGQCQ------ACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALRygndgtKGTCGEGC 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   821 SVSYYLDHSSE-----GGYKSCKRCDNS----------------CLTCNGPGFKN--CSSCPSGYLLDLGTC-------- 869
Cdd:pfam03302  150 TTGTGAGACKTcgltiDGTSYCSECATEteypqngvctstaaraTATCKASSVANgmCSSCANGYFRMNGGCyettkfpg 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   870 -------QMGAICKDGE--YIDDQGHCQTCEASCAKCWGPTqeDCISCPVTRVLDDGRCVMNCPSWkfefkKQCHPCHYT 940
Cdd:pfam03302  230 ksvceeaNSGGTCQKEApgYKLNNGDLVTCSPGCKTCTSNT--VCTTCMDGYVKTSDSCTKCDSSC-----ETCTGATTT 302

                          330       340
                   ....*....|....*....|....*
gi 569006570   941 CQGC------QGSGPSNCTSCRADK 959
Cdd:pfam03302  303 CKTCatgyykSGTGCVSCTSSESDN 327
 
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 ...
 128-422 1.75e-165

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: 488.22  E-value: 1.75e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  128 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 206
Cdd:cd04059     1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  207 DasNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGP 286
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  287 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 365
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569006570  366 SYDKKIITTDLR--QRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd04059   239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 164-447 2.61e-66

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


Pssm-ID: 395035 [Multi-domain]  Cd Length: 287  Bit Score: 225.03  E-value: 2.61e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNG----NDLDPMPRYDASNENKHGTRCAGEVAATANNSHCTVGIAFNA 239
Cdd:pfam00082    1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEAsvdfNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   240 KIGGVRML-DGDVTDMVEAKSVSYN-PQHVHIYSASWGPDddgKTVDGPAPLTRQAFENGvrmGRRGLGSVFVWASGNGG 317
Cdd:pfam00082   81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   318 RSKDHCSCDGY-TNSIYTISISSTaesgkkpwylEECSSTLATTYSS----------------GESY-------DKKIIT 373
Cdd:pfam00082  155 PGGNNGSSVGYpAQYKNVIAVGAV----------DEASEGNLASFSSygptldgrlkpdivapGGNItggnissTLLTTT 224

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006570   374 TDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNAndwktnaagfkVSHLYGFG 447
Cdd:pfam00082  225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAG-----------LDRLFGYG 287
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 507-597 5.44e-39

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


Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 139.33  E-value: 5.44e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   507 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 586
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75

                           90
                   ....*....|.
gi 569006570   587 PGKLKEWSLVL 597
Cdd:pfam01483   76 TGTLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 40-116 3.61e-37

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


Pssm-ID: 465126  Cd Length: 77  Bit Score: 133.88  E-value: 3.61e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006570    40 HWAVKIAGGFAEADRIASKYGFINVGQIGALKDYYHFYHSRTIKRSVLSSRGTHSFISMEPKVEWIQQQVVKKRTKR 116
Cdd:pfam16470    1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 156-422 1.65e-34

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 138.31  E-value: 1.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  156 GAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCdVNGNDldpmpryDASNENKHGTRCAGEVAATANNSHCTVGI 235
Cdd:COG1404   100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDF-VDGDG-------DPSDDNGHGTHVAGIIAANGNNGGGVAGV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  236 AFNAKIGGVRMLD----GDVTDMVEA--KSVSynpQHVHIYSASWGPDDDGKTvdgpaPLTRQAFENGvrmgrRGLGSVF 309
Cdd:COG1404   172 APGAKLLPVRVLDdngsGTTSDIAAAidWAAD---NGADVINLSLGGPADGYS-----DALAAAVDYA-----VDKGVLV 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  310 VWASGNGGRSkdhCSCDGYTNSIY-TISISSTAESGKKPWYleecSSTlattyssGESYD-----KKIITTDLRQRcTDN 383
Cdd:COG1404   239 VAAAGNSGSD---DATVSYPAAYPnVIAVGAVDANGQLASF----SNY-------GPKVDvaapgVDILSTYPGGG-YAT 303

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 569006570  384 HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:COG1404   304 LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTAT 342
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 508-599 2.88e-18

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: 90.27  E-value: 2.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  508 EHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLfdHSMEGFkNWEFMTIHCWGERAAGDWVLEVYDTPSQlrnfkTP 587
Cdd:COG4935   558 EDVTVTVDITHTYRGDLVITLISPDGTTVVLKNRSG--GSADNI-NATFDVANFSGESANGTWTLRVVDTAGG-----DT 629

                          90
                  ....*....|..
gi 569006570  588 GKLKEWSLVLYG 599
Cdd:COG4935   630 GTLNSWSLTFTG 641
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 637-746 1.64e-12

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: 65.47  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   637 PCDPECSEVGCDGPGPDHCSDCLHYyyklkNNTRICVSSCP-----PGHYhADKKRCRKCAPNCE------SCFGSHGNQ 705
Cdd:pfam14843    1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNilqgePREY-VVNSTCVPCHPECLpqngtaTCSGPGADN 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 569006570   706 CLSCKYgyflNEETSSCVTQCPDGSYEDI--------KKNVCGKCSENC 746
Cdd:pfam14843   75 CTKCAH----FRDGPHCVSSCPSGVLGENdliwkyadANGVCQPCHPNC 119
VSP pfam03302
Giardia variant-specific surface protein;
674-959 8.88e-11

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 64.99  E-value: 8.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   674 SSCPPGH-YHADKKRCRKCAP----NCESCFGSHGNQCLSCKYGYFLNEeTSSCVTQCpdgsyEDIKKNVCGKCSENCKA 748
Cdd:pfam03302    2 DECKPGYeLSADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYLTP-TSQCIDDC-----AKIGNYYYTTNANNKKI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   749 CIGFH--NCTECKGGLSLQgsrcsvTCEDGQFFNGHDCQPCHRFCATCSGAGADGCINCTEGYVME------EGRCVQSC 820
Cdd:pfam03302   76 CKECTvaNCKTCEDQGQCQ------ACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALRygndgtKGTCGEGC 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   821 SVSYYLDHSSE-----GGYKSCKRCDNS----------------CLTCNGPGFKN--CSSCPSGYLLDLGTC-------- 869
Cdd:pfam03302  150 TTGTGAGACKTcgltiDGTSYCSECATEteypqngvctstaaraTATCKASSVANgmCSSCANGYFRMNGGCyettkfpg 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   870 -------QMGAICKDGE--YIDDQGHCQTCEASCAKCWGPTqeDCISCPVTRVLDDGRCVMNCPSWkfefkKQCHPCHYT 940
Cdd:pfam03302  230 ksvceeaNSGGTCQKEApgYKLNNGDLVTCSPGCKTCTSNT--VCTTCMDGYVKTSDSCTKCDSSC-----ETCTGATTT 302

                          330       340
                   ....*....|....*....|....*
gi 569006570   941 CQGC------QGSGPSNCTSCRADK 959
Cdd:pfam03302  303 CKTCatgyykSGTGCVSCTSSESDN 327
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 169-413 1.59e-09

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 61.91  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  169 VTILDDGIERTHPDLMQNY---------------------DALASCDVNGNDLDPMprydasNENKHGTRCAGEVAATAN 227
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM------DDNYHGTHVSGIISAIGN 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  228 NSHCTVGIAFNAKIGGVRMLD----GDVTDMVeaKSVSY-NPQHVHIYSASWGPDDDGKTvdgpapltrqaFENGVRMGR 302
Cdd:PTZ00262  394 NNIGIVGVDKRSKLIICKALDshklGRLGDMF--KCFDYcISREAHMINGSFSFDEYSGI-----------FNESVKYLE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  303 RgLGSVFVWASGN----GGRSKDHCSCDGYTNSIYTISISSTAES---------GKKPWYLEECSSTLATTYSSGESYDK 369
Cdd:PTZ00262  461 E-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYPPILSKKLRNvitvsnlikDKNNQYSLSPNSFYSAKYCQLAAPGT 539

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 569006570  370 KIITTDLRQRCTDNhTGTSASAPMAAGIIALALEANPFLTWRDV 413
Cdd:PTZ00262  540 NIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
FU smart00261
Furin-like repeats;
781-825 3.47e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 53.28  E-value: 3.47e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 569006570    781 GHDCQPCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYY 825
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 690-739 1.93e-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: 1.93e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 569006570  690 KCAPNCESCFGSHGNQCLSCKYGYFLNEETssCVTQCPDGSYEDIKKNVC 739
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGT--CVSECPEGTYADTEGGVC 48
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 786-827 3.34e-08

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 50.60  E-value: 3.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 569006570  786 PCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYYLD 827
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 712-1006 3.68e-08

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 57.62  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  712 GYFLNEETSSCVTQCPDGSYEDiKKNVCGKCSENC---------KACIGFHN--CTECKGGLSLQGSRCSVTCEDGQFFN 780
Cdd:PTZ00214  350 GYLCGDATNGGVSGCATCGYNS-GAVTCTRCSAGYlgvdgkscsESCSGDTRgvCTKVAEGSESTEVSCRCVCKPTFYNS 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  781 GHDCQPCHRFCATCSGAGADGCINCTEGYVM-------EEGRCVQSCSVSyylDHSSE-----GGYKSCKRC-DNSCLTC 847
Cdd:PTZ00214  429 SGTCTPCTDSCAVCKDGTPTGCQQCSPGKILefsivssESADCVDQCSVG---SECAEcgitiDGSRYCTRCkDASTYPF 505

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  848 NGPGFKNcsscpsgylldlgtCQMGAICKDGEyiddQGHCQTCEASCAKCWGP--TQEDCISCPVTRVLDDGRCVMNCPS 925
Cdd:PTZ00214  506 NGVCIPN--------------TQRDAYCTSTA----NGACTTCSGAAFLMNGGcyTTEHYPGSTICDKQSNGKCTTTKKG 567

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  926 WKFEFKKQCHPCHYTCQGCQGSGPSNCTSCRADK-HGQERFLYHGECLE-NCPVGHYPAKGHACLPCPD-NCELCYNPHV 1002
Cdd:PTZ00214  568 YGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKlLKRASGAATGSCVDpGACVDGYYADGDACLPCATpGCKTCGHASF 647


                  ....
gi 569006570 1003 CSRC 1006
Cdd:PTZ00214  648 CTEC 651
FU smart00261
Furin-like repeats;
685-731 2.30e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 48.27  E-value: 2.30e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 569006570    685 KKRCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETssCVTQCPDGSY 731
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGK--CVSECPPGTY 45
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
687-822 2.99e-05

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 47.71  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  687 RCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETSSCVTQCPDGSYEDIKKNVCGKCSENCKACIGFHNCTECKGGLSLQG 766
Cdd:COG4624     2 LLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006570  767 SRCSVTCEDGqffNGHDCQPCHRFCATCSGAGADG--------CINCtegyvmeeGRCVQSCSV 822
Cdd:COG4624    82 RGPSIIRDKE---KCKNCYPCVRACPVKAIKVDDGkaeideekCISC--------GQCVAVCPF 134
 
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 ...
 128-422 1.75e-165

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: 488.22  E-value: 1.75e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  128 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 206
Cdd:cd04059     1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  207 DasNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGP 286
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  287 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 365
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569006570  366 SYDKKIITTDLR--QRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd04059   239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 164-447 2.61e-66

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


Pssm-ID: 395035 [Multi-domain]  Cd Length: 287  Bit Score: 225.03  E-value: 2.61e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNG----NDLDPMPRYDASNENKHGTRCAGEVAATANNSHCTVGIAFNA 239
Cdd:pfam00082    1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEAsvdfNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   240 KIGGVRML-DGDVTDMVEAKSVSYN-PQHVHIYSASWGPDddgKTVDGPAPLTRQAFENGvrmGRRGLGSVFVWASGNGG 317
Cdd:pfam00082   81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   318 RSKDHCSCDGY-TNSIYTISISSTaesgkkpwylEECSSTLATTYSS----------------GESY-------DKKIIT 373
Cdd:pfam00082  155 PGGNNGSSVGYpAQYKNVIAVGAV----------DEASEGNLASFSSygptldgrlkpdivapGGNItggnissTLLTTT 224

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006570   374 TDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNAndwktnaagfkVSHLYGFG 447
Cdd:pfam00082  225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAG-----------LDRLFGYG 287
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 507-597 5.44e-39

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


Pssm-ID: 460225 [Multi-domain]  Cd Length: 86  Bit Score: 139.33  E-value: 5.44e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   507 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 586
Cdd:pfam01483    1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75

                           90
                   ....*....|.
gi 569006570   587 PGKLKEWSLVL 597
Cdd:pfam01483   76 TGTLNSWQLTL 86
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 40-116 3.61e-37

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


Pssm-ID: 465126  Cd Length: 77  Bit Score: 133.88  E-value: 3.61e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006570    40 HWAVKIAGGFAEADRIASKYGFINVGQIGALKDYYHFYHSRTIKRSVLSSRGTHSFISMEPKVEWIQQQVVKKRTKR 116
Cdd:pfam16470    1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 167-420 1.14e-35

Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173822 [Multi-domain]  Cd Length: 242  Bit Score: 135.93  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  167 IVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPmprydaSNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRM 246
Cdd:cd07498     1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPT------SDIDGHGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  247 LDGD--VTDMVEAKSVSYNPQH-VHIYSASWGPDDdgktvdgPAPLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDhc 323
Cdd:cd07498    75 ADSLgyAYWSDIAQAITWAADNgADVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLFAAGNSGRSVS-- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  324 scDGYTNSIYTISISSTAESGKKPWY--------LEECSSTLATTYSSGESydkkiiTTDLRQRCTDNHTGTSASAPMAA 395
Cdd:cd07498   146 --SGYAANPSVIAVAATDSNDARASYsnygnyvdLVAPGVGIWTTGTGRGS------AGDYPGGGYGSFSGTSFASPVAA 217

                         250       260
                  ....*....|....*....|....*
gi 569006570  396 GIIALALEANPFLTWRDVQHVIVRT 420
Cdd:cd07498   218 GVAALILSANPNLTPAEVEDILTST 242
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 156-422 1.65e-34

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 138.31  E-value: 1.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  156 GAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCdVNGNDldpmpryDASNENKHGTRCAGEVAATANNSHCTVGI 235
Cdd:COG1404   100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDF-VDGDG-------DPSDDNGHGTHVAGIIAANGNNGGGVAGV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  236 AFNAKIGGVRMLD----GDVTDMVEA--KSVSynpQHVHIYSASWGPDDDGKTvdgpaPLTRQAFENGvrmgrRGLGSVF 309
Cdd:COG1404   172 APGAKLLPVRVLDdngsGTTSDIAAAidWAAD---NGADVINLSLGGPADGYS-----DALAAAVDYA-----VDKGVLV 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  310 VWASGNGGRSkdhCSCDGYTNSIY-TISISSTAESGKKPWYleecSSTlattyssGESYD-----KKIITTDLRQRcTDN 383
Cdd:COG1404   239 VAAAGNSGSD---DATVSYPAAYPnVIAVGAVDANGQLASF----SNY-------GPKVDvaapgVDILSTYPGGG-YAT 303

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 569006570  384 HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:COG1404   304 LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTAT 342
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 167-420 3.92e-30

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: 120.00  E-value: 3.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  167 IVVTILDDGIERTHPDLmqnyDALASCDVNGNDLDPMPRY--DASNENKHGTRCAGEVAATANNSHCtVGIAFNAKIGGV 244
Cdd:cd00306     1 VTVAVIDTGVDPDHPDL----DGLFGGGDGGNDDDDNENGptDPDDGNGHGTHVAGIIAASANNGGG-VGVAPGAKLIPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  245 RMLD----GDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGktvdgPAPLTRQAFENGVRMgrrgLGSVFVWASGNGGRSK 320
Cdd:cd00306    76 KVLDgdgsGSSSDIAAAIDYAAADQGADVINLSLGGPGSP-----PSSALSEAIDYALAK----LGVLVVAAAGNDGPDG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  321 DHCScDGYTNSIYTISISSTAESGKKPWYLEeCSSTLATTYSSGESYdkkIITTDLRQRCTDNHTGTSASAPMAAGIIAL 400
Cdd:cd00306   147 GTNI-GYPAASPNVIAVGAVDRDGTPASPSS-NGGAGVDIAAPGGDI---LSSPTTGGGGYATLSGTSMAAPIVAGVAAL 221

                         250       260
                  ....*....|....*....|
gi 569006570  401 ALEANPFLTWRDVQHVIVRT 420
Cdd:cd00306   222 LLSANPDLTPAQVKAALLST 241
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 165-422 4.63e-27

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: 111.52  E-value: 4.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  165 KNIVVTILDDGIERTHPDLMQNY--DALASC-------------DVNG-----NDLDPMPrydasnENKHGTRCAGEVAA 224
Cdd:cd07473     2 GDVVVAVIDTGVDYNHPDLKDNMwvNPGEIPgngidddgngyvdDIYGwnfvnNDNDPMD------DNGHGTHVAGIIGA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  225 TANNSHCTVGIAFNAKIGGVRMLD----GDVTDMVEA--KSVSYNpqhVHIYSASWGPdddgktvDGPAPLTRQAFEngv 298
Cdd:cd07473    76 VGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAidYAVDMG---AKIINNSWGG-------GGPSQALRDAIA--- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  299 RMGRRGLgsVFVWASGNGGRSKDH-----CScdgYTNSiYTISISSTAESGKKPWYleecSSTLATT---YSSGESydkk 370
Cdd:cd07473   143 RAIDAGI--LFVAAAGNDGTNNDKtptypAS---YDLD-NIISVAATDSNDALASF----SNYGKKTvdlAAPGVD---- 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569006570  371 IITTDLRQRcTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07473   209 ILSTSPGGG-YGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 129-422 1.08e-21

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: 95.79  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  129 NDPKWPSMWYMHcsdnthpcqsDMNIEGAWKRGyTGKNIVVTILDDGIERTHPDLM-----QNYDAlascdVNGNDldpm 203
Cdd:cd07484     3 NDPYYSYQWNLD----------QIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLLkvkfvLGYDF-----VDNDS---- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  204 pryDASNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLD----GDVTDMVEAksvsynpqhvhIYsasWGPDDD 279
Cdd:cd07484    63 ---DAMDDNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANG-----------IR---YAADKG 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  280 GKTVD---GpAPLTRQAFENGVRMGRRGlGSVFVWASGNGGRSKdhCScdgYTNSI-YTISISSTAESGKKPWYleecss 355
Cdd:cd07484   126 AKVINlslG-GGLGSTALQEAINYAWNK-GVVVVAAAGNEGVSS--VS---YPAAYpGAIAVAATDQDDKRASF------ 192

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006570  356 tlaTTYSS-------GESydkkIITTDLRQRcTDNHTGTSASAPMAAGIIALALEANPfLTWRDVQHVIVRTSR 422
Cdd:cd07484   193 ---SNYGKwvdvsapGGG----ILSTTPDGD-YAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDALKKTAD 257
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 163-422 1.47e-21

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: 95.47  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  163 TGKNIVVTILDDGIERTHPDLMQNYDALAScdvNGNDLDPMPRYDASNENkHGTRCAGEVAATANNSHcTVGIAFNAKIG 242
Cdd:cd04848     1 TGAGVKVGVIDSGIDLSHPEFAGRVSEASY---YVAVNDAGYASNGDGDS-HGTHVAGVIAAARDGGG-MHGVAPDATLY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  243 GVRMLDGDVTdmveAKSVSYNPQH--------VHIYSASWGPDDDGKTVDGPAPL---TRQAFENGVRMGRRGLGSVFVW 311
Cdd:cd04848    76 SARASASAGS----TFSDADIAAAydflaasgVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVF 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  312 ASGNGGRSKDhcscDGYTNSIY--------------------TISISSTAESGK--KPWYLeecsST-----LATTYSSG 364
Cdd:cd04848   152 AAGNDGQANP----SLAAAALPylepeleggwiavvavdpngTIASYSYSNRCGvaANWCL----AApgeniYSTDPDGG 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569006570  365 ESYDKKIittdlrqrctdnhtGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd04848   224 NGYGRVS--------------GTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTAT 267
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 166-409 4.45e-21

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: 94.67  E-value: 4.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  166 NIVVTILDDGIeRTHPDLMQN-----YD----ALASCDVNGNDLDP----------------MPRYDASNENKHGTRCAG 220
Cdd:cd07496     1 GVVVAVLDTGV-LFHHPDLAGvllpgYDfisdPAIANDGDGRDSDPtdpgdwvtgddvppggFCGSGVSPSSWHGTHVAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  221 EVAATANNSHCTVGIAFNAKIGGVRML---DGDVTDMVEA---------KSVSYNPQHVHIYSASWGPDddgktvdGPAP 288
Cdd:cd07496    80 TIAAVTNNGVGVAGVAWGARILPVRVLgkcGGTLSDIVDGmrwaaglpvPGVPVNPNPAKVINLSLGGD-------GACS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  289 LTRQAFENGVRmgrrGLGSVFVWASGNGGRSKDH---CSCDGytnsiyTISISSTAESGKKPWYLE------------EC 353
Cdd:cd07496   153 ATMQNAINDVR----ARGVLVVVAAGNEGSSASVdapANCRG------VIAVGATDLRGQRASYSNygpavdvsapggDC 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006570  354 SSTL---------ATTYSSGE-SYDkkiittdlrqrctdNHTGTSASAPMAAGIIALALEANPFLT 409
Cdd:cd07496   223 ASDVngdgypdsnTGTTSPGGsTYG--------------FLQGTSMAAPHVAGVAALMKSVNPSLT 274
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 157-406 3.74e-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: 88.70  E-value: 3.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  157 AWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALA-SCDVNGNDLDPMPRYDA---SNENKHGTRCAGEVAATANNSHCT 232
Cdd:cd07485     2 AWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGyDPAVNGYNFVPNVGDIDndvSVGGGHGTHVAGTIAAVNNNGGGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  233 VGIAFN------AKIGGVRMLDGD--VTDMVEAKSVSYNPQH-VHIYSASWGpdddGKTVDGPAPLTRQAFENGVRMGRR 303
Cdd:cd07485    82 GGIAGAggvapgVKIMSIQIFAGRyyVGDDAVAAAIVYAADNgAVILQNSWG----GTGGGIYSPLLKDAFDYFIENAGG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  304 GL--GSVFVWASGNGGRSKDH--CSCDGytnsiyTISISSTAESGKKPWYleecsSTLATTYSSGESYDKKIITTDLRQR 379
Cdd:cd07485   158 SPldGGIVVFSAGNSYTDEHRfpAAYPG------VIAVAALDTNDNKASF-----SNYGRWVDIAAPGVGTILSTVPKLD 226

                         250       260       270
                  ....*....|....*....|....*....|..
gi 569006570  380 CTDNHT-----GTSASAPMAAGIIALALEANP 406
Cdd:cd07485   227 GDGGGNyeylsGTSMAAPHVSGVAALVLSKFP 258
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 164-420 1.68e-18

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: 86.49  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMprYDasnENKHGTRCAGEVAATANNSHCTV-GIAFNAKIG 242
Cdd:cd07487     1 GKGITVAVLDTGIDAPHPDFDGRIIRFADFVNTVNGRTTP--YD---DNGHGTHVAGIIAGSGRASNGKYkGVAPGANLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  243 GVRMLD----GDVTDMVEAksVSY-----NPQHVHIYSASWG-PDDDGktvDGPAPLtRQAFENGVRMgrrglGSVFVWA 312
Cdd:cd07487    76 GVKVLDdsgsGSESDIIAG--IDWvvennEKYNIRVVNLSLGaPPDPS---YGEDPL-CQAVERLWDA-----GIVVVVA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  313 SGNGGRSKDHCSCDGytNSIYTISISSTAESGKKPWYLEECSS---TL-----------ATTYSSGESYDKKIITTDLRQ 378
Cdd:cd07487   145 AGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSSrgpTGdgrikpdvvapGENIVSCRSPGGNPGAGVGSG 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 569006570  379 RCTDnhTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRT 420
Cdd:cd07487   223 YFEM--SGTSMATPHVSGAIALLLQANPILTPDEVKCILRDT 262
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 508-599 2.88e-18

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: 90.27  E-value: 2.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  508 EHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLfdHSMEGFkNWEFMTIHCWGERAAGDWVLEVYDTPSQlrnfkTP 587
Cdd:COG4935   558 EDVTVTVDITHTYRGDLVITLISPDGTTVVLKNRSG--GSADNI-NATFDVANFSGESANGTWTLRVVDTAGG-----DT 629

                          90
                  ....*....|..
gi 569006570  588 GKLKEWSLVLYG 599
Cdd:COG4935   630 GTLNSWSLTFTG 641
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 166-420 5.47e-18

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: 84.12  E-value: 5.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  166 NIVVTILDDGIERTHPDLMQNYdalascdVNGNDLDPMPRYDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKIGGVR 245
Cdd:cd07477     1 GVKVAVIDTGIDSSHPDLKLNI-------VGGANFTGDDNNDYQDGNGHGTHVAGIIAALDNGVG-VVGVAPEADLYAVK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  246 MLD----GDVTDMVEAKSVSYNpQHVHIYSASWGpdddgktVDGPAPLTRQAFENGVrmgRRGLgsVFVWASGNggrskd 321
Cdd:cd07477    73 VLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLG-------GPSDSPALREAIKKAY---AAGI--LVVAAAGN------ 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  322 hcscDGYTNSIYT--------ISISSTAESGKKpwyleecsstlaTTYSS----------GESydkkIITTDLRQRCTDN 383
Cdd:cd07477   134 ----SGNGDSSYDypakypsvIAVGAVDSNNNR------------ASFSStgpevelaapGVD----ILSTYPNNDYAYL 193

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 569006570  384 hTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRT 420
Cdd:cd07477   194 -SGTSMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 159-404 6.59e-15

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: 76.60  E-value: 6.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  159 KRGYTGKNIVVTILDDGIERTHPDLMqnydalascDVNGNDLDPMPR----YDASNENK-----HGTRCAGEVAATANNS 229
Cdd:cd04842     1 GLGLTGKGQIVGVADTGLDTNHCFFY---------DPNFNKTNLFHRkivrYDSLSDTKddvdgHGTHVAGIIAGKGNDS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  230 HCTV---GIAFNAKIGGVRM------------LDGDVTDMVEAKSvsynpqhvHIYSASWGPDDDG------KTVDgpap 288
Cdd:cd04842    72 SSISlykGVAPKAKLYFQDIgdtsgnlssppdLNKLFSPMYDAGA--------RISSNSWGSPVNNgytllaRAYD---- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  289 ltRQAFENgvrmgrRGLgsVFVWASGNGGrskdhcscDGYTNSIYTISIS-----------STAESGKKPWYLEECSSTL 357
Cdd:cd04842   140 --QFAYNN------PDI--LFVFSAGNDG--------NDGSNTIGSPATAknvltvgasnnPSVSNGEGGLGQSDNSDTV 201

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006570  358 ATTYSSGESYD--KK---------IITTDLRQR----CTDNH----TGTSASAPMAAGIIALALEA 404
Cdd:cd04842   202 ASFSSRGPTYDgrIKpdlvapgtgILSARSGGGgigdTSDSAytskSGTSMATPLVAGAAALLRQY 267
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 164-430 1.56e-14

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: 75.44  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  164 GKNIVVTILDDGIERTHPDLMQNYDALASC----DVNGNDLDPMPR---------YDASNENKHGTRCAGEVAATANNSH 230
Cdd:cd07474     1 GKGVKVAVIDTGIDYTHPDLGGPGFPNDKVkggyDFVDDDYDPMDTrpypsplgdASAGDATGHGTHVAGIIAGNGVNVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  231 CTVGIAFNAKIGGVRMLDGD---VTDMVEA---KSVSynpQHVHIYSASWG-----PDDDGKtvdgpapltrQAFENGVR 299
Cdd:cd07474    81 TIKGVAPKADLYAYKVLGPGgsgTTDVIIAaieQAVD---DGMDVINLSLGssvngPDDPDA----------IAINNAVK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  300 mgrrgLGSVFVWASGNGGrskDHCSCDGyTNSIYTISISSTAESGKKPWYleecSSTLATTYSSGESYDKKIITTDL--- 376
Cdd:cd07474   148 -----AGVVVVAAAGNSG---PAPYTIG-SPATAPSAITVGASTVADVAE----ADTVGPSSSRGPPTSDSAIKPDIvap 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006570  377 -------RQRCTDN---HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTsrAGHLNAND 430
Cdd:cd07474   215 gvdimstAPGSGTGyarMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNT--AKPLYDSD 276
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 637-746 1.64e-12

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: 65.47  E-value: 1.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   637 PCDPECSEVGCDGPGPDHCSDCLHYyyklkNNTRICVSSCP-----PGHYhADKKRCRKCAPNCE------SCFGSHGNQ 705
Cdd:pfam14843    1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNilqgePREY-VVNSTCVPCHPECLpqngtaTCSGPGADN 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 569006570   706 CLSCKYgyflNEETSSCVTQCPDGSYEDI--------KKNVCGKCSENC 746
Cdd:pfam14843   75 CTKCAH----FRDGPHCVSSCPSGVLGENdliwkyadANGVCQPCHPNC 119
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 162-421 6.78e-11

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: 63.69  E-value: 6.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  162 YTGKNIVVTILDDGIERTHPDLMQNydALASCDVNGNDldpmpryDASNENKHGTRCAGEVAATannshcTVGIAFNAKI 241
Cdd:cd04077    22 STGSGVDVYVLDTGIRTTHVEFGGR--AIWGADFVGGD-------PDSDCNGHGTHVAGTVGGK------TYGVAKKANL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  242 GGVRMLD----GDVTDMVEAksvsYNpqhvhiYSASWGPDDDGKTV-----DGPAPltrQAFENGV-RMGRRGLgsVFVW 311
Cdd:cd04077    87 VAVKVLDcngsGTLSGIIAG----LE------WVANDATKRGKPAVanmslGGGAS---TALDAAVaAAVNAGV--VVVV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  312 ASGNGGRskDHCscdGYT--NSIYTISISSTAESGKKPWYLE--ECSSTLAttysSGESYDKKIITTDlrqRCTDNHTGT 387
Cdd:cd04077   152 AAGNSNQ--DAC---NYSpaSAPEAITVGATDSDDARASFSNygSCVDIFA----PGVDILSAWIGSD---TATATLSGT 219

                         250       260       270
                  ....*....|....*....|....*....|....
gi 569006570  388 SASAPMAAGIIALALEANPFLTWRDVQHVIVRTS 421
Cdd:cd04077   220 SMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLA 253
VSP pfam03302
Giardia variant-specific surface protein;
674-959 8.88e-11

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 64.99  E-value: 8.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   674 SSCPPGH-YHADKKRCRKCAP----NCESCFGSHGNQCLSCKYGYFLNEeTSSCVTQCpdgsyEDIKKNVCGKCSENCKA 748
Cdd:pfam03302    2 DECKPGYeLSADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYLTP-TSQCIDDC-----AKIGNYYYTTNANNKKI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   749 CIGFH--NCTECKGGLSLQgsrcsvTCEDGQFFNGHDCQPCHRFCATCSGAGADGCINCTEGYVME------EGRCVQSC 820
Cdd:pfam03302   76 CKECTvaNCKTCEDQGQCQ------ACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALRygndgtKGTCGEGC 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   821 SVSYYLDHSSE-----GGYKSCKRCDNS----------------CLTCNGPGFKN--CSSCPSGYLLDLGTC-------- 869
Cdd:pfam03302  150 TTGTGAGACKTcgltiDGTSYCSECATEteypqngvctstaaraTATCKASSVANgmCSSCANGYFRMNGGCyettkfpg 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   870 -------QMGAICKDGE--YIDDQGHCQTCEASCAKCWGPTqeDCISCPVTRVLDDGRCVMNCPSWkfefkKQCHPCHYT 940
Cdd:pfam03302  230 ksvceeaNSGGTCQKEApgYKLNNGDLVTCSPGCKTCTSNT--VCTTCMDGYVKTSDSCTKCDSSC-----ETCTGATTT 302

                          330       340
                   ....*....|....*....|....*
gi 569006570   941 CQGC------QGSGPSNCTSCRADK 959
Cdd:pfam03302  303 CKTCatgyykSGTGCVSCTSSESDN 327
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 889-995 1.54e-10

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: 60.08  E-value: 1.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   889 TCEASCAK--CWGPTQEDCISCpvTRVLDDGRCVMNCPSWKFEFK-----KQCHPCHYTCQG------CQGSGPSNCTSC 955
Cdd:pfam14843    1 VCDPLCSSegCWGPGPDQCLSC--RNFSRGGTCVESCNILQGEPReyvvnSTCVPCHPECLPqngtatCSGPGADNCTKC 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 569006570   956 RADKHGQErflyhgeCLENCP---------VGHYPAKGHACLPCPDNCE 995
Cdd:pfam14843   79 AHFRDGPH-------CVSSCPsgvlgendlIWKYADANGVCQPCHPNCT 120
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 160-423 2.87e-10

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: 62.62  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  160 RGYTGKNIVVTILDDGIERTHPDL----MQNYDALASCDVNGNDLD----PMPRYDASNENKHGTRCAGEVAATANNSHC 231
Cdd:cd07489     8 EGITGKGVKVAVVDTGIDYTHPALggcfGPGCKVAGGYDFVGDDYDgtnpPVPDDDPMDCQGHGTHVAGIIAANPNAYGF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  232 TvGIAFNAKIGGVRMLD--GDVTD--MVEAKSVSYNpQHVHIYSASWGpDDDGKTVDGPAPLTRQAFENGVRM------- 300
Cdd:cd07489    88 T-GVAPEATLGAYRVFGcsGSTTEdtIIAAFLRAYE-DGADVITASLG-GPSGWSEDPWAVVASRIVDAGVVVtiaagnd 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  301 GRRGLgsvfvWASGNGGRSKDHCSCdGYTNSIYTiSISSTAESGKKPWYLEECSSTLATTYSSGESYDkkIIttdlrqrc 380
Cdd:cd07489   165 GERGP-----FYASSPASGRGVIAV-ASVDSYFS-SWGPTNELYLKPDVAAPGGNILSTYPLAGGGYA--VL-------- 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 569006570  381 tdnhTGTSASAPMAAGIIALALEA-NPFLTWRDVQHVIVRTSRA 423
Cdd:cd07489   228 ----SGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKP 267
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
 152-430 6.41e-10

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: 61.72  E-value: 6.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  152 MNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALAScdvngndLDPMPRYDASNENKHGTrcaGEVAAtannshc 231
Cdd:cd07494     8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQVRVV-------LAPGATDPACDENGHGT---GESAN------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  232 TVGIAFNAKIGGVRMLDGDVTDMVEA--KSVSYNPQhvhIYSASWGPD--DDGKTVDGPAPLTRQAFE----NGVrmgRR 303
Cdd:cd07494    71 LFAIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSPD---IISNSWGYDlrSPGTSWSRSLPNALKALAatlqDAV---AR 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  304 GLgsVFVWASGNGGRS-----KDHCSCDG-YTNSIYTISISSTAESGKKPWY-------------LEECSSTLATTYSSG 364
Cdd:cd07494   145 GI--VVVFSAGNGGWSfpaqhPEVIAAGGvFVDEDGARRASSYASGFRSKIYpgrqvpdvcglvgMLPHAAYLMLPVPPG 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006570  365 ESYDKKIITTDLRQRCTDN---HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRA---GHLNAND 430
Cdd:cd07494   223 SQLDRSCAAFPDGTPPNDGwgvFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTARDvtkGASAQGT 294
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 169-422 1.44e-09

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: 59.87  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  169 VTILDDGIERTHPDLMQNYDALASCDVNGNDLDPmpryDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKiggvrMLD 248
Cdd:cd07490     4 VAVLDTGVDADHPDLAGRVAQWADFDENRRISAT----EVFDAGGHGTHVSGTIGGGGAKGV-YIGVAPEAD-----LLH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  249 GDVTDMVEAksvsynPQHVHIYSASWGPDDDGKTV-------DGPAPLTRQAFEngvrMGRRGLGSVFVWASGNGGRSKD 321
Cdd:cd07490    74 GKVLDDGGG------SLSQIIAGMEWAVEKDADVVsmslggtYYSEDPLEEAVE----ALSNQTGALFVVSAGNEGHGTS 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  322 HCSCDGYTnsiyTISISSTAESGKKPWYlEECSSTLATTYSSGESYDKKIITTDL-----------RQRCTDNH----TG 386
Cdd:cd07490   144 GSPGSAYA----ALSVGAVDRDDEDAWF-SSFGSSGASLVSAPDSPPDEYTKPDVaapgvdvysarQGANGDGQytrlSG 218

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 569006570  387 TSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07490   219 TSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 169-413 1.59e-09

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 61.91  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  169 VTILDDGIERTHPDLMQNY---------------------DALASCDVNGNDLDPMprydasNENKHGTRCAGEVAATAN 227
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM------DDNYHGTHVSGIISAIGN 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  228 NSHCTVGIAFNAKIGGVRMLD----GDVTDMVeaKSVSY-NPQHVHIYSASWGPDDDGKTvdgpapltrqaFENGVRMGR 302
Cdd:PTZ00262  394 NNIGIVGVDKRSKLIICKALDshklGRLGDMF--KCFDYcISREAHMINGSFSFDEYSGI-----------FNESVKYLE 460

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  303 RgLGSVFVWASGN----GGRSKDHCSCDGYTNSIYTISISSTAES---------GKKPWYLEECSSTLATTYSSGESYDK 369
Cdd:PTZ00262  461 E-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYPPILSKKLRNvitvsnlikDKNNQYSLSPNSFYSAKYCQLAAPGT 539

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 569006570  370 KIITTDLRQRCTDNhTGTSASAPMAAGIIALALEANPFLTWRDV 413
Cdd:PTZ00262  540 NIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
VSP pfam03302
Giardia variant-specific surface protein;
706-1050 2.52e-09

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 60.75  E-value: 2.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   706 CLSCKYGYFLNEETSSCVTQcpdgsyedikknvcGKC-SENCKACI--GFHNCTECKGGLSL-QGSRCSVTCEDGQFFNG 781
Cdd:pfam03302    1 CDECKPGYELSADKTKCTSS--------------APCkTENCKACSndKREVCEECNSNNYLtPTSQCIDDCAKIGNYYY 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   782 HDCQPCHRFCATCSGAGADGCinctegyvmEEGRCVQSCSVSYYLDHsseggyKSCKRCDNSCLTCNGPGFKNCSSCPSG 861
Cdd:pfam03302   67 TTNANNKKICKECTVANCKTC---------EDQGQCQACNDGFYKSG------DACSPCHESCKTCSGGTASDCTECLTG 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   862 YLLDLGT--------------CQMGAICKDGEYIDDQGHCQTCEAS--------CAKCWGPTQEDCISCPVTrvldDGRC 919
Cdd:pfam03302  132 KALRYGNdgtkgtcgegcttgTGAGACKTCGLTIDGTSYCSECATEteypqngvCTSTAARATATCKASSVA----NGMC 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   920 vMNCPSWKFEFKKQCHpchytcQGCQGSGPSNCTSCRADKHGQErflyhgeclencPVGHYPAKGHACLPCPDNCELCYN 999
Cdd:pfam03302  208 -SSCANGYFRMNGGCY------ETTKFPGKSVCEEANSGGTCQK------------EAPGYKLNNGDLVTCSPGCKTCTS 268

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 569006570  1000 PHVCSRCMSGYViiPPNHTCQKLecrqgefqDSEYEECMPCEEGCLGCTEG 1050
Cdd:pfam03302  269 NTVCTTCMDGYV--KTSDSCTKC--------DSSCETCTGATTTCKTCATG 309
FU smart00261
Furin-like repeats;
781-825 3.47e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 53.28  E-value: 3.47e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 569006570    781 GHDCQPCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYY 825
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 690-739 1.93e-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: 1.93e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 569006570  690 KCAPNCESCFGSHGNQCLSCKYGYFLNEETssCVTQCPDGSYEDIKKNVC 739
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGT--CVSECPEGTYADTEGGVC 48
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 162-315 2.13e-08

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: 57.00  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  162 YTGKNIVVTILDDGIERTHPDLMqnydalascDVNGNDLDPMPRYDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKI 241
Cdd:cd07480     5 FTGAGVRVAVLDTGIDLTHPAFA---------GRDITTKSFVGGEDVQDGHGHGTHCAGTIFGRDVPGP-RYGVARGAEI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  242 --GGVRMLDGDVTDMVEAKSVSYNPQH-VHIYSASWGPDDDGKTVDG--PAPLTRQAFE----------NGVRMGRR--- 303
Cdd:cd07480    75 alIGKVLGDGGGGDGGILAGIQWAVANgADVISMSLGADFPGLVDQGwpPGLAFSRALEayrqrarlfdALMTLVAAqaa 154

                         170
                  ....*....|...
gi 569006570  304 -GLGSVFVWASGN 315
Cdd:cd07480   155 lARGTLIVAAAGN 167
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 786-827 3.34e-08

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 50.60  E-value: 3.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 569006570  786 PCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYYLD 827
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 712-1006 3.68e-08

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 57.62  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  712 GYFLNEETSSCVTQCPDGSYEDiKKNVCGKCSENC---------KACIGFHN--CTECKGGLSLQGSRCSVTCEDGQFFN 780
Cdd:PTZ00214  350 GYLCGDATNGGVSGCATCGYNS-GAVTCTRCSAGYlgvdgkscsESCSGDTRgvCTKVAEGSESTEVSCRCVCKPTFYNS 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  781 GHDCQPCHRFCATCSGAGADGCINCTEGYVM-------EEGRCVQSCSVSyylDHSSE-----GGYKSCKRC-DNSCLTC 847
Cdd:PTZ00214  429 SGTCTPCTDSCAVCKDGTPTGCQQCSPGKILefsivssESADCVDQCSVG---SECAEcgitiDGSRYCTRCkDASTYPF 505

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  848 NGPGFKNcsscpsgylldlgtCQMGAICKDGEyiddQGHCQTCEASCAKCWGP--TQEDCISCPVTRVLDDGRCVMNCPS 925
Cdd:PTZ00214  506 NGVCIPN--------------TQRDAYCTSTA----NGACTTCSGAAFLMNGGcyTTEHYPGSTICDKQSNGKCTTTKKG 567

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  926 WKFEFKKQCHPCHYTCQGCQGSGPSNCTSCRADK-HGQERFLYHGECLE-NCPVGHYPAKGHACLPCPD-NCELCYNPHV 1002
Cdd:PTZ00214  568 YGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKlLKRASGAATGSCVDpGACVDGYYADGDACLPCATpGCKTCGHASF 647


                  ....
gi 569006570 1003 CSRC 1006
Cdd:PTZ00214  648 CTEC 651
Furin-like pfam00757
Furin-like cysteine rich region;
638-746 8.56e-08

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 52.44  E-value: 8.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   638 CDPECSEvGCDGPGPDHCSDCLHYYYklknnTRICVSSCPPGHYHADkkrcRKCApNCESCFGSHGNQClsckygYFLNE 717
Cdd:pfam00757   49 CHEQCLG-GCTGPNDSDCLACRHFND-----EGTCVDQCPPGTYQFG----WRCV-TFKECPKSHLPGY------NPLVI 111

                           90       100       110
                   ....*....|....*....|....*....|
gi 569006570   718 ETSSCVTQCPDGSYEDIKKNV-CGKCSENC 746
Cdd:pfam00757  112 HNGECVRECPSGYTEVENNSRkCEPCEGLC 141
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 671-729 1.78e-07

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


Pssm-ID: 464939 [Multi-domain]  Cd Length: 102  Bit Score: 50.12  E-value: 1.78e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006570   671 ICVSSCPPGHY---HADKKRCRKC-APNCESCFGShgNQCLSCKYGYFLNEetSSCVTQCPDG 729
Cdd:pfam15913   34 VCLHSCPPGYFgirGQEVNRCTKCkAENCESCFSK--DFCTKCKEGFYLHK--GKCLDTCPEG 92
FU smart00261
Furin-like repeats;
885-928 1.83e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 48.27  E-value: 1.83e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 569006570    885 GHCQTCEASCAKCWGPTQEDCISCPVTRVLDDGRCVMNCPSWKF 928
Cdd:smart00261    2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
FU smart00261
Furin-like repeats;
685-731 2.30e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 48.27  E-value: 2.30e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 569006570    685 KKRCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETssCVTQCPDGSY 731
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGK--CVSECPPGTY 45
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 786-906 3.02e-07

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


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 50.45  E-value: 3.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   786 PCHRFC--ATCSGAGADGCINCTegYVMEEGRCVQSCSVSYYLDHSSEGGyKSCKRCDNSCL------TCNGPGFKNC-- 855
Cdd:pfam14843    1 VCDPLCssEGCWGPGPDQCLSCR--NFSRGGTCVESCNILQGEPREYVVN-STCVPCHPECLpqngtaTCSGPGADNCtk 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006570   856 -----------SSCPSGYlldlgtcqMGAICKDGEYIDDQGHCQTCEASCAK-CWGPTQEDCI 906
Cdd:pfam14843   78 cahfrdgphcvSSCPSGV--------LGENDLIWKYADANGVCQPCHPNCTQgCTGPGLTGCP 132
FU smart00261
Furin-like repeats;
931-980 3.79e-07

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 47.50  E-value: 3.79e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 569006570    931 KKQCHPCHYTCQGCQGSGPSNCTSCRADkhgqeRFLYHGECLENCPVGHY 980
Cdd:smart00261    1 DGECKPCHPECATCTGPGPDDCTSCKHG-----FFLDGGKCVSECPPGTY 45
VSP pfam03302
Giardia variant-specific surface protein;
653-908 3.90e-07

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 53.82  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   653 DHCSDCLHYYYKLKNNtricvsscppghyhaDKKRCRKCAP-NCESCfgSHGNQCLSCKYGYFLNEETSSCVTQ----CP 727
Cdd:pfam03302   56 DDCAKIGNYYYTTNAN---------------NKKICKECTVaNCKTC--EDQGQCQACNDGFYKSGDACSPCHEscktCS 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   728 DGSYEDIKKNVCGK------------CSENCKACIGFHNCTECkgGLSLQG----SRCSVTCEDGQffNGHDCQPCHRFC 791
Cdd:pfam03302  119 GGTASDCTECLTGKalrygndgtkgtCGEGCTTGTGAGACKTC--GLTIDGtsycSECATETEYPQ--NGVCTSTAARAT 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   792 ATC-SGAGADG-CINCTEGYVMEEGRCVQSCSVSYYLDHSSEGGYKSCK------RCDNSCLTCNGPGFKNCSSCPsgyl 863
Cdd:pfam03302  195 ATCkASSVANGmCSSCANGYFRMNGGCYETTKFPGKSVCEEANSGGTCQkeapgyKLNNGDLVTCSPGCKTCTSNT---- 270

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 569006570   864 ldlgTCQMgaiCKDGeYIDDQGHCQTCEASCAKCWGPTQEdCISC 908
Cdd:pfam03302  271 ----VCTT---CMDG-YVKTSDSCTKCDSSCETCTGATTT-CKTC 306
FU smart00261
Furin-like repeats;
835-880 1.28e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.96  E-value: 1.28e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 569006570    835 KSCKRCDNSCLTCNGPGFKNCSSCPSGYLLDLGTCQmgAICKDGEY 880
Cdd:smart00261    2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCV--SECPPGTY 45
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 169-422 1.37e-06

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: 50.41  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  169 VTILDDGIERTHPDLmqnyDALASCDVNGNDLDPMPRYD-ASNENKHGTRCAGEVAATANnshctvgiafNAKIGGVRML 247
Cdd:cd07492     4 VAVIDSGVDTDHPDL----GNLALDGEVTIDLEIIVVSAeGGDKDGHGTACAGIIKKYAP----------EAEIGSIKIL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  248 DGDVTDMVE--AKSVSY-NPQHVHIYSASWgpdddGKTVDGPAPLTRQAFENGVRMGRrglgsVFVWASGNGGRskdhcs 324
Cdd:cd07492    70 GEDGRCNSFvlEKALRAcVENDIRIVNLSL-----GGPGDRDFPLLKELLEYAYKAGG-----IIVAAAPNNND------ 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  325 cDGYTNSIYTISI---SSTAESGKKPWYLEECSSTlattyssgesyDKKIITTDLRQRCTDNHTGTSASAPMAAGIIALA 401
Cdd:cd07492   134 -IGTPPASFPNVIgvkSDTADDPKSFWYIYVEFSA-----------DGVDIIAPAPHGRYLTVSGNSFAAPHVTGMVALL 201

                         250       260
                  ....*....|....*....|.
gi 569006570  402 LEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07492   202 LSEKPDIDANDLKRLLQRLAV 222
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 637-689 1.54e-06

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: 45.97  E-value: 1.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 569006570  637 PCDPECSevGCDGPGPDHCSDCLHYYYklkNNTRICVSSCPPGHYH-ADKKRCR 689
Cdd:cd00064     1 PCHPSCA--TCTGPGPDQCTSCRHGFY---LDGGTCVSECPEGTYAdTEGGVCL 49
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 936-981 1.74e-06

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: 45.97  E-value: 1.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 569006570  936 PCHYTCQGCQGSGPSNCTSCRADKHgqerfLYHGECLENCPVGHYP 981
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFY-----LDGGTCVSECPEGTYA 41
FU smart00261
Furin-like repeats;
637-681 2.07e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.58  E-value: 2.07e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 569006570    637 PCDPECSevGCDGPGPDHCSDCLHYYYKLKNntrICVSSCPPGHY 681
Cdd:smart00261    6 PCHPECA--TCTGPGPDDCTSCKHGFFLDGG---KCVSECPPGTY 45
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 166-409 4.06e-06

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: 49.67  E-value: 4.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  166 NIVVTILDDGIERTHPDLMQNYdalascDVNGNDLDPMPRYDASNE------------NKHGTRCAGEVAATANNShctv 233
Cdd:cd07482     1 KVTVAVIDSGIDPDHPDLKNSI------SSYSKNLVPKGGYDGKEAgetgdindivdkLGHGTAVAGQIAANGNIK---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  234 GIAFNAKIGGVRMLD----GDVTDMVEAKSVSYNpQHVHIYSASWGPDDDGKTVDGPAPLTRQAFENGVRMGRRGlGSVF 309
Cdd:cd07482    71 GVAPGIGIVSYRVFGscgsAESSWIIKAIIDAAD-DGVDVINLSLGGYLIIGGEYEDDDVEYNAYKKAINYAKSK-GSIV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  310 VWASGNGGRS-------KDHCSCDGY--TNSIY---------TISISSTAESGkkpwYLEECSS------TLAT---TYS 362
Cdd:cd07482   149 VAAAGNDGLDvsnkqelLDFLSSGDDfsVNGEVydvpaslpnVITVSATDNNG----NLSSFSNygnsriDLAApggDFL 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569006570  363 SGESYDK------------KIITTDLRQrCTDNHTGTSASAPMAAGIIALALEANPFLT 409
Cdd:cd07482   225 LLDQYGKekwvnnglmtkeQILTTAPEG-GYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 152-402 7.02e-06

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: 48.85  E-value: 7.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  152 MNIEGAWKR-GYTGKNIVVTILDDGIERTHPDLMQNydaLAScdvngndldPMPRYDASNENKHGTRCAGEVAATANNSH 230
Cdd:cd04843     2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGN---GIT---------LISGLTDQADSDHGTAVLGIIVAKDNGIG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  231 CTvGIAFNAKIGGV-----------------RMLDGDVTdMVEAK----SVSYNPQHVHIYSASWGPdddgktvdgpapl 289
Cdd:cd04843    70 VT-GIAHGAQAAVVsstrvsntadaildaadYLSPGDVI-LLEMQtggpNNGYPPLPVEYEQANFDA------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  290 TRQAFENGVrmgrrglgsVFVWASGNGGRSKDHCS-CDGYTNSIYTISIS---------STAESGKKPWyleeCSSTLAT 359
Cdd:cd04843   135 IRTATDLGI---------IVVEAAGNGGQDLDAPVyNRGPILNRFSPDFRdsgaimvgaGSSTTGHTRL----AFSNYGS 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 569006570  360 ---TYSSGE-----SYDKKIITTDLRQRCTDNHTGTSASAPMAAGiiALAL 402
Cdd:cd04843   202 rvdVYGWGEnvtttGYGDLQDLGGENQDYTDSFSGTSSASPIVAG--AAAS 250
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 840-886 9.03e-06

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: 9.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 569006570  840 CDNSCLTCNGPGFKNCSSCPSGYLLDLGTCQmgAICKDGEYIDDQGH 886
Cdd:cd00064     2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCV--SECPEGTYADTEGG 46
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 890-929 9.68e-06

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: 9.68e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 569006570  890 CEASCAKCWGPTQEDCISCPVTRVLDDGRCVMNCPSWKFE 929
Cdd:cd00064     2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYA 41
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 383-455 1.01e-05

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: 48.44  E-value: 1.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006570  383 NHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIvrTSRAGHLNANDWktnaagfkvSHLYGFGLMDAEAMV 455
Cdd:cd05562   212 NFFGTSAAAPHAAGVAALVLSANPGLTPADIRDAL--RSTALDMGEPGY---------DNASGSGLVDADRAV 273
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
687-822 2.99e-05

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 47.71  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  687 RCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETSSCVTQCPDGSYEDIKKNVCGKCSENCKACIGFHNCTECKGGLSLQG 766
Cdd:COG4624     2 LLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006570  767 SRCSVTCEDGqffNGHDCQPCHRFCATCSGAGADG--------CINCtegyvmeeGRCVQSCSV 822
Cdd:COG4624    82 RGPSIIRDKE---KCKNCYPCVRACPVKAIKVDDGkaeideekCISC--------GQCVAVCPF 134
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 695-782 3.19e-05

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


Pssm-ID: 464939 [Multi-domain]  Cd Length: 102  Bit Score: 43.96  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   695 CESCfgSHGNQCLSCKYGYFL------NEETSSCVTQCPDGSY--EDIKKNVCGKC-SENCKACIGFHNCTECKGGLSLQ 765
Cdd:pfam15913    4 CVLC--SEENGCLTCQPRLFLllerngIRQYGVCLHSCPPGYFgiRGQEVNRCTKCkAENCESCFSKDFCTKCKEGFYLH 81

                           90
                   ....*....|....*..
gi 569006570   766 GSRCSVTCEDGQFFNGH 782
Cdd:pfam15913   82 KGKCLDTCPEGTAAQNS 98
Furin-like pfam00757
Furin-like cysteine rich region;
847-994 3.65e-04

Furin-like cysteine rich region;


Pssm-ID: 395614 [Multi-domain]  Cd Length: 143  Bit Score: 42.04  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   847 CNGPGFKNCSSCPSGYLLDLGTCQMGAICKDGEYIDDQGHCqtCEASCA-KCWGPTQEDCISCpvTRVLDDGRCVMNCPS 925
Cdd:pfam00757    8 CPGTMEKCHSCCNNGYCWGPGHCQKVCPEQCKKRCTKPGEC--CHEQCLgGCTGPNDSDCLAC--RHFNDEGTCVDQCPP 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006570   926 WKFEFKKQChpchYTCQGCQGSGPSNCTscradkhgqERFLYHGECLENCPVGHYPAKGH--ACLPCPDNC 994
Cdd:pfam00757   84 GTYQFGWRC----VTFKECPKSHLPGYN---------PLVIHNGECVRECPSGYTEVENNsrKCEPCEGLC 141
FU smart00261
Furin-like repeats;
736-778 6.68e-04

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 38.26  E-value: 6.68e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 569006570    736 KNVCGKCSENCKACIG--FHNCTECKGGLSLQGSRCSVTCEDGQF 778
Cdd:smart00261    1 DGECKPCHPECATCTGpgPDDCTSCKHGFFLDGGKCVSECPPGTY 45
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 164-404 1.42e-03

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: 42.07  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  164 GKNIVVTILDDGIERTHPDLMQ--NYDALASCDVNGN---DLDPMPRYDA--SNENKHGTRCAgEVAATANNSHCT---- 232
Cdd:cd07497     1 GEGVVIAIVDTGVDYSHPDLDIygNFSWKLKFDYKAYllpGMDKWGGFYVimYDFFSHGTSCA-SVAAGRGKMEYNlygy 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  233 ------VGIAFNAKIGGVRMLD-GDVT---------DMVEAKSV-SYNPQH-VHIYSASWGPDDDGKTVDGPAPLTRQAF 294
Cdd:cd07497    80 tgkfliRGIAPDAKIAAVKALWfGDVIyawlwtagfDPVDRKLSwIYTGGPrVDVISNSWGISNFAYTGYAPGLDISSLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570  295 ENGVRMGRrglGSVFVWASGNGGRSKDHCSCDGytNSIYTISISSTAESGKKPWYLeecssTLATTYSSGEsydkkIITT 374
Cdd:cd07497   160 IDALVTYT---GVPIVSAAGNGGPGYGTITAPG--AASLAISVGAATNFDYRPFYL-----FGYLPGGSGD-----VVSW 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006570  375 DLR----------------------QRCTDNHT------------GTSASAPMAAGIIALALEA 404
Cdd:cd07497   225 SSRgpsiagdpkpdlaaigafawapGRVLDSGGaldgneafdlfgGTSMATPMTAGSAALVISA 288
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 742-855 1.63e-03

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: 39.66  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006570   742 CSENCKA--CIGF--HNCTECKGglSLQGSRCSVTC-----EDGQFFNGHDCQPCHRFC------ATCSGAGADGCINCT 806
Cdd:pfam14843    2 CDPLCSSegCWGPgpDQCLSCRN--FSRGGTCVESCnilqgEPREYVVNSTCVPCHPEClpqngtATCSGPGADNCTKCA 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 569006570   807 egYVMEEGRCVQSCSVSYYLDHSSEGGY----KSCKRCDNSC-LTCNGPGFKNC 855
Cdd:pfam14843   80 --HFRDGPHCVSSCPSGVLGENDLIWKYadanGVCQPCHPNCtQGCTGPGLTGC 131
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 741-780 7.88e-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: 35.57  E-value: 7.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 569006570  741 KCSENCKACIG--FHNCTECKGGLSLQGSRCSVTCEDGQFFN 780
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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