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Conserved domains on  [gi|755520810|ref|XP_011249124|]
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furin isoform X1 [Mus musculus]

Protein Classification

S8 family peptidase( domain architecture ID 11243032)

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

CATH:  3.40.50.200
EC:  3.4.-.-
Gene Ontology:  GO:0004252|GO:0006508
MEROPS:  S8
PubMed:  8439290|9070434
SCOP:  3000226

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 ...
 113-412 3.85e-174

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: 502.48  E-value: 3.85e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 113 PTDPKFPQQWYLSGVTQR------DLNVKEAWAQGFTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRY 186
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 187 TqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGaplfppplrpGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGP 266
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLG----------GIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 267 EDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSST 346
Cdd:cd04059  149 DDDGKTVDGPGPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSV 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755520810 347 LATTYSSGNQN-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSK 412
Cdd:cd04059  229 LASAPSGGSGNpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 33-107 2.13e-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: 134.27  E-value: 2.13e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755520810   33 TWAVHIPGGPAVADRVAQKHGFHNLGQIFG--DYYHFWHRAVTKRSLSPHRPRHSRLQREPQVKWLEQQVAKRRAKR 107
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 494-580 3.26e-37

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: 133.93  E-value: 3.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  494 LEHVQARLTLSYNRRGDLAIHLISPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPAGEWVLEIENTsEANNYGTL 573
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79


                  ....*..
gi 755520810  574 TKFTLVL 580
Cdd:pfam01483  80 NSWQLTL 86
FU smart00261
Furin-like repeats;
648-685 6.49e-10

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 55.21  E-value: 6.49e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 755520810   648 ASVCTPCHASCATCQGPAPTDCLSCPSHASLDpvEQTC 685
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKC 36
FU smart00261
Furin-like repeats;
591-629 1.36e-06

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.58  E-value: 1.36e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 755520810   591 PPESSGCKTLTSSQA--CVVCEEGYSLHQKSCVQHCPPGFI 629
Cdd:smart00261   5 KPCHPECATCTGPGPddCTSCKHGFFLDGGKCVSECPPGTY 45
 
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 ...
 113-412 3.85e-174

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: 502.48  E-value: 3.85e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 113 PTDPKFPQQWYLSGVTQR------DLNVKEAWAQGFTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRY 186
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 187 TqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGaplfppplrpGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGP 266
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLG----------GIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 267 EDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSST 346
Cdd:cd04059  149 DDDGKTVDGPGPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSV 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755520810 347 LATTYSSGNQN-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSK 412
Cdd:cd04059  229 LASAPSGGSGNpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 144-437 3.53e-60

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: 205.39  E-value: 3.53e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  144 GHGIVVSILDDGIEKNHPDLAGNYDPGASFD----VNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNA 219
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDpeasVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  220 RIGaplfppplrpGVRML-DGEVTDAVEARSLGLN-PNHIHIYSASWGPEddgKTVDGPARLAEEAFFRGvsqGRGGLGS 297
Cdd:pfam00082  81 KIL----------GVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  298 IFVWASGNGGREHDSCNCDGY-TNSIYTLSISSATQF--GNVPWYSEACSS-------TLA----TTYSSGNQNEKQIVT 363
Cdd:pfam00082 145 LFVWAAGNGSPGGNNGSSVGYpAQYKNVIAVGAVDEAseGNLASFSSYGPTldgrlkpDIVapggNITGGNISSTLLTTT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755520810  364 TDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpahlnaddwATNGVGRKVSHSYGYG 437
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNT-----------ATDLGDAGLDRLFGYG 287
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 33-107 2.13e-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: 134.27  E-value: 2.13e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755520810   33 TWAVHIPGGPAVADRVAQKHGFHNLGQIFG--DYYHFWHRAVTKRSLSPHRPRHSRLQREPQVKWLEQQVAKRRAKR 107
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 494-580 3.26e-37

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: 133.93  E-value: 3.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  494 LEHVQARLTLSYNRRGDLAIHLISPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPAGEWVLEIENTsEANNYGTL 573
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79


                  ....*..
gi 755520810  574 TKFTLVL 580
Cdd:pfam01483  80 NSWQLTL 86
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 81-450 4.59e-36

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 142.16  E-value: 4.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  81 RPRHSRLQREPQVKWLEQQVAKRRAKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKEAWAQGFTGHGIVVSILDDGIEKNH 160
Cdd:COG1404   45 AAALVAAAAAAAVAAALAAPLAPAALAAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADH 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 161 PDLAGNYDPGASFDVNDQDPDpqprytqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGAplfppplrpgVRMLD-- 238
Cdd:COG1404  125 PDLAGRVVGGYDFVDGDGDPS--------DDNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLP----------VRVLDdn 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 239 GEVTDAVEARslGLN---PNHIHIYSASWGPEDDGKTvDGPARLAEEAFFRGVsqgrgglgsIFVWASGNGGrehDSCNC 315
Cdd:COG1404  187 GSGTTSDIAA--AIDwaaDNGADVINLSLGGPADGYS-DALAAAVDYAVDKGV---------LVVAAAGNSG---SDDAT 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 316 DGYTNSIY-TLSISSATQFGNVPWYSeacsstlattySSGNQNE-----KQIVTTDLRQKcTESHTGTSASAPLAAGIIA 389
Cdd:COG1404  252 VSYPAAYPnVIAVGAVDANGQLASFS-----------NYGPKVDvaapgVDILSTYPGGG-YATLSGTSMAAPHVAGAAA 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755520810 390 LTLEANKNLTWRDMQHLVVQTSKPAHLNADDwatngvgrkvshsYGYGLLDAGAMVALAQN 450
Cdd:COG1404  320 LLLSANPDLTPAQVRAILLNTATPLGAPGPY-------------YGYGLLADGAAGATSAG 367
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 132-446 1.14e-11

type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair]


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 66.96  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  132 LNVKEAWAQGfTGHGIVVSILDDGIEKnHPDLAGNYDPGASFdVNDQDpdpqprytQMND-NRHGTRCAGEVAAVANNGV 210
Cdd:TIGR03921   1 LSLEQAWKFS-TGAGVTVAVIDTGVDD-HPRLPGLVLPGGDF-VGSGD--------GTDDcDGHGTLVAGIIAGRPGEGD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  211 CGVGVAYNARI-----GAPLFPPPLRPG----VRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDdgktvdgpARLAE 281
Cdd:TIGR03921  70 GFSGVAPDARIlpirqTSAAFEPDEGTSgvgdLGTLAKAIRRAADLGADVINISLVACLPAGSGADD--------PELGA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  282 ---EAFFRGVsqgrgglgsIFVWASGNGGrehDSCNCDgyTNSI-----YTLSISSATQFGNVPWYSEACSSTLATTYSS 353
Cdd:TIGR03921 142 avrYALDKGV---------VVVAAAGNTG---GDGQKT--TVVYpawypGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGE 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  354 GnqnekqIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpahlnADDWATNGvgrkVSHS 433
Cdd:TIGR03921 208 N------IVSLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEAT-------ADHPARGG----RDDY 270

                         330
                  ....*....|...
gi 755520810  434 YGYGLLDAGAMVA 446
Cdd:TIGR03921 271 VGYGVVDPVAALT 283
FU smart00261
Furin-like repeats;
648-685 6.49e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 55.21  E-value: 6.49e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 755520810   648 ASVCTPCHASCATCQGPAPTDCLSCPSHASLDpvEQTC 685
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKC 36
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 653-685 2.34e-07

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 47.90  E-value: 2.34e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 755520810 653 PCHASCATCQGPAPTDCLSCPSHASLDpvEQTC 685
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLD--GGTC 31
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 149-422 9.58e-07

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 52.28  E-value: 9.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 149 VSILDDGIEKNHPDLAGNYDP-----------------------GASFDVNDQDPdpqprytqMNDNRHGTRCAGEVAAV 205
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIDVnvkelhgrkgidddnngnvddeyGANFVNNDGGP--------MDDNYHGTHVSGIISAI 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 206 ANNGVCGVGVAYNARIGAplfppplrpgVRMLD----GEVTDAVEARSLGLNPNhIHIYSASWGPEDDGKTVDGPARLAE 281
Cdd:PTZ00262 392 GNNNIGIVGVDKRSKLII----------CKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFNESVKYLE 460

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 282 EaffrgvsqgrggLGSIFVWASGNGGREHDSCN----CDGYTNSIY----------TLSISSATQFGNVPwYSEACSSTL 347
Cdd:PTZ00262 461 E------------KGILFVVSASNCSHTKESKPdipkCDLDVNKVYppilskklrnVITVSNLIKDKNNQ-YSLSPNSFY 527

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755520810 348 ATTYSSGNQNEKQIVTTDLRQKCTEShTGTSASAPLAAGIIALTLEANKNLTWRD----MQHLVVQTskPAHLNADDWA 422
Cdd:PTZ00262 528 SAKYCQLAAPGTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEviriLKESIVQL--PSLKNKVKWG 603
FU smart00261
Furin-like repeats;
591-629 1.36e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.58  E-value: 1.36e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 755520810   591 PPESSGCKTLTSSQA--CVVCEEGYSLHQKSCVQHCPPGFI 629
Cdd:smart00261   5 KPCHPECATCTGPGPddCTSCKHGFFLDGGKCVSECPPGTY 45
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 594-631 1.21e-05

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 43.28  E-value: 1.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755520810 594 SSGCKTLTSS--QACVVCEEGYSLHQKSCVQHCPPGFIPQ 631
Cdd:cd00064    3 HPSCATCTGPgpDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 594-631 1.39e-03

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: 38.95  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 755520810  594 SSGCKTLTSSQACVVCEEGYSLHQKSCVQHCPPGFIPQ 631
Cdd:pfam15913  59 AENCESCFSKDFCTKCKEGFYLHKGKCLDTCPEGTAAQ 96
 
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 ...
 113-412 3.85e-174

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: 502.48  E-value: 3.85e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 113 PTDPKFPQQWYLSGVTQR------DLNVKEAWAQGFTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRY 186
Cdd:cd04059    1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 187 TqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGaplfppplrpGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGP 266
Cdd:cd04059   81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLG----------GIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 267 EDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSST 346
Cdd:cd04059  149 DDDGKTVDGPGPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSV 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755520810 347 LATTYSSGNQN-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSK 412
Cdd:cd04059  229 LASAPSGGSGNpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
 144-437 3.53e-60

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: 205.39  E-value: 3.53e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  144 GHGIVVSILDDGIEKNHPDLAGNYDPGASFD----VNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNA 219
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDpeasVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  220 RIGaplfppplrpGVRML-DGEVTDAVEARSLGLN-PNHIHIYSASWGPEddgKTVDGPARLAEEAFFRGvsqGRGGLGS 297
Cdd:pfam00082  81 KIL----------GVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  298 IFVWASGNGGREHDSCNCDGY-TNSIYTLSISSATQF--GNVPWYSEACSS-------TLA----TTYSSGNQNEKQIVT 363
Cdd:pfam00082 145 LFVWAAGNGSPGGNNGSSVGYpAQYKNVIAVGAVDEAseGNLASFSSYGPTldgrlkpDIVapggNITGGNISSTLLTTT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755520810  364 TDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpahlnaddwATNGVGRKVSHSYGYG 437
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNT-----------ATDLGDAGLDRLFGYG 287
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
 33-107 2.13e-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: 134.27  E-value: 2.13e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755520810   33 TWAVHIPGGPAVADRVAQKHGFHNLGQIFG--DYYHFWHRAVTKRSLSPHRPRHSRLQREPQVKWLEQQVAKRRAKR 107
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
 494-580 3.26e-37

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: 133.93  E-value: 3.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  494 LEHVQARLTLSYNRRGDLAIHLISPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPAGEWVLEIENTsEANNYGTL 573
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79


                  ....*..
gi 755520810  574 TKFTLVL 580
Cdd:pfam01483  80 NSWQLTL 86
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
 81-450 4.59e-36

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 142.16  E-value: 4.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  81 RPRHSRLQREPQVKWLEQQVAKRRAKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKEAWAQGFTGHGIVVSILDDGIEKNH 160
Cdd:COG1404   45 AAALVAAAAAAAVAAALAAPLAPAALAAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADH 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 161 PDLAGNYDPGASFDVNDQDPDpqprytqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGAplfppplrpgVRMLD-- 238
Cdd:COG1404  125 PDLAGRVVGGYDFVDGDGDPS--------DDNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLP----------VRVLDdn 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 239 GEVTDAVEARslGLN---PNHIHIYSASWGPEDDGKTvDGPARLAEEAFFRGVsqgrgglgsIFVWASGNGGrehDSCNC 315
Cdd:COG1404  187 GSGTTSDIAA--AIDwaaDNGADVINLSLGGPADGYS-DALAAAVDYAVDKGV---------LVVAAAGNSG---SDDAT 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 316 DGYTNSIY-TLSISSATQFGNVPWYSeacsstlattySSGNQNE-----KQIVTTDLRQKcTESHTGTSASAPLAAGIIA 389
Cdd:COG1404  252 VSYPAAYPnVIAVGAVDANGQLASFS-----------NYGPKVDvaapgVDILSTYPGGG-YATLSGTSMAAPHVAGAAA 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755520810 390 LTLEANKNLTWRDMQHLVVQTSKPAHLNADDwatngvgrkvshsYGYGLLDAGAMVALAQN 450
Cdd:COG1404  320 LLLSANPDLTPAQVRAILLNTATPLGAPGPY-------------YGYGLLADGAAGATSAG 367
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
 147-410 9.07e-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: 132.85  E-value: 9.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 147 IVVSILDDGIEKNHPDLAG--NYDPGasFDVNDQDPDPQPRYTqmndnrHGTRCAGEVAAVANNGVCGVGVAYNARIgap 224
Cdd:cd07498    1 VVVAIIDTGVDLNHPDLSGkpKLVPG--WNFVSNNDPTSDIDG------HGTACAGVAAAVGNNGLGVAGVAPGAKL--- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 225 lfppplRPgVRMLDGEVTDAVEARSLGLN---PNHIHIYSASWGPEDdgktvdgPARLAEEAFFRGVSQGRGGLGSIFVW 301
Cdd:cd07498   70 ------MP-VRIADSLGYAYWSDIAQAITwaaDNGADVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLF 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 302 ASGNGGREHDScncdGYTNSIYTLSISSATQFGNVPWYSE--------ACSSTLATTySSGNQNEKQIVTTDlrqkcTES 373
Cdd:cd07498  136 AAGNSGRSVSS----GYAANPSVIAVAATDSNDARASYSNygnyvdlvAPGVGIWTT-GTGRGSAGDYPGGG-----YGS 205

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 755520810 374 HTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQT 410
Cdd:cd07498  206 FSGTSFASPVAAGVAALILSANPNLTPAEVEDILTST 242
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 146-412 5.56e-26

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


Pssm-ID: 173799 [Multi-domain]  Cd Length: 259  Bit Score: 107.66  E-value: 5.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 146 GIVVSILDDGIEKNHPDLAGN------YDPGASFDvNDQ---------------DPDPqprytqMNDNRHGTRCAGEVAA 204
Cdd:cd07473    3 DVVVAVIDTGVDYNHPDLKDNmwvnpgEIPGNGID-DDGngyvddiygwnfvnnDNDP------MDDNGHGTHVAGIIGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 205 VANNGVCGVGVAYNARIgAPLfppplrpgvRMLD----GEVTDAVE----ARSLGlnpnhIHIYSASWGPeddgktvDGP 276
Cdd:cd07473   76 VGNNGIGIAGVAWNVKI-MPL---------KFLGadgsGTTSDAIKaidyAVDMG-----AKIINNSWGG-------GGP 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 277 ARLAEEAFFRGVSQgrgglGSIFVWASGNGGREHDSCNC--DGYTNSiYTLSISSATQFGNVPWYSEACSST--LA---- 348
Cdd:cd07473  134 SQALRDAIARAIDA-----GILFVAAAGNDGTNNDKTPTypASYDLD-NIISVAATDSNDALASFSNYGKKTvdLAapgv 207

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755520810 349 ---TTYSSGNQNEKqivttdlrqkcteshTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSK 412
Cdd:cd07473  208 dilSTSPGGGYGYM---------------SGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 147-410 4.27e-25

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: 104.97  E-value: 4.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 147 IVVSILDDGIEKNHPDLAGNYDPGASFdvNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVcGVGVAYNARIGAplf 226
Cdd:cd00306    1 VTVAVIDTGVDPDHPDLDGLFGGGDGG--NDDDDNENGPTDPDDGNGHGTHVAGIIAASANNGG-GVGVAPGAKLIP--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 227 ppplrpgVRMLDGEVTDAVEARSLGLN----PNHIHIYSASWGPEDDGKTvDGPARLAEEAFFRgvsqgrggLGSIFVWA 302
Cdd:cd00306   75 -------VKVLDGDGSGSSSDIAAAIDyaaaDQGADVINLSLGGPGSPPS-SALSEAIDYALAK--------LGVLVVAA 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 303 SGNGGREHDScNCDGYTNSIYTLSISSATQFGNVPWYSeACSSTLATTYSSGNQnekQIVTTDLRQKCTESHTGTSASAP 382
Cdd:cd00306  139 AGNDGPDGGT-NIGYPAASPNVIAVGAVDRDGTPASPS-SNGGAGVDIAAPGGD---ILSSPTTGGGGYATLSGTSMAAP 213

                        250       260
                 ....*....|....*....|....*...
gi 755520810 383 LAAGIIALTLEANKNLTWRDMQHLVVQT 410
Cdd:cd00306  214 IVAGVAALLLSANPDLTPAQVKAALLST 241
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
 112-390 8.42e-23

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


Pssm-ID: 173810 [Multi-domain]  Cd Length: 260  Bit Score: 98.49  E-value: 8.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 112 EPTDPKFPQQWYLsgvtqRDLNVKEAWAQGfTGHGIVVSILDDGIEKNHPDLA-GNYDPGASFDVNDQDPdpqprytqMN 190
Cdd:cd07484    1 TPNDPYYSYQWNL-----DQIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLLkVKFVLGYDFVDNDSDA--------MD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 191 DNRHGTRCAGEVAAVANNGVCGVGVAYNARIgaplFPpplrpgVRMLD--GEVTDAVEARSLglnpnhihIYSAswgpeD 268
Cdd:cd07484   67 DNGHGTHVAGIIAAATNNGTGVAGVAPKAKI----MP------VKVLDanGSGSLADIANGI--------RYAA-----D 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 269 DGKTV-------DGPARLAEEAFFRGVSQgrgglGSIFVWASGNGGREHDScncdgYTNSI-YTLSISSATQFGNVPWYS 340
Cdd:cd07484  124 KGAKVinlslggGLGSTALQEAINYAWNK-----GVVVVAAAGNEGVSSVS-----YPAAYpGAIAVAATDQDDKRASFS 193

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 755520810 341 EAcSSTLATTYSSGNqnekqIVTTDLRQKcTESHTGTSASAPLAAGIIAL 390
Cdd:cd07484  194 NY-GKWVDVSAPGGG-----ILSTTPDGD-YAYMSGTSMATPHVAGVAAL 236
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
 136-397 1.06e-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: 89.85  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 136 EAWAQGFTGHGIVVSILDDGIEKNHPDLAGNYD-PGASFDVNDQDPDPQ---PRYTQMNDNRHGTRCAGEVAAVANN--G 209
Cdd:cd07485    1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDgDGYDPAVNGYNFVPNvgdIDNDVSVGGGHGTHVAGTIAAVNNNggG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 210 VCGV----GVAYNARI-GAPLFPPplrPGVRMLDGEVTDAVEARSLGLNpnhihIYSASWGpeddGKTVDGPARLAEEAF 284
Cdd:cd07485   81 VGGIagagGVAPGVKImSIQIFAG---RYYVGDDAVAAAIVYAADNGAV-----ILQNSWG----GTGGGIYSPLLKDAF 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 285 FRGVSQGRGGL--GSIFVWASGNggrEHDSCncdGYTNSIYTLSISSATQFGNvpwYSEACSSTLATTYSSGNQNEKQIV 362
Cdd:cd07485  149 DYFIENAGGSPldGGIVVFSAGN---SYTDE---HRFPAAYPGVIAVAALDTN---DNKASFSNYGRWVDIAAPGVGTIL 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 755520810 363 TTDLRQKCTESHT-----GTSASAPLAAGIIALTLEANKN 397
Cdd:cd07485  220 STVPKLDGDGGGNyeylsGTSMAAPHVSGVAALVLSKFPD 259
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
 143-410 3.47e-19

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: 88.15  E-value: 3.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 143 TGHGIVVSILDDGIEKNHPDLAGNYDP-GASFDVNDQDPDPQPRYtqmndNRHGTRCAGeVAAVANNGVCGVGVAYNARI 221
Cdd:cd04848    1 TGAGVKVGVIDSGIDLSHPEFAGRVSEaSYYVAVNDAGYASNGDG-----DSHGTHVAG-VIAAARDGGGMHGVAPDATL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 222 -GAPLFPPPLRPGVRMLDGEVTDAvearslgLNPNHIHIYSASWGPEDDGKTVDGPARL--------AEEAFFRGVSQgr 292
Cdd:cd04848   75 ySARASASAGSTFSDADIAAAYDF-------LAASGVRIINNSWGGNPAIDTVSTTYKGsaatqgntLLAALARAANA-- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 293 gglGSIFVWASGNGGREHDSCNCDGYT-------NSIytLSISSATQFGNVP--WYSEAC----SSTLA-------TTYS 352
Cdd:cd04848  146 ---GGLFVFAAGNDGQANPSLAAAALPylepeleGGW--IAVVAVDPNGTIAsySYSNRCgvaaNWCLAapgeniySTDP 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755520810 353 SGNQNEKQIvttdlrqkcteshTGTSASAPLAAGIIALTLEANKNLTwrdmQHLVVQT 410
Cdd:cd04848  221 DGGNGYGRV-------------SGTSFAAPHVSGAAALLAQKFPWLT----ADQVRQT 261
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
 146-399 7.00e-19

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: 86.43  E-value: 7.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 146 GIVVSILDDGIEKNHPDLAGNYDPGASFdVNDQDPDPQprytqmNDNRHGTRCAGEVAAvANNGVCGVGVAYNARIGApl 225
Cdd:cd07477    1 GVKVAVIDTGIDSSHPDLKLNIVGGANF-TGDDNNDYQ------DGNGHGTHVAGIIAA-LDNGVGVVGVAPEADLYA-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 226 fppplrpgVRMLD----GEVTDAVEARSLGLNpNHIHIYSASWGPEDDGKTVdgparlaEEAFFRGVSQGrgglgsIF-V 300
Cdd:cd07477   71 --------VKVLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLGGPSDSPAL-------REAIKKAYAAG------ILvV 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 301 WASGNggrehdscncDGYTNSIYT--------LSISSATQFGNVPWYSeacsstlattySSGNQNE-----KQIVTTDLR 367
Cdd:cd07477  129 AAAGN----------SGNGDSSYDypakypsvIAVGAVDSNNNRASFS-----------STGPEVElaapgVDILSTYPN 187

                        250       260       270
                 ....*....|....*....|....*....|..
gi 755520810 368 QKcTESHTGTSASAPLAAGIIALTLEANKNLT 399
Cdd:cd07477  188 ND-YAYLSGTSMATPHVAGVAALVWSKRPELT 218
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
 144-420 8.02e-18

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: 84.69  E-value: 8.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 144 GHGIVVSILDDGIEKNHPDLAG------NYDPGASFDVNDQDPDPQPRYTQMNDNR-------HGTRCAGEVAAVANNGV 210
Cdd:cd07474    1 GKGVKVAVIDTGIDYTHPDLGGpgfpndKVKGGYDFVDDDYDPMDTRPYPSPLGDAsagdatgHGTHVAGIIAGNGVNVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 211 CGVGVAYNARIGAplfppplrpgVRMLD--GEVTDAVEARSL--GLNPnHIHIYSASWGPEDDGKtvDGPARLAEEAFFR 286
Cdd:cd07474   81 TIKGVAPKADLYA----------YKVLGpgGSGTTDVIIAAIeqAVDD-GMDVINLSLGSSVNGP--DDPDAIAINNAVK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 287 gvsqgrggLGSIFVWASGNGGrehDSCNCDGyTNSIYTLSISSATQFGNVPWYSEacssTLATTYSSGNQNEKQIVTTDL 366
Cdd:cd07474  148 --------AGVVVVAAAGNSG---PAPYTIG-SPATAPSAITVGASTVADVAEAD----TVGPSSSRGPPTSDSAIKPDI 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755520810 367 -------------RQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNADD 420
Cdd:cd07474  212 vapgvdimstapgSGTGYARMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLYDSDGV 278
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
 146-399 3.34e-16

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: 79.64  E-value: 3.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 146 GIVVSILDDGIEKNHPDLAGNYDPGASF----------DVNDQDP-DPQPRYTQMNDNR-------------HGTRCAGE 201
Cdd:cd07496    1 GVVVAVLDTGVLFHHPDLAGVLLPGYDFisdpaiandgDGRDSDPtDPGDWVTGDDVPPggfcgsgvspsswHGTHVAGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 202 VAAVANNGVcGV-GVAYNARIgaplFPpplrpgVRML---DGEVTDAVEArslglnpnhihIYSASWGPEDDGKTVDGPA 277
Cdd:cd07496   81 IAAVTNNGV-GVaGVAWGARI----LP------VRVLgkcGGTLSDIVDG-----------MRWAAGLPVPGVPVNPNPA 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 278 R-----LAEEAFFRGVSQ----GRGGLGSIFVWASGNGGR--EHDS-CNCDGytnsiyTLSISSATQFGNVPWYSEACSS 345
Cdd:cd07496  139 KvinlsLGGDGACSATMQnainDVRARGVLVVVAAGNEGSsaSVDApANCRG------VIAVGATDLRGQRASYSNYGPA 212

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755520810 346 T-LAT----TYSSGNQNEKQIVTTDLRQKCTESHT---GTSASAPLAAGIIALTLEANKNLT 399
Cdd:cd07496  213 VdVSApggdCASDVNGDGYPDSNTGTTSPGGSTYGflqGTSMAAPHVAGVAALMKSVNPSLT 274
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
 134-413 9.39e-13

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: 69.94  E-value: 9.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 134 VKEAWAQGFTGHGIVVSILDDGIEKNHPDLAGNYDPGASF--------DVNDQDPDPQPRYTQMNDNRHGTRCAGEVAav 205
Cdd:cd07489    2 VDKLHAEGITGKGVKVAVVDTGIDYTHPALGGCFGPGCKVaggydfvgDDYDGTNPPVPDDDPMDCQGHGTHVAGIIA-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 206 ANNGVCG-VGVAYNARIGA-PLFPPPLRPGVRMLDGEVTDAVEARSlglnpnhiHIYSASWGpeDDGKTVDGPA-----R 278
Cdd:cd07489   80 ANPNAYGfTGVAPEATLGAyRVFGCSGSTTEDTIIAAFLRAYEDGA--------DVITASLG--GPSGWSEDPWavvasR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 279 LAEEAFFRGVSQG-RGGLGSifvWASGNGGrehdscncdgytNSIYTLSISSAtqfgnvpwyseacsstlATTYSS-GNQ 356
Cdd:cd07489  150 IVDAGVVVTIAAGnDGERGP---FYASSPA------------SGRGVIAVASV-----------------DSYFSSwGPT 197

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 357 NEKQ-----------IVTTDLRQKCT-ESHTGTSASAPLAAGIIALTLEA-NKNLTWRDMQHLVVQTSKP 413
Cdd:cd07489  198 NELYlkpdvaapggnILSTYPLAGGGyAVLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKP 267
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
 146-399 1.61e-12

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: 68.34  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 146 GIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPrytqMNDNRHGTRCAGEVAAVANNGVcGVGVAynarigapl 225
Cdd:cd07490    1 GVTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEV----FDAGGHGTHVSGTIGGGGAKGV-YIGVA--------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 226 fppplrPGVRMLDGEVTDAVEARSLGLnpnhihIYSASWGPEDDGKTVD---GPARLAEEAFFRGVSQGRGGLGSIFVWA 302
Cdd:cd07490   67 ------PEADLLHGKVLDDGGGSLSQI------IAGMEWAVEKDADVVSmslGGTYYSEDPLEEAVEALSNQTGALFVVS 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 303 SGNGGreHDSCNCDGYTNSiyTLSISSATQFGNVPWYSeACSSTLATTYSSGNQNEKQIVTTDLRQKCT----------- 371
Cdd:cd07490  135 AGNEG--HGTSGSPGSAYA--ALSVGAVDRDDEDAWFS-SFGSSGASLVSAPDSPPDEYTKPDVAAPGVdvysarqgang 209

                        250       260       270
                 ....*....|....*....|....*....|..
gi 755520810 372 ----ESHTGTSASAPLAAGIIALTLEANKNLT 399
Cdd:cd07490  210 dgqyTRLSGTSMAAPHVAGVAALLAAAHPDLS 241
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
 137-582 3.10e-12

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: 70.24  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 137 AWAQGFTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVA 216
Cdd:COG4935  223 GAGLAAAGGGGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 217 YNARIGAPLFPPPLRPGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLG 296
Cdd:COG4935  303 AGTGNAAAAAAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAAG 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 297 SIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDlrqkcTESHTG 376
Cdd:COG4935  383 AAAGAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADA-----GSTSTG 457

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 377 TSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNADDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAp 456
Cdd:COG4935  458 TGSAAGAAGGTTTATSGLASSTTAAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVA- 536

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 457 qrkciveIlvePKDIGKRLEVRKAVTACLgepnhitRLEHVQARLTLSYNRRGDLAIHLISPMGTRSTLLAarPHDYSAD 536
Cdd:COG4935  537 -------I---PDNGPAGVTSTITVSGGG-------AVEDVTVTVDITHTYRGDLVITLISPDGTTVVLKN--RSGGSAD 597

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 755520810 537 GFNdWAFMTTHSWDEDPAGEWVLEIENTSEANNyGTLTKFTLVLYG 582
Cdd:COG4935  598 NIN-ATFDVANFSGESANGTWTLRVVDTAGGDT-GTLNSWSLTFTG 641
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
 132-446 1.14e-11

type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair]


Pssm-ID: 274856 [Multi-domain]  Cd Length: 350  Bit Score: 66.96  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  132 LNVKEAWAQGfTGHGIVVSILDDGIEKnHPDLAGNYDPGASFdVNDQDpdpqprytQMND-NRHGTRCAGEVAAVANNGV 210
Cdd:TIGR03921   1 LSLEQAWKFS-TGAGVTVAVIDTGVDD-HPRLPGLVLPGGDF-VGSGD--------GTDDcDGHGTLVAGIIAGRPGEGD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  211 CGVGVAYNARI-----GAPLFPPPLRPG----VRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDdgktvdgpARLAE 281
Cdd:TIGR03921  70 GFSGVAPDARIlpirqTSAAFEPDEGTSgvgdLGTLAKAIRRAADLGADVINISLVACLPAGSGADD--------PELGA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  282 ---EAFFRGVsqgrgglgsIFVWASGNGGrehDSCNCDgyTNSI-----YTLSISSATQFGNVPWYSEACSSTLATTYSS 353
Cdd:TIGR03921 142 avrYALDKGV---------VVVAAAGNTG---GDGQKT--TVVYpawypGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGE 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  354 GnqnekqIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpahlnADDWATNGvgrkVSHS 433
Cdd:TIGR03921 208 N------IVSLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEAT-------ADHPARGG----RDDY 270

                         330
                  ....*....|...
gi 755520810  434 YGYGLLDAGAMVA 446
Cdd:TIGR03921 271 VGYGVVDPVAALT 283
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
 144-399 9.62e-11

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: 62.99  E-value: 9.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 144 GHGIVVSILDDGIEKNHPDLAGNYDPGASFdVNDQDPDPQPRytqmNDNRHGTRCAGEVAA--VANNGVcGVGVAYNARI 221
Cdd:cd07487    1 GKGITVAVLDTGIDAPHPDFDGRIIRFADF-VNTVNGRTTPY----DDNGHGTHVAGIIAGsgRASNGK-YKGVAPGANL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 222 gaplfppplrPGVRMLD----GEVTDAVEA----RSLGlNPNHIHIYSASWGPEDDGKTVDGPARLA-EEAFFRGVsqgr 292
Cdd:cd07487   75 ----------VGVKVLDdsgsGSESDIIAGidwvVENN-EKYNIRVVNLSLGAPPDPSYGEDPLCQAvERLWDAGI---- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 293 gglgsIFVWASGNGGREHDSCNCDGytNSIYTLSISSATQFGNVPWYSEACSS---TLA--------------TTYSSGN 355
Cdd:cd07487  140 -----VVVVAAGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSSrgpTGDgrikpdvvapgeniVSCRSPG 212

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 755520810 356 QNEKQIVTTDLRQKcteshTGTSASAPLAAGIIALTLEANKNLT 399
Cdd:cd07487  213 GNPGAGVGSGYFEM-----SGTSMATPHVSGAIALLLQANPILT 251
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
 142-305 3.51e-10

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: 62.01  E-value: 3.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 142 FTGHGIVVSILDDGIEKNHPDLAGNYDPGASF----DVNDQdpdpqprytqmndNRHGTRCAGEVAAVANNGVcGVGVAY 217
Cdd:cd07480    5 FTGAGVRVAVLDTGIDLTHPAFAGRDITTKSFvggeDVQDG-------------HGHGTHCAGTIFGRDVPGP-RYGVAR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 218 NARI--GAPLfpppLRPGVRMlDGEVTDAVE-ARSLGlnpnhIHIYSASWG-----PEDDGKTVDGPARLAEEAFFRGV- 288
Cdd:cd07480   71 GAEIalIGKV----LGDGGGG-DGGILAGIQwAVANG-----ADVISMSLGadfpgLVDQGWPPGLAFSRALEAYRQRAr 140

                        170       180
                 ....*....|....*....|....*..
gi 755520810 289 ----------SQGRGGLGSIFVWASGN 305
Cdd:cd07480  141 lfdalmtlvaAQAALARGTLIVAAAGN 167
FU smart00261
Furin-like repeats;
648-685 6.49e-10

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 55.21  E-value: 6.49e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 755520810   648 ASVCTPCHASCATCQGPAPTDCLSCPSHASLDpvEQTC 685
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKC 36
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
 122-399 1.97e-09

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: 59.07  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 122 WYLSGVTQRDLNVKEAWAQGF-TGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPqprytqmndNRHGTRCAG 200
Cdd:cd04077    1 WGLDRISQRDLPLDGTYYYDSsTGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDC---------NGHGTHVAG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 201 EVAAVAnngvcgVGVAYNARIgaplfppplrPGVRMLD----GEVTDAVEarslGLNpnhihiYSASWGPEDDGKTV--- 273
Cdd:cd04077   72 TVGGKT------YGVAKKANL----------VAVKVLDcngsGTLSGIIA----GLE------WVANDATKRGKPAVanm 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 274 --DGPARLAEEAFFRGVSQGrgglGSIFVWASGNGGRehDSCNcdgYT--NSIYTLSISSATQFGNVPWYSE--AC---- 343
Cdd:cd04077  126 slGGGASTALDAAVAAAVNA----GVVVVVAAGNSNQ--DACN---YSpaSAPEAITVGATDSDDARASFSNygSCvdif 196

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755520810 344 ---SSTLATTYSSGNqnekqivttdlrqkCTESHTGTSASAPLAAGIIALTLEANKNLT 399
Cdd:cd04077  197 apgVDILSAWIGSDT--------------ATATLSGTSMAAPHVAGLAAYLLSLGPDLS 241
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 653-685 2.34e-07

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 47.90  E-value: 2.34e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 755520810 653 PCHASCATCQGPAPTDCLSCPSHASLDpvEQTC 685
Cdd:cd00064    1 PCHPSCATCTGPGPDQCTSCRHGFYLD--GGTC 31
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
 141-390 3.77e-07

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: 52.72  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 141 GFTGHGIVVSILDDGIEKNHPDLagnYDPGASfDVNDQDP-----DPQPRYTQMNDNrHGTRCAGEVAAVANNGVCGV-- 213
Cdd:cd04842    3 GLTGKGQIVGVADTGLDTNHCFF---YDPNFN-KTNLFHRkivryDSLSDTKDDVDG-HGTHVAGIIAGKGNDSSSISly 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 214 -GVAYNARI--------GAPLFPPPlrpgvrMLDGEVTDAVEARSlglnpnhiHIYSASWGPEDDG------KTVDGPAR 278
Cdd:cd04842   78 kGVAPKAKLyfqdigdtSGNLSSPP------DLNKLFSPMYDAGA--------RISSNSWGSPVNNgytllaRAYDQFAY 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 279 LAEEAffrgvsqgrgglgsIFVWASGNGGrehdscncDGYTNSIYTLSISSatqfgNVpwYSEACSSTLATTYSSGNQNE 358
Cdd:cd04842  144 NNPDI--------------LFVFSAGNDG--------NDGSNTIGSPATAK-----NV--LTVGASNNPSVSNGEGGLGQ 194

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755520810 359 KQIV-----------TTDLRQK----------------------CTESH----TGTSASAPLAAGIIAL 390
Cdd:cd04842  195 SDNSdtvasfssrgpTYDGRIKpdlvapgtgilsarsggggigdTSDSAytskSGTSMATPLVAGAAAL 263
Peptidases_S8_7 cd07491
Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the ...
 147-392 4.79e-07

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


Pssm-ID: 173816  Cd Length: 247  Bit Score: 51.95  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 147 IVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPD-PQPRYtqMNDNRHGTRCAGEVAAvanngVCGVGVAYNARIGApl 225
Cdd:cd07491    5 IKVALIDDGVDILDSDLQGKIIGGKSFSPYEGDGNkVSPYY--VSADGHGTAMARMICR-----ICPSAKLYVIKLED-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 226 FPPPLRPGVRMLDGEVTDAVEARSlglnPNHIHIYSASWGPEDDGKTVDGPARLaEEAFFRGVSQGrgglgsIFVWAS-- 303
Cdd:cd07491   76 RPSPDSNKRSITPQSAAKAIEAAV----EKKVDIISMSWTIKKPEDNDNDINEL-ENAIKEALDRG------ILLFCSas 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 304 --GNGGREHDSCnCDGYTNsiyTLSISSATQFGNV--PWYSEacssTLATTYSSGNQnekqiVTTDLRQKCTES---HTG 376
Cdd:cd07491  145 dqGAFTGDTYPP-PAARDR---IFRIGAADEDGGAdaPVGDE----DRVDYILPGEN-----VEARDRPPLSNSfvtHTG 211

                        250
                 ....*....|....*.
gi 755520810 377 TSASAPLAAGIIALTL 392
Cdd:cd07491  212 SSVATALAAGLAALIL 227
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
 149-422 9.58e-07

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 52.28  E-value: 9.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 149 VSILDDGIEKNHPDLAGNYDP-----------------------GASFDVNDQDPdpqprytqMNDNRHGTRCAGEVAAV 205
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIDVnvkelhgrkgidddnngnvddeyGANFVNNDGGP--------MDDNYHGTHVSGIISAI 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 206 ANNGVCGVGVAYNARIGAplfppplrpgVRMLD----GEVTDAVEARSLGLNPNhIHIYSASWGPEDDGKTVDGPARLAE 281
Cdd:PTZ00262 392 GNNNIGIVGVDKRSKLII----------CKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFNESVKYLE 460

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 282 EaffrgvsqgrggLGSIFVWASGNGGREHDSCN----CDGYTNSIY----------TLSISSATQFGNVPwYSEACSSTL 347
Cdd:PTZ00262 461 E------------KGILFVVSASNCSHTKESKPdipkCDLDVNKVYppilskklrnVITVSNLIKDKNNQ-YSLSPNSFY 527

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755520810 348 ATTYSSGNQNEKQIVTTDLRQKCTEShTGTSASAPLAAGIIALTLEANKNLTWRD----MQHLVVQTskPAHLNADDWA 422
Cdd:PTZ00262 528 SAKYCQLAAPGTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEviriLKESIVQL--PSLKNKVKWG 603
FU smart00261
Furin-like repeats;
591-629 1.36e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.58  E-value: 1.36e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 755520810   591 PPESSGCKTLTSSQA--CVVCEEGYSLHQKSCVQHCPPGFI 629
Cdd:smart00261   5 KPCHPECATCTGPGPddCTSCKHGFFLDGGKCVSECPPGTY 45
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
 144-398 1.63e-06

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


Pssm-ID: 173807 [Multi-domain]  Cd Length: 264  Bit Score: 50.45  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 144 GHGIVVSILDDGIEKNHPDLAGNYDP--GASFDVNDQDPDPQPRYTQMND-NRHGTRCAGevAAVANNGV-CGVGVAYNA 219
Cdd:cd07481    1 GTGIVVANIDTGVDWTHPALKNKYRGwgGGSADHDYNWFDPVGNTPLPYDdNGHGTHTMG--TMVGNDGDgQQIGVAPGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 220 R-IGAplfppplrpgvRMLD---GEVTDAVEARSLGLNPNHI-----------HIYSASWGpeddgktvdGPARLAEeaF 284
Cdd:cd07481   79 RwIAC-----------RALDrngGNDADYLRCAQWMLAPTDSagnpadpdlapDVINNSWG---------GPSGDNE--W 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 285 FRGVSQGRGGLGSIFVWASGNGGREHDSCNCD--GYTNSIYTLSISSATQFGNVpwyseacSSTLATTYSSGNQNekqIV 362
Cdd:cd07481  137 LQPAVAAWRAAGIFPVFAAGNDGPRCSTLNAPpaNYPESFAVGATDRNDVLADF-------SSRGPSTYGRIKPD---IS 206

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755520810 363 T--TDLRQKCTE----SHTGTSASAPLAAGIIALTLEANKNL 398
Cdd:cd07481  207 ApgVNIRSAVPGggygSSSGTSMAAPHVAGVAALLWSANPSL 248
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
 132-390 5.99e-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: 5.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 132 LNVKEAWAQ-GFTGHGIVVSILDDGIEKNHPDLAGNydpGASfdvndqdpdPQPRYTQMNDNRHGTRCAGEVAAvANNGV 210
Cdd:cd04843    2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGN---GIT---------LISGLTDQADSDHGTAVLGIIVA-KDNGI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 211 CGVGVAYNARIGapLFPPPLRPGVRmldgevtDAVEARSLGLNPNHIHIYSASWGPEDdgktVDGPARLAE--EAFFRGV 288
Cdd:cd04843   69 GVTGIAHGAQAA--VVSSTRVSNTA-------DAILDAADYLSPGDVILLEMQTGGPN----NGYPPLPVEyeQANFDAI 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 289 SQGRgGLGSIFVWASGNGGREHDSC-NCDGYTNSIYTLSI-----------SSATQfgnvpwYSEACSST---------- 346
Cdd:cd04843  136 RTAT-DLGIIVVEAAGNGGQDLDAPvYNRGPILNRFSPDFrdsgaimvgagSSTTG------HTRLAFSNygsrvdvygw 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 755520810 347 ---LATTYSSGNQNEKqivttDLRQKCTESHTGTSASAPLAAGIIAL 390
Cdd:cd04843  209 genVTTTGYGDLQDLG-----GENQDYTDSFSGTSSASPIVAGAAAS 250
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
 375-447 1.08e-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: 48.06  E-value: 1.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755520810 375 TGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpahlnADDWATNGvgrkVSHSYGYGLLDAGAMVAL 447
Cdd:cd05562  214 FGTSAAAPHAAGVAALVLSANPGLTPADIRDALRST-------ALDMGEPG----YDNASGSGLVDADRAVAA 275
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
 146-213 1.18e-05

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: 47.33  E-value: 1.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755520810 146 GIVVSILDDGIEKNHPDLAGN------YDPGASFDVNDQDPDpqprytqmnDNRHGTRCAGEVAAVANNGVCGV 213
Cdd:cd07492    1 GVRVAVIDSGVDTDHPDLGNLaldgevTIDLEIIVVSAEGGD---------KDGHGTACAGIIKKYAPEAEIGS 65
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
 594-631 1.21e-05

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 43.28  E-value: 1.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755520810 594 SSGCKTLTSS--QACVVCEEGYSLHQKSCVQHCPPGFIPQ 631
Cdd:cd00064    3 HPSCATCTGPgpDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
 136-420 1.91e-05

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


Pssm-ID: 173801 [Multi-domain]  Cd Length: 346  Bit Score: 47.65  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 136 EAWAQG-FTGHGIVVSILDDGIEKNHPDLAGNyDPGA-----SFDVNDQDPDPQP------------RYTQMNDN----- 192
Cdd:cd07475    1 PLWDKGgYKGEGMVVAVIDSGVDPTHDAFRLD-DDSKakyseEFEAKKKKAGIGYgkyynekvpfayNYADNNDDilded 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 193 ---RHGTRCAGEVAAVANNGVCG---VGVAYNARI-GAPLFPPPLRPGVRMLD--GEVTDAVEarslgLNPNHIhiySAS 263
Cdd:cd07475   80 dgsSHGMHVAGIVAGNGDEEDNGegiKGVAPEAQLlAMKVFSNPEGGSTYDDAyaKAIEDAVK-----LGADVI---NMS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 264 WGPEDDGKTVDGPARLA-EEAFFRGVsqgrgglgsIFVWASGNggrehdscncDGYTNSIYTLSISSATQFGNVPWYSEA 342
Cdd:cd07475  152 LGSTAGFVDLDDPEQQAiKRAREAGV---------VVVVAAGN----------DGNSGSGTSKPLATNNPDTGTVGSPAT 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 343 CSSTLAT---TYSSGNQNEKQI-------VTTDLRQK-----------CT------ESHTGTSASAPLAAGIIALTLEA- 394
Cdd:cd07475  213 ADDVLTVasaNKKVPNPNGGQMsgfsswgPTPDLDLKpditapggniySTvndntyGYMSGTSMASPHVAGASALVKQRl 292

                        330       340       350
                 ....*....|....*....|....*....|...
gi 755520810 395 ---NKNLTWRDMQHLVVQ----TSKPAHLNADD 420
Cdd:cd07475  293 kekYPKLSGEELVDLVKNllmnTATPPLDSEDT 325
VSP pfam03302
Giardia variant-specific surface protein;
604-678 1.94e-05

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 47.66  E-value: 1.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755520810  604 QACVVCEEGYSL--HQKSCVQHCPPGFipqvldthYSTendveiirASVCTPCHASCATCQGPAPTDCLSCPSHASL 678
Cdd:pfam03302  74 KICKECTVANCKtcEDQGQCQACNDGF--------YKS--------GDACSPCHESCKTCSGGTASDCTECLTGKAL 134
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
 147-221 5.38e-05

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: 45.82  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 147 IVVSILDDGIEKNHPDLAGNYDPGasfdVNDQDPDPQPRYTQMND----------NRHGTRCAGEVAAVANNGvcgvGVA 216
Cdd:cd07482    2 VTVAVIDSGIDPDHPDLKNSISSY----SKNLVPKGGYDGKEAGEtgdindivdkLGHGTAVAGQIAANGNIK----GVA 73


                 ....*
gi 755520810 217 YNARI 221
Cdd:cd07482   74 PGIGI 78
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
 144-339 9.84e-05

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: 45.15  E-value: 9.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 144 GHGIVVSILDDGIEKNHPDLA--GNYDPGASFDvndqDP-------DPQPR-YTQMND-NRHGTRCAGEVAAVANNGVCG 212
Cdd:cd07497    1 GEGVVIAIVDTGVDYSHPDLDiyGNFSWKLKFD----YKayllpgmDKWGGfYVIMYDfFSHGTSCASVAAGRGKMEYNL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 213 ---------VGVAYNARIGAPLFpppLRPGVRMLDGEVTDAVEARSLGLNPNH-----IHIYSASWGPEDDGKTVDGPAR 278
Cdd:cd07497   77 ygytgkfliRGIAPDAKIAAVKA---LWFGDVIYAWLWTAGFDPVDRKLSWIYtggprVDVISNSWGISNFAYTGYAPGL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755520810 279 LAEEAFFRGVSQGRgglGSIFVWASGNGGREHDSCNCDGytNSIYTLSISSATQFGNVPWY 339
Cdd:cd07497  154 DISSLVIDALVTYT---GVPIVSAAGNGGPGYGTITAPG--AASLAISVGAATNFDYRPFY 209
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
 606-672 1.01e-04

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


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 42.75  E-value: 1.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755520810  606 CVVCEegYSLHQKSCVQHCPpgfIPQVLDTHYSTEndveiiraSVCTPCHASC------ATCQGPAPTDCLSC 672
Cdd:pfam14843  19 CLSCR--NFSRGGTCVESCN---ILQGEPREYVVN--------STCVPCHPEClpqngtATCSGPGADNCTKC 78
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
 594-631 1.39e-03

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: 38.95  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 755520810  594 SSGCKTLTSSQACVVCEEGYSLHQKSCVQHCPPGFIPQ 631
Cdd:pfam15913  59 AENCESCFSKDFCTKCKEGFYLHKGKCLDTCPEGTAAQ 96
TNFRSF1B cd10577
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B ...
 606-685 2.29e-03

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism).


Pssm-ID: 276903 [Multi-domain]  Cd Length: 163  Bit Score: 39.38  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 606 CVVCEEGYSLHQKSCVQHCPPGFIPQVLDTHYSTendveiiraSVCTPCHASCATCQGPAPTDCLSCPSHASLDPVE-QT 684
Cdd:cd10577    1 CRNSKEYYDEKAQMCCSKCPPGQHVKHSCTKTSD---------TVCAPCEESTYTQLWNWVPECLSCSSPCSSDQVEtQA 71


                 .
gi 755520810 685 C 685
Cdd:cd10577   72 C 72
VSP pfam03302
Giardia variant-specific surface protein;
592-674 3.07e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 40.72  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810  592 PESSGCKTLTSSQACVVCEEGYSLHQKSCVQhCPPGFIPQVLDTHYSTENDVEIIRASVCTPCHASCATCQGpAPTDCLS 671
Cdd:pfam03302 228 PGKSVCEEANSGGTCQKEAPGYKLNNGDLVT-CSPGCKTCTSNTVCTTCMDGYVKTSDSCTKCDSSCETCTG-ATTTCKT 305


                  ...
gi 755520810  672 CPS 674
Cdd:pfam03302 306 CAT 308
PTZ00214 PTZ00214
high cysteine membrane protein Group 4; Provisional
 595-680 4.88e-03

high cysteine membrane protein Group 4; Provisional


Pssm-ID: 173479 [Multi-domain]  Cd Length: 800  Bit Score: 40.67  E-value: 4.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755520810 595 SGCKTL---TSSQACVVCEEGY-SLHQKSCVQHCP---PGFIPQVLDTHYSTENDVEII-------RASVCTPCHASCAT 660
Cdd:PTZ00214 362 SGCATCgynSGAVTCTRCSAGYlGVDGKSCSESCSgdtRGVCTKVAEGSESTEVSCRCVckptfynSSGTCTPCTDSCAV 441

                         90       100
                 ....*....|....*....|
gi 755520810 661 CQGPAPTDCLSCPSHASLDP 680
Cdd:PTZ00214 442 CKDGTPTGCQQCSPGKILEF 461
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
 138-161 9.14e-03

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


Pssm-ID: 173805 [Multi-domain]  Cd Length: 255  Bit Score: 38.59  E-value: 9.14e-03
                         10        20
                 ....*....|....*....|....
gi 755520810 138 WAQGFTGHGIVVSILDDGIEKNHP 161
Cdd:cd07479    1 WQLGYTGAGVKVAVFDTGLAKDHP 24
 
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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