NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1843419910|ref|NP_001369548|]
View 

furin isoform 1 preproprotein [Homo sapiens]

Protein Classification

Peptidases_S8_Protein_convertases_Kexins_Furin-lik and P_proprotein domain-containing protein( domain architecture ID 11243032)

protein containing domains S8_pro-domain, Peptidases_S8_Protein_convertases_Kexins_Furin-lik, P_proprotein, and FU

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
113-402 1.76e-175

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: 505.56  E-value: 1.76e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 113 PTDPKFPQQWYLSGVTQR------DLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRY 186
Cdd:cd04059     1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 187 TqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGP 266
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 267 ARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQ 346
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1843419910 347 N-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSK 402
Cdd:cd04059   239 NpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
33-107 2.83e-36

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: 131.19  E-value: 2.83e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1843419910  33 TWAVRIPGGPAVANSVARKHGFLNLGQIFG--DYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKR 107
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
484-570 9.74e-36

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: 129.70  E-value: 9.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 484 LEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTsEANNYGTL 563
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79

                  ....*..
gi 1843419910 564 TKFTLVL 570
Cdd:pfam01483  80 NSWQLTL 86
FU smart00261
Furin-like repeats;
638-675 6.52e-09

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 52.13  E-value: 6.52e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1843419910  638 ASVCAPCHASCATCQGPALTDCLSCPSHASLDpvEQTC 675
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKC 36
FU smart00261
Furin-like repeats;
581-618 1.25e-06

Furin-like repeats;


:

Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.58  E-value: 1.25e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1843419910  581 PPESSGCKTLTSSQA--CVVCEEGFSLHQKSCVQHCPPGF 618
Cdd:smart00261   5 KPCHPECATCTGPGPddCTSCKHGFFLDGGKCVSECPPGT 44
 
Name Accession Description Interval E-value
Peptidases_S8_Protein_convertases_Kexins_Furin-lik cd04059
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ...
113-402 1.76e-175

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: 505.56  E-value: 1.76e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 113 PTDPKFPQQWYLSGVTQR------DLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRY 186
Cdd:cd04059     1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 187 TqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGP 266
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 267 ARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQ 346
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1843419910 347 N-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSK 402
Cdd:cd04059   239 NpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
144-427 6.95e-62

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: 210.01  E-value: 6.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 144 GHGIVVSILDDGIEKNHPDLAGNYDPGASFD----VNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNA 219
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDpeasVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 220 RIGGVRML-DGEVTDAVEARSLGLN-PNHIHIYSASWGPEddgKTVDGPARLAEEAFFRGvsqGRGGLGSIFVWASGNGG 297
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 298 REHDSCNCDGY-TNSIYTLSISSATQF--GNVPWYSEACSS-------TLA----TTYSSGNQNEKQIVTTDLRQKCTES 363
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVDEAseGNLASFSSYGPTldgrlkpDIVapggNITGGNISSTLLTTTSDPPNQGYDS 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1843419910 364 HTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpahlnandwATNGVGRKVSHSYGYG 427
Cdd:pfam00082 235 MSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNT-----------ATDLGDAGLDRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
81-440 3.05e-37

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 145.63  E-value: 3.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910  81 RPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNH 160
Cdd:COG1404    45 AAALVAAAAAAAVAAALAAPLAPAALAAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADH 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 161 PDLAGNYDPGASFDVNDQDPDpqprytqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLD--GEVTDAVEAR 238
Cdd:COG1404   125 PDLAGRVVGGYDFVDGDGDPS--------DDNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDdnGSGTTSDIAA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 239 slGLN---PNHIHIYSASWGPEDDGKTvDGPARLAEEAFFRGVsqgrgglgsIFVWASGNGGrehDSCNCDGYTNSIY-T 314
Cdd:COG1404   197 --AIDwaaDNGADVINLSLGGPADGYS-DALAAAVDYAVDKGV---------LVVAAAGNSG---SDDATVSYPAAYPnV 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 315 LSISSATQFGNVPWYSeacsstlattySSGNQNE-----KQIVTTDLRQKcTESHTGTSASAPLAAGIIALTLEANKNLT 389
Cdd:COG1404   262 IAVGAVDANGQLASFS-----------NYGPKVDvaapgVDILSTYPGGG-YATLSGTSMAAPHVAGAAALLLSANPDLT 329
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1843419910 390 WRDMQHLVVQTSKPAHLNANDwatngvgrkvshsYGYGLLDAGAMVALAQN 440
Cdd:COG1404   330 PAQVRAILLNTATPLGAPGPY-------------YGYGLLADGAAGATSAG 367
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
33-107 2.83e-36

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: 131.19  E-value: 2.83e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1843419910  33 TWAVRIPGGPAVANSVARKHGFLNLGQIFG--DYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKR 107
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
484-570 9.74e-36

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: 129.70  E-value: 9.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 484 LEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTsEANNYGTL 563
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79

                  ....*..
gi 1843419910 564 TKFTLVL 570
Cdd:pfam01483  80 NSWQLTL 86
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
132-436 7.00e-12

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: 67.73  E-value: 7.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 132 LNVKAAWAQGyTGHGIVVSILDDGIEKnHPDLAGNYDPGASFdVNDQDpdpqprytQMND-NRHGTRCAGEVAAVANNGV 210
Cdd:TIGR03921   1 LSLEQAWKFS-TGAGVTVAVIDTGVDD-HPRLPGLVLPGGDF-VGSGD--------GTDDcDGHGTLVAGIIAGRPGEGD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 211 CGVGVAYNARIGGVRMLDGEVTDAVEARSLGlNPNH---------------IHIYSASWGPEDDGktVDGPARLA--EEA 273
Cdd:TIGR03921  70 GFSGVAPDARILPIRQTSAAFEPDEGTSGVG-DLGTlakairraadlgadvINISLVACLPAGSG--ADDPELGAavRYA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 274 FFRGVsqgrgglgsIFVWASGNGGrehDSCNCDgyTNSI-----YTLSISSATQFGNVPWYSEACSSTLATTYSSGnqne 348
Cdd:TIGR03921 147 LDKGV---------VVVAAAGNTG---GDGQKT--TVVYpawypGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGEN---- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 349 kqIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpAHLNAndwatnGVGRkvSHSYGYGL 428
Cdd:TIGR03921 209 --IVSLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEAT---ADHPA------RGGR--DDYVGYGV 275

                  ....*...
gi 1843419910 429 LDAGAMVA 436
Cdd:TIGR03921 276 VDPVAALT 283
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
149-412 5.67e-09

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 59.60  E-value: 5.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 149 VSILDDGIEKNHPDLAGNYDP-----------------------GASFDVNDQDPdpqprytqMNDNRHGTRCAGEVAAV 205
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIDVnvkelhgrkgidddnngnvddeyGANFVNNDGGP--------MDDNYHGTHVSGIISAI 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 206 ANNGVCGVGVAYNARIGGVRMLD----GEVTDAVEARSLGLNPNhIHIYSASWGPEDDGKTVDGPARLAEEaffrgvsqg 281
Cdd:PTZ00262  392 GNNNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFNESVKYLEE--------- 461
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 282 rggLGSIFVWASGNGGREHDSCN----CDGYTNSIY----------TLSISSATQFGNVPwYSEACSSTLATTYSSGNQN 347
Cdd:PTZ00262  462 ---KGILFVVSASNCSHTKESKPdipkCDLDVNKVYppilskklrnVITVSNLIKDKNNQ-YSLSPNSFYSAKYCQLAAP 537
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1843419910 348 EKQIVTTDLRQKCTEShTGTSASAPLAAGIIALTLEANKNLTWRD----MQHLVVQTskPAHLNANDWA 412
Cdd:PTZ00262  538 GTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEviriLKESIVQL--PSLKNKVKWG 603
FU smart00261
Furin-like repeats;
638-675 6.52e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 52.13  E-value: 6.52e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1843419910  638 ASVCAPCHASCATCQGPALTDCLSCPSHASLDpvEQTC 675
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKC 36
FU smart00261
Furin-like repeats;
581-618 1.25e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.58  E-value: 1.25e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1843419910  581 PPESSGCKTLTSSQA--CVVCEEGFSLHQKSCVQHCPPGF 618
Cdd:smart00261   5 KPCHPECATCTGPGPddCTSCKHGFFLDGGKCVSECPPGT 44
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
643-675 1.36e-06

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 45.59  E-value: 1.36e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1843419910 643 PCHASCATCQGPALTDCLSCPSHASLDpvEQTC 675
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFYLD--GGTC 31
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
584-618 1.29e-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: 42.89  E-value: 1.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1843419910 584 SSGCKTLTSS--QACVVCEEGFSLHQKSCVQHCPPGF 618
Cdd:cd00064     3 HPSCATCTGPgpDQCTSCRHGFYLDGGTCVSECPEGT 39
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
584-621 2.36e-04

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


Pssm-ID: 464939 [Multi-domain]  Cd Length: 102  Bit Score: 40.88  E-value: 2.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1843419910 584 SSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQ 621
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 ...
113-402 1.76e-175

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: 505.56  E-value: 1.76e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 113 PTDPKFPQQWYLSGVTQR------DLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRY 186
Cdd:cd04059     1 PNDPLFPYQWYLKNTGQAggtpglDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 187 TqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGP 266
Cdd:cd04059    81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 267 ARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQ 346
Cdd:cd04059   159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSG 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1843419910 347 N-EKQIVTTDLR--QKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSK 402
Cdd:cd04059   239 NpEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
Peptidase_S8 pfam00082
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
144-427 6.95e-62

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: 210.01  E-value: 6.95e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 144 GHGIVVSILDDGIEKNHPDLAGNYDPGASFD----VNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNA 219
Cdd:pfam00082   1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDpeasVDFNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 220 RIGGVRML-DGEVTDAVEARSLGLN-PNHIHIYSASWGPEddgKTVDGPARLAEEAFFRGvsqGRGGLGSIFVWASGNGG 297
Cdd:pfam00082  81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 298 REHDSCNCDGY-TNSIYTLSISSATQF--GNVPWYSEACSS-------TLA----TTYSSGNQNEKQIVTTDLRQKCTES 363
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAVDEAseGNLASFSSYGPTldgrlkpDIVapggNITGGNISSTLLTTTSDPPNQGYDS 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1843419910 364 HTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpahlnandwATNGVGRKVSHSYGYG 427
Cdd:pfam00082 235 MSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNT-----------ATDLGDAGLDRLFGYG 287
AprE COG1404
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ...
81-440 3.05e-37

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


Pssm-ID: 441014 [Multi-domain]  Cd Length: 456  Bit Score: 145.63  E-value: 3.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910  81 RPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNH 160
Cdd:COG1404    45 AAALVAAAAAAAVAAALAAPLAPAALAAPAPLPVPAAAPAAVRAAQAALLAAAAAGSSAAGLTGAGVTVAVIDTGVDADH 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 161 PDLAGNYDPGASFDVNDQDPDpqprytqmNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLD--GEVTDAVEAR 238
Cdd:COG1404   125 PDLAGRVVGGYDFVDGDGDPS--------DDNGHGTHVAGIIAANGNNGGGVAGVAPGAKLLPVRVLDdnGSGTTSDIAA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 239 slGLN---PNHIHIYSASWGPEDDGKTvDGPARLAEEAFFRGVsqgrgglgsIFVWASGNGGrehDSCNCDGYTNSIY-T 314
Cdd:COG1404   197 --AIDwaaDNGADVINLSLGGPADGYS-DALAAAVDYAVDKGV---------LVVAAAGNSG---SDDATVSYPAAYPnV 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 315 LSISSATQFGNVPWYSeacsstlattySSGNQNE-----KQIVTTDLRQKcTESHTGTSASAPLAAGIIALTLEANKNLT 389
Cdd:COG1404   262 IAVGAVDANGQLASFS-----------NYGPKVDvaapgVDILSTYPGGG-YATLSGTSMAAPHVAGAAALLLSANPDLT 329
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1843419910 390 WRDMQHLVVQTSKPAHLNANDwatngvgrkvshsYGYGLLDAGAMVALAQN 440
Cdd:COG1404   330 PAQVRAILLNTATPLGAPGPY-------------YGYGLLADGAAGATSAG 367
S8_pro-domain pfam16470
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ...
33-107 2.83e-36

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: 131.19  E-value: 2.83e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1843419910  33 TWAVRIPGGPAVANSVARKHGFLNLGQIFG--DYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKR 107
Cdd:pfam16470   1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGleDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
P_proprotein pfam01483
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ...
484-570 9.74e-36

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: 129.70  E-value: 9.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 484 LEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTsEANNYGTL 563
Cdd:pfam01483   1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-APGDTGTL 79

                  ....*..
gi 1843419910 564 TKFTLVL 570
Cdd:pfam01483  80 NSWQLTL 86
Peptidases_S8_15 cd07498
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
147-400 1.61e-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: 134.78  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 147 IVVSILDDGIEKNHPDLAG--NYDPGasFDVNDQDPDPQPRYTqmndnrHGTRCAGEVAAVANNGVCGVGVAYNARIGGV 224
Cdd:cd07498     1 VVVAIIDTGVDLNHPDLSGkpKLVPG--WNFVSNNDPTSDIDG------HGTACAGVAAAVGNNGLGVAGVAPGAKLMPV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 225 RMLDGEVTDAVEARSLGLN---PNHIHIYSASWGPEDdgktvdgPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHD 301
Cdd:cd07498    73 RIADSLGYAYWSDIAQAITwaaDNGADVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLFAAGNSGRSVS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 302 ScncdGYTNSIYTLSISSATQFGNVPWYSE--------ACSSTLATTySSGNQNEKQIVTTDlrqkcTESHTGTSASAPL 373
Cdd:cd07498   146 S----GYAANPSVIAVAATDSNDARASYSNygnyvdlvAPGVGIWTT-GTGRGSAGDYPGGG-----YGSFSGTSFASPV 215
                         250       260
                  ....*....|....*....|....*..
gi 1843419910 374 AAGIIALTLEANKNLTWRDMQHLVVQT 400
Cdd:cd07498   216 AAGVAALILSANPNLTPAEVEDILTST 242
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
146-402 2.49e-27

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


Pssm-ID: 173799 [Multi-domain]  Cd Length: 259  Bit Score: 111.90  E-value: 2.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 146 GIVVSILDDGIEKNHPDLAGN------YDPGASFDvNDQ---------------DPDPqprytqMNDNRHGTRCAGEVAA 204
Cdd:cd07473     3 DVVVAVIDTGVDYNHPDLKDNmwvnpgEIPGNGID-DDGngyvddiygwnfvnnDNDP------MDDNGHGTHVAGIIGA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 205 VANNGVCGVGVAYNARIGGVRMLD----GEVTDAVE----ARSLGlnpnhIHIYSASWGPeddgktvDGPARLAEEAFFR 276
Cdd:cd07473    76 VGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKaidyAVDMG-----AKIINNSWGG-------GGPSQALRDAIAR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 277 GVSQgrgglGSIFVWASGNGGREHDSCNC--DGYTNSiYTLSISSATQFGNVPWYSEACSST--LA-------TTYSSGN 345
Cdd:cd07473   144 AIDA-----GILFVAAAGNDGTNNDKTPTypASYDLD-NIISVAATDSNDALASFSNYGKKTvdLAapgvdilSTSPGGG 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1843419910 346 QNEKqivttdlrqkcteshTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSK 402
Cdd:cd07473   218 YGYM---------------SGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
Peptidases_S8_S53 cd00306
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
147-400 1.07e-26

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: 109.60  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 147 IVVSILDDGIEKNHPDLAGNYDPGASFdvNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVcGVGVAYNARIGGVRM 226
Cdd:cd00306     1 VTVAVIDTGVDPDHPDLDGLFGGGDGG--NDDDDNENGPTDPDDGNGHGTHVAGIIAASANNGG-GVGVAPGAKLIPVKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 227 LDGEVTDAVEARSLGLN----PNHIHIYSASWGPEDDGKTvDGPARLAEEAFFRgvsqgrggLGSIFVWASGNGGREHDS 302
Cdd:cd00306    78 LDGDGSGSSSDIAAAIDyaaaDQGADVINLSLGGPGSPPS-SALSEAIDYALAK--------LGVLVVAAAGNDGPDGGT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 303 cNCDGYTNSIYTLSISSATQFGNVPWYSeACSSTLATTYSSGNQnekQIVTTDLRQKCTESHTGTSASAPLAAGIIALTL 382
Cdd:cd00306   149 -NIGYPAASPNVIAVGAVDRDGTPASPS-SNGGAGVDIAAPGGD---ILSSPTTGGGGYATLSGTSMAAPIVAGVAALLL 223
                         250
                  ....*....|....*...
gi 1843419910 383 EANKNLTWRDMQHLVVQT 400
Cdd:cd00306   224 SANPDLTPAQVKAALLST 241
Peptidases_S8_Thermitase_like cd07484
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ...
112-380 7.56e-24

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: 101.57  E-value: 7.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 112 EPTDPKFPQQWYLsgvtqRDLNVKAAWAQGyTGHGIVVSILDDGIEKNHPDLA-GNYDPGASFDVNDQDPdpqprytqMN 190
Cdd:cd07484     1 TPNDPYYSYQWNL-----DQIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLLkVKFVLGYDFVDNDSDA--------MD 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 191 DNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLD--GEVTDAVEARSLglnpnhihIYSAswgpeDDGKTV----- 263
Cdd:cd07484    67 DNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDanGSGSLADIANGI--------RYAA-----DKGAKVinlsl 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 264 --DGPARLAEEAFFRGVSQgrgglGSIFVWASGNGGREHDScncdgYTNSI-YTLSISSATQFGNVPWYSEAcSSTLATT 340
Cdd:cd07484   134 ggGLGSTALQEAINYAWNK-----GVVVVAAAGNEGVSSVS-----YPAAYpGAIAVAATDQDDKRASFSNY-GKWVDVS 202
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1843419910 341 YSSGNqnekqIVTTDLRQKcTESHTGTSASAPLAAGIIAL 380
Cdd:cd07484   203 APGGG-----ILSTTPDGD-YAYMSGTSMATPHVAGVAAL 236
Peptidases_S8_Subtilisin_subset cd07477
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ...
146-389 1.26e-20

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: 91.44  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 146 GIVVSILDDGIEKNHPDLAGNYDPGASFdVNDQDPDPQprytqmNDNRHGTRCAGEVAAvANNGVCGVGVAYNARIGGVR 225
Cdd:cd07477     1 GVKVAVIDTGIDSSHPDLKLNIVGGANF-TGDDNNDYQ------DGNGHGTHVAGIIAA-LDNGVGVVGVAPEADLYAVK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 226 MLD----GEVTDAVEARSLGLNpNHIHIYSASWGPEDDGKTVdgparlaEEAFFRGVSQGrgglgsIF-VWASGNggreh 300
Cdd:cd07477    73 VLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLGGPSDSPAL-------REAIKKAYAAG------ILvVAAAGN----- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 301 dscncDGYTNSIYT--------LSISSATQFGNVPWYSeacsstlattySSGNQNE-----KQIVTTDLRQKcTESHTGT 367
Cdd:cd07477   134 -----SGNGDSSYDypakypsvIAVGAVDSNNNRASFS-----------STGPEVElaapgVDILSTYPNND-YAYLSGT 196
                         250       260
                  ....*....|....*....|..
gi 1843419910 368 SASAPLAAGIIALTLEANKNLT 389
Cdd:cd07477   197 SMATPHVAGVAALVWSKRPELT 218
Peptidases_S8_Fervidolysin_like cd07485
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ...
136-387 4.29e-20

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: 91.01  E-value: 4.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 136 AAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYD-PGASFDVNDQDPDPQ---PRYTQMNDNRHGTRCAGEVAAVANN--G 209
Cdd:cd07485     1 AAWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDgDGYDPAVNGYNFVPNvgdIDNDVSVGGGHGTHVAGTIAAVNNNggG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 210 VCGV----GVAYNARIGGVRMLDGE--VTDAVEARSLGL-NPNHIHIYSASWGpeddGKTVDGPARLAEEAFFRGVSQGR 282
Cdd:cd07485    81 VGGIagagGVAPGVKIMSIQIFAGRyyVGDDAVAAAIVYaADNGAVILQNSWG----GTGGGIYSPLLKDAFDYFIENAG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 283 GGL--GSIFVWASGNggrEHDSCncdGYTNSIYTLSISSATQFGNvpwYSEACSSTLATTYSSGNQNEKQIVTTDLRQKC 360
Cdd:cd07485   157 GSPldGGIVVFSAGN---SYTDE---HRFPAAYPGVIAVAALDTN---DNKASFSNYGRWVDIAAPGVGTILSTVPKLDG 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1843419910 361 TESHT-----GTSASAPLAAGIIALTLEANKN 387
Cdd:cd07485   228 DGGGNyeylsGTSMAAPHVSGVAALVLSKFPD 259
Peptidases_S8_subtilisin_Vpr-like cd07474
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ...
144-410 1.51e-19

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: 90.08  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 144 GHGIVVSILDDGIEKNHPDLAG------NYDPGASFDVNDQDPDPQPRYTQMNDNR-------HGTRCAGEVAAVANNGV 210
Cdd:cd07474     1 GKGVKVAVIDTGIDYTHPDLGGpgfpndKVKGGYDFVDDDYDPMDTRPYPSPLGDAsagdatgHGTHVAGIIAGNGVNVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 211 CGVGVAYNARIGGVRMLD--GEVTDAVEARSL--GLNPnHIHIYSASWGPEDDGKtvDGPARLAEEAFFRgvsqgrggLG 286
Cdd:cd07474    81 TIKGVAPKADLYAYKVLGpgGSGTTDVIIAAIeqAVDD-GMDVINLSLGSSVNGP--DDPDAIAINNAVK--------AG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 287 SIFVWASGNGGrehDSCNCDGyTNSIYTLSISSATQFGNVPWYSEacssTLATTYSSGNQNEKQIVTTDL---------- 356
Cdd:cd07474   150 VVVVAAAGNSG---PAPYTIG-SPATAPSAITVGASTVADVAEAD----TVGPSSSRGPPTSDSAIKPDIvapgvdimst 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1843419910 357 ---RQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNAND 410
Cdd:cd07474   222 apgSGTGYARMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNTAKPLYDSDGV 278
Peptidases_S8_Autotransporter_serine_protease_like cd04848
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ...
143-400 1.94e-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: 88.92  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 143 TGHGIVVSILDDGIEKNHPDLAGNYDP-GASFDVNDQDPDPQPRYtqmndNRHGTRCAGeVAAVANNGVCGVGVAYNARI 221
Cdd:cd04848     1 TGAGVKVGVIDSGIDLSHPEFAGRVSEaSYYVAVNDAGYASNGDG-----DSHGTHVAG-VIAAARDGGGMHGVAPDATL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 222 GGVRMLDG---EVTDAVEARSL-GLNPNHIHIYSASWGPEDDGKTVDGPARL--------AEEAFFRGVSQgrgglGSIF 289
Cdd:cd04848    75 YSARASASagsTFSDADIAAAYdFLAASGVRIINNSWGGNPAIDTVSTTYKGsaatqgntLLAALARAANA-----GGLF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 290 VWASGNGGREHDSCNCDGYT-------NSIytLSISSATQFGNVP--WYSEAC----SSTLA-------TTYSSGNQNEK 349
Cdd:cd04848   150 VFAAGNDGQANPSLAAAALPylepeleGGW--IAVVAVDPNGTIAsySYSNRCgvaaNWCLAapgeniySTDPDGGNGYG 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1843419910 350 QIvttdlrqkcteshTGTSASAPLAAGIIALTLEANKNLTwrdmQHLVVQT 400
Cdd:cd04848   228 RV-------------SGTSFAAPHVSGAAALLAQKFPWLT----ADQVRQT 261
Peptidases_S8_13 cd07496
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ...
146-389 1.67e-17

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: 83.50  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 146 GIVVSILDDGIEKNHPDLAGNYDPGASF----------DVNDQDP-DPQPRYTQMNDNR-------------HGTRCAGE 201
Cdd:cd07496     1 GVVVAVLDTGVLFHHPDLAGVLLPGYDFisdpaiandgDGRDSDPtDPGDWVTGDDVPPggfcgsgvspsswHGTHVAGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 202 VAAVANNGVCGVGVAYNARIGGVRML---DGEVTDAVEArslglnpnhihIYSASWGPEDDGKTVDGPAR-----LAEEA 273
Cdd:cd07496    81 IAAVTNNGVGVAGVAWGARILPVRVLgkcGGTLSDIVDG-----------MRWAAGLPVPGVPVNPNPAKvinlsLGGDG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 274 FFRGVSQ----GRGGLGSIFVWASGNGGR--EHDS-CNCDGytnsiyTLSISSATQFGNVPWYSEACSST-LAT----TY 341
Cdd:cd07496   150 ACSATMQnainDVRARGVLVVVAAGNEGSsaSVDApANCRG------VIAVGATDLRGQRASYSNYGPAVdVSApggdCA 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1843419910 342 SSGNQNEKQIVTTDLRQKCTESHT---GTSASAPLAAGIIALTLEANKNLT 389
Cdd:cd07496   224 SDVNGDGYPDSNTGTTSPGGSTYGflqGTSMAAPHVAGVAALMKSVNPSLT 274
Peptidases_S8_5 cd07489
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ...
139-431 9.09e-14

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


Pssm-ID: 173814 [Multi-domain]  Cd Length: 312  Bit Score: 73.02  E-value: 9.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 139 AQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASF--------DVNDQDPDPQPRYTQMNDNRHGTRCAGEVAavANNGV 210
Cdd:cd07489     7 AEGITGKGVKVAVVDTGIDYTHPALGGCFGPGCKVaggydfvgDDYDGTNPPVPDDDPMDCQGHGTHVAGIIA--ANPNA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 211 CG-VGVAYNARIGGVRMLD--GEVTDAVEARSL------GlnpnhIHIYSASWGpeDDGKTVDGPA-----RLAEEAFFR 276
Cdd:cd07489    85 YGfTGVAPEATLGAYRVFGcsGSTTEDTIIAAFlrayedG-----ADVITASLG--GPSGWSEDPWavvasRIVDAGVVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 277 GVSQG-RGGLGSifvWASGNGGrehdscncdgytNSIYTLSISSAtqfgnvpwyseacsstlATTYSS-GNQNEKQ---- 350
Cdd:cd07489   158 TIAAGnDGERGP---FYASSPA------------SGRGVIAVASV-----------------DSYFSSwGPTNELYlkpd 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 351 -------IVTTDLRQKCT-ESHTGTSASAPLAAGIIALTLEA-NKNLTWRDMQHLVVQTSKPahLNANDWATNGVGRKVS 421
Cdd:cd07489   206 vaapggnILSTYPLAGGGyAVLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKP--LPWSDGTSALPDLAPV 283
                         330
                  ....*....|
gi 1843419910 422 HSYGYGLLDA 431
Cdd:cd07489   284 AQQGAGLVNA 293
Peptidases_S8_1 cd07487
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ...
144-389 4.19e-13

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: 70.31  E-value: 4.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 144 GHGIVVSILDDGIEKNHPDLAGNYDPGASFdVNDQDPDPQPRytqmNDNRHGTRCAGEVAA--VANNGVcGVGVAYNARI 221
Cdd:cd07487     1 GKGITVAVLDTGIDAPHPDFDGRIIRFADF-VNTVNGRTTPY----DDNGHGTHVAGIIAGsgRASNGK-YKGVAPGANL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 222 GGVRMLD----GEVTDAVEA----RSLGlNPNHIHIYSASWGPEDDGKTVDGPARLA-EEAFFRGVsqgrgglgsIFVWA 292
Cdd:cd07487    75 VGVKVLDdsgsGSESDIIAGidwvVENN-EKYNIRVVNLSLGAPPDPSYGEDPLCQAvERLWDAGI---------VVVVA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 293 SGNGGREHDSCNCDGytNSIYTLSISSATQFGNVPWYSEACSS---TLA--------------TTYSSGNQNEKQIVTTD 355
Cdd:cd07487   145 AGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSSrgpTGDgrikpdvvapgeniVSCRSPGGNPGAGVGSG 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1843419910 356 LRQKcteshTGTSASAPLAAGIIALTLEANKNLT 389
Cdd:cd07487   223 YFEM-----SGTSMATPHVSGAIALLLQANPILT 251
T7SS_mycosin TIGR03921
type VII secretion-associated serine protease mycosin; Members of this family are ...
132-436 7.00e-12

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: 67.73  E-value: 7.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 132 LNVKAAWAQGyTGHGIVVSILDDGIEKnHPDLAGNYDPGASFdVNDQDpdpqprytQMND-NRHGTRCAGEVAAVANNGV 210
Cdd:TIGR03921   1 LSLEQAWKFS-TGAGVTVAVIDTGVDD-HPRLPGLVLPGGDF-VGSGD--------GTDDcDGHGTLVAGIIAGRPGEGD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 211 CGVGVAYNARIGGVRMLDGEVTDAVEARSLGlNPNH---------------IHIYSASWGPEDDGktVDGPARLA--EEA 273
Cdd:TIGR03921  70 GFSGVAPDARILPIRQTSAAFEPDEGTSGVG-DLGTlakairraadlgadvINISLVACLPAGSG--ADDPELGAavRYA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 274 FFRGVsqgrgglgsIFVWASGNGGrehDSCNCDgyTNSI-----YTLSISSATQFGNVPWYSEACSSTLATTYSSGnqne 348
Cdd:TIGR03921 147 LDKGV---------VVVAAAGNTG---GDGQKT--TVVYpawypGVLAVGSIDRDGTPSSFSLPGPWVDLAAPGEN---- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 349 kqIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpAHLNAndwatnGVGRkvSHSYGYGL 428
Cdd:TIGR03921 209 --IVSLSPGGDGLATTSGTSFAAPFVSGTAALVRSRFPDLTAAQVRRRIEAT---ADHPA------RGGR--DDYVGYGV 275

                  ....*...
gi 1843419910 429 LDAGAMVA 436
Cdd:TIGR03921 276 VDPVAALT 283
Peptidases_S8_6 cd07490
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ...
146-389 8.19e-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: 66.03  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 146 GIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPrytqMNDNRHGTRCAGEVAAVANNGVcGVGVAynariGGVR 225
Cdd:cd07490     1 GVTVAVLDTGVDADHPDLAGRVAQWADFDENRRISATEV----FDAGGHGTHVSGTIGGGGAKGV-YIGVA-----PEAD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 226 MLDGEVTDAVEARSLGLnpnhihIYSASWGPEDDGKTVD---GPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGreHDS 302
Cdd:cd07490    71 LLHGKVLDDGGGSLSQI------IAGMEWAVEKDADVVSmslGGTYYSEDPLEEAVEALSNQTGALFVVSAGNEG--HGT 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 303 CNCDGYTNSiyTLSISSATQFGNVPWYSeACSSTLATTYSSGNQNEKQIVTTDLRQKCT---------------ESHTGT 367
Cdd:cd07490   143 SGSPGSAYA--ALSVGAVDRDDEDAWFS-SFGSSGASLVSAPDSPPDEYTKPDVAAPGVdvysarqgangdgqyTRLSGT 219
                         250       260
                  ....*....|....*....|..
gi 1843419910 368 SASAPLAAGIIALTLEANKNLT 389
Cdd:cd07490   220 SMAAPHVAGVAALLAAAHPDLS 241
Peptidases_S8_PCSK9_ProteinaseK_like cd04077
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ...
122-389 1.37e-11

Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.


Pssm-ID: 173790 [Multi-domain]  Cd Length: 255  Bit Score: 65.62  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 122 WYLSGVTQRDLNVKAAWAQG-YTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPqprytqmndNRHGTRCAG 200
Cdd:cd04077     1 WGLDRISQRDLPLDGTYYYDsSTGSGVDVYVLDTGIRTTHVEFGGRAIWGADFVGGDPDSDC---------NGHGTHVAG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 201 EVAAVAnngvcgVGVAYNARIGGVRMLD----GEVTDAVEarslGLNpnhihiYSASWGPEDDGKTV-----DGPARLAE 271
Cdd:cd04077    72 TVGGKT------YGVAKKANLVAVKVLDcngsGTLSGIIA----GLE------WVANDATKRGKPAVanmslGGGASTAL 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 272 EAFFRGVSQGrgglGSIFVWASGNGGRehDSCNcdgYT--NSIYTLSISSATQFGNVPWYSE--AC-------SSTLATT 340
Cdd:cd04077   136 DAAVAAAVNA----GVVVVVAAGNSNQ--DACN---YSpaSAPEAITVGATDSDDARASFSNygSCvdifapgVDILSAW 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1843419910 341 YSSGNqnekqivttdlrqkCTESHTGTSASAPLAAGIIALTLEANKNLT 389
Cdd:cd04077   207 IGSDT--------------ATATLSGTSMAAPHVAGLAAYLLSLGPDLS 241
COG4935 COG4935
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...
136-572 2.23e-11

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: 67.54  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 136 AAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGV 215
Cdd:COG4935   222 GGAGLAAAGGGGGGAAAAAAAGVGGLGAAATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVG 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 216 AYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGN 295
Cdd:COG4935   302 AAGTGNAAAAAAASAGSGGGGGSAAAAGAAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAAA 381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 296 GGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAA 375
Cdd:COG4935   382 GAAAGAAAGAAAGAAAAGGVASAAGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSA 461
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 376 GIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDIL 455
Cdd:COG4935   462 AGAAGGTTTATSGLASSTTAAAAAAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVAIPDNG 541
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 456 TEPkdigkrLEVRKTVTACLgepnhitRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAarPHDYSADGFNdWAFMT 535
Cdd:COG4935   542 PAG------VTSTITVSGGG-------AVEDVTVTVDITHTYRGDLVITLISPDGTTVVLKN--RSGGSADNIN-ATFDV 605
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1843419910 536 THSWDEDPSGEWVLEIENTSEANNyGTLTKFTLVLYG 572
Cdd:COG4935   606 ANFSGESANGTWTLRVVDTAGGDT-GTLNSWSLTFTG 641
Peptidases_S8_12 cd07480
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ...
142-295 5.90e-11

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: 64.32  E-value: 5.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 142 YTGHGIVVSILDDGIEKNHPDLAGNYDPGASF----DVNDQdpdpqprytqmndNRHGTRCAGEVAAVANNGVcGVGVAY 217
Cdd:cd07480     5 FTGAGVRVAVLDTGIDLTHPAFAGRDITTKSFvggeDVQDG-------------HGHGTHCAGTIFGRDVPGP-RYGVAR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 218 NARI--GGVRMLDGEVTDA--VEARSLGLNpNHIHIYSASWG-----PEDDGKTVDGPARLAEEAFFRGV---------- 278
Cdd:cd07480    71 GAEIalIGKVLGDGGGGDGgiLAGIQWAVA-NGADVISMSLGadfpgLVDQGWPPGLAFSRALEAYRQRArlfdalmtlv 149
                         170
                  ....*....|....*...
gi 1843419910 279 -SQGRGGLGSIFVWASGN 295
Cdd:cd07480   150 aAQAALARGTLIVAAAGN 167
PTZ00262 PTZ00262
subtilisin-like protease; Provisional
149-412 5.67e-09

subtilisin-like protease; Provisional


Pssm-ID: 240338 [Multi-domain]  Cd Length: 639  Bit Score: 59.60  E-value: 5.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 149 VSILDDGIEKNHPDLAGNYDP-----------------------GASFDVNDQDPdpqprytqMNDNRHGTRCAGEVAAV 205
Cdd:PTZ00262  320 ICVIDSGIDYNHPDLHDNIDVnvkelhgrkgidddnngnvddeyGANFVNNDGGP--------MDDNYHGTHVSGIISAI 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 206 ANNGVCGVGVAYNARIGGVRMLD----GEVTDAVEARSLGLNPNhIHIYSASWGPEDDGKTVDGPARLAEEaffrgvsqg 281
Cdd:PTZ00262  392 GNNNIGIVGVDKRSKLIICKALDshklGRLGDMFKCFDYCISRE-AHMINGSFSFDEYSGIFNESVKYLEE--------- 461
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 282 rggLGSIFVWASGNGGREHDSCN----CDGYTNSIY----------TLSISSATQFGNVPwYSEACSSTLATTYSSGNQN 347
Cdd:PTZ00262  462 ---KGILFVVSASNCSHTKESKPdipkCDLDVNKVYppilskklrnVITVSNLIKDKNNQ-YSLSPNSFYSAKYCQLAAP 537
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1843419910 348 EKQIVTTDLRQKCTEShTGTSASAPLAAGIIALTLEANKNLTWRD----MQHLVVQTskPAHLNANDWA 412
Cdd:PTZ00262  538 GTNIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEviriLKESIVQL--PSLKNKVKWG 603
FU smart00261
Furin-like repeats;
638-675 6.52e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 52.13  E-value: 6.52e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1843419910  638 ASVCAPCHASCATCQGPALTDCLSCPSHASLDpvEQTC 675
Cdd:smart00261   1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKC 36
Peptidases_S8_7 cd07491
Peptidase S8 family domain, uncharacterized subfamily 7; This family is a member of the ...
147-382 7.58e-09

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: 57.34  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 147 IVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPD-PQPRYtqMNDNRHGT---RCAGEVAAVANNGVCGVGVaYNARIG 222
Cdd:cd07491     5 IKVALIDDGVDILDSDLQGKIIGGKSFSPYEGDGNkVSPYY--VSADGHGTamaRMICRICPSAKLYVIKLED-RPSPDS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 223 GVRMLDGE-VTDAVEARSlglnPNHIHIYSASWGPEDDGKTVDGPARLaEEAFFRGVSQGrgglgsIFVWAS----GNGG 297
Cdd:cd07491    82 NKRSITPQsAAKAIEAAV----EKKVDIISMSWTIKKPEDNDNDINEL-ENAIKEALDRG------ILLFCSasdqGAFT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 298 REHDSCnCDGYTNsiyTLSISSATQFGNV--PWYSEacssTLATTYSSGNQnekqiVTTDLRQKCTES---HTGTSASAP 372
Cdd:cd07491   151 GDTYPP-PAARDR---IFRIGAADEDGGAdaPVGDE----DRVDYILPGEN-----VEARDRPPLSNSfvtHTGSSVATA 217
                         250
                  ....*....|
gi 1843419910 373 LAAGIIALTL 382
Cdd:cd07491   218 LAAGLAALIL 227
Peptidases_S8_Kp43_protease cd04842
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ...
141-380 1.37e-08

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: 56.95  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 141 GYTGHGIVVSILDDGIEKNHPDLagnYDPGASfDVNDQDP-----DPQPRYTQMNDNrHGTRCAGEVAAVANNGVCGV-- 213
Cdd:cd04842     3 GLTGKGQIVGVADTGLDTNHCFF---YDPNFN-KTNLFHRkivryDSLSDTKDDVDG-HGTHVAGIIAGKGNDSSSISly 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 214 -GVAYNARIGGVRMLDGEVTDAVEARSLGL----NPNHIHIYSASWGPEDDG------KTVDGPARLAEEAffrgvsqgr 282
Cdd:cd04842    78 kGVAPKAKLYFQDIGDTSGNLSSPPDLNKLfspmYDAGARISSNSWGSPVNNgytllaRAYDQFAYNNPDI--------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 283 gglgsIFVWASGNGGrehdscncDGYTNSIYTLSISSatqfgNVpwYSEACSSTLATTYSSGNQNEKQIV---------- 352
Cdd:cd04842   149 -----LFVFSAGNDG--------NDGSNTIGSPATAK-----NV--LTVGASNNPSVSNGEGGLGQSDNSdtvasfssrg 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1843419910 353 -TTDLRQK----------------------CTESH----TGTSASAPLAAGIIAL 380
Cdd:cd04842   209 pTYDGRIKpdlvapgtgilsarsggggigdTSDSAytskSGTSMATPLVAGAAAL 263
Peptidases_S8_BacillopeptidaseF-like cd07481
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ...
144-388 3.70e-08

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: 55.46  E-value: 3.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 144 GHGIVVSILDDGIEKNHPDLAGNYDP--GASFDVNDQDPDPQPRYTQMND-NRHGTRCAGevAAVANNGV-CGVGVAYNA 219
Cdd:cd07481     1 GTGIVVANIDTGVDWTHPALKNKYRGwgGGSADHDYNWFDPVGNTPLPYDdNGHGTHTMG--TMVGNDGDgQQIGVAPGA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 220 RIGGVRMLD---GEVTDAVEARSLGLNPNHI-----------HIYSASWGpeddgktvdGPARLAEeaFFRGVSQGRGGL 285
Cdd:cd07481    79 RWIACRALDrngGNDADYLRCAQWMLAPTDSagnpadpdlapDVINNSWG---------GPSGDNE--WLQPAVAAWRAA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 286 GSIFVWASGNGGREHDSCNCD--GYTNSIYTLSISSATQFGNVpwyseacSSTLATTYSSGNQNekqIVT--TDLRQKCT 361
Cdd:cd07481   148 GIFPVFAAGNDGPRCSTLNAPpaNYPESFAVGATDRNDVLADF-------SSRGPSTYGRIKPD---ISApgVNIRSAVP 217
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1843419910 362 E----SHTGTSASAPLAAGIIALTLEANKNL 388
Cdd:cd07481   218 GggygSSSGTSMAAPHVAGVAALLWSANPSL 248
Peptidases_S8_Lantibiotic_specific_protease cd07482
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ...
147-389 2.43e-07

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: 53.14  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 147 IVVSILDDGIEKNHPDLAGNYDPGasfdVNDQDPDPQPRYTQMND----------NRHGTRCAGEVAAVANNGvcgvGVA 216
Cdd:cd07482     2 VTVAVIDSGIDPDHPDLKNSISSY----SKNLVPKGGYDGKEAGEtgdindivdkLGHGTAVAGQIAANGNIK----GVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 217 YNARIGGVRMLD----GEVTDAVEARSLGLNpNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGlGSIFVWA 292
Cdd:cd07482    74 PGIGIVSYRVFGscgsAESSWIIKAIIDAAD-DGVDVINLSLGGYLIIGGEYEDDDVEYNAYKKAINYAKSK-GSIVVAA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 293 SGNGGRE---------HDSCNCDGYTNSIY---------TLSISSATQFGNVPWYSEACSS--TLATTYSSGNQNEKQIV 352
Cdd:cd07482   152 AGNDGLDvsnkqelldFLSSGDDFSVNGEVydvpaslpnVITVSATDNNGNLSSFSNYGNSriDLAAPGGDFLLLDQYGK 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1843419910 353 TTDLRQK--------------CTESHTGTSASAPLAAGIIALTLEANKNLT 389
Cdd:cd07482   232 EKWVNNGlmtkeqilttapegGYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
Peptidases_S8_C5a_Peptidase cd07475
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ...
136-410 9.19e-07

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: 51.88  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 136 AAWAQG-YTGHGIVVSILDDGIEKNHPDLAGNyDPGA-----SFDVNDQDPDPQP------------RYTQMNDN----- 192
Cdd:cd07475     1 PLWDKGgYKGEGMVVAVIDSGVDPTHDAFRLD-DDSKakyseEFEAKKKKAGIGYgkyynekvpfayNYADNNDDilded 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 193 ---RHGTRCAGEVAAVANNGVCG---VGVAYNARIGGVRMLDG-------------EVTDAVEarslgLNPNHIhiySAS 253
Cdd:cd07475    80 dgsSHGMHVAGIVAGNGDEEDNGegiKGVAPEAQLLAMKVFSNpeggstyddayakAIEDAVK-----LGADVI---NMS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 254 WGPEDDGKTVDGPARLA-EEAFFRGVsqgrgglgsIFVWASGNggrehdscncDGYTNSIYTLSISSATQFGNVPWYSEA 332
Cdd:cd07475   152 LGSTAGFVDLDDPEQQAiKRAREAGV---------VVVVAAGN----------DGNSGSGTSKPLATNNPDTGTVGSPAT 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 333 CSSTLAT---TYSSGNQNEKQI-------VTTDLRQK-----------CT------ESHTGTSASAPLAAGIIALTLEA- 384
Cdd:cd07475   213 ADDVLTVasaNKKVPNPNGGQMsgfsswgPTPDLDLKpditapggniySTvndntyGYMSGTSMASPHVAGASALVKQRl 292
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1843419910 385 ---NKNLTWRDMQHLVVQ----TSKPAHLNAND 410
Cdd:cd07475   293 kekYPKLSGEELVDLVKNllmnTATPPLDSEDT 325
FU smart00261
Furin-like repeats;
581-618 1.25e-06

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 45.58  E-value: 1.25e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1843419910  581 PPESSGCKTLTSSQA--CVVCEEGFSLHQKSCVQHCPPGF 618
Cdd:smart00261   5 KPCHPECATCTGPGPddCTSCKHGFFLDGGKCVSECPPGT 44
Peptidases_S8_11 cd04843
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ...
132-297 1.34e-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: 50.77  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 132 LNVKAAWAQ-GYTGHGIVVSILDDGIEKNHPDLAGNydpGASfdvndqdpdPQPRYTQMNDNRHGTRCAGEVAAvANNGV 210
Cdd:cd04843     2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGN---GIT---------LISGLTDQADSDHGTAVLGIIVA-KDNGI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 211 CGVGVAYNARIGGVRMLDGEVT-DAVEARSLGLNPNHIHIYSASWGPEDdgktVDGPARLAE--EAFFRGVSQGRgGLGS 287
Cdd:cd04843    69 GVTGIAHGAQAAVVSSTRVSNTaDAILDAADYLSPGDVILLEMQTGGPN----NGYPPLPVEyeQANFDAIRTAT-DLGI 143
                         170
                  ....*....|
gi 1843419910 288 IFVWASGNGG 297
Cdd:cd04843   144 IVVEAAGNGG 153
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
643-675 1.36e-06

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


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 45.59  E-value: 1.36e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1843419910 643 PCHASCATCQGPALTDCLSCPSHASLDpvEQTC 675
Cdd:cd00064     1 PCHPSCATCTGPGPDQCTSCRHGFYLD--GGTC 31
Peptidases_S8_8 cd07492
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ...
146-402 2.19e-06

Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173817 [Multi-domain]  Cd Length: 222  Bit Score: 49.26  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 146 GIVVSILDDGIEKNHPDLAGN------YDPGASFDVNDQDPDpqprytqmnDNRHGTRCAGEVAAVANNGVcgvgvayna 219
Cdd:cd07492     1 GVRVAVIDSGVDTDHPDLGNLaldgevTIDLEIIVVSAEGGD---------KDGHGTACAGIIKKYAPEAE--------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 220 rIGGVRML--DGEVTDAVEARSLG-LNPNHIHIYSASWG-PEDDGKTVDGpaRLAEEAFFRGVsqgrgglgsIFVWASGN 295
Cdd:cd07492    63 -IGSIKILgeDGRCNSFVLEKALRaCVENDIRIVNLSLGgPGDRDFPLLK--ELLEYAYKAGG---------IIVAAAPN 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 296 GGREhdscncdGYTNSIYTLSI---SSATQFGNVPWYSEACsstlattYSSGNQNekqiVTTDLRQKCTESHTGTSASAP 372
Cdd:cd07492   131 NNDI-------GTPPASFPNVIgvkSDTADDPKSFWYIYVE-------FSADGVD----IIAPAPHGRYLTVSGNSFAAP 192
                         250       260       270
                  ....*....|....*....|....*....|
gi 1843419910 373 LAAGIIALTLEANKNLTWRDMQHLVVQTSK 402
Cdd:cd07492   193 HVTGMVALLLSEKPDIDANDLKRLLQRLAV 222
Peptidases_S8_14 cd07497
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ...
144-329 7.77e-06

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


Pssm-ID: 173821 [Multi-domain]  Cd Length: 311  Bit Score: 48.62  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 144 GHGIVVSILDDGIEKNHPDLA--GNYDPGASFDvndqDP-------DPQPR-YTQMND-NRHGTRCAGEVAAVANNGVCG 212
Cdd:cd07497     1 GEGVVIAIVDTGVDYSHPDLDiyGNFSWKLKFD----YKayllpgmDKWGGfYVIMYDfFSHGTSCASVAAGRGKMEYNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 213 ---------VGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNH------------IHIYSASWGPEDDGKTVDGPARLAE 271
Cdd:cd07497    77 ygytgkfliRGIAPDAKIAAVKALWFGDVIYAWLWTAGFDPVDrklswiytggprVDVISNSWGISNFAYTGYAPGLDIS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1843419910 272 EAFFRGVSQGRgglGSIFVWASGNGGREHDSCNCDGytNSIYTLSISSATQFGNVPWY 329
Cdd:cd07497   157 SLVIDALVTYT---GVPIVSAAGNGGPGYGTITAPG--AASLAISVGAATNFDYRPFY 209
VSP pfam03302
Giardia variant-specific surface protein;
594-668 9.14e-06

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 48.81  E-value: 9.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1843419910 594 QACVVCEEGFSL--HQKSCVQHCPPGFapqvldthYSTendvetirASVCAPCHASCATCQGPALTDCLSCPSHASL 668
Cdd:pfam03302  74 KICKECTVANCKtcEDQGQCQACNDGF--------YKS--------GDACSPCHESCKTCSGGTASDCTECLTGKAL 134
Peptidases_S8_10 cd07494
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ...
132-415 9.74e-06

Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173819 [Multi-domain]  Cd Length: 298  Bit Score: 48.24  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 132 LNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNY------DPGASfdvndqDPdpqprytQMNDNRHGTrcaGEVAAV 205
Cdd:cd07494     8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYqvrvvlAPGAT------DP-------ACDENGHGT---GESANL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 206 anngvcgVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHiHIYSASWGPEDDGKTVDGPARLA----------EEAFF 275
Cdd:cd07494    72 -------FAIAPGAQFIGVKLGGPDLVNSVGAFKKAISLSP-DIISNSWGYDLRSPGTSWSRSLPnalkalaatlQDAVA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 276 RGV----SQGRGGL------------GSIFVwasGNGGREHDSCNCDGYTNSIYtlsisSATQfgnVPwysEAC------ 333
Cdd:cd07494   144 RGIvvvfSAGNGGWsfpaqhpeviaaGGVFV---DEDGARRASSYASGFRSKIY-----PGRQ---VP---DVCglvgml 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 334 --SSTLATTYSSGNQNEkqiVTTDLRQKCTESH------TGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAH 405
Cdd:cd07494   210 phAAYLMLPVPPGSQLD---RSCAAFPDGTPPNdgwgvfSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTARDVT 286
                         330
                  ....*....|
gi 1843419910 406 LNANDWATNG 415
Cdd:cd07494   287 KGASAQGTSA 296
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
584-618 1.29e-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: 42.89  E-value: 1.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1843419910 584 SSGCKTLTSS--QACVVCEEGFSLHQKSCVQHCPPGF 618
Cdd:cd00064     3 HPSCATCTGPgpDQCTSCRHGFYLDGGTCVSECPEGT 39
Peptidases_S53_like cd05562
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ...
365-437 6.80e-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: 45.36  E-value: 6.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1843419910 365 TGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTskpahlnANDWATNGvgrkVSHSYGYGLLDAGAMVAL 437
Cdd:cd05562   214 FGTSAAAPHAAGVAALVLSANPGLTPADIRDALRST-------ALDMGEPG----YDNASGSGLVDADRAVAA 275
Furin-like_2 pfam15913
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ...
584-621 2.36e-04

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


Pssm-ID: 464939 [Multi-domain]  Cd Length: 102  Bit Score: 40.88  E-value: 2.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1843419910 584 SSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQ 621
Cdd:pfam15913  59 AENCESCFSKDFCTKCKEGFYLHKGKCLDTCPEGTAAQ 96
TNFRSF1B cd10577
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B ...
596-675 9.15e-04

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: 40.54  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 596 CVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTendvetiraSVCAPCHASCATCQGPALTDCLSCPSHASLDPVE-QT 674
Cdd:cd10577     1 CRNSKEYYDEKAQMCCSKCPPGQHVKHSCTKTSD---------TVCAPCEESTYTQLWNWVPECLSCSSPCSSDQVEtQA 71

                  .
gi 1843419910 675 C 675
Cdd:cd10577    72 C 72
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
596-662 3.49e-03

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


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 38.51  E-value: 3.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1843419910 596 CVVCEeGFSLHqKSCVQHCP-PGFAPQvldthystendvETIRASVCAPCHASC------ATCQGPALTDCLSC 662
Cdd:pfam14843  19 CLSCR-NFSRG-GTCVESCNiLQGEPR------------EYVVNSTCVPCHPEClpqngtATCSGPGADNCTKC 78
GF_recep_IV pfam14843
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ...
610-660 3.49e-03

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


Pssm-ID: 464344 [Multi-domain]  Cd Length: 132  Bit Score: 38.51  E-value: 3.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1843419910 610 CVQHCPPG-FAPQVLDTHYSTENDVetirasvCAPCHASCAT-CQGPALTDCL 660
Cdd:pfam14843  87 CVSSCPSGvLGENDLIWKYADANGV-------CQPCHPNCTQgCTGPGLTGCP 132
Peptidases_S8_SKI-1_like cd07479
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ...
138-161 8.55e-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: 38.97  E-value: 8.55e-03
                          10        20
                  ....*....|....*....|....
gi 1843419910 138 WAQGYTGHGIVVSILDDGIEKNHP 161
Cdd:cd07479     1 WQLGYTGAGVKVAVFDTGLAKDHP 24
VSP pfam03302
Giardia variant-specific surface protein;
582-664 9.75e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 39.18  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843419910 582 PESSGCKTLTSSQACVVCEEGFSLHQKSCVQhCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPAlTDCLS 661
Cdd:pfam03302 228 PGKSVCEEANSGGTCQKEAPGYKLNNGDLVT-CSPGCKTCTSNTVCTTCMDGYVKTSDSCTKCDSSCETCTGAT-TTCKT 305

                  ...
gi 1843419910 662 CPS 664
Cdd:pfam03302 306 CAT 308
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH