|
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 ... |
126-420 |
4.56e-163 |
|
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: 499.01 E-value: 4.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 126 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 204
Cdd:cd04059 1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 205 DasNENKHGTRCAGEVAAAANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSFNPQHVHIYSASWGPDDDGKTVDGP 284
Cdd:cd04059 81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 285 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 363
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 299523015 364 SYDKKIITTDLR--QRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 420
Cdd:cd04059 239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
|
|
| Peptidase_S8 |
pfam00082 |
Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
162-445 |
2.50e-65 |
|
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: 223.88 E-value: 2.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 162 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNG----NDLDPMPRYDASNENKHGTRCAGEVAAAANNSHCTVGIAFNA 237
Cdd:pfam00082 1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEAsvdfNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 238 KIGGVRML-DGDVTDMVEAKSVSFN-PQHVHIYSASWGPDddgKTVDGPAPLTRQAFENGvrmGRRGLGSVFVWASGNGG 315
Cdd:pfam00082 81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 316 RSKDHCSCDGY-TNSIYTISISSTaesgkkpwylEECSSTLATTYSS----------------GESY-------DKKIIT 371
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAV----------DEASEGNLASFSSygptldgrlkpdivapGGNItggnissTLLTTT 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299523015 372 TDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNAndwktnaagfkVSHLYGFG 445
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAG-----------LDRLFGYG 287
|
|
| P_proprotein |
pfam01483 |
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ... |
505-595 |
9.74e-39 |
|
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.
Pssm-ID: 460225 [Multi-domain] Cd Length: 86 Bit Score: 139.33 E-value: 9.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 505 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 584
Cdd:pfam01483 1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75
|
90
....*....|.
gi 299523015 585 PGKLKEWSLVL 595
Cdd:pfam01483 76 TGTLNSWQLTL 86
|
|
| S8_pro-domain |
pfam16470 |
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ... |
38-114 |
2.58e-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: 132.34 E-value: 2.58e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299523015 38 HWAVKIAGGFPEANRIASKYGFINIGQIGALKDYYHFYHSRTIKRSVISSRGTHSFISMEPKVEWIQQQVVKKRTKR 114
Cdd:pfam16470 1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
|
|
| AprE |
COG1404 |
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
154-420 |
4.11e-34 |
|
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 138.31 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 154 GAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCdVNGNDldpmpryDASNENKHGTRCAGEVAAAANNSHCTVGI 233
Cdd:COG1404 100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDF-VDGDG-------DPSDDNGHGTHVAGIIAANGNNGGGVAGV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 234 AFNAKIGGVRMLD----GDVTDMVEA--KSVSfnpQHVHIYSASWGPDDDGKTvdgpaPLTRQAFENGvrmgrRGLGSVF 307
Cdd:COG1404 172 APGAKLLPVRVLDdngsGTTSDIAAAidWAAD---NGADVINLSLGGPADGYS-----DALAAAVDYA-----VDKGVLV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 308 VWASGNGGRSkdhCSCDGYTNSIY-TISISSTAESGKKPWYleecSSTlattyssGESYD-----KKIITTDLRQRcTDN 381
Cdd:COG1404 239 VAAAGNSGSD---DATVSYPAAYPnVIAVGAVDANGQLASF----SNY-------GPKVDvaapgVDILSTYPGGG-YAT 303
|
250 260 270
....*....|....*....|....*....|....*....
gi 299523015 382 HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 420
Cdd:COG1404 304 LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTAT 342
|
|
| COG4935 |
COG4935 |
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ... |
506-597 |
6.26e-18 |
|
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443962 [Multi-domain] Cd Length: 641 Bit Score: 90.27 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 506 EHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLfdHSMEGFkNWEFMTIHCWGERAAGDWVLEVYDTPSQlrnfkTP 585
Cdd:COG4935 558 EDVTVTVDITHTYRGDLVITLISPDGTTVVLKNRSG--GSADNI-NATFDVANFSGESANGTWTLRVVDTAGG-----DT 629
|
90
....*....|..
gi 299523015 586 GKLKEWSLVLYG 597
Cdd:COG4935 630 GTLNSWSLTFTG 641
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
635-744 |
3.22e-11 |
|
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: 62.78 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 635 PCDPECSEVGCDGPGPDHCNDCLHYyyklkNNTRICVSSCP-----PGHYhADKKRCRKCAPNCE------SCFGSHGDQ 703
Cdd:pfam14843 1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNilqgePREY-VVNSTCVPCHPECLpqngtaTCSGPGADN 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 299523015 704 CMSCKygYFLNEETnsCVTHCPDGSYQD--------TKKNLCRKCSENC 744
Cdd:pfam14843 75 CTKCA--HFRDGPH--CVSSCPSGVLGEndliwkyaDANGVCQPCHPNC 119
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1264-1549 |
9.11e-11 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 66.15 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1264 SKCPEGSYAEDGICERCSSPcrtcegNATNCHSCEGGHVLHH-GVCQENCPERHVAVKGVCKHCPEMCQDCIHEKtCKEC 1342
Cdd:pfam03302 15 TKCTSSAPCKTENCKACSND------KREVCEECNSNNYLTPtSQCIDDCAKIGNYYYTTNANNKKICKECTVAN-CKTC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1343 TpefflhDDMCHQSCPRGFYADSRHCVPCHKDCLECSGPKADDCELCLESSWVLYD-----GLCLEECPAGTYYEK---- 1413
Cdd:pfam03302 88 E------DQGQCQACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALRYGndgtkGTCGEGCTTGTGAGAcktc 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1414 -----ETKECRDCH----------------KSCLTCSSS----GTCTTCQKG-LIMNprGSCMANEKCsPSEYWDEDAPG 1467
Cdd:pfam03302 162 gltidGTSYCSECAteteypqngvctstaaRATATCKASsvanGMCSSCANGyFRMN--GGCYETTKF-PGKSVCEEANS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1468 CKPCHVKCFHCMGPAEDQCQTCPMNSLLLNTTCVKDCPEGYYADEDSnrCAHCHSSCRTCEGRhSRQCHSCRPGWFQLGK 1547
Cdd:pfam03302 239 GGTCQKEAPGYKLNNGDLVTCSPGCKTCTSNTVCTTCMDGYVKTSDS--CTKCDSSCETCTGA-TTTCKTCATGYYKSGT 315
|
..
gi 299523015 1548 EC 1549
Cdd:pfam03302 316 GC 317
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
681-1100 |
3.50e-10 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 64.22 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 681 ADKKRCRKCAP----NCESCFGSHGDQCMSCKYGYFLNEeTNSCVTHCpdgsyQDTKKNLCRKCSENCKTCTEFH--NCT 754
Cdd:pfam03302 12 ADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYLTP-TSQCIDDC-----AKIGNYYYTTNANNKKICKECTvaNCK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 755 ECRDGLSLQgsrcsvSCEDGRYFNGQDCQPCHRFCATCAGAGADGCINCTEGYFMEDGrcvqscsisyyfdhssENGYKS 834
Cdd:pfam03302 86 TCEDQGQCQ------ACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALRYG----------------NDGTKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 835 ckKCDISCLTCNGPGfkNCTSCPsgylLDLGMCQMGAICKDGEYVDEHGHCQTCEASCAKCqgptqedCTTCPMTrifdD 914
Cdd:pfam03302 144 --TCGEGCTTGTGAG--ACKTCG----LTIDGTSYCSECATETEYPQNGVCTSTAARATAT-------CKASSVA----N 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 915 GRCvSNCPSWKFEFENQCHpchhtcQRCQGSGPTHCTSCGADnygrehflyqGECGDSCPEghYATEGNTCLPCPDNCEL 994
Cdd:pfam03302 205 GMC-SSCANGYFRMNGGCY------ETTKFPGKSVCEEANSG----------GTCQKEAPG--YKLNNGDLVTCSPGCKT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 995 CHSVHVCTRCMKGYFiaptnhtcqklecgqgevqdPDYEECVPCEEGCLGCSlDDPGTCTSCAMGYYrfdhhcyktcpeK 1074
Cdd:pfam03302 266 CTSNTVCTTCMDGYV--------------------KTSDSCTKCDSSCETCT-GATTTCKTCATGYY------------K 312
|
410 420
....*....|....*....|....*.
gi 299523015 1075 TYSEEVECKACDSNCGSCDQNGCYWC 1100
Cdd:pfam03302 313 SGTGCVSCTSSESDNGITGVKGCLNC 338
|
|
| PTZ00262 |
PTZ00262 |
subtilisin-like protease; Provisional |
167-411 |
6.27e-09 |
|
subtilisin-like protease; Provisional
Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 60.75 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 167 VTILDDGIERTHPDLMQNY---------------------DALASCDVNGNDLDPMprydasNENKHGTRCAGEVAAAAN 225
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM------DDNYHGTHVSGIISAIGN 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 226 NSHCTVGIAFNAKIGGVRMLD----GDVTDMVeaKSVSF-NPQHVHIYSASWGPDDDGKTvdgpapltrqaFENGVRMGR 300
Cdd:PTZ00262 394 NNIGIVGVDKRSKLIICKALDshklGRLGDMF--KCFDYcISREAHMINGSFSFDEYSGI-----------FNESVKYLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 301 RgLGSVFVWASGN----GGRSKDHCSCDGYTNSIYTISISSTAES---------GKKPWYLEECSSTLATTYSSGESYDK 367
Cdd:PTZ00262 461 E-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYPPILSKKLRNvitvsnlikDKNNQYSLSPNSFYSAKYCQLAAPGT 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 299523015 368 KIITTDLRQRCTDNhTGTSASAPMAAGIIALALEANPFLTWRDV 411
Cdd:PTZ00262 540 NIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1470-1518 |
1.90e-08 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 52.14 E-value: 1.90e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 299523015 1470 PCHVKCFHCMGPAEDQCQTCPMNSLLLNTTCVKDCPEGYYADEDSNRCA 1518
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
773-1057 |
5.19e-07 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 54.92 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 773 DGRYFNGQDCQPCHRFCATCA-GAGADGCINCTEGYFMEDGR-CVQSCS-----ISYYFDHSSE---------------N 830
Cdd:PTZ00214 348 GDGYLCGDATNGGVSGCATCGyNSGAVTCTRCSAGYLGVDGKsCSESCSgdtrgVCTKVAEGSEstevscrcvckptfyN 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 831 GYKSCKKCDISCLTCNGPGFKNCTSCPSGYLLDLGM-----------CQMGAICKD-GEYVDEHGHCQTCEASC------ 892
Cdd:PTZ00214 428 SSGTCTPCTDSCAVCKDGTPTGCQQCSPGKILEFSIvssesadcvdqCSVGSECAEcGITIDGSRYCTRCKDAStypfng 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 893 ---------AKCQGPTQEDCTTC-----------------PMTRIFD---DGRCVSNCPSWKFEFENQCHPCHHTCQRCQ 943
Cdd:PTZ00214 508 vcipntqrdAYCTSTANGACTTCsgaaflmnggcyttehyPGSTICDkqsNGKCTTTKKGYGISPDGKLLECDPTCLACT 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 944 GSGPTHCTSCGADN-YGREHFLYQGECGD--SCPEGHYAtEGNTCLPCPD-NCELCHSVHVCTRCMKGYFIAPTNHTC-- 1017
Cdd:PTZ00214 588 APGPGRCTRCPSDKlLKRASGAATGSCVDpgACVDGYYA-DGDACLPCATpGCKTCGHASFCTECAGELFVSLDGQSCle 666
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 299523015 1018 ---------------QKLECGQGEVQDPDYEECVP---CEEGCLGC-SLDDPGTCTSCA 1057
Cdd:PTZ00214 667 ectgdkvvgevsggvRRCWCERGFLPALDRSGCVLpteCPPDMPSCaACDESGRCLLCV 725
|
|
| FU |
smart00261 |
Furin-like repeats; |
782-823 |
7.33e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 47.50 E-value: 7.33e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 299523015 782 CQPCHRFCATCAGAGADGCINCTEGYFMEDGRCVQSCSISYY 823
Cdd:smart00261 4 CKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
1569-1686 |
1.71e-06 |
|
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: 48.91 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1569 CNRSCK--GCQGPRPTDCLSCDRFFFllrsKGECHRSCPDHYYVEQSTQ---TCERCHPTCDQ------CKGKGALNCLS 1637
Cdd:pfam14843 2 CDPLCSseGCWGPGPDQCLSCRNFSR----GGTCVESCNILQGEPREYVvnsTCVPCHPECLPqngtatCSGPGADNCTK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1638 CVwsyHLMGGI-CTSDC---------LVGEYRVGEGEkfnCEKCHESCME-CKGPGAKNC 1686
Cdd:pfam14843 78 CA---HFRDGPhCVSSCpsgvlgendLIWKYADANGV---CQPCHPNCTQgCTGPGLTGC 131
|
|
| FU |
smart00261 |
Furin-like repeats; |
1514-1558 |
2.81e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 45.96 E-value: 2.81e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 299523015 1514 SNRCAHCHSSCRTCEGRHSRQCHSCRPGWFQLGKECLLQCREGYY 1558
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
784-825 |
3.68e-06 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 45.59 E-value: 3.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 299523015 784 PCHRFCATCAGAGADGCINCTEGYFMEDGRCVQSCSISYYFD 825
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1182-1229 |
6.69e-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: 44.82 E-value: 6.69e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 299523015 1182 PCHSSCKTCNGS-ATLCTSCPKGAYLLAQACVSSCPQGTWPSVRSGSCE 1229
Cdd:cd00064 1 PCHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
688-738 |
7.24e-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: 44.82 E-value: 7.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 299523015 688 KCAPNCESCFGSHGDQCMSCKYGYFLNEetNSCVTHCPDGSYQDTKKNLCR 738
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDG--GTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
1563-1609 |
1.37e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.04 E-value: 1.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 299523015 1563 TGRCERCNRSCKGCQGPRPTDCLSCDRFFFLLrsKGECHRSCPDHYY 1609
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1181-1220 |
1.98e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 43.27 E-value: 1.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 299523015 1181 QPCHSSCKTCNGS-ATLCTSCPKGAYLLAQACVSSCPQGTW 1220
Cdd:smart00261 5 KPCHPECATCTGPgPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1569-1618 |
2.60e-05 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 43.28 E-value: 2.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 299523015 1569 CNRSCKGCQGPRPTDCLSCDRFFFLLrsKGECHRSCPDHYYVEQSTQTCE 1618
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
683-729 |
3.40e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 42.88 E-value: 3.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 299523015 683 KKRCRKCAPNCESCFGSHGDQCMSCKYGYFLNEETnsCVTHCPDGSY 729
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGK--CVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1126-1162 |
1.56e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 40.96 E-value: 1.56e-04
10 20 30
....*....|....*....|....*....|....*..
gi 299523015 1126 GECESCHRACETCTGPGHDECSSCQEGLQLLRGMCVH 1162
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVS 38
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1084-1129 |
2.77e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 40.19 E-value: 2.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 299523015 1084 ACDSNCGSC---DQNGCYWCEEGFFLLGGSCVRKCGPGFYGDQEMGECE 1129
Cdd:cd00064 1 PCHPSCATCtgpGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
1353-1643 |
3.64e-04 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 45.68 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1353 CHQSCPRGFYADSRHCVPCHKDCLECSGPKADDCELC-----LESSWVLYDGL-CLEECPAGTYYEK------ETKECRD 1420
Cdd:PTZ00214 417 CRCVCKPTFYNSSGTCTPCTDSCAVCKDGTPTGCQQCspgkiLEFSIVSSESAdCVDQCSVGSECAEcgitidGSRYCTR 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1421 CHKSCL-----------------TCSSSGTCTTCQK-GLIMNprGSC--------------MANEKCSPSE--YWDEDAP 1466
Cdd:PTZ00214 497 CKDASTypfngvcipntqrdaycTSTANGACTTCSGaAFLMN--GGCyttehypgsticdkQSNGKCTTTKkgYGISPDG 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1467 GCKPCHVKCFHCMGPAEDQCQTCPMNSLLLNTT------CVKD--CPEGYYADEDSnrCAHCHS-SCRTCEgrHSRQCHS 1537
Cdd:PTZ00214 575 KLLECDPTCLACTAPGPGRCTRCPSDKLLKRASgaatgsCVDPgaCVDGYYADGDA--CLPCATpGCKTCG--HASFCTE 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1538 CRPGWFQL--GKECLLQCREGYYADNSTGRCERCnrsckgcqgprptdclSCDRFFFLLRSKGEChrscpdhyyveQSTQ 1615
Cdd:PTZ00214 651 CAGELFVSldGQSCLEECTGDKVVGEVSGGVRRC----------------WCERGFLPALDRSGC-----------VLPT 703
|
330 340
....*....|....*....|....*...
gi 299523015 1616 TCERCHPTCDQCKGKGalNCLSCVWSYH 1643
Cdd:PTZ00214 704 ECPPDMPSCAACDESG--RCLLCVTSGH 729
|
|
| FU |
smart00261 |
Furin-like repeats; |
1081-1120 |
1.21e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 38.26 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 299523015 1081 ECKACDSNCGSC---DQNGCYWCEEGFFLLGGSCVRKCGPGFY 1120
Cdd:smart00261 3 ECKPCHPECATCtgpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1131-1162 |
1.44e-03 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 38.27 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|..
gi 299523015 1131 CHRACETCTGPGHDECSSCQEGLQLLRGMCVH 1162
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVS 33
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
1087-1160 |
2.77e-03 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 38.95 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1087 SNCGSC-DQNGCYWCEEGFFLL--------GGSCVRKCGPGFYG--DQEMGECESCH-RACETCTGpgHDECSSCQEGLQ 1154
Cdd:pfam15913 2 SGCVLCsEENGCLTCQPRLFLLlerngirqYGVCLHSCPPGYFGirGQEVNRCTKCKaENCESCFS--KDFCTKCKEGFY 79
|
....*.
gi 299523015 1155 LLRGMC 1160
Cdd:pfam15913 80 LHKGKC 85
|
|
| FU |
smart00261 |
Furin-like repeats; |
1668-1709 |
5.74e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 36.33 E-value: 5.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 299523015 1668 CEKCHESCMECKGPGAKNCTLCPANLVLHmdDSHCLHCCNTS 1709
Cdd:smart00261 4 CKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPG 43
|
|
| |
|
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 ... |
126-420 |
4.56e-163 |
|
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: 499.01 E-value: 4.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 126 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 204
Cdd:cd04059 1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 205 DasNENKHGTRCAGEVAAAANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSFNPQHVHIYSASWGPDDDGKTVDGP 284
Cdd:cd04059 81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 285 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 363
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 299523015 364 SYDKKIITTDLR--QRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 420
Cdd:cd04059 239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
|
|
| Peptidase_S8 |
pfam00082 |
Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
162-445 |
2.50e-65 |
|
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: 223.88 E-value: 2.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 162 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNG----NDLDPMPRYDASNENKHGTRCAGEVAAAANNSHCTVGIAFNA 237
Cdd:pfam00082 1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEAsvdfNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 238 KIGGVRML-DGDVTDMVEAKSVSFN-PQHVHIYSASWGPDddgKTVDGPAPLTRQAFENGvrmGRRGLGSVFVWASGNGG 315
Cdd:pfam00082 81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 316 RSKDHCSCDGY-TNSIYTISISSTaesgkkpwylEECSSTLATTYSS----------------GESY-------DKKIIT 371
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAV----------DEASEGNLASFSSygptldgrlkpdivapGGNItggnissTLLTTT 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299523015 372 TDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNAndwktnaagfkVSHLYGFG 445
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAG-----------LDRLFGYG 287
|
|
| P_proprotein |
pfam01483 |
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ... |
505-595 |
9.74e-39 |
|
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein convertases is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain.
Pssm-ID: 460225 [Multi-domain] Cd Length: 86 Bit Score: 139.33 E-value: 9.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 505 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 584
Cdd:pfam01483 1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75
|
90
....*....|.
gi 299523015 585 PGKLKEWSLVL 595
Cdd:pfam01483 76 TGTLNSWQLTL 86
|
|
| S8_pro-domain |
pfam16470 |
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ... |
38-114 |
2.58e-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: 132.34 E-value: 2.58e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299523015 38 HWAVKIAGGFPEANRIASKYGFINIGQIGALKDYYHFYHSRTIKRSVISSRGTHSFISMEPKVEWIQQQVVKKRTKR 114
Cdd:pfam16470 1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
|
|
| Peptidases_S8_15 |
cd07498 |
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ... |
165-418 |
3.11e-35 |
|
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173822 [Multi-domain] Cd Length: 242 Bit Score: 135.55 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 165 IVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPmprydaSNENKHGTRCAGEVAAAANNSHCTVGIAFNAKIGGVRM 244
Cdd:cd07498 1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPT------SDIDGHGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 245 LDGD--VTDMVEAKSVSFNPQH-VHIYSASWGPDDdgktvdgPAPLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDhc 321
Cdd:cd07498 75 ADSLgyAYWSDIAQAITWAADNgADVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLFAAGNSGRSVS-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 322 scDGYTNSIYTISISSTAESGKKPWY--------LEECSSTLATTYSSGESydkkiiTTDLRQRCTDNHTGTSASAPMAA 393
Cdd:cd07498 146 --SGYAANPSVIAVAATDSNDARASYsnygnyvdLVAPGVGIWTTGTGRGS------AGDYPGGGYGSFSGTSFASPVAA 217
|
250 260
....*....|....*....|....*
gi 299523015 394 GIIALALEANPFLTWRDVQHVIVRT 418
Cdd:cd07498 218 GVAALILSANPNLTPAEVEDILTST 242
|
|
| AprE |
COG1404 |
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
154-420 |
4.11e-34 |
|
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 138.31 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 154 GAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCdVNGNDldpmpryDASNENKHGTRCAGEVAAAANNSHCTVGI 233
Cdd:COG1404 100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDF-VDGDG-------DPSDDNGHGTHVAGIIAANGNNGGGVAGV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 234 AFNAKIGGVRMLD----GDVTDMVEA--KSVSfnpQHVHIYSASWGPDDDGKTvdgpaPLTRQAFENGvrmgrRGLGSVF 307
Cdd:COG1404 172 APGAKLLPVRVLDdngsGTTSDIAAAidWAAD---NGADVINLSLGGPADGYS-----DALAAAVDYA-----VDKGVLV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 308 VWASGNGGRSkdhCSCDGYTNSIY-TISISSTAESGKKPWYleecSSTlattyssGESYD-----KKIITTDLRQRcTDN 381
Cdd:COG1404 239 VAAAGNSGSD---DATVSYPAAYPnVIAVGAVDANGQLASF----SNY-------GPKVDvaapgVDILSTYPGGG-YAT 303
|
250 260 270
....*....|....*....|....*....|....*....
gi 299523015 382 HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 420
Cdd:COG1404 304 LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTAT 342
|
|
| Peptidases_S8_S53 |
cd00306 |
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ... |
165-418 |
5.33e-30 |
|
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173787 [Multi-domain] Cd Length: 241 Bit Score: 120.38 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 165 IVVTILDDGIERTHPDLmqnyDALASCDVNGNDLDPMPRY--DASNENKHGTRCAGEVAAAANNSHCtVGIAFNAKIGGV 242
Cdd:cd00306 1 VTVAVIDTGVDPDHPDL----DGLFGGGDGGNDDDDNENGptDPDDGNGHGTHVAGIIAASANNGGG-VGVAPGAKLIPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 243 RMLD----GDVTDMVEAKSVSFNPQHVHIYSASWGPDDDGktvdgPAPLTRQAFENGVRMgrrgLGSVFVWASGNGGRSK 318
Cdd:cd00306 76 KVLDgdgsGSSSDIAAAIDYAAADQGADVINLSLGGPGSP-----PSSALSEAIDYALAK----LGVLVVAAAGNDGPDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 319 DHCScDGYTNSIYTISISSTAESGKKPWYLEeCSSTLATTYSSGESYdkkIITTDLRQRCTDNHTGTSASAPMAAGIIAL 398
Cdd:cd00306 147 GTNI-GYPAASPNVIAVGAVDRDGTPASPSS-NGGAGVDIAAPGGDI---LSSPTTGGGGYATLSGTSMAAPIVAGVAAL 221
|
250 260
....*....|....*....|
gi 299523015 399 ALEANPFLTWRDVQHVIVRT 418
Cdd:cd00306 222 LLSANPDLTPAQVKAALLST 241
|
|
| Peptidases_S8_Subtilisin_like |
cd07473 |
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ... |
163-420 |
2.18e-26 |
|
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173799 [Multi-domain] Cd Length: 259 Bit Score: 110.36 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 163 KNIVVTILDDGIERTHPDLMQNY--DALASC-------------DVNG-----NDLDPMPrydasnENKHGTRCAGEVAA 222
Cdd:cd07473 2 GDVVVAVIDTGVDYNHPDLKDNMwvNPGEIPgngidddgngyvdDIYGwnfvnNDNDPMD------DNGHGTHVAGIIGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 223 AANNSHCTVGIAFNAKIGGVRMLD----GDVTDMVEA--KSVSFNpqhVHIYSASWGPdddgktvDGPAPLTRQAFEngv 296
Cdd:cd07473 76 VGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAidYAVDMG---AKIINNSWGG-------GGPSQALRDAIA--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 297 RMGRRGLgsVFVWASGNGGRSKDH-----CScdgYTNSiYTISISSTAESGKKPWYleecSSTLATT---YSSGESydkk 368
Cdd:cd07473 143 RAIDAGI--LFVAAAGNDGTNNDKtptypAS---YDLD-NIISVAATDSNDALASF----SNYGKKTvdlAAPGVD---- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 299523015 369 IITTDLRQRcTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 420
Cdd:cd07473 209 ILSTSPGGG-YGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
|
|
| Peptidases_S8_Autotransporter_serine_protease_like |
cd04848 |
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ... |
161-420 |
3.54e-22 |
|
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: 98.17 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 161 TGKNIVVTILDDGIERTHPDLMQNYDALAScdvNGNDLDPMPRYDASNENkHGTRCAGeVAAAANNSHCTVGIAFNAKIG 240
Cdd:cd04848 1 TGAGVKVGVIDSGIDLSHPEFAGRVSEASY---YVAVNDAGYASNGDGDS-HGTHVAG-VIAAARDGGGMHGVAPDATLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 241 GVRMLDGDVT---DMVEAKSVSFNP-QHVHIYSASWGPDDDGKTVDGPAPL---TRQAFENGVRMGRRGLGSVFVWASGN 313
Cdd:cd04848 76 SARASASAGStfsDADIAAAYDFLAaSGVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVFAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 314 GGRSKDhcscDGYTNSIY--------------------TISISSTAESGK--KPWYLeecsST-----LATTYSSGESYD 366
Cdd:cd04848 156 DGQANP----SLAAAALPylepeleggwiavvavdpngTIASYSYSNRCGvaANWCL----AApgeniYSTDPDGGNGYG 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 299523015 367 KKIittdlrqrctdnhtGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 420
Cdd:cd04848 228 RVS--------------GTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTAT 267
|
|
| Peptidases_S8_Thermitase_like |
cd07484 |
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ... |
127-420 |
9.39e-22 |
|
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173810 [Multi-domain] Cd Length: 260 Bit Score: 96.95 E-value: 9.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 127 NDPKWPSMWYMHcsdnthpcqsDMNIEGAWKRGyTGKNIVVTILDDGIERTHPDLM-----QNYDAlascdVNGNDldpm 201
Cdd:cd07484 3 NDPYYSYQWNLD----------QIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLLkvkfvLGYDF-----VDNDS---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 202 pryDASNENKHGTRCAGEVAAAANNSHCTVGIAFNAKIGGVRMLD----GDVTDMVEAksvsfnpqhvhIYsasWGPDDD 277
Cdd:cd07484 63 ---DAMDDNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANG-----------IR---YAADKG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 278 GKTVD---GpAPLTRQAFENGVRMGRRGlGSVFVWASGNGGRSKdhCScdgYTNSI-YTISISSTAESGKKPWYleecss 353
Cdd:cd07484 126 AKVINlslG-GGLGSTALQEAINYAWNK-GVVVVAAAGNEGVSS--VS---YPAAYpGAIAVAATDQDDKRASF------ 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299523015 354 tlaTTYSS-------GESydkkIITTDLRQRcTDNHTGTSASAPMAAGIIALALEANPfLTWRDVQHVIVRTSR 420
Cdd:cd07484 193 ---SNYGKwvdvsapGGG----ILSTTPDGD-YAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDALKKTAD 257
|
|
| Peptidases_S8_13 |
cd07496 |
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ... |
164-407 |
1.95e-21 |
|
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173820 [Multi-domain] Cd Length: 285 Bit Score: 96.59 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 164 NIVVTILDDGIeRTHPDLMQN-----YD----ALASCDVNGNDLDP----------------MPRYDASNENKHGTRCAG 218
Cdd:cd07496 1 GVVVAVLDTGV-LFHHPDLAGvllpgYDfisdPAIANDGDGRDSDPtdpgdwvtgddvppggFCGSGVSPSSWHGTHVAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 219 EVAAAANNSHCTVGIAFNAKIGGVRML---DGDVTDMVEA---------KSVSFNPQHVHIYSASWGPDddgktvdGPAP 286
Cdd:cd07496 80 TIAAVTNNGVGVAGVAWGARILPVRVLgkcGGTLSDIVDGmrwaaglpvPGVPVNPNPAKVINLSLGGD-------GACS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 287 LTRQAFENGVRmgrrGLGSVFVWASGNGGRSKDH---CSCDGytnsiyTISISSTAESGKKPWYLE------------EC 351
Cdd:cd07496 153 ATMQNAINDVR----ARGVLVVVAAGNEGSSASVdapANCRG------VIAVGATDLRGQRASYSNygpavdvsapggDC 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299523015 352 SSTL---------ATTYSSGE-SYDkkiittdlrqrctdNHTGTSASAPMAAGIIALALEANPFLT 407
Cdd:cd07496 223 ASDVngdgypdsnTGTTSPGGsTYG--------------FLQGTSMAAPHVAGVAALMKSVNPSLT 274
|
|
| Peptidases_S8_Subtilisin_subset |
cd07477 |
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ... |
164-418 |
1.92e-18 |
|
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173803 [Multi-domain] Cd Length: 229 Bit Score: 86.43 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 164 NIVVTILDDGIERTHPDLMQNYdalascdVNGNDLDPMPRYDASNENKHGTRCAGEVAAAANNSHcTVGIAFNAKIGGVR 243
Cdd:cd07477 1 GVKVAVIDTGIDSSHPDLKLNI-------VGGANFTGDDNNDYQDGNGHGTHVAGIIAALDNGVG-VVGVAPEADLYAVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 244 MLD----GDVTDMVEAKSVSFNpQHVHIYSASWGpdddgktVDGPAPLTRQAFENGVrmgRRGLgsVFVWASGNggrskd 319
Cdd:cd07477 73 VLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLG-------GPSDSPALREAIKKAY---AAGI--LVVAAAGN------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 320 hcscDGYTNSIYT--------ISISSTAESGKKpwyleecsstlaTTYSS----------GESydkkIITTDLRQRCTDN 381
Cdd:cd07477 134 ----SGNGDSSYDypakypsvIAVGAVDSNNNR------------ASFSStgpevelaapGVD----ILSTYPNNDYAYL 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 299523015 382 hTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRT 418
Cdd:cd07477 194 -SGTSMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
|
|
| Peptidases_S8_Fervidolysin_like |
cd07485 |
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ... |
155-404 |
5.50e-18 |
|
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: 86.00 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 155 AWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALA-SCDVNGNDLDPMPRYDA---SNENKHGTRCAGEVAAAANNSHCT 230
Cdd:cd07485 2 AWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGyDPAVNGYNFVPNVGDIDndvSVGGGHGTHVAGTIAAVNNNGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 231 VGIAFN------AKIGGVRMLDGD--VTDMVEAKSVSFNPQH-VHIYSASWGpdddGKTVDGPAPLTRQAFENGVRMGRR 301
Cdd:cd07485 82 GGIAGAggvapgVKIMSIQIFAGRyyVGDDAVAAAIVYAADNgAVILQNSWG----GTGGGIYSPLLKDAFDYFIENAGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 302 GL--GSVFVWASGNGGRSKDH--CSCDGytnsiyTISISSTAESGKKPWYleecsSTLATTYSSGESYDKKIITTDLRQR 377
Cdd:cd07485 158 SPldGGIVVFSAGNSYTDEHRfpAAYPG------VIAVAALDTNDNKASF-----SNYGRWVDIAAPGVGTILSTVPKLD 226
|
250 260 270
....*....|....*....|....*....|..
gi 299523015 378 CTDNHT-----GTSASAPMAAGIIALALEANP 404
Cdd:cd07485 227 GDGGGNyeylsGTSMAAPHVSGVAALVLSKFP 258
|
|
| COG4935 |
COG4935 |
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ... |
506-597 |
6.26e-18 |
|
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443962 [Multi-domain] Cd Length: 641 Bit Score: 90.27 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 506 EHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLfdHSMEGFkNWEFMTIHCWGERAAGDWVLEVYDTPSQlrnfkTP 585
Cdd:COG4935 558 EDVTVTVDITHTYRGDLVITLISPDGTTVVLKNRSG--GSADNI-NATFDVANFSGESANGTWTLRVVDTAGG-----DT 629
|
90
....*....|..
gi 299523015 586 GKLKEWSLVLYG 597
Cdd:COG4935 630 GTLNSWSLTFTG 641
|
|
| Peptidases_S8_1 |
cd07487 |
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ... |
162-418 |
2.66e-17 |
|
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: 83.79 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 162 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMprYDasnENKHGTRCAGEVAAAANNSHCTV-GIAFNAKIG 240
Cdd:cd07487 1 GKGITVAVLDTGIDAPHPDFDGRIIRFADFVNTVNGRTTP--YD---DNGHGTHVAGIIAGSGRASNGKYkGVAPGANLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 241 GVRMLD----GDVTDMVEAksVSF-----NPQHVHIYSASWG-PDDDGktvDGPAPLtRQAFENGVRMgrrglGSVFVWA 310
Cdd:cd07487 76 GVKVLDdsgsGSESDIIAG--IDWvvennEKYNIRVVNLSLGaPPDPS---YGEDPL-CQAVERLWDA-----GIVVVVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 311 SGNGGRSKDHCSCDGytNSIYTISISSTAESGKKPWYLEECSS---TL-----------ATTYSSGESYDKKIITTDLRQ 376
Cdd:cd07487 145 AGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSSrgpTGdgrikpdvvapGENIVSCRSPGGNPGAGVGSG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 299523015 377 RCTDnhTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRT 418
Cdd:cd07487 223 YFEM--SGTSMATPHVSGAIALLLQANPILTPDEVKCILRDT 262
|
|
| Peptidases_S8_Kp43_protease |
cd04842 |
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ... |
157-402 |
1.49e-14 |
|
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases
Pssm-ID: 173791 [Multi-domain] Cd Length: 293 Bit Score: 76.21 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 157 KRGYTGKNIVVTILDDGIERTHPDLMqnydalascDVNGNDLDPMPR----YDASNENK-----HGTRCAGEVAAAANNS 227
Cdd:cd04842 1 GLGLTGKGQIVGVADTGLDTNHCFFY---------DPNFNKTNLFHRkivrYDSLSDTKddvdgHGTHVAGIIAGKGNDS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 228 HCTV---GIAFNAKIGGVRM------------LDGDVTDMVEAKSvsfnpqhvHIYSASWGPDDDG------KTVDgpap 286
Cdd:cd04842 72 SSISlykGVAPKAKLYFQDIgdtsgnlssppdLNKLFSPMYDAGA--------RISSNSWGSPVNNgytllaRAYD---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 287 ltRQAFENgvrmgrRGLgsVFVWASGNGGrskdhcscDGYTNSIYTISIS-----------STAESGKKPWYLEECSSTL 355
Cdd:cd04842 140 --QFAYNN------PDI--LFVFSAGNDG--------NDGSNTIGSPATAknvltvgasnnPSVSNGEGGLGQSDNSDTV 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299523015 356 ATTYSSGESYD--KK---------IITTDLRQR----CTDNH----TGTSASAPMAAGIIALALEA 402
Cdd:cd04842 202 ASFSSRGPTYDgrIKpdlvapgtgILSARSGGGgigdTSDSAytskSGTSMATPLVAGAAALLRQY 267
|
|
| Peptidases_S8_subtilisin_Vpr-like |
cd07474 |
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ... |
162-428 |
3.53e-14 |
|
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173800 [Multi-domain] Cd Length: 295 Bit Score: 75.44 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 162 GKNIVVTILDDGIERTHPDLMQNYDALASC----DVNGNDLDPMPR---------YDASNENKHGTRCAGEVAAAANNSH 228
Cdd:cd07474 1 GKGVKVAVIDTGIDYTHPDLGGPGFPNDKVkggyDFVDDDYDPMDTrpypsplgdASAGDATGHGTHVAGIIAGNGVNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 229 CTVGIAFNAKIGGVRMLDGD---VTDMVEA---KSVSfnpQHVHIYSASWG-----PDDDGKtvdgpapltrQAFENGVR 297
Cdd:cd07474 81 TIKGVAPKADLYAYKVLGPGgsgTTDVIIAaieQAVD---DGMDVINLSLGssvngPDDPDA----------IAINNAVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 298 mgrrgLGSVFVWASGNGGrskDHCSCDGyTNSIYTISISSTAESGKKPWYleecSSTLATTYSSGESYDKKIITTDL--- 374
Cdd:cd07474 148 -----AGVVVVAAAGNSG---PAPYTIG-SPATAPSAITVGASTVADVAE----ADTVGPSSSRGPPTSDSAIKPDIvap 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299523015 375 -------RQRCTDN---HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTsrAGHLNAND 428
Cdd:cd07474 215 gvdimstAPGSGTGyarMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNT--AKPLYDSD 276
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
635-744 |
3.22e-11 |
|
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: 62.78 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 635 PCDPECSEVGCDGPGPDHCNDCLHYyyklkNNTRICVSSCP-----PGHYhADKKRCRKCAPNCE------SCFGSHGDQ 703
Cdd:pfam14843 1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNilqgePREY-VVNSTCVPCHPECLpqngtaTCSGPGADN 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 299523015 704 CMSCKygYFLNEETnsCVTHCPDGSYQD--------TKKNLCRKCSENC 744
Cdd:pfam14843 75 CTKCA--HFRDGPH--CVSSCPSGVLGEndliwkyaDANGVCQPCHPNC 119
|
|
| Peptidases_S8_PCSK9_ProteinaseK_like |
cd04077 |
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ... |
160-419 |
4.02e-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: 65.23 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 160 YTGKNIVVTILDDGIERTHPDLMQNydALASCDVNGNDldpmpryDASNENKHGTRCAGEVAAAannshcTVGIAFNAKI 239
Cdd:cd04077 22 STGSGVDVYVLDTGIRTTHVEFGGR--AIWGADFVGGD-------PDSDCNGHGTHVAGTVGGK------TYGVAKKANL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 240 GGVRMLD----GDVTDMVEAksvsFNpqhvhiYSASWGPDDDGKTV-----DGPAPltrQAFENGV-RMGRRGLgsVFVW 309
Cdd:cd04077 87 VAVKVLDcngsGTLSGIIAG----LE------WVANDATKRGKPAVanmslGGGAS---TALDAAVaAAVNAGV--VVVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 310 ASGNGGRskDHCscdGYT--NSIYTISISSTAESGKKPWYLE--ECSSTLAttysSGESYDKKIITTDlrqRCTDNHTGT 385
Cdd:cd04077 152 AAGNSNQ--DAC---NYSpaSAPEAITVGATDSDDARASFSNygSCVDIFA----PGVDILSAWIGSD---TATATLSGT 219
|
250 260 270
....*....|....*....|....*....|....
gi 299523015 386 SASAPMAAGIIALALEANPFLTWRDVQHVIVRTS 419
Cdd:cd04077 220 SMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLA 253
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1264-1549 |
9.11e-11 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 66.15 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1264 SKCPEGSYAEDGICERCSSPcrtcegNATNCHSCEGGHVLHH-GVCQENCPERHVAVKGVCKHCPEMCQDCIHEKtCKEC 1342
Cdd:pfam03302 15 TKCTSSAPCKTENCKACSND------KREVCEECNSNNYLTPtSQCIDDCAKIGNYYYTTNANNKKICKECTVAN-CKTC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1343 TpefflhDDMCHQSCPRGFYADSRHCVPCHKDCLECSGPKADDCELCLESSWVLYD-----GLCLEECPAGTYYEK---- 1413
Cdd:pfam03302 88 E------DQGQCQACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALRYGndgtkGTCGEGCTTGTGAGAcktc 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1414 -----ETKECRDCH----------------KSCLTCSSS----GTCTTCQKG-LIMNprGSCMANEKCsPSEYWDEDAPG 1467
Cdd:pfam03302 162 gltidGTSYCSECAteteypqngvctstaaRATATCKASsvanGMCSSCANGyFRMN--GGCYETTKF-PGKSVCEEANS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1468 CKPCHVKCFHCMGPAEDQCQTCPMNSLLLNTTCVKDCPEGYYADEDSnrCAHCHSSCRTCEGRhSRQCHSCRPGWFQLGK 1547
Cdd:pfam03302 239 GGTCQKEAPGYKLNNGDLVTCSPGCKTCTSNTVCTTCMDGYVKTSDS--CTKCDSSCETCTGA-TTTCKTCATGYYKSGT 315
|
..
gi 299523015 1548 EC 1549
Cdd:pfam03302 316 GC 317
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
681-1100 |
3.50e-10 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 64.22 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 681 ADKKRCRKCAP----NCESCFGSHGDQCMSCKYGYFLNEeTNSCVTHCpdgsyQDTKKNLCRKCSENCKTCTEFH--NCT 754
Cdd:pfam03302 12 ADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYLTP-TSQCIDDC-----AKIGNYYYTTNANNKKICKECTvaNCK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 755 ECRDGLSLQgsrcsvSCEDGRYFNGQDCQPCHRFCATCAGAGADGCINCTEGYFMEDGrcvqscsisyyfdhssENGYKS 834
Cdd:pfam03302 86 TCEDQGQCQ------ACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALRYG----------------NDGTKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 835 ckKCDISCLTCNGPGfkNCTSCPsgylLDLGMCQMGAICKDGEYVDEHGHCQTCEASCAKCqgptqedCTTCPMTrifdD 914
Cdd:pfam03302 144 --TCGEGCTTGTGAG--ACKTCG----LTIDGTSYCSECATETEYPQNGVCTSTAARATAT-------CKASSVA----N 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 915 GRCvSNCPSWKFEFENQCHpchhtcQRCQGSGPTHCTSCGADnygrehflyqGECGDSCPEghYATEGNTCLPCPDNCEL 994
Cdd:pfam03302 205 GMC-SSCANGYFRMNGGCY------ETTKFPGKSVCEEANSG----------GTCQKEAPG--YKLNNGDLVTCSPGCKT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 995 CHSVHVCTRCMKGYFiaptnhtcqklecgqgevqdPDYEECVPCEEGCLGCSlDDPGTCTSCAMGYYrfdhhcyktcpeK 1074
Cdd:pfam03302 266 CTSNTVCTTCMDGYV--------------------KTSDSCTKCDSSCETCT-GATTTCKTCATGYY------------K 312
|
410 420
....*....|....*....|....*.
gi 299523015 1075 TYSEEVECKACDSNCGSCDQNGCYWC 1100
Cdd:pfam03302 313 SGTGCVSCTSSESDNGITGVKGCLNC 338
|
|
| Peptidases_S8_5 |
cd07489 |
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ... |
158-421 |
5.80e-10 |
|
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173814 [Multi-domain] Cd Length: 312 Bit Score: 62.62 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 158 RGYTGKNIVVTILDDGIERTHPDL----MQNYDALASCDVNGNDLD----PMPRYDASNENKHGTRCAGEVAAAANNSHC 229
Cdd:cd07489 8 EGITGKGVKVAVVDTGIDYTHPALggcfGPGCKVAGGYDFVGDDYDgtnpPVPDDDPMDCQGHGTHVAGIIAANPNAYGF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 230 TvGIAFNAKIGGVRMLD--GDVTD--MVEAksvsFNPQH---VHIYSASWGpDDDGKTVDGPAPLTRQAFENGVRM---- 298
Cdd:cd07489 88 T-GVAPEATLGAYRVFGcsGSTTEdtIIAA----FLRAYedgADVITASLG-GPSGWSEDPWAVVASRIVDAGVVVtiaa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 299 ---GRRGLgsvfvWASGNGGRSKDHCSCdGYTNSIYTiSISSTAESGKKPWYLEECSSTLATTYSSGESYDkkIIttdlr 375
Cdd:cd07489 162 gndGERGP-----FYASSPASGRGVIAV-ASVDSYFS-SWGPTNELYLKPDVAAPGGNILSTYPLAGGGYA--VL----- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 299523015 376 qrctdnhTGTSASAPMAAGIIALALEA-NPFLTWRDVQHVIVRTSRA 421
Cdd:cd07489 228 -------SGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKP 267
|
|
| Peptidases_S8_10 |
cd07494 |
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ... |
150-428 |
1.47e-09 |
|
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173819 [Multi-domain] Cd Length: 298 Bit Score: 61.34 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 150 MNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALAScdvngndLDPMPRYDASNENKHGTrcaGEVAAaannshc 229
Cdd:cd07494 8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQVRVV-------LAPGATDPACDENGHGT---GESAN------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 230 TVGIAFNAKIGGVRMLDGDVTDMVEA--KSVSFNPQhvhIYSASWGPD--DDGKTVDGPAPLTRQAFE----NGVrmgRR 301
Cdd:cd07494 71 LFAIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSPD---IISNSWGYDlrSPGTSWSRSLPNALKALAatlqDAV---AR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 302 GLgsVFVWASGNGGRS-----KDHCSCDG-YTNSIYTISISSTAESGKKPWY-------------LEECSSTLATTYSSG 362
Cdd:cd07494 145 GI--VVVFSAGNGGWSfpaqhPEVIAAGGvFVDEDGARRASSYASGFRSKIYpgrqvpdvcglvgMLPHAAYLMLPVPPG 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299523015 363 ESYDKKIITTDLRQRCTDN---HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRA---GHLNAND 428
Cdd:cd07494 223 SQLDRSCAAFPDGTPPNDGwgvFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTARDvtkGASAQGT 294
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
842-1213 |
2.88e-09 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 61.14 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 842 CLTCNGPGFKNCTSCPSGYLLDLGMCQMGAICKDGEYvdehgHCQTCEASCAKCQGPTQEDCTTCpmtrifDDGRCVSNC 921
Cdd:pfam03302 28 CKACSNDKREVCEECNSNNYLTPTSQCIDDCAKIGNY-----YYTTNANNKKICKECTVANCKTC------EDQGQCQAC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 922 PSWKFEFENQCHPCHHTCQRCQGSGPTHCTSC---GADNYGREHflYQGECGDSCPEGHYATEGNTCLPCPDNCELCHSV 998
Cdd:pfam03302 97 NDGFYKSGDACSPCHESCKTCSGGTASDCTECltgKALRYGNDG--TKGTCGEGCTTGTGAGACKTCGLTIDGTSYCSEC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 999 HVCTRCMKGYFIAPTNHTCQKLeCGQGEVQDpdyeecvpceegclgcslddpGTCTSCAMGYYRFDHHCYKTC--PEKTY 1076
Cdd:pfam03302 175 ATETEYPQNGVCTSTAARATAT-CKASSVAN---------------------GMCSSCANGYFRMNGGCYETTkfPGKSV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1077 SEEveckacDSNCGSCdqngcywceegffllggscvRKCGPGFYGDQemGECESCHRACETCTGpgHDECSSCQEGLQLL 1156
Cdd:pfam03302 233 CEE------ANSGGTC--------------------QKEAPGYKLNN--GDLVTCSPGCKTCTS--NTVCTTCMDGYVKT 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 299523015 1157 RGMCVHatktqeegkfwndilrklqpCHSSCKTCNGSATLCTSCPKGAYLLAQACVS 1213
Cdd:pfam03302 283 SDSCTK--------------------CDSSCETCTGATTTCKTCATGYYKSGTGCVS 319
|
|
| Peptidases_S8_6 |
cd07490 |
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ... |
167-420 |
3.00e-09 |
|
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173815 [Multi-domain] Cd Length: 254 Bit Score: 59.87 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 167 VTILDDGIERTHPDLMQNYDALASCDVNGNDLDPmpryDASNENKHGTRCAGEVAAAANNSHcTVGIAFNAKiggvrMLD 246
Cdd:cd07490 4 VAVLDTGVDADHPDLAGRVAQWADFDENRRISAT----EVFDAGGHGTHVSGTIGGGGAKGV-YIGVAPEAD-----LLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 247 GDVTDMVEAksvsfnPQHVHIYSASWGPDDDGKTV-------DGPAPLTRQAFEngvrMGRRGLGSVFVWASGNGGRSKD 319
Cdd:cd07490 74 GKVLDDGGG------SLSQIIAGMEWAVEKDADVVsmslggtYYSEDPLEEAVE----ALSNQTGALFVVSAGNEGHGTS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 320 HCSCDGYTnsiyTISISSTAESGKKPWYlEECSSTLATTYSSGESYDKKIITTDL-----------RQRCTDNH----TG 384
Cdd:cd07490 144 GSPGSAYA----ALSVGAVDRDDEDAWF-SSFGSSGASLVSAPDSPPDEYTKPDVaapgvdvysarQGANGDGQytrlSG 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 299523015 385 TSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 420
Cdd:cd07490 219 TSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
|
|
| PTZ00262 |
PTZ00262 |
subtilisin-like protease; Provisional |
167-411 |
6.27e-09 |
|
subtilisin-like protease; Provisional
Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 60.75 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 167 VTILDDGIERTHPDLMQNY---------------------DALASCDVNGNDLDPMprydasNENKHGTRCAGEVAAAAN 225
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM------DDNYHGTHVSGIISAIGN 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 226 NSHCTVGIAFNAKIGGVRMLD----GDVTDMVeaKSVSF-NPQHVHIYSASWGPDDDGKTvdgpapltrqaFENGVRMGR 300
Cdd:PTZ00262 394 NNIGIVGVDKRSKLIICKALDshklGRLGDMF--KCFDYcISREAHMINGSFSFDEYSGI-----------FNESVKYLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 301 RgLGSVFVWASGN----GGRSKDHCSCDGYTNSIYTISISSTAES---------GKKPWYLEECSSTLATTYSSGESYDK 367
Cdd:PTZ00262 461 E-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYPPILSKKLRNvitvsnlikDKNNQYSLSPNSFYSAKYCQLAAPGT 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 299523015 368 KIITTDLRQRCTDNhTGTSASAPMAAGIIALALEANPFLTWRDV 411
Cdd:PTZ00262 540 NIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1470-1518 |
1.90e-08 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 52.14 E-value: 1.90e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 299523015 1470 PCHVKCFHCMGPAEDQCQTCPMNSLLLNTTCVKDCPEGYYADEDSNRCA 1518
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| Peptidases_S8_12 |
cd07480 |
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ... |
160-313 |
2.23e-08 |
|
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173806 [Multi-domain] Cd Length: 297 Bit Score: 57.77 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 160 YTGKNIVVTILDDGIERTHPDLMqnydalascDVNGNDLDPMPRYDASNENKHGTRCAGEVAAAANNSHcTVGIAFNAKI 239
Cdd:cd07480 5 FTGAGVRVAVLDTGIDLTHPAFA---------GRDITTKSFVGGEDVQDGHGHGTHCAGTIFGRDVPGP-RYGVARGAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 240 --GGVRMLDGDVTDMVEAKSVSFNPQH-VHIYSASWGPDDDGKTVDG--PAPLTRQAFE----------NGVRMGRR--- 301
Cdd:cd07480 75 alIGKVLGDGGGGDGGILAGIQWAVANgADVISMSLGADFPGLVDQGwpPGLAFSRALEayrqrarlfdALMTLVAAqaa 154
|
170
....*....|...
gi 299523015 302 -GLGSVFVWASGN 313
Cdd:cd07480 155 lARGTLIVAAAGN 167
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
773-1057 |
5.19e-07 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 54.92 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 773 DGRYFNGQDCQPCHRFCATCA-GAGADGCINCTEGYFMEDGR-CVQSCS-----ISYYFDHSSE---------------N 830
Cdd:PTZ00214 348 GDGYLCGDATNGGVSGCATCGyNSGAVTCTRCSAGYLGVDGKsCSESCSgdtrgVCTKVAEGSEstevscrcvckptfyN 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 831 GYKSCKKCDISCLTCNGPGFKNCTSCPSGYLLDLGM-----------CQMGAICKD-GEYVDEHGHCQTCEASC------ 892
Cdd:PTZ00214 428 SSGTCTPCTDSCAVCKDGTPTGCQQCSPGKILEFSIvssesadcvdqCSVGSECAEcGITIDGSRYCTRCKDAStypfng 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 893 ---------AKCQGPTQEDCTTC-----------------PMTRIFD---DGRCVSNCPSWKFEFENQCHPCHHTCQRCQ 943
Cdd:PTZ00214 508 vcipntqrdAYCTSTANGACTTCsgaaflmnggcyttehyPGSTICDkqsNGKCTTTKKGYGISPDGKLLECDPTCLACT 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 944 GSGPTHCTSCGADN-YGREHFLYQGECGD--SCPEGHYAtEGNTCLPCPD-NCELCHSVHVCTRCMKGYFIAPTNHTC-- 1017
Cdd:PTZ00214 588 APGPGRCTRCPSDKlLKRASGAATGSCVDpgACVDGYYA-DGDACLPCATpGCKTCGHASFCTECAGELFVSLDGQSCle 666
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 299523015 1018 ---------------QKLECGQGEVQDPDYEECVP---CEEGCLGC-SLDDPGTCTSCA 1057
Cdd:PTZ00214 667 ectgdkvvgevsggvRRCWCERGFLPALDRSGCVLpteCPPDMPSCaACDESGRCLLCV 725
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1520-1567 |
6.61e-07 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 47.51 E-value: 6.61e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 299523015 1520 CHSSCRTCEGRHSRQCHSCRPGWFQLGKECLLQCREGYYADNSTGRCE 1567
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
782-823 |
7.33e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 47.50 E-value: 7.33e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 299523015 782 CQPCHRFCATCAGAGADGCINCTEGYFMEDGRCVQSCSISYY 823
Cdd:smart00261 4 CKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
1569-1686 |
1.71e-06 |
|
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: 48.91 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1569 CNRSCK--GCQGPRPTDCLSCDRFFFllrsKGECHRSCPDHYYVEQSTQ---TCERCHPTCDQ------CKGKGALNCLS 1637
Cdd:pfam14843 2 CDPLCSseGCWGPGPDQCLSCRNFSR----GGTCVESCNILQGEPREYVvnsTCVPCHPECLPqngtatCSGPGADNCTK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1638 CVwsyHLMGGI-CTSDC---------LVGEYRVGEGEkfnCEKCHESCME-CKGPGAKNC 1686
Cdd:pfam14843 78 CA---HFRDGPhCVSSCpsgvlgendLIWKYADANGV---CQPCHPNCTQgCTGPGLTGC 131
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
895-993 |
2.58e-06 |
|
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: 48.52 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 895 CQGPTQEDCTTCpmtRIFDDGR-CVSNCPSWK-----FEFENQCHPCHHTCQR------CQGSGPTHCTSCgadnygrEH 962
Cdd:pfam14843 11 CWGPGPDQCLSC---RNFSRGGtCVESCNILQgepreYVVNSTCVPCHPECLPqngtatCSGPGADNCTKC-------AH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 299523015 963 FLYQGECGDSCPEG---------HYATEGNTCLPCPDNCE 993
Cdd:pfam14843 81 FRDGPHCVSSCPSGvlgendliwKYADANGVCQPCHPNCT 120
|
|
| FU |
smart00261 |
Furin-like repeats; |
1514-1558 |
2.81e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 45.96 E-value: 2.81e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 299523015 1514 SNRCAHCHSSCRTCEGRHSRQCHSCRPGWFQLGKECLLQCREGYY 1558
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1187-1502 |
3.24e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 51.51 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1187 CKTC-NGSATLCTSCPKGAYLL-AQACVSSCPQgtWPSVRSGSCENCTEACAICSGADlCKKCQMQPghplflhegrCYS 1264
Cdd:pfam03302 28 CKACsNDKREVCEECNSNNYLTpTSQCIDDCAK--IGNYYYTTNANNKKICKECTVAN-CKTCEDQG----------QCQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1265 KCPEGSYAEDGICERCSSPCRTCE-GNATNCHSCEGGHVLHHG------VCQENCPERHVAvkGVCKHC------PEMCQ 1331
Cdd:pfam03302 95 ACNDGFYKSGDACSPCHESCKTCSgGTASDCTECLTGKALRYGndgtkgTCGEGCTTGTGA--GACKTCgltidgTSYCS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1332 DCIHEKTCKE---CTPEfflhDDMCHQSCPRGFYADSRhCVPCHKDCLECSGPkaddcelCLESSWVLYDGLCLEECPAG 1408
Cdd:pfam03302 173 ECATETEYPQngvCTST----AARATATCKASSVANGM-CSSCANGYFRMNGG-------CYETTKFPGKSVCEEANSGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1409 TY------YEKETKECRDCHKSCLTCSSSGTCTTCQKGLImnprgscmanekcspseywdEDAPGCKPCHVKCFHCMGPA 1482
Cdd:pfam03302 241 TCqkeapgYKLNNGDLVTCSPGCKTCTSNTVCTTCMDGYV--------------------KTSDSCTKCDSSCETCTGAT 300
|
330 340
....*....|....*....|
gi 299523015 1483 EdQCQTCPMNSLLLNTTCVK 1502
Cdd:pfam03302 301 T-TCKTCATGYYKSGTGCVS 319
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
784-825 |
3.68e-06 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 45.59 E-value: 3.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 299523015 784 PCHRFCATCAGAGADGCINCTEGYFMEDGRCVQSCSISYYFD 825
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1370-1419 |
6.01e-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: 44.82 E-value: 6.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 299523015 1370 PCHKDCLECSGPKADDCELClESSWVLYDGLCLEECPAGTYYEKETKECR 1419
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSC-RHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1182-1229 |
6.69e-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: 44.82 E-value: 6.69e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 299523015 1182 PCHSSCKTCNGS-ATLCTSCPKGAYLLAQACVSSCPQGTWPSVRSGSCE 1229
Cdd:cd00064 1 PCHPSCATCTGPgPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| Peptidases_S8_11 |
cd04843 |
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ... |
150-400 |
6.87e-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: 50.00 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 150 MNIEGAWKR-GYTGKNIVVTILDDGIERTHPDLMQNydaLAScdvngndldPMPRYDASNENKHGTRCAGEVAAAANNSH 228
Cdd:cd04843 2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGN---GIT---------LISGLTDQADSDHGTAVLGIIVAKDNGIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 229 CTvGIAFNAKIG--GVRMLDGDVTDMVEAKSVsFNPQHVHIYSASWGPDDDGKTvdgPAPL---------TRQAFENGVr 297
Cdd:cd04843 70 VT-GIAHGAQAAvvSSTRVSNTADAILDAADY-LSPGDVILLEMQTGGPNNGYP---PLPVeyeqanfdaIRTATDLGI- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 298 mgrrglgsVFVWASGNGGRSKDHCS-CDGYTNSIYTISIS---------STAESGKKPWyleeCSSTLAT---TYSSGE- 363
Cdd:cd04843 144 --------IVVEAAGNGGQDLDAPVyNRGPILNRFSPDFRdsgaimvgaGSSTTGHTRL----AFSNYGSrvdVYGWGEn 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 299523015 364 ----SYDKKIITTDLRQRCTDNHTGTSASAPMAAGiiALAL 400
Cdd:cd04843 212 vtttGYGDLQDLGGENQDYTDSFSGTSSASPIVAG--AAAS 250
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
688-738 |
7.24e-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: 44.82 E-value: 7.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 299523015 688 KCAPNCESCFGSHGDQCMSCKYGYFLNEetNSCVTHCPDGSYQDTKKNLCR 738
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDG--GTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
1468-1509 |
8.28e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.42 E-value: 8.28e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 299523015 1468 CKPCHVKCFHCMGPAEDQCQTCPMNSLLLNTTCVKDCPEGYY 1509
Cdd:smart00261 4 CKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
670-897 |
8.44e-06 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 51.07 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 670 CVSSCPPGHYHADKKrCRKCAPNCESCFGSHGDQCMSCKYGYFLN-----EETNSCVTHCPDGSyqdtkknlcrkcsenc 744
Cdd:PTZ00214 417 CRCVCKPTFYNSSGT-CTPCTDSCAVCKDGTPTGCQQCSPGKILEfsivsSESADCVDQCSVGS---------------- 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 745 ktctefhNCTECrdGLSLQGSRCSVSCEDGRY--FNGQdCQPCHRFCATCAGAGADGCINCTEGYFMEDGRCVQSCSI-- 820
Cdd:PTZ00214 480 -------ECAEC--GITIDGSRYCTRCKDASTypFNGV-CIPNTQRDAYCTSTANGACTTCSGAAFLMNGGCYTTEHYpg 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 821 SYYFDHSSENGYKSCKK------------CDISCLTCNGPGFKNCTSCPSGYLLD------LGMCQMGAICKDGEYVDEH 882
Cdd:PTZ00214 550 STICDKQSNGKCTTTKKgygispdgklleCDPTCLACTAPGPGRCTRCPSDKLLKrasgaaTGSCVDPGACVDGYYADGD 629
|
250 260
....*....|....*....|....
gi 299523015 883 G-------HCQTC--EASCAKCQG 897
Cdd:PTZ00214 630 AclpcatpGCKTCghASFCTECAG 653
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
784-903 |
8.61e-06 |
|
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).
Pssm-ID: 464344 [Multi-domain] Cd Length: 132 Bit Score: 46.98 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 784 PCHRFC--ATCAGAGADGCINCTegYFMEDGRCVQSCSISYYFDHSSENGyKSCKKCDISCL------TCNGPGFKNCT- 854
Cdd:pfam14843 1 VCDPLCssEGCWGPGPDQCLSCR--NFSRGGTCVESCNILQGEPREYVVN-STCVPCHPECLpqngtaTCSGPGADNCTk 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299523015 855 ------------SCPSGYlldlgmcqMGAICKDGEYVDEHGHCQTCEASCAK-CQGPTQEDC 903
Cdd:pfam14843 78 cahfrdgphcvsSCPSGV--------LGENDLIWKYADANGVCQPCHPNCTQgCTGPGLTGC 131
|
|
| Peptidases_S8_Lantibiotic_specific_protease |
cd07482 |
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ... |
164-407 |
1.05e-05 |
|
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173808 [Multi-domain] Cd Length: 294 Bit Score: 49.29 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 164 NIVVTILDDGIERTHPDLMQNYdalascDVNGNDLDPMPRYDASNE------------NKHGTRCAGEVAAAANNShctv 231
Cdd:cd07482 1 KVTVAVIDSGIDPDHPDLKNSI------SSYSKNLVPKGGYDGKEAgetgdindivdkLGHGTAVAGQIAANGNIK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 232 GIAFNAKIGGVRMLD----GDVTDMVEAKSVSFNpQHVHIYSASWGPDDDGKTVDGPAPLTRQAFENGVRMGRRGlGSVF 307
Cdd:cd07482 71 GVAPGIGIVSYRVFGscgsAESSWIIKAIIDAAD-DGVDVINLSLGGYLIIGGEYEDDDVEYNAYKKAINYAKSK-GSIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 308 VWASGNGGRS-------KDHCSCDGY--TNSIY---------TISISSTAESGkkpwYLEECSS------TLAT---TYS 360
Cdd:cd07482 149 VAAAGNDGLDvsnkqelLDFLSSGDDfsVNGEVydvpaslpnVITVSATDNNG----NLSSFSNygnsriDLAApggDFL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 299523015 361 SGESYDK------------KIITTDLRQrCTDNHTGTSASAPMAAGIIALALEANPFLT 407
Cdd:cd07482 225 LLDQYGKekwvnnglmtkeQILTTAPEG-GYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
|
|
| FU |
smart00261 |
Furin-like repeats; |
1563-1609 |
1.37e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.04 E-value: 1.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 299523015 1563 TGRCERCNRSCKGCQGPRPTDCLSCDRFFFLLrsKGECHRSCPDHYY 1609
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPGTY 45
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
669-727 |
1.47e-05 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 45.50 E-value: 1.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299523015 669 ICVSSCPPGHY---HADKKRCRKC-APNCESCFGShgDQCMSCKYGYFLNEetNSCVTHCPDG 727
Cdd:pfam15913 34 VCLHSCPPGYFgirGQEVNRCTKCkAENCESCFSK--DFCTKCKEGFYLHK--GKCLDTCPEG 92
|
|
| Peptidases_S8_8 |
cd07492 |
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ... |
167-420 |
1.53e-05 |
|
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173817 [Multi-domain] Cd Length: 222 Bit Score: 48.10 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 167 VTILDDGIERTHPDLmqnyDALASCDVNGNDLDPMPRYD-ASNENKHGTRCAGEVAAAANnshctvgiafNAKIGGVRML 245
Cdd:cd07492 4 VAVIDSGVDTDHPDL----GNLALDGEVTIDLEIIVVSAeGGDKDGHGTACAGIIKKYAP----------EAEIGSIKIL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 246 DGDVTDMVE--AKSVSF-NPQHVHIYSASWgpdddGKTVDGPAPLTRQAFENGVRMGRrglgsVFVWASGNGGRskdhcs 322
Cdd:cd07492 70 GEDGRCNSFvlEKALRAcVENDIRIVNLSL-----GGPGDRDFPLLKELLEYAYKAGG-----IIVAAAPNNND------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 323 cDGYTNSIYTISI---SSTAESGKKPWYLEECSSTlattyssgesyDKKIITTDLRQRCTDNHTGTSASAPMAAGIIALA 399
Cdd:cd07492 134 -IGTPPASFPNVIgvkSDTADDPKSFWYIYVEFSA-----------DGVDIIAPAPHGRYLTVSGNSFAAPHVTGMVALL 201
|
250 260
....*....|....*....|.
gi 299523015 400 LEANPFLTWRDVQHVIVRTSR 420
Cdd:cd07492 202 LSEKPDIDANDLKRLLQRLAV 222
|
|
| Peptidases_S53_like |
cd05562 |
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ... |
381-453 |
1.91e-05 |
|
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.
Pssm-ID: 173798 [Multi-domain] Cd Length: 275 Bit Score: 48.44 E-value: 1.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299523015 381 NHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIvrTSRAGHLNANDWktnaagfkvSHLYGFGLMDAEAMV 453
Cdd:cd05562 212 NFFGTSAAAPHAAGVAALVLSANPGLTPADIRDAL--RSTALDMGEPGY---------DNASGSGLVDADRAV 273
|
|
| FU |
smart00261 |
Furin-like repeats; |
1181-1220 |
1.98e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 43.27 E-value: 1.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 299523015 1181 QPCHSSCKTCNGS-ATLCTSCPKGAYLLAQACVSSCPQGTW 1220
Cdd:smart00261 5 KPCHPECATCTGPgPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
1477-1585 |
2.23e-05 |
|
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).
Pssm-ID: 464344 [Multi-domain] Cd Length: 132 Bit Score: 45.83 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1477 HCMGPAEDQCQTCpmNSLLLNTTCVKDCPEGYYAD---EDSNRCAHCHSSC------RTCEGRHSRQCHSCRPgwFQLGK 1547
Cdd:pfam14843 10 GCWGPGPDQCLSC--RNFSRGGTCVESCNILQGEPreyVVNSTCVPCHPEClpqngtATCSGPGADNCTKCAH--FRDGP 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 299523015 1548 ECLLQCREGYYADNST--------GRCERCNRSCK-GCQGPRPTDCL 1585
Cdd:pfam14843 86 HCVSSCPSGVLGENDLiwkyadanGVCQPCHPNCTqGCTGPGLTGCP 132
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1569-1618 |
2.60e-05 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 43.28 E-value: 2.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 299523015 1569 CNRSCKGCQGPRPTDCLSCDRFFFLLrsKGECHRSCPDHYYVEQSTQTCE 1618
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLD--GGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
683-729 |
3.40e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 42.88 E-value: 3.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 299523015 683 KKRCRKCAPNCESCFGSHGDQCMSCKYGYFLNEETnsCVTHCPDGSY 729
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGK--CVSECPPGTY 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1040-1301 |
3.57e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 48.43 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1040 EGCLGCSLDDPGTCTSCAMGYYRFD-HHCYKTCPEKTYSEEVECKACDSNCGSCDQNGCYWCEEgffllgGSCVRKCGPG 1118
Cdd:pfam03302 26 ENCKACSNDKREVCEECNSNNYLTPtSQCIDDCAKIGNYYYTTNANNKKICKECTVANCKTCED------QGQCQACNDG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1119 FYGDQEmgECESCHRACETCTGPGHDECSSCQEGLQLLRGmcVHATKTQEEGKFWNdilrklQPCHSSCKTCN---GSAT 1195
Cdd:pfam03302 100 FYKSGD--ACSPCHESCKTCSGGTASDCTECLTGKALRYG--NDGTKGTCGEGCTT------GTGAGACKTCGltiDGTS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1196 LCTSCP-KGAYLLAQACVSSCPQGT----WPSVRSGSCENCTEAC----------------AICSGADLCKKCQMQ-PGH 1253
Cdd:pfam03302 170 YCSECAtETEYPQNGVCTSTAARATatckASSVANGMCSSCANGYfrmnggcyettkfpgkSVCEEANSGGTCQKEaPGY 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 299523015 1254 PLFLHEGRCYSK-------------CPEGSYAEDGICERCSSPCRTCEGNATNCHSCEGGH 1301
Cdd:pfam03302 250 KLNNGDLVTCSPgcktctsntvcttCMDGYVKTSDSCTKCDSSCETCTGATTTCKTCATGY 310
|
|
| Furin-like |
pfam00757 |
Furin-like cysteine rich region; |
636-744 |
3.91e-05 |
|
Furin-like cysteine rich region;
Pssm-ID: 395614 [Multi-domain] Cd Length: 143 Bit Score: 45.50 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 636 CDPECSEvGCDGPGPDHCNDCLHYYYklknnTRICVSSCPPGHYHADkkrcRKCApNCESCFGSHGDQCmsckygYFLNE 715
Cdd:pfam00757 49 CHEQCLG-GCTGPNDSDCLACRHFND-----EGTCVDQCPPGTYQFG----WRCV-TFKECPKSHLPGY------NPLVI 111
|
90 100 110
....*....|....*....|....*....|
gi 299523015 716 ETNSCVTHCPDGSYQDTKKNL-CRKCSENC 744
Cdd:pfam00757 112 HNGECVRECPSGYTEVENNSRkCEPCEGLC 141
|
|
| FU |
smart00261 |
Furin-like repeats; |
1614-1658 |
4.62e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 42.50 E-value: 4.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 299523015 1614 TQTCERCHPTCDQCKGKGALNCLSCVWSYHLMGGICTSDCLVGEY 1658
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1365-1410 |
5.51e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 42.11 E-value: 5.51e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 299523015 1365 SRHCVPCHKDCLECSGPKADDCELClESSWVLYDGLCLEECPAGTY 1410
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSC-KHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
833-867 |
5.73e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 42.11 E-value: 5.73e-05
10 20 30
....*....|....*....|....*....|....*
gi 299523015 833 KSCKKCDISCLTCNGPGFKNCTSCPSGYLLDLGMC 867
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKC 36
|
|
| FU |
smart00261 |
Furin-like repeats; |
883-926 |
6.32e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 42.11 E-value: 6.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 299523015 883 GHCQTCEASCAKCQGPTQEDCTTCPMTRIFDDGRCVSNCPSWKF 926
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
934-983 |
1.35e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 41.35 E-value: 1.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 299523015 934 PCHHTCQRCQGSGPTHCTSCGADNYgrehfLYQGECGDSCPEGHYATEGN 983
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFY-----LDGGTCVSECPEGTYADTEG 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
929-978 |
1.42e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 40.96 E-value: 1.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 299523015 929 ENQCHPCHHTCQRCQGSGPTHCTSCGADnygreHFLYQGECGDSCPEGHY 978
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHG-----FFLDGGKCVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1126-1162 |
1.56e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 40.96 E-value: 1.56e-04
10 20 30
....*....|....*....|....*....|....*..
gi 299523015 1126 GECESCHRACETCTGPGHDECSSCQEGLQLLRGMCVH 1162
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVS 38
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
635-685 |
1.73e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 40.97 E-value: 1.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 299523015 635 PCDPECSevGCDGPGPDHCNDCLHYYYklkNNTRICVSSCPPGHYHADKKR 685
Cdd:cd00064 1 PCHPSCA--TCTGPGPDQCTSCRHGFY---LDGGTCVSECPEGTYADTEGG 46
|
|
| FU |
smart00261 |
Furin-like repeats; |
1034-1076 |
2.23e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 40.57 E-value: 2.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 299523015 1034 ECVPCEEGCLGCSLDDPGTCTSCAMGYYRFDHHCYKTCPEKTY 1076
Cdd:smart00261 3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1084-1129 |
2.77e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 40.19 E-value: 2.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 299523015 1084 ACDSNCGSC---DQNGCYWCEEGFFLLGGSCVRKCGPGFYGDQEMGECE 1129
Cdd:cd00064 1 PCHPSCATCtgpGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
635-679 |
3.02e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 40.19 E-value: 3.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 299523015 635 PCDPECSevGCDGPGPDHCNDCLHYYYKLKNntrICVSSCPPGHY 679
Cdd:smart00261 6 PCHPECA--TCTGPGPDDCTSCKHGFFLDGG---KCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
837-886 |
3.31e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 40.19 E-value: 3.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 299523015 837 KCDISCLTCNGPGFKNCTSCPSGYLLDLGMCQmgAICKDGEY-VDEHGHCQ 886
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCV--SECPEGTYaDTEGGVCL 49
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
1353-1643 |
3.64e-04 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 45.68 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1353 CHQSCPRGFYADSRHCVPCHKDCLECSGPKADDCELC-----LESSWVLYDGL-CLEECPAGTYYEK------ETKECRD 1420
Cdd:PTZ00214 417 CRCVCKPTFYNSSGTCTPCTDSCAVCKDGTPTGCQQCspgkiLEFSIVSSESAdCVDQCSVGSECAEcgitidGSRYCTR 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1421 CHKSCL-----------------TCSSSGTCTTCQK-GLIMNprGSC--------------MANEKCSPSE--YWDEDAP 1466
Cdd:PTZ00214 497 CKDASTypfngvcipntqrdaycTSTANGACTTCSGaAFLMN--GGCyttehypgsticdkQSNGKCTTTKkgYGISPDG 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1467 GCKPCHVKCFHCMGPAEDQCQTCPMNSLLLNTT------CVKD--CPEGYYADEDSnrCAHCHS-SCRTCEgrHSRQCHS 1537
Cdd:PTZ00214 575 KLLECDPTCLACTAPGPGRCTRCPSDKLLKRASgaatgsCVDPgaCVDGYYADGDA--CLPCATpGCKTCG--HASFCTE 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1538 CRPGWFQL--GKECLLQCREGYYADNSTGRCERCnrsckgcqgprptdclSCDRFFFLLRSKGEChrscpdhyyveQSTQ 1615
Cdd:PTZ00214 651 CAGELFVSldGQSCLEECTGDKVVGEVSGGVRRC----------------WCERGFLPALDRSGC-----------VLPT 703
|
330 340
....*....|....*....|....*...
gi 299523015 1616 TCERCHPTCDQCKGKGalNCLSCVWSYH 1643
Cdd:PTZ00214 704 ECPPDMPSCAACDESG--RCLLCVTSGH 729
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1037-1079 |
4.19e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 39.81 E-value: 4.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 299523015 1037 PCEEGCLGCSLDDPGTCTSCAMGYYRFDHHCYKTCPEKTYSEE 1079
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADT 43
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
888-930 |
7.28e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 39.04 E-value: 7.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 299523015 888 CEASCAKCQGPTQEDCTTCPMTRIFDDGRCVSNCPSWKFEFEN 930
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTE 44
|
|
| Furin-like |
pfam00757 |
Furin-like cysteine rich region; |
845-992 |
8.02e-04 |
|
Furin-like cysteine rich region;
Pssm-ID: 395614 [Multi-domain] Cd Length: 143 Bit Score: 41.65 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 845 CNGPGFKNCTSCPSGYLLDLGMCQMGAICKDGEYVDEHGHCqtCEASCA-KCQGPTQEDCTTCpmTRIFDDGRCVSNCPS 923
Cdd:pfam00757 8 CPGTMEKCHSCCNNGYCWGPGHCQKVCPEQCKKRCTKPGEC--CHEQCLgGCTGPNDSDCLAC--RHFNDEGTCVDQCPP 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 299523015 924 WKFEFENQChpchHTCQRCQGSGPTHCTscgadnygrEHFLYQGECGDSCPEGHYATEGNT--CLPCPDNC 992
Cdd:pfam00757 84 GTYQFGWRC----VTFKECPKSHLPGYN---------PLVIHNGECVRECPSGYTEVENNSrkCEPCEGLC 141
|
|
| FU |
smart00261 |
Furin-like repeats; |
1081-1120 |
1.21e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 38.26 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 299523015 1081 ECKACDSNCGSC---DQNGCYWCEEGFFLLGGSCVRKCGPGFY 1120
Cdd:smart00261 3 ECKPCHPECATCtgpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1131-1162 |
1.44e-03 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 38.27 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|..
gi 299523015 1131 CHRACETCTGPGHDECSSCQEGLQLLRGMCVH 1162
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVS 33
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
1500-1566 |
1.67e-03 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 39.72 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1500 CVKDCPEGYYA--DEDSNRCAHCHSScrTCEGRHSRQ-CHSCRPGWFQLGKECLLQCREGYYADNSTGRC 1566
Cdd:pfam15913 35 CLHSCPPGYFGirGQEVNRCTKCKAE--NCESCFSKDfCTKCKEGFYLHKGKCLDTCPEGTAAQNSTMEC 102
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
1185-1278 |
1.74e-03 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 39.72 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1185 SSCKTCNGSATLCTSCPKGAYLLAQ-------ACVSSCPQGTWpSVRSGSCENCT----EACAICSGADLCKKCQMQpgh 1253
Cdd:pfam15913 2 SGCVLCSEENGCLTCQPRLFLLLERngirqygVCLHSCPPGYF-GIRGQEVNRCTkckaENCESCFSKDFCTKCKEG--- 77
|
90 100
....*....|....*....|....*
gi 299523015 1254 pLFLHEGRCYSKCPEGSYAEDGICE 1278
Cdd:pfam15913 78 -FYLHKGKCLDTCPEGTAAQNSTME 101
|
|
| FU |
smart00261 |
Furin-like repeats; |
1274-1314 |
1.81e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 37.87 E-value: 1.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 299523015 1274 DGICERCSSPCRTCEG-NATNCHSCEGGHVLHHGVCQENCPE 1314
Cdd:smart00261 1 DGECKPCHPECATCTGpGPDDCTSCKHGFFLDGGKCVSECPP 42
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
1620-1729 |
1.91e-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: 40.44 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1620 CHPTC--DQCKGKGALNCLSCvwSYHLMGGICTSDC--LVGEYRVGEGEKfNCEKCHESCME------CKGPGAKNCTLC 1689
Cdd:pfam14843 2 CDPLCssEGCWGPGPDQCLSC--RNFSRGGTCVESCniLQGEPREYVVNS-TCVPCHPECLPqngtatCSGPGADNCTKC 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 299523015 1690 panlVLHMDDSHCLHCCNTSDPPSAQECCDCQDTTDECIL 1729
Cdd:pfam14843 79 ----AHFRDGPHCVSSCPSGVLGENDLIWKYADANGVCQP 114
|
|
| Peptidases_S8_14 |
cd07497 |
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ... |
162-402 |
2.33e-03 |
|
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173821 [Multi-domain] Cd Length: 311 Bit Score: 42.07 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 162 GKNIVVTILDDGIERTHPDLMQ--NYDALASCDVNGN---DLDPMPRYDA--SNENKHGTRCAgEVAAAANNSHCT---- 230
Cdd:cd07497 1 GEGVVIAIVDTGVDYSHPDLDIygNFSWKLKFDYKAYllpGMDKWGGFYVimYDFFSHGTSCA-SVAAGRGKMEYNlygy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 231 ------VGIAFNAKIGGVRMLDGDVTDMVEAKSVSFNPQH------------VHIYSASWGPDDDGKTVDGPAPLTRQAF 292
Cdd:cd07497 80 tgkfliRGIAPDAKIAAVKALWFGDVIYAWLWTAGFDPVDrklswiytggprVDVISNSWGISNFAYTGYAPGLDISSLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 293 ENGVRMGRrglGSVFVWASGNGGRSKDHCSCDGytNSIYTISISSTAESGKKPWYLeecssTLATTYSSGEsydkkIITT 372
Cdd:cd07497 160 IDALVTYT---GVPIVSAAGNGGPGYGTITAPG--AASLAISVGAATNFDYRPFYL-----FGYLPGGSGD-----VVSW 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 299523015 373 DLR----------------------QRCTDNHT------------GTSASAPMAAGIIALALEA 402
Cdd:cd07497 225 SSRgpsiagdpkpdlaaigafawapGRVLDSGGaldgneafdlfgGTSMATPMTAGSAALVISA 288
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
1307-1425 |
2.45e-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: 40.05 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1307 VCQENCPERHVAVKGvckhcPEMCQDCIHEKTCKECTpefflhdDMCH--QSCPRGFYADSRhCVPCHKDCLE------C 1378
Cdd:pfam14843 1 VCDPLCSSEGCWGPG-----PDQCLSCRNFSRGGTCV-------ESCNilQGEPREYVVNST-CVPCHPECLPqngtatC 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 299523015 1379 SGPKADDCELCLEsswvLYDGL-CLEECPAGTYYEK--------ETKECRDCHKSC 1425
Cdd:pfam14843 68 SGPGADNCTKCAH----FRDGPhCVSSCPSGVLGENdliwkyadANGVCQPCHPNC 119
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1620-1663 |
2.64e-03 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 37.50 E-value: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 299523015 1620 CHPTCDQCKGKGALNCLSCVWSYHLMGGICTSDCLVGEYRVGEG 1663
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEG 45
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
1087-1160 |
2.77e-03 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 38.95 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1087 SNCGSC-DQNGCYWCEEGFFLL--------GGSCVRKCGPGFYG--DQEMGECESCH-RACETCTGpgHDECSSCQEGLQ 1154
Cdd:pfam15913 2 SGCVLCsEENGCLTCQPRLFLLlerngirqYGVCLHSCPPGYFGirGQEVNRCTKCKaENCESCFS--KDFCTKCKEGFY 79
|
....*.
gi 299523015 1155 LLRGMC 1160
Cdd:pfam15913 80 LHKGKC 85
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
693-774 |
2.85e-03 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 38.95 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 693 CESCFGSHGdqCMSCKYGYFLNEETN------SCVTHCPDGSY--QDTKKNLCRKC-SENCKTCTEFHNCTECRDGLSLQ 763
Cdd:pfam15913 4 CVLCSEENG--CLTCQPRLFLLLERNgirqygVCLHSCPPGYFgiRGQEVNRCTKCkAENCESCFSKDFCTKCKEGFYLH 81
|
90
....*....|.
gi 299523015 764 GSRCSVSCEDG 774
Cdd:pfam15913 82 KGKCLDTCPEG 92
|
|
| FU |
smart00261 |
Furin-like repeats; |
734-776 |
5.57e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 36.33 E-value: 5.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 299523015 734 KNLCRKCSENCKTCT--EFHNCTECRDGLSLQGSRCSVSCEDGRY 776
Cdd:smart00261 1 DGECKPCHPECATCTgpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1668-1709 |
5.74e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 36.33 E-value: 5.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 299523015 1668 CEKCHESCMECKGPGAKNCTLCPANLVLHmdDSHCLHCCNTS 1709
Cdd:smart00261 4 CKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPG 43
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1562-1695 |
8.84e-03 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 40.72 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299523015 1562 STGRCERCNrsCKGCQGPRPTDCLSCDRFFFLLRSKgECHRSC---PDHYYveqstQTCERCHPTCDQCKgkgALNCLSC 1638
Cdd:pfam03302 19 SSAPCKTEN--CKACSNDKREVCEECNSNNYLTPTS-QCIDDCakiGNYYY-----TTNANNKKICKECT---VANCKTC 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 299523015 1639 VwsyhlmGGICTSDCLVGEYRVGEgekfNCEKCHESCMECKGPGAKNCTLCPANLVL 1695
Cdd:pfam03302 88 E------DQGQCQACNDGFYKSGD----ACSPCHESCKTCSGGTASDCTECLTGKAL 134
|
|
| |
