|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidases_S8_Protein_convertases_Kexins_Furin-lik |
cd04059 |
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ... |
128-422 |
7.04e-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: 498.62 E-value: 7.04e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 128 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 206
Cdd:cd04059 1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 207 DasNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGP 286
Cdd:cd04059 81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 287 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 365
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958641647 366 SYDKKIITTDLR--QRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd04059 239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
|
|
| Peptidase_S8 |
pfam00082 |
Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
164-447 |
9.65e-66 |
|
Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
Pssm-ID: 395035 [Multi-domain] Cd Length: 287 Bit Score: 225.03 E-value: 9.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNG----NDLDPMPRYDASNENKHGTRCAGEVAATANNSHCTVGIAFNA 239
Cdd:pfam00082 1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEAsvdfNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 240 KIGGVRML-DGDVTDMVEAKSVSYN-PQHVHIYSASWGPDddgKTVDGPAPLTRQAFENGvrmGRRGLGSVFVWASGNGG 317
Cdd:pfam00082 81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 318 RSKDHCSCDGY-TNSIYTISISSTaesgkkpwylEECSSTLATTYSS----------------GESY-------DKKIIT 373
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAV----------DEASEGNLASFSSygptldgrlkpdivapGGNItggnissTLLTTT 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641647 374 TDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNAndwktnaagfkVSHLYGFG 447
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAG-----------LDRLFGYG 287
|
|
| P_proprotein |
pfam01483 |
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ... |
507-597 |
9.84e-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: 9.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 507 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 586
Cdd:pfam01483 1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75
|
90
....*....|.
gi 1958641647 587 PGKLKEWSLVL 597
Cdd:pfam01483 76 TGTLNSWQLTL 86
|
|
| S8_pro-domain |
pfam16470 |
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ... |
40-116 |
6.50e-37 |
|
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to family S8.
Pssm-ID: 465126 Cd Length: 77 Bit Score: 133.88 E-value: 6.50e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958641647 40 HWAVKIAGGFAEADRIASKYGFINVGQIGALKDYYHFYHSRTIKRSVLSSRGTHSFISMEPKVEWIQQQVVKKRTKR 116
Cdd:pfam16470 1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
|
|
| AprE |
COG1404 |
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
156-422 |
3.62e-34 |
|
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 138.31 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 156 GAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCdVNGNDldpmpryDASNENKHGTRCAGEVAATANNSHCTVGI 235
Cdd:COG1404 100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDF-VDGDG-------DPSDDNGHGTHVAGIIAANGNNGGGVAGV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 236 AFNAKIGGVRMLD----GDVTDMVEA--KSVSynpQHVHIYSASWGPDDDGKTvdgpaPLTRQAFENGvrmgrRGLGSVF 309
Cdd:COG1404 172 APGAKLLPVRVLDdngsGTTSDIAAAidWAAD---NGADVINLSLGGPADGYS-----DALAAAVDYA-----VDKGVLV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 310 VWASGNGGRSkdhCSCDGYTNSIY-TISISSTAESGKKPWYleecSSTlattyssGESYD-----KKIITTDLRQRcTDN 383
Cdd:COG1404 239 VAAAGNSGSD---DATVSYPAAYPnVIAVGAVDANGQLASF----SNY-------GPKVDvaapgVDILSTYPGGG-YAT 303
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958641647 384 HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:COG1404 304 LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTAT 342
|
|
| COG4935 |
COG4935 |
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ... |
508-599 |
6.34e-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: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 508 EHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLfdHSMEGFkNWEFMTIHCWGERAAGDWVLEVYDTPSQlrnfkTP 587
Cdd:COG4935 558 EDVTVTVDITHTYRGDLVITLISPDGTTVVLKNRSG--GSADNI-NATFDVANFSGESANGTWTLRVVDTAGG-----DT 629
|
90
....*....|..
gi 1958641647 588 GKLKEWSLVLYG 599
Cdd:COG4935 630 GTLNSWSLTFTG 641
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
637-751 |
3.31e-12 |
|
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).
Pssm-ID: 464344 [Multi-domain] Cd Length: 132 Bit Score: 65.47 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 637 PCDPECSEVGCDGPGPDHCTDCLHYhyklkNNTRICVSSCPPGHF----HADKKRCRKCAPNCE------SCFGSHADQC 706
Cdd:pfam14843 1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNILQGepreYVVNSTCVPCHPECLpqngtaTCSGPGADNC 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958641647 707 LSCKYgyflNEETSSCVAQCPEGSYQDI--------KKNICGKCSENCKT-CTG 751
Cdd:pfam14843 76 TKCAH----FRDGPHCVSSCPSGVLGENdliwkyadANGVCQPCHPNCTQgCTG 125
|
|
| PTZ00262 |
PTZ00262 |
subtilisin-like protease; Provisional |
169-413 |
3.20e-09 |
|
subtilisin-like protease; Provisional
Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 61.91 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 169 VTILDDGIERTHPDLMQNY---------------------DALASCDVNGNDLDPMprydasNENKHGTRCAGEVAATAN 227
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM------DDNYHGTHVSGIISAIGN 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 228 NSHCTVGIAFNAKIGGVRMLD----GDVTDMVeaKSVSY-NPQHVHIYSASWGPDDDGKTvdgpapltrqaFENGVRMGR 302
Cdd:PTZ00262 394 NNIGIVGVDKRSKLIICKALDshklGRLGDMF--KCFDYcISREAHMINGSFSFDEYSGI-----------FNESVKYLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 303 RgLGSVFVWASGN----GGRSKDHCSCDGYTNSIYTISISSTAES---------GKKPWYLEECSSTLATTYSSGESYDK 369
Cdd:PTZ00262 461 E-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYPPILSKKLRNvitvsnlikDKNNQYSLSPNSFYSAKYCQLAAPGT 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958641647 370 KIITTDLRQRCTDNhTGTSASAPMAAGIIALALEANPFLTWRDV 413
Cdd:PTZ00262 540 NIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
889-995 |
3.77e-08 |
|
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: 53.92 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 889 ICDASCAK--CWGPTQDDCISCpiTRVFDDGRCVMNCPSWKFELK-----KQCHPCHHTCQG------CQGSGPSNCTSC 955
Cdd:pfam14843 1 VCDPLCSSegCWGPGPDQCLSC--RNFSRGGTCVESCNILQGEPReyvvnSTCVPCHPECLPqngtatCSGPGADNCTKC 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958641647 956 KADKHGQeyflykgECLENCPMG---------HYPAKGHACLPCPDNCE 995
Cdd:pfam14843 79 AHFRDGP-------HCVSSCPSGvlgendliwKYADANGVCQPCHPNCT 120
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1293-1618 |
4.51e-08 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 57.67 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1293 CPEGFYAKDGVCEHCSSPcktckgNATSCHSCEGDFVLDH-GVCWETCPEKHVAVEGVCKHCPERCQDCIHEKtCKECMp 1371
Cdd:pfam03302 17 CTSSAPCKTENCKACSND------KREVCEECNSNNYLTPtSQCIDDCAKIGNYYYTTNANNKKICKECTVAN-CKTCE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1372 dfflyNDMCHHSCPKNFYPDMRQCVPCHKNCLGCNGPKEDDCKACAdTSKVLH------NGLCLDECPKGTykdeVNDEC 1445
Cdd:pfam03302 89 -----DQGQCQACNDGFYKSGDACSPCHESCKTCSGGTASDCTECL-TGKALRygndgtKGTCGEGCTTGT----GAGAC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1446 RDCPescLICSSAWTCLTCREGFTVVQD-VCT--APKECAAIEYWDVGSHRCQPCHRKCSRCSG--------PSENQCYT 1514
Cdd:pfam03302 159 KTCG---LTIDGTSYCSECATETEYPQNgVCTstAARATATCKASSVANGMCSSCANGYFRMNGgcyettkfPGKSVCEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1515 CPRetfllNTTCVKECPeGYHTdkDSHQCVPCHSSCRTCEGPHSMQclscrpgwfqlgkecllQCRDGYYgeSTSGRCEK 1594
Cdd:pfam03302 236 ANS-----GGTCQKEAP-GYKL--NNGDLVTCSPGCKTCTSNTVCT-----------------TCMDGYV--KTSDSCTK 288
|
330 340
....*....|....*....|....
gi 1958641647 1595 CDKSCKTCRGpQPTDCQSCDTFFF 1618
Cdd:pfam03302 289 CDSSCETCTG-ATTTCKTCATGYY 311
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1545-1593 |
5.11e-08 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 50.98 E-value: 5.11e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958641647 1545 PCHSSCRTCEGPHSMQCLSCRPGWFQLGKECLLQCRDGYYGESTSGRCE 1593
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
1540-1584 |
8.57e-08 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 50.20 E-value: 8.57e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 1540 SHQCVPCHSSCRTCEGPHSMQCLSCRPGWFQLGKECLLQCRDGYY 1584
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
674-1063 |
8.76e-08 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 56.52 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 674 SSCPPGH-FHADKKRCRKCAP----NCESCFGSHADQCLSCKYGYFLNEeTSSCVAQCpegsyQDIKKNICGKCSEN--- 745
Cdd:pfam03302 2 DECKPGYeLSADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYLTP-TSQCIDDC-----AKIGNYYYTTNANNkki 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 746 CKTCTGfHNCTECKGGLSLQgsrcsvTCEDGQFFSGHDCQPCHRFCATCAGAGADGCINCTEGYVMEegrcvqscsvsyY 825
Cdd:pfam03302 76 CKECTV-ANCKTCEDQGQCQ------ACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALR------------Y 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 826 LDHSLEGgyksckRCDNSCLTCNGPGfkNCSSCpsgylldlgmcqmgaickdGEYIDEQGHCQICDAS--------CAKC 897
Cdd:pfam03302 137 GNDGTKG------TCGEGCTTGTGAG--ACKTC-------------------GLTIDGTSYCSECATEteypqngvCTST 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 898 WGPTQDDCISCPITrvfdDGRCvMNCPSWKFELKKQCHpchhtcQGCQGSGPSNCTSCKADKHGQEyflykgeclencPM 977
Cdd:pfam03302 190 AARATATCKASSVA----NGMC-SSCANGYFRMNGGCY------ETTKFPGKSVCEEANSGGTCQK------------EA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 978 GHYPAKGHACLPCPDNCELCYNPHVCSRCMSGYviVPTNHTCQKlecrqgefqdseygecmpCEEGCVGCTvDDPGACTS 1057
Cdd:pfam03302 247 PGYKLNNGDLVTCSPGCKTCTSNTVCTTCMDGY--VKTSDSCTK------------------CDSSCETCT-GATTTCKT 305
|
....*.
gi 1958641647 1058 CATGYY 1063
Cdd:pfam03302 306 CATGYY 311
|
|
| FU |
smart00261 |
Furin-like repeats; |
781-825 |
5.20e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 47.89 E-value: 5.20e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 781 GHDCQPCHRFCATCAGAGADGCINCTEGYVMEEGRCVQSCSVSYY 825
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1003-1324 |
5.85e-07 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 54.21 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1003 CSRCMSGYVIVPTNHTCQKLEcrqgefqdseygecmPCE-EGCVGCTVDDPGACTSCATGYYMFE-RHCYKACPEKTFGE 1080
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSA---------------PCKtENCKACSNDKREVCEECNSNNYLTPtSQCIDDCAKIGNYY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1081 KWECKACGTNCGSCDQHECYWCEEGfflssgSCVQDCDPGFYGDQElgECKPCHRACETCTGLGYNQCSSCPEGLQLWHG 1160
Cdd:pfam03302 66 YTTNANNKKICKECTVANCKTCEDQ------GQCQACNDGFYKSGD--ACSPCHESCKTCSGGTASDCTECLTGKALRYG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1161 T----------CIWPTWP--------HVEGKVWNEAVPTEKPSLVRSLPQDRRKWKVQIKRDAT--------------RQ 1208
Cdd:pfam03302 138 NdgtkgtcgegCTTGTGAgacktcglTIDGTSYCSECATETEYPQNGVCTSTAARATATCKASSvangmcsscangyfRM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1209 YQPCHSSCKTCNGSLCTSCPAGtylwlQACVPSCPQgtwLSVRSSSCEKCAEGCASCSGDDLCQRCLsqpsntlllhegr 1288
Cdd:pfam03302 218 NGGCYETTKFPGKSVCEEANSG-----GTCQKEAPG---YKLNNGDLVTCSPGCKTCTSNTVCTTCM------------- 276
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958641647 1289 cyhscpEGFYAKDGVCEHCSSPCKTCKGNATSCHSC 1324
Cdd:pfam03302 277 ------DGYVKTSDSCTKCDSSCETCTGATTTCKTC 306
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
690-739 |
7.88e-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: 7.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958641647 690 KCAPNCESCFGSHADQCLSCKYGYFLNEETssCVAQCPEGSYQDIKKNIC 739
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGT--CVSECPEGTYADTEGGVC 48
|
|
| FU |
smart00261 |
Furin-like repeats; |
685-731 |
1.88e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 46.35 E-value: 1.88e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958641647 685 KKRCRKCAPNCESCFGSHADQCLSCKYGYFLNEETssCVAQCPEGSY 731
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGK--CVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
786-827 |
4.65e-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: 45.20 E-value: 4.65e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958641647 786 PCHRFCATCAGAGADGCINCTEGYVMEEGRCVQSCSVSYYLD 827
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
|
|
| FU |
smart00261 |
Furin-like repeats; |
1642-1684 |
5.48e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.81 E-value: 5.48e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958641647 1642 TCERCHPTCDKCSGKEAWNCLSCVWSYHLLKGICTPECIVGEY 1684
Cdd:smart00261 3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1211-1256 |
1.05e-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: 44.43 E-value: 1.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958641647 1211 PCHSSCKTCNGSL---CTSCPAGTYLWLQACVPSCPQGTWLSVRSSSCE 1256
Cdd:cd00064 1 PCHPSCATCTGPGpdqCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
885-928 |
1.09e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.04 E-value: 1.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958641647 885 GHCQICDASCAKCWGPTQDDCISCPITRVFDDGRCVMNCPSWKF 928
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
712-1006 |
1.77e-05 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 49.91 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 712 GYFLNEETSSCVAQCPEGSYQDiKKNICGKCSENC---------KTCTGFHN--CTECKGGLSLQGSRCSVTCEDGQFFS 780
Cdd:PTZ00214 350 GYLCGDATNGGVSGCATCGYNS-GAVTCTRCSAGYlgvdgkscsESCSGDTRgvCTKVAEGSESTEVSCRCVCKPTFYNS 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 781 GHDCQPCHRFCATCAGAGADGCINCTEGYVM-------EEGRCVQSCSVSyylDHSLE-----GGYKSCKRC-DNSCLTC 847
Cdd:PTZ00214 429 SGTCTPCTDSCAVCKDGTPTGCQQCSPGKILefsivssESADCVDQCSVG---SECAEcgitiDGSRYCTRCkDASTYPF 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 848 NGPGFKN--------------CSSCPSGYLLDLGMCQMGAICKDGEYIDEQghcqicdaSCAKCWGPTQDDCIScpitrv 913
Cdd:PTZ00214 506 NGVCIPNtqrdayctstangaCTTCSGAAFLMNGGCYTTEHYPGSTICDKQ--------SNGKCTTTKKGYGIS------ 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 914 fDDGRCVmncpswkfelkkQCHPchhTCQGCQGSGPSNCTSCKADK-HGQEYFLYKGECLE--NCPMGHYpAKGHACLPC 990
Cdd:PTZ00214 572 -PDGKLL------------ECDP---TCLACTAPGPGRCTRCPSDKlLKRASGAATGSCVDpgACVDGYY-ADGDACLPC 634
|
330
....*....|....*..
gi 1958641647 991 PD-NCELCYNPHVCSRC 1006
Cdd:PTZ00214 635 ATpGCKTCGHASFCTEC 651
|
|
| FU |
smart00261 |
Furin-like repeats; |
1128-1163 |
2.02e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 43.27 E-value: 2.02e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1958641647 1128 GECKPCHRACETCTGLGYNQCSSCPEGLQLWHGTCI 1163
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCV 37
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
936-981 |
2.54e-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: 2.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958641647 936 PCHHTCQGCQGSGPSNCTSCKADkhgqeYFLYKGECLENCPMGHYP 981
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHG-----FYLDGGTCVSECPEGTYA 41
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1646-1689 |
9.88e-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: 41.74 E-value: 9.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958641647 1646 CHPTCDKCSGKEAWNCLSCVWSYHLLKGICTPECIVGEYRDGKG 1689
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEG 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1694-1737 |
8.82e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 38.64 E-value: 8.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958641647 1694 CKKCHESCMECKGPGSKNCTGCSAGLLLqmDDSRCLRCCNASHP 1737
Cdd:smart00261 4 CKPCHPECATCTGPGPDDCTSCKHGFFL--DGGKCVSECPPGTY 45
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
687-822 |
9.99e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 43.86 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 687 RCRKCAPNCESCFGSHADQCLSCKYGYFLNEETSSCVAQCPEGSYQDIKKNICGKCSENCKTCTGFHNCTECKGGLSLQG 766
Cdd:COG4624 2 LLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641647 767 SRCSVTCEDGqffSGHDCQPCHRFCATCAGAGADG--------CINCtegyvmeeGRCVQSCSV 822
Cdd:COG4624 82 RGPSIIRDKE---KCKNCYPCVRACPVKAIKVDDGkaeideekCISC--------GQCVAVCPF 134
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
1214-1590 |
2.21e-03 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 42.98 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1214 SSCKTCN----GSLCTSCPAGtylwlqacvpscpqgtWLSVRSSSCEKcaegcaSCSGDD--LCQRCLSQPSNTlllhEG 1287
Cdd:PTZ00214 362 SGCATCGynsgAVTCTRCSAG----------------YLGVDGKSCSE------SCSGDTrgVCTKVAEGSEST----EV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1288 RCYHSCPEGFYAKDGVCEHCSSPCKTCK-GNATSCHSCEGDFVLDHGVcwetcpekhvavegVCKHCPERCQDCIHEKTC 1366
Cdd:PTZ00214 416 SCRCVCKPTFYNSSGTCTPCTDSCAVCKdGTPTGCQQCSPGKILEFSI--------------VSSESADCVDQCSVGSEC 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1367 KECmpdfflyndmchhscpknfypdmrqcvpchknclGCNGPKEDDCKACADTSKVLHNGLCLDECPKGTY-KDEVNDEC 1445
Cdd:PTZ00214 482 AEC----------------------------------GITIDGSRYCTRCKDASTYPFNGVCIPNTQRDAYcTSTANGAC 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1446 RDCPESCLICSSAWTCLTCREGFTVVQDVCTAPKECAAIEYWDVGSHRCQPCHRKCSRCSGPSENQCYTCPRETFLLNTT 1525
Cdd:PTZ00214 528 TTCSGAAFLMNGGCYTTEHYPGSTICDKQSNGKCTTTKKGYGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKLLKRAS 607
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958641647 1526 ------CVK--ECPEGYHTDKDShqCVPCHS-SCRTCegPHSMQCLSCRPGWFQL--GKECLLQCR-DGYYGESTSG 1590
Cdd:PTZ00214 608 gaatgsCVDpgACVDGYYADGDA--CLPCATpGCKTC--GHASFCTECAGELFVSldGQSCLEECTgDKVVGEVSGG 680
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidases_S8_Protein_convertases_Kexins_Furin-lik |
cd04059 |
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ... |
128-422 |
7.04e-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: 498.62 E-value: 7.04e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 128 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 206
Cdd:cd04059 1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 207 DasNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGP 286
Cdd:cd04059 81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 287 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 365
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958641647 366 SYDKKIITTDLR--QRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd04059 239 NPEASIVTTDLGgnCNCTSSHNGTSAAAPLAAGVIALMLEANPNLTWRDVQHILALTAR 297
|
|
| Peptidase_S8 |
pfam00082 |
Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
164-447 |
9.65e-66 |
|
Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
Pssm-ID: 395035 [Multi-domain] Cd Length: 287 Bit Score: 225.03 E-value: 9.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNG----NDLDPMPRYDASNENKHGTRCAGEVAATANNSHCTVGIAFNA 239
Cdd:pfam00082 1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEAsvdfNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 240 KIGGVRML-DGDVTDMVEAKSVSYN-PQHVHIYSASWGPDddgKTVDGPAPLTRQAFENGvrmGRRGLGSVFVWASGNGG 317
Cdd:pfam00082 81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 318 RSKDHCSCDGY-TNSIYTISISSTaesgkkpwylEECSSTLATTYSS----------------GESY-------DKKIIT 373
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAV----------DEASEGNLASFSSygptldgrlkpdivapGGNItggnissTLLTTT 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641647 374 TDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNAndwktnaagfkVSHLYGFG 447
Cdd:pfam00082 225 SDPPNQGYDSMSGTSMATPHVAGAAALLKQAYPNLTPETLKALLVNTATDLGDAG-----------LDRLFGYG 287
|
|
| P_proprotein |
pfam01483 |
Proprotein convertase P-domain; A unique feature of the eukaryotic subtilisin-like proprotein ... |
507-597 |
9.84e-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: 9.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 507 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 586
Cdd:pfam01483 1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75
|
90
....*....|.
gi 1958641647 587 PGKLKEWSLVL 597
Cdd:pfam01483 76 TGTLNSWQLTL 86
|
|
| S8_pro-domain |
pfam16470 |
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to ... |
40-116 |
6.50e-37 |
|
Peptidase S8 pro-domain; This domain is the pro-domain of several peptidases belonging to family S8.
Pssm-ID: 465126 Cd Length: 77 Bit Score: 133.88 E-value: 6.50e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958641647 40 HWAVKIAGGFAEADRIASKYGFINVGQIGALKDYYHFYHSRTIKRSVLSSRGTHSFISMEPKVEWIQQQVVKKRTKR 116
Cdd:pfam16470 1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
|
|
| Peptidases_S8_15 |
cd07498 |
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ... |
167-420 |
1.37e-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: 136.32 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 167 IVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPmprydaSNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRM 246
Cdd:cd07498 1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPT------SDIDGHGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 247 LDGD--VTDMVEAKSVSYNPQH-VHIYSASWGPDDdgktvdgPAPLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDhc 323
Cdd:cd07498 75 ADSLgyAYWSDIAQAITWAADNgADVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLFAAGNSGRSVS-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 324 scDGYTNSIYTISISSTAESGKKPWY--------LEECSSTLATTYSSGESydkkiiTTDLRQRCTDNHTGTSASAPMAA 395
Cdd:cd07498 146 --SGYAANPSVIAVAATDSNDARASYsnygnyvdLVAPGVGIWTTGTGRGS------AGDYPGGGYGSFSGTSFASPVAA 217
|
250 260
....*....|....*....|....*
gi 1958641647 396 GIIALALEANPFLTWRDVQHVIVRT 420
Cdd:cd07498 218 GVAALILSANPNLTPAEVEDILTST 242
|
|
| AprE |
COG1404 |
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
156-422 |
3.62e-34 |
|
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 138.31 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 156 GAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCdVNGNDldpmpryDASNENKHGTRCAGEVAATANNSHCTVGI 235
Cdd:COG1404 100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDF-VDGDG-------DPSDDNGHGTHVAGIIAANGNNGGGVAGV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 236 AFNAKIGGVRMLD----GDVTDMVEA--KSVSynpQHVHIYSASWGPDDDGKTvdgpaPLTRQAFENGvrmgrRGLGSVF 309
Cdd:COG1404 172 APGAKLLPVRVLDdngsGTTSDIAAAidWAAD---NGADVINLSLGGPADGYS-----DALAAAVDYA-----VDKGVLV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 310 VWASGNGGRSkdhCSCDGYTNSIY-TISISSTAESGKKPWYleecSSTlattyssGESYD-----KKIITTDLRQRcTDN 383
Cdd:COG1404 239 VAAAGNSGSD---DATVSYPAAYPnVIAVGAVDANGQLASF----SNY-------GPKVDvaapgVDILSTYPGGG-YAT 303
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958641647 384 HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:COG1404 304 LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTAT 342
|
|
| Peptidases_S8_S53 |
cd00306 |
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ... |
167-420 |
7.61e-30 |
|
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173787 [Multi-domain] Cd Length: 241 Bit Score: 120.00 E-value: 7.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 167 IVVTILDDGIERTHPDLmqnyDALASCDVNGNDLDPMPRY--DASNENKHGTRCAGEVAATANNSHCtVGIAFNAKIGGV 244
Cdd:cd00306 1 VTVAVIDTGVDPDHPDL----DGLFGGGDGGNDDDDNENGptDPDDGNGHGTHVAGIIAASANNGGG-VGVAPGAKLIPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 245 RMLD----GDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGktvdgPAPLTRQAFENGVRMgrrgLGSVFVWASGNGGRSK 320
Cdd:cd00306 76 KVLDgdgsGSSSDIAAAIDYAAADQGADVINLSLGGPGSP-----PSSALSEAIDYALAK----LGVLVVAAAGNDGPDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 321 DHCScDGYTNSIYTISISSTAESGKKPWYLEeCSSTLATTYSSGESYdkkIITTDLRQRCTDNHTGTSASAPMAAGIIAL 400
Cdd:cd00306 147 GTNI-GYPAASPNVIAVGAVDRDGTPASPSS-NGGAGVDIAAPGGDI---LSSPTTGGGGYATLSGTSMAAPIVAGVAAL 221
|
250 260
....*....|....*....|
gi 1958641647 401 ALEANPFLTWRDVQHVIVRT 420
Cdd:cd00306 222 LLSANPDLTPAQVKAALLST 241
|
|
| Peptidases_S8_Subtilisin_like |
cd07473 |
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ... |
165-422 |
9.06e-27 |
|
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173799 [Multi-domain] Cd Length: 259 Bit Score: 111.52 E-value: 9.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 165 KNIVVTILDDGIERTHPDLMQNY--DALASC-------------DVNG-----NDLDPMPrydasnENKHGTRCAGEVAA 224
Cdd:cd07473 2 GDVVVAVIDTGVDYNHPDLKDNMwvNPGEIPgngidddgngyvdDIYGwnfvnNDNDPMD------DNGHGTHVAGIIGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 225 TANNSHCTVGIAFNAKIGGVRMLD----GDVTDMVEA--KSVSYNpqhVHIYSASWGPdddgktvDGPAPLTRQAFEngv 298
Cdd:cd07473 76 VGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAidYAVDMG---AKIINNSWGG-------GGPSQALRDAIA--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 299 RMGRRGLgsVFVWASGNGGRSKDH-----CScdgYTNSiYTISISSTAESGKKPWYleecSSTLATT---YSSGESydkk 370
Cdd:cd07473 143 RAIDAGI--LFVAAAGNDGTNNDKtptypAS---YDLD-NIISVAATDSNDALASF----SNYGKKTvdlAAPGVD---- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958641647 371 IITTDLRQRcTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07473 209 ILSTSPGGG-YGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
|
|
| Peptidases_S8_Thermitase_like |
cd07484 |
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ... |
129-422 |
2.11e-21 |
|
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173810 [Multi-domain] Cd Length: 260 Bit Score: 95.79 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 129 NDPKWPSMWYMHcsdnthpcqsDMNIEGAWKRGyTGKNIVVTILDDGIERTHPDLM-----QNYDAlascdVNGNDldpm 203
Cdd:cd07484 3 NDPYYSYQWNLD----------QIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLLkvkfvLGYDF-----VDNDS---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 204 pryDASNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLD----GDVTDMVEAksvsynpqhvhIYsasWGPDDD 279
Cdd:cd07484 63 ---DAMDDNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANG-----------IR---YAADKG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 280 GKTVD---GpAPLTRQAFENGVRMGRRGlGSVFVWASGNGGRSKdhCScdgYTNSI-YTISISSTAESGKKPWYleecss 355
Cdd:cd07484 126 AKVINlslG-GGLGSTALQEAINYAWNK-GVVVVAAAGNEGVSS--VS---YPAAYpGAIAVAATDQDDKRASF------ 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641647 356 tlaTTYSS-------GESydkkIITTDLRQRcTDNHTGTSASAPMAAGIIALALEANPfLTWRDVQHVIVRTSR 422
Cdd:cd07484 193 ---SNYGKwvdvsapGGG----ILSTTPDGD-YAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDALKKTAD 257
|
|
| Peptidases_S8_Autotransporter_serine_protease_like |
cd04848 |
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ... |
163-422 |
2.88e-21 |
|
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.
Pssm-ID: 173794 [Multi-domain] Cd Length: 267 Bit Score: 95.47 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 163 TGKNIVVTILDDGIERTHPDLMQNYDALAScdvNGNDLDPMPRYDASNENkHGTRCAGEVAATANNSHcTVGIAFNAKIG 242
Cdd:cd04848 1 TGAGVKVGVIDSGIDLSHPEFAGRVSEASY---YVAVNDAGYASNGDGDS-HGTHVAGVIAAARDGGG-MHGVAPDATLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 243 GVRMLDGDVTdmveAKSVSYNPQH--------VHIYSASWGPDDDGKTVDGPAPL---TRQAFENGVRMGRRGLGSVFVW 311
Cdd:cd04848 76 SARASASAGS----TFSDADIAAAydflaasgVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 312 ASGNGGRSKDhcscDGYTNSIY--------------------TISISSTAESGK--KPWYLeecsST-----LATTYSSG 364
Cdd:cd04848 152 AAGNDGQANP----SLAAAALPylepeleggwiavvavdpngTIASYSYSNRCGvaANWCL----AApgeniYSTDPDGG 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958641647 365 ESYDKKIittdlrqrctdnhtGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd04848 224 NGYGRVS--------------GTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTAT 267
|
|
| Peptidases_S8_13 |
cd07496 |
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ... |
166-409 |
8.81e-21 |
|
Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173820 [Multi-domain] Cd Length: 285 Bit Score: 94.67 E-value: 8.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 166 NIVVTILDDGIeRTHPDLMQN-----YD----ALASCDVNGNDLDP----------------MPRYDASNENKHGTRCAG 220
Cdd:cd07496 1 GVVVAVLDTGV-LFHHPDLAGvllpgYDfisdPAIANDGDGRDSDPtdpgdwvtgddvppggFCGSGVSPSSWHGTHVAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 221 EVAATANNSHCTVGIAFNAKIGGVRML---DGDVTDMVEA---------KSVSYNPQHVHIYSASWGPDddgktvdGPAP 288
Cdd:cd07496 80 TIAAVTNNGVGVAGVAWGARILPVRVLgkcGGTLSDIVDGmrwaaglpvPGVPVNPNPAKVINLSLGGD-------GACS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 289 LTRQAFENGVRmgrrGLGSVFVWASGNGGRSKDH---CSCDGytnsiyTISISSTAESGKKPWYLE------------EC 353
Cdd:cd07496 153 ATMQNAINDVR----ARGVLVVVAAGNEGSSASVdapANCRG------VIAVGATDLRGQRASYSNygpavdvsapggDC 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958641647 354 SSTL---------ATTYSSGE-SYDkkiittdlrqrctdNHTGTSASAPMAAGIIALALEANPFLT 409
Cdd:cd07496 223 ASDVngdgypdsnTGTTSPGGsTYG--------------FLQGTSMAAPHVAGVAALMKSVNPSLT 274
|
|
| Peptidases_S8_Fervidolysin_like |
cd07485 |
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ... |
157-406 |
7.35e-19 |
|
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans is an extracellular subtilisin-like keratinase. It is contains a signal peptide, a propeptide, and a catalytic region. The tertiary structure of fervidolysin is similar to that of subtilisin. It contains a Asp/His/Ser catalytic triad and is a member of the peptidase S8 (subtilisin and kexin) family. The catalytic triad is similar to that found in trypsin-like proteases, but it does not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173811 [Multi-domain] Cd Length: 273 Bit Score: 88.70 E-value: 7.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 157 AWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALA-SCDVNGNDLDPMPRYDA---SNENKHGTRCAGEVAATANNSHCT 232
Cdd:cd07485 2 AWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGyDPAVNGYNFVPNVGDIDndvSVGGGHGTHVAGTIAAVNNNGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 233 VGIAFN------AKIGGVRMLDGD--VTDMVEAKSVSYNPQH-VHIYSASWGpdddGKTVDGPAPLTRQAFENGVRMGRR 303
Cdd:cd07485 82 GGIAGAggvapgVKIMSIQIFAGRyyVGDDAVAAAIVYAADNgAVILQNSWG----GTGGGIYSPLLKDAFDYFIENAGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 304 GL--GSVFVWASGNGGRSKDH--CSCDGytnsiyTISISSTAESGKKPWYleecsSTLATTYSSGESYDKKIITTDLRQR 379
Cdd:cd07485 158 SPldGGIVVFSAGNSYTDEHRfpAAYPG------VIAVAALDTNDNKASF-----SNYGRWVDIAAPGVGTILSTVPKLD 226
|
250 260 270
....*....|....*....|....*....|..
gi 1958641647 380 CTDNHT-----GTSASAPMAAGIIALALEANP 406
Cdd:cd07485 227 GDGGGNyeylsGTSMAAPHVSGVAALVLSKFP 258
|
|
| Peptidases_S8_1 |
cd07487 |
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ... |
164-420 |
3.28e-18 |
|
Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173812 [Multi-domain] Cd Length: 264 Bit Score: 86.49 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMprYDasnENKHGTRCAGEVAATANNSHCTV-GIAFNAKIG 242
Cdd:cd07487 1 GKGITVAVLDTGIDAPHPDFDGRIIRFADFVNTVNGRTTP--YD---DNGHGTHVAGIIAGSGRASNGKYkGVAPGANLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 243 GVRMLD----GDVTDMVEAksVSY-----NPQHVHIYSASWG-PDDDGktvDGPAPLtRQAFENGVRMgrrglGSVFVWA 312
Cdd:cd07487 76 GVKVLDdsgsGSESDIIAG--IDWvvennEKYNIRVVNLSLGaPPDPS---YGEDPL-CQAVERLWDA-----GIVVVVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 313 SGNGGRSKDHCSCDGytNSIYTISISSTAESGKKPWYLEECSS---TL-----------ATTYSSGESYDKKIITTDLRQ 378
Cdd:cd07487 145 AGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSSrgpTGdgrikpdvvapGENIVSCRSPGGNPGAGVGSG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958641647 379 RCTDnhTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRT 420
Cdd:cd07487 223 YFEM--SGTSMATPHVSGAIALLLQANPILTPDEVKCILRDT 262
|
|
| COG4935 |
COG4935 |
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ... |
508-599 |
6.34e-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: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 508 EHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLfdHSMEGFkNWEFMTIHCWGERAAGDWVLEVYDTPSQlrnfkTP 587
Cdd:COG4935 558 EDVTVTVDITHTYRGDLVITLISPDGTTVVLKNRSG--GSADNI-NATFDVANFSGESANGTWTLRVVDTAGG-----DT 629
|
90
....*....|..
gi 1958641647 588 GKLKEWSLVLYG 599
Cdd:COG4935 630 GTLNSWSLTFTG 641
|
|
| Peptidases_S8_Subtilisin_subset |
cd07477 |
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ... |
166-420 |
1.05e-17 |
|
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173803 [Multi-domain] Cd Length: 229 Bit Score: 84.12 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 166 NIVVTILDDGIERTHPDLMQNYdalascdVNGNDLDPMPRYDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKIGGVR 245
Cdd:cd07477 1 GVKVAVIDTGIDSSHPDLKLNI-------VGGANFTGDDNNDYQDGNGHGTHVAGIIAALDNGVG-VVGVAPEADLYAVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 246 MLD----GDVTDMVEAKSVSYNpQHVHIYSASWGpdddgktVDGPAPLTRQAFENGVrmgRRGLgsVFVWASGNggrskd 321
Cdd:cd07477 73 VLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLG-------GPSDSPALREAIKKAY---AAGI--LVVAAAGN------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 322 hcscDGYTNSIYT--------ISISSTAESGKKpwyleecsstlaTTYSS----------GESydkkIITTDLRQRCTDN 383
Cdd:cd07477 134 ----SGNGDSSYDypakypsvIAVGAVDSNNNR------------ASFSStgpevelaapGVD----ILSTYPNNDYAYL 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958641647 384 hTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRT 420
Cdd:cd07477 194 -SGTSMATPHVAGVAALVWSKRPELTNAQVRQALNKT 229
|
|
| Peptidases_S8_Kp43_protease |
cd04842 |
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ... |
159-404 |
1.30e-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: 76.60 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 159 KRGYTGKNIVVTILDDGIERTHPDLMqnydalascDVNGNDLDPMPR----YDASNENK-----HGTRCAGEVAATANNS 229
Cdd:cd04842 1 GLGLTGKGQIVGVADTGLDTNHCFFY---------DPNFNKTNLFHRkivrYDSLSDTKddvdgHGTHVAGIIAGKGNDS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 230 HCTV---GIAFNAKIGGVRM------------LDGDVTDMVEAKSvsynpqhvHIYSASWGPDDDG------KTVDgpap 288
Cdd:cd04842 72 SSISlykGVAPKAKLYFQDIgdtsgnlssppdLNKLFSPMYDAGA--------RISSNSWGSPVNNgytllaRAYD---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 289 ltRQAFENgvrmgrRGLgsVFVWASGNGGrskdhcscDGYTNSIYTISIS-----------STAESGKKPWYLEECSSTL 357
Cdd:cd04842 140 --QFAYNN------PDI--LFVFSAGNDG--------NDGSNTIGSPATAknvltvgasnnPSVSNGEGGLGQSDNSDTV 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958641647 358 ATTYSSGESYD--KK---------IITTDLRQR----CTDNH----TGTSASAPMAAGIIALALEA 404
Cdd:cd04842 202 ASFSSRGPTYDgrIKpdlvapgtgILSARSGGGgigdTSDSAytskSGTSMATPLVAGAAALLRQY 267
|
|
| Peptidases_S8_subtilisin_Vpr-like |
cd07474 |
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ... |
164-430 |
3.08e-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: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 164 GKNIVVTILDDGIERTHPDLMQNYDALASC----DVNGNDLDPMPR---------YDASNENKHGTRCAGEVAATANNSH 230
Cdd:cd07474 1 GKGVKVAVIDTGIDYTHPDLGGPGFPNDKVkggyDFVDDDYDPMDTrpypsplgdASAGDATGHGTHVAGIIAGNGVNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 231 CTVGIAFNAKIGGVRMLDGD---VTDMVEA---KSVSynpQHVHIYSASWG-----PDDDGKtvdgpapltrQAFENGVR 299
Cdd:cd07474 81 TIKGVAPKADLYAYKVLGPGgsgTTDVIIAaieQAVD---DGMDVINLSLGssvngPDDPDA----------IAINNAVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 300 mgrrgLGSVFVWASGNGGrskDHCSCDGyTNSIYTISISSTAESGKKPWYleecSSTLATTYSSGESYDKKIITTDL--- 376
Cdd:cd07474 148 -----AGVVVVAAAGNSG---PAPYTIG-SPATAPSAITVGASTVADVAE----ADTVGPSSSRGPPTSDSAIKPDIvap 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641647 377 -------RQRCTDN---HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTsrAGHLNAND 430
Cdd:cd07474 215 gvdimstAPGSGTGyarMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNT--AKPLYDSD 276
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
637-751 |
3.31e-12 |
|
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).
Pssm-ID: 464344 [Multi-domain] Cd Length: 132 Bit Score: 65.47 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 637 PCDPECSEVGCDGPGPDHCTDCLHYhyklkNNTRICVSSCPPGHF----HADKKRCRKCAPNCE------SCFGSHADQC 706
Cdd:pfam14843 1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNILQGepreYVVNSTCVPCHPECLpqngtaTCSGPGADNC 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958641647 707 LSCKYgyflNEETSSCVAQCPEGSYQDI--------KKNICGKCSENCKT-CTG 751
Cdd:pfam14843 76 TKCAH----FRDGPHCVSSCPSGVLGENdliwkyadANGVCQPCHPNCTQgCTG 125
|
|
| Peptidases_S8_PCSK9_ProteinaseK_like |
cd04077 |
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ... |
162-421 |
5.04e-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: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 162 YTGKNIVVTILDDGIERTHPDLMQNydALASCDVNGNDldpmpryDASNENKHGTRCAGEVAATannshcTVGIAFNAKI 241
Cdd:cd04077 22 STGSGVDVYVLDTGIRTTHVEFGGR--AIWGADFVGGD-------PDSDCNGHGTHVAGTVGGK------TYGVAKKANL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 242 GGVRMLD----GDVTDMVEAksvsYNpqhvhiYSASWGPDDDGKTV-----DGPAPltrQAFENGV-RMGRRGLgsVFVW 311
Cdd:cd04077 87 VAVKVLDcngsGTLSGIIAG----LE------WVANDATKRGKPAVanmslGGGAS---TALDAAVaAAVNAGV--VVVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 312 ASGNGGRskDHCscdGYT--NSIYTISISSTAESGKKPWYLE--ECSSTLAttysSGESYDKKIITTDlrqRCTDNHTGT 387
Cdd:cd04077 152 AAGNSNQ--DAC---NYSpaSAPEAITVGATDSDDARASFSNygSCVDIFA----PGVDILSAWIGSD---TATATLSGT 219
|
250 260 270
....*....|....*....|....*....|....
gi 1958641647 388 SASAPMAAGIIALALEANPFLTWRDVQHVIVRTS 421
Cdd:cd04077 220 SMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLA 253
|
|
| Peptidases_S8_5 |
cd07489 |
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ... |
160-423 |
5.65e-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: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 160 RGYTGKNIVVTILDDGIERTHPDL----MQNYDALASCDVNGNDLD----PMPRYDASNENKHGTRCAGEVAATANNSHC 231
Cdd:cd07489 8 EGITGKGVKVAVVDTGIDYTHPALggcfGPGCKVAGGYDFVGDDYDgtnpPVPDDDPMDCQGHGTHVAGIIAANPNAYGF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 232 TvGIAFNAKIGGVRMLD--GDVTD--MVEAKSVSYNpQHVHIYSASWGpDDDGKTVDGPAPLTRQAFENGVRM------- 300
Cdd:cd07489 88 T-GVAPEATLGAYRVFGcsGSTTEdtIIAAFLRAYE-DGADVITASLG-GPSGWSEDPWAVVASRIVDAGVVVtiaagnd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 301 GRRGLgsvfvWASGNGGRSKDHCSCdGYTNSIYTiSISSTAESGKKPWYLEECSSTLATTYSSGESYDkkIIttdlrqrc 380
Cdd:cd07489 165 GERGP-----FYASSPASGRGVIAV-ASVDSYFS-SWGPTNELYLKPDVAAPGGNILSTYPLAGGGYA--VL-------- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958641647 381 tdnhTGTSASAPMAAGIIALALEA-NPFLTWRDVQHVIVRTSRA 423
Cdd:cd07489 228 ----SGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKP 267
|
|
| Peptidases_S8_10 |
cd07494 |
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ... |
152-430 |
1.25e-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: 61.72 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 152 MNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALAScdvngndLDPMPRYDASNENKHGTrcaGEVAAtannshc 231
Cdd:cd07494 8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQVRVV-------LAPGATDPACDENGHGT---GESAN------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 232 TVGIAFNAKIGGVRMLDGDVTDMVEA--KSVSYNPQhvhIYSASWGPD--DDGKTVDGPAPLTRQAFE----NGVrmgRR 303
Cdd:cd07494 71 LFAIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSPD---IISNSWGYDlrSPGTSWSRSLPNALKALAatlqDAV---AR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 304 GLgsVFVWASGNGGRS-----KDHCSCDG-YTNSIYTISISSTAESGKKPWY-------------LEECSSTLATTYSSG 364
Cdd:cd07494 145 GI--VVVFSAGNGGWSfpaqhPEVIAAGGvFVDEDGARRASSYASGFRSKIYpgrqvpdvcglvgMLPHAAYLMLPVPPG 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958641647 365 ESYDKKIITTDLRQRCTDN---HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRA---GHLNAND 430
Cdd:cd07494 223 SQLDRSCAAFPDGTPPNDGwgvFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTARDvtkGASAQGT 294
|
|
| Peptidases_S8_6 |
cd07490 |
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ... |
169-422 |
2.79e-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: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 169 VTILDDGIERTHPDLMQNYDALASCDVNGNDLDPmpryDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKiggvrMLD 248
Cdd:cd07490 4 VAVLDTGVDADHPDLAGRVAQWADFDENRRISAT----EVFDAGGHGTHVSGTIGGGGAKGV-YIGVAPEAD-----LLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 249 GDVTDMVEAksvsynPQHVHIYSASWGPDDDGKTV-------DGPAPLTRQAFEngvrMGRRGLGSVFVWASGNGGRSKD 321
Cdd:cd07490 74 GKVLDDGGG------SLSQIIAGMEWAVEKDADVVsmslggtYYSEDPLEEAVE----ALSNQTGALFVVSAGNEGHGTS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 322 HCSCDGYTnsiyTISISSTAESGKKPWYlEECSSTLATTYSSGESYDKKIITTDL-----------RQRCTDNH----TG 386
Cdd:cd07490 144 GSPGSAYA----ALSVGAVDRDDEDAWF-SSFGSSGASLVSAPDSPPDEYTKPDVaapgvdvysarQGANGDGQytrlSG 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958641647 387 TSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07490 219 TSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
|
|
| PTZ00262 |
PTZ00262 |
subtilisin-like protease; Provisional |
169-413 |
3.20e-09 |
|
subtilisin-like protease; Provisional
Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 61.91 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 169 VTILDDGIERTHPDLMQNY---------------------DALASCDVNGNDLDPMprydasNENKHGTRCAGEVAATAN 227
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM------DDNYHGTHVSGIISAIGN 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 228 NSHCTVGIAFNAKIGGVRMLD----GDVTDMVeaKSVSY-NPQHVHIYSASWGPDDDGKTvdgpapltrqaFENGVRMGR 302
Cdd:PTZ00262 394 NNIGIVGVDKRSKLIICKALDshklGRLGDMF--KCFDYcISREAHMINGSFSFDEYSGI-----------FNESVKYLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 303 RgLGSVFVWASGN----GGRSKDHCSCDGYTNSIYTISISSTAES---------GKKPWYLEECSSTLATTYSSGESYDK 369
Cdd:PTZ00262 461 E-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYPPILSKKLRNvitvsnlikDKNNQYSLSPNSFYSAKYCQLAAPGT 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958641647 370 KIITTDLRQRCTDNhTGTSASAPMAAGIIALALEANPFLTWRDV 413
Cdd:PTZ00262 540 NIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
889-995 |
3.77e-08 |
|
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: 53.92 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 889 ICDASCAK--CWGPTQDDCISCpiTRVFDDGRCVMNCPSWKFELK-----KQCHPCHHTCQG------CQGSGPSNCTSC 955
Cdd:pfam14843 1 VCDPLCSSegCWGPGPDQCLSC--RNFSRGGTCVESCNILQGEPReyvvnSTCVPCHPECLPqngtatCSGPGADNCTKC 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958641647 956 KADKHGQeyflykgECLENCPMG---------HYPAKGHACLPCPDNCE 995
Cdd:pfam14843 79 AHFRDGP-------HCVSSCPSGvlgendliwKYADANGVCQPCHPNCT 120
|
|
| Peptidases_S8_12 |
cd07480 |
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ... |
162-315 |
4.15e-08 |
|
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173806 [Multi-domain] Cd Length: 297 Bit Score: 57.00 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 162 YTGKNIVVTILDDGIERTHPDLMqnydalascDVNGNDLDPMPRYDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKI 241
Cdd:cd07480 5 FTGAGVRVAVLDTGIDLTHPAFA---------GRDITTKSFVGGEDVQDGHGHGTHCAGTIFGRDVPGP-RYGVARGAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 242 --GGVRMLDGDVTDMVEAKSVSYNPQH-VHIYSASWGPDDDGKTVDG--PAPLTRQAFE----------NGVRMGRR--- 303
Cdd:cd07480 75 alIGKVLGDGGGGDGGILAGIQWAVANgADVISMSLGADFPGLVDQGwpPGLAFSRALEayrqrarlfdALMTLVAAqaa 154
|
170
....*....|...
gi 1958641647 304 -GLGSVFVWASGN 315
Cdd:cd07480 155 lARGTLIVAAAGN 167
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1293-1618 |
4.51e-08 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 57.67 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1293 CPEGFYAKDGVCEHCSSPcktckgNATSCHSCEGDFVLDH-GVCWETCPEKHVAVEGVCKHCPERCQDCIHEKtCKECMp 1371
Cdd:pfam03302 17 CTSSAPCKTENCKACSND------KREVCEECNSNNYLTPtSQCIDDCAKIGNYYYTTNANNKKICKECTVAN-CKTCE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1372 dfflyNDMCHHSCPKNFYPDMRQCVPCHKNCLGCNGPKEDDCKACAdTSKVLH------NGLCLDECPKGTykdeVNDEC 1445
Cdd:pfam03302 89 -----DQGQCQACNDGFYKSGDACSPCHESCKTCSGGTASDCTECL-TGKALRygndgtKGTCGEGCTTGT----GAGAC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1446 RDCPescLICSSAWTCLTCREGFTVVQD-VCT--APKECAAIEYWDVGSHRCQPCHRKCSRCSG--------PSENQCYT 1514
Cdd:pfam03302 159 KTCG---LTIDGTSYCSECATETEYPQNgVCTstAARATATCKASSVANGMCSSCANGYFRMNGgcyettkfPGKSVCEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1515 CPRetfllNTTCVKECPeGYHTdkDSHQCVPCHSSCRTCEGPHSMQclscrpgwfqlgkecllQCRDGYYgeSTSGRCEK 1594
Cdd:pfam03302 236 ANS-----GGTCQKEAP-GYKL--NNGDLVTCSPGCKTCTSNTVCT-----------------TCMDGYV--KTSDSCTK 288
|
330 340
....*....|....*....|....
gi 1958641647 1595 CDKSCKTCRGpQPTDCQSCDTFFF 1618
Cdd:pfam03302 289 CDSSCETCTG-ATTTCKTCATGYY 311
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1545-1593 |
5.11e-08 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 50.98 E-value: 5.11e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958641647 1545 PCHSSCRTCEGPHSMQCLSCRPGWFQLGKECLLQCRDGYYGESTSGRCE 1593
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
1496-1611 |
8.17e-08 |
|
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: 52.76 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1496 PCHRKCSR--CSGPSENQCYTCprETFLLNTTCVKECPEGYHTDK---DSHQCVPCHSSC------RTCEGPHSMQCLSC 1564
Cdd:pfam14843 1 VCDPLCSSegCWGPGPDQCLSC--RNFSRGGTCVESCNILQGEPReyvVNSTCVPCHPEClpqngtATCSGPGADNCTKC 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958641647 1565 RPgwFQLGKECLLQCRDGYYGEST--------SGRCEKCDKSCKT-CRGPQPTDCQ 1611
Cdd:pfam14843 79 AH--FRDGPHCVSSCPSGVLGENDliwkyadaNGVCQPCHPNCTQgCTGPGLTGCP 132
|
|
| FU |
smart00261 |
Furin-like repeats; |
1540-1584 |
8.57e-08 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 50.20 E-value: 8.57e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 1540 SHQCVPCHSSCRTCEGPHSMQCLSCRPGWFQLGKECLLQCRDGYY 1584
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
674-1063 |
8.76e-08 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 56.52 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 674 SSCPPGH-FHADKKRCRKCAP----NCESCFGSHADQCLSCKYGYFLNEeTSSCVAQCpegsyQDIKKNICGKCSEN--- 745
Cdd:pfam03302 2 DECKPGYeLSADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYLTP-TSQCIDDC-----AKIGNYYYTTNANNkki 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 746 CKTCTGfHNCTECKGGLSLQgsrcsvTCEDGQFFSGHDCQPCHRFCATCAGAGADGCINCTEGYVMEegrcvqscsvsyY 825
Cdd:pfam03302 76 CKECTV-ANCKTCEDQGQCQ------ACNDGFYKSGDACSPCHESCKTCSGGTASDCTECLTGKALR------------Y 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 826 LDHSLEGgyksckRCDNSCLTCNGPGfkNCSSCpsgylldlgmcqmgaickdGEYIDEQGHCQICDAS--------CAKC 897
Cdd:pfam03302 137 GNDGTKG------TCGEGCTTGTGAG--ACKTC-------------------GLTIDGTSYCSECATEteypqngvCTST 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 898 WGPTQDDCISCPITrvfdDGRCvMNCPSWKFELKKQCHpchhtcQGCQGSGPSNCTSCKADKHGQEyflykgeclencPM 977
Cdd:pfam03302 190 AARATATCKASSVA----NGMC-SSCANGYFRMNGGCY------ETTKFPGKSVCEEANSGGTCQK------------EA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 978 GHYPAKGHACLPCPDNCELCYNPHVCSRCMSGYviVPTNHTCQKlecrqgefqdseygecmpCEEGCVGCTvDDPGACTS 1057
Cdd:pfam03302 247 PGYKLNNGDLVTCSPGCKTCTSNTVCTTCMDGY--VKTSDSCTK------------------CDSSCETCT-GATTTCKT 305
|
....*.
gi 1958641647 1058 CATGYY 1063
Cdd:pfam03302 306 CATGYY 311
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1397-1446 |
1.98e-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: 49.05 E-value: 1.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1397 PCHKNCLGCNGPKEDDCKACADtSKVLHNGLCLDECPKGTYKDEVNDECR 1446
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRH-GFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
1491-1535 |
3.41e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 48.27 E-value: 3.41e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 1491 SHRCQPCHRKCSRCSGPSENQCYTCPRETFLLNTTCVKECPEGYH 1535
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
781-825 |
5.20e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 47.89 E-value: 5.20e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 781 GHDCQPCHRFCATCAGAGADGCINCTEGYVMEEGRCVQSCSVSYY 825
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1496-1544 |
5.76e-07 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 47.90 E-value: 5.76e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958641647 1496 PCHRKCSRCSGPSENQCYTCPRETFLLNTTCVKECPEGYHTDKDSHQCV 1544
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1003-1324 |
5.85e-07 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 54.21 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1003 CSRCMSGYVIVPTNHTCQKLEcrqgefqdseygecmPCE-EGCVGCTVDDPGACTSCATGYYMFE-RHCYKACPEKTFGE 1080
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSA---------------PCKtENCKACSNDKREVCEECNSNNYLTPtSQCIDDCAKIGNYY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1081 KWECKACGTNCGSCDQHECYWCEEGfflssgSCVQDCDPGFYGDQElgECKPCHRACETCTGLGYNQCSSCPEGLQLWHG 1160
Cdd:pfam03302 66 YTTNANNKKICKECTVANCKTCEDQ------GQCQACNDGFYKSGD--ACSPCHESCKTCSGGTASDCTECLTGKALRYG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1161 T----------CIWPTWP--------HVEGKVWNEAVPTEKPSLVRSLPQDRRKWKVQIKRDAT--------------RQ 1208
Cdd:pfam03302 138 NdgtkgtcgegCTTGTGAgacktcglTIDGTSYCSECATETEYPQNGVCTSTAARATATCKASSvangmcsscangyfRM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1209 YQPCHSSCKTCNGSLCTSCPAGtylwlQACVPSCPQgtwLSVRSSSCEKCAEGCASCSGDDLCQRCLsqpsntlllhegr 1288
Cdd:pfam03302 218 NGGCYETTKFPGKSVCEEANSG-----GTCQKEAPG---YKLNNGDLVTCSPGCKTCTSNTVCTTCM------------- 276
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958641647 1289 cyhscpEGFYAKDGVCEHCSSPCKTCKGNATSCHSC 1324
Cdd:pfam03302 277 ------DGYVKTSDSCTKCDSSCETCTGATTTCKTC 306
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
690-739 |
7.88e-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: 7.88e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958641647 690 KCAPNCESCFGSHADQCLSCKYGYFLNEETssCVAQCPEGSYQDIKKNIC 739
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGT--CVSECPEGTYADTEGGVC 48
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
671-729 |
1.62e-06 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 48.20 E-value: 1.62e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958641647 671 ICVSSCPPGHF---HADKKRCRKC-APNCESCFGShaDQCLSCKYGYFLNEetSSCVAQCPEG 729
Cdd:pfam15913 34 VCLHSCPPGYFgirGQEVNRCTKCkAENCESCFSK--DFCTKCKEGFYLHK--GKCLDTCPEG 92
|
|
| FU |
smart00261 |
Furin-like repeats; |
685-731 |
1.88e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 46.35 E-value: 1.88e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958641647 685 KKRCRKCAPNCESCFGSHADQCLSCKYGYFLNEETssCVAQCPEGSY 731
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGK--CVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1393-1437 |
2.03e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 46.35 E-value: 2.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 1393 RQCVPCHKNCLGCNGPKEDDCKACAdTSKVLHNGLCLDECPKGTY 1437
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCK-HGFFLDGGKCVSECPPGTY 45
|
|
| Peptidases_S8_8 |
cd07492 |
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ... |
169-422 |
2.60e-06 |
|
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173817 [Multi-domain] Cd Length: 222 Bit Score: 50.41 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 169 VTILDDGIERTHPDLmqnyDALASCDVNGNDLDPMPRYD-ASNENKHGTRCAGEVAATANnshctvgiafNAKIGGVRML 247
Cdd:cd07492 4 VAVIDSGVDTDHPDL----GNLALDGEVTIDLEIIVVSAeGGDKDGHGTACAGIIKKYAP----------EAEIGSIKIL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 248 DGDVTDMVE--AKSVSY-NPQHVHIYSASWgpdddGKTVDGPAPLTRQAFENGVRMGRrglgsVFVWASGNGGRskdhcs 324
Cdd:cd07492 70 GEDGRCNSFvlEKALRAcVENDIRIVNLSL-----GGPGDRDFPLLKELLEYAYKAGG-----IIVAAAPNNND------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 325 cDGYTNSIYTISI---SSTAESGKKPWYLEECSSTlattyssgesyDKKIITTDLRQRCTDNHTGTSASAPMAAGIIALA 401
Cdd:cd07492 134 -IGTPPASFPNVIgvkSDTADDPKSFWYIYVEFSA-----------DGVDIIAPAPHGRYLTVSGNSFAAPHVTGMVALL 201
|
250 260
....*....|....*....|.
gi 1958641647 402 LEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07492 202 LSEKPDIDANDLKRLLQRLAV 222
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1205-1528 |
3.13e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 51.51 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1205 ATRQYQPCHSSCKTCNGSLCTSCPAgtylwlQACvPSCPQGTWLSVRSSSCEKCAE----GCASCSGDD-LCQRClsQPS 1279
Cdd:pfam03302 12 ADKTKCTSSAPCKTENCKACSNDKR------EVC-EECNSNNYLTPTSQCIDDCAKignyYYTTNANNKkICKEC--TVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1280 NTLLLHEGRCYHSCPEGFYAKDGVCEHCSSPCKTCKGNATS-CHSCEGDFVLDHG------VCWETCPEKhvAVEGVCKH 1352
Cdd:pfam03302 83 NCKTCEDQGQCQACNDGFYKSGDACSPCHESCKTCSGGTASdCTECLTGKALRYGndgtkgTCGEGCTTG--TGAGACKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1353 C------PERCQDCIHEKTCKE---CMPDFFLYNDMCHHSCPKNfypdmRQCVPCHKNCLGCNGpkeddckACADTSKVL 1423
Cdd:pfam03302 161 CgltidgTSYCSECATETEYPQngvCTSTAARATATCKASSVAN-----GMCSSCANGYFRMNG-------GCYETTKFP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1424 HNGLCLDECPKGTYKDEV------NDECRDCPESCLICSSAWTCLTCREGFTVVQDVCTApkecaaieywdvgshrcqpC 1497
Cdd:pfam03302 229 GKSVCEEANSGGTCQKEApgyklnNGDLVTCSPGCKTCTSNTVCTTCMDGYVKTSDSCTK-------------------C 289
|
330 340 350
....*....|....*....|....*....|.
gi 1958641647 1498 HRKCSRCSGpSENQCYTCPRETFLLNTTCVK 1528
Cdd:pfam03302 290 DSSCETCTG-ATTTCKTCATGYYKSGTGCVS 319
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
786-827 |
4.65e-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: 45.20 E-value: 4.65e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1958641647 786 PCHRFCATCAGAGADGCINCTEGYVMEEGRCVQSCSVSYYLD 827
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
|
|
| FU |
smart00261 |
Furin-like repeats; |
1642-1684 |
5.48e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.81 E-value: 5.48e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958641647 1642 TCERCHPTCDKCSGKEAWNCLSCVWSYHLLKGICTPECIVGEY 1684
Cdd:smart00261 3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1594-1644 |
6.37e-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: 6.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958641647 1594 KCDKSCKTCRGPQPTDCQSCDTFFFLLrsKGQCHLACPEHYYADQHAQTCE 1644
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLD--GGTCVSECPEGTYADTEGGVCL 49
|
|
| Peptidases_S8_Lantibiotic_specific_protease |
cd07482 |
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ... |
166-409 |
7.84e-06 |
|
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173808 [Multi-domain] Cd Length: 294 Bit Score: 49.67 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 166 NIVVTILDDGIERTHPDLMQNYdalascDVNGNDLDPMPRYDASNE------------NKHGTRCAGEVAATANNShctv 233
Cdd:cd07482 1 KVTVAVIDSGIDPDHPDLKNSI------SSYSKNLVPKGGYDGKEAgetgdindivdkLGHGTAVAGQIAANGNIK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 234 GIAFNAKIGGVRMLD----GDVTDMVEAKSVSYNpQHVHIYSASWGPDDDGKTVDGPAPLTRQAFENGVRMGRRGlGSVF 309
Cdd:cd07482 71 GVAPGIGIVSYRVFGscgsAESSWIIKAIIDAAD-DGVDVINLSLGGYLIIGGEYEDDDVEYNAYKKAINYAKSK-GSIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 310 VWASGNGGRS-------KDHCSCDGY--TNSIY---------TISISSTAESGkkpwYLEECSS------TLAT---TYS 362
Cdd:cd07482 149 VAAAGNDGLDvsnkqelLDFLSSGDDfsVNGEVydvpaslpnVITVSATDNNG----NLSSFSNygnsriDLAApggDFL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958641647 363 SGESYDK------------KIITTDLRQrCTDNHTGTSASAPMAAGIIALALEANPFLT 409
Cdd:cd07482 225 LLDQYGKekwvnnglmtkeQILTTAPEG-GYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1211-1256 |
1.05e-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: 44.43 E-value: 1.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958641647 1211 PCHSSCKTCNGSL---CTSCPAGTYLWLQACVPSCPQGTWLSVRSSSCE 1256
Cdd:cd00064 1 PCHPSCATCTGPGpdqCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| FU |
smart00261 |
Furin-like repeats; |
885-928 |
1.09e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.04 E-value: 1.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958641647 885 GHCQICDASCAKCWGPTQDDCISCPITRVFDDGRCVMNCPSWKF 928
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
1237-1305 |
1.18e-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: 45.88 E-value: 1.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958641647 1237 ACVPSCPQGtWLSVRSSSCEKC----AEGCASCSGDDLCQRCLSQpsntLLLHEGRCYHSCPEGFYAKDGVCE 1305
Cdd:pfam15913 34 VCLHSCPPG-YFGIRGQEVNRCtkckAENCESCFSKDFCTKCKEG----FYLHKGKCLDTCPEGTAAQNSTME 101
|
|
| FU |
smart00261 |
Furin-like repeats; |
1589-1635 |
1.29e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.04 E-value: 1.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958641647 1589 SGRCEKCDKSCKTCRGPQPTDCQSCDTFFFLLrsKGQCHLACPEHYY 1635
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLD--GGKCVSECPPGTY 45
|
|
| Peptidases_S8_11 |
cd04843 |
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ... |
152-402 |
1.35e-05 |
|
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173792 Cd Length: 277 Bit Score: 48.85 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 152 MNIEGAWKR-GYTGKNIVVTILDDGIERTHPDLMQNydaLAScdvngndldPMPRYDASNENKHGTRCAGEVAATANNSH 230
Cdd:cd04843 2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGN---GIT---------LISGLTDQADSDHGTAVLGIIVAKDNGIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 231 CTvGIAFNAKIGGV-----------------RMLDGDVTdMVEAK----SVSYNPQHVHIYSASWGPdddgktvdgpapl 289
Cdd:cd04843 70 VT-GIAHGAQAAVVsstrvsntadaildaadYLSPGDVI-LLEMQtggpNNGYPPLPVEYEQANFDA------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 290 TRQAFENGVrmgrrglgsVFVWASGNGGRSKDHCS-CDGYTNSIYTISIS---------STAESGKKPWyleeCSSTLAT 359
Cdd:cd04843 135 IRTATDLGI---------IVVEAAGNGGQDLDAPVyNRGPILNRFSPDFRdsgaimvgaGSSTTGHTRL----AFSNYGS 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958641647 360 ---TYSSGE-----SYDKKIITTDLRQRCTDNHTGTSASAPMAAGiiALAL 402
Cdd:cd04843 202 rvdVYGWGEnvtttGYGDLQDLGGENQDYTDSFSGTSSASPIVAG--AAAS 250
|
|
| FU |
smart00261 |
Furin-like repeats; |
931-980 |
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 50
....*....|....*....|....*....|....*....|....*....|
gi 1958641647 931 KKQCHPCHHTCQGCQGSGPSNCTSCKADkhgqeYFLYKGECLENCPMGHY 980
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHG-----FFLDGGKCVSECPPGTY 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1579-1725 |
1.70e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 49.20 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1579 CRDGYYGESTSGRCEKCDK----SCKTCRGPQPTDCQSCDTFFFLLRSKgQCHLACPEhyYADQHAQTCERCHPTCDKCs 1654
Cdd:pfam03302 4 CKPGYELSADKTKCTSSAPckteNCKACSNDKREVCEECNSNNYLTPTS-QCIDDCAK--IGNYYYTTNANNKKICKEC- 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958641647 1655 gkEAWNCLSCVwsyhllKGICTPECIVGEYRDGKgenfNCKKCHESCMECKGPGSKNCTGCSAGLLLQMDD 1725
Cdd:pfam03302 80 --TVANCKTCE------DQGQCQACNDGFYKSGD----ACSPCHESCKTCSGGTASDCTECLTGKALRYGN 138
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
712-1006 |
1.77e-05 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 49.91 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 712 GYFLNEETSSCVAQCPEGSYQDiKKNICGKCSENC---------KTCTGFHN--CTECKGGLSLQGSRCSVTCEDGQFFS 780
Cdd:PTZ00214 350 GYLCGDATNGGVSGCATCGYNS-GAVTCTRCSAGYlgvdgkscsESCSGDTRgvCTKVAEGSESTEVSCRCVCKPTFYNS 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 781 GHDCQPCHRFCATCAGAGADGCINCTEGYVM-------EEGRCVQSCSVSyylDHSLE-----GGYKSCKRC-DNSCLTC 847
Cdd:PTZ00214 429 SGTCTPCTDSCAVCKDGTPTGCQQCSPGKILefsivssESADCVDQCSVG---SECAEcgitiDGSRYCTRCkDASTYPF 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 848 NGPGFKN--------------CSSCPSGYLLDLGMCQMGAICKDGEYIDEQghcqicdaSCAKCWGPTQDDCIScpitrv 913
Cdd:PTZ00214 506 NGVCIPNtqrdayctstangaCTTCSGAAFLMNGGCYTTEHYPGSTICDKQ--------SNGKCTTTKKGYGIS------ 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 914 fDDGRCVmncpswkfelkkQCHPchhTCQGCQGSGPSNCTSCKADK-HGQEYFLYKGECLE--NCPMGHYpAKGHACLPC 990
Cdd:PTZ00214 572 -PDGKLL------------ECDP---TCLACTAPGPGRCTRCPSDKlLKRASGAATGSCVDpgACVDGYY-ADGDACLPC 634
|
330
....*....|....*..
gi 1958641647 991 PD-NCELCYNPHVCSRC 1006
Cdd:PTZ00214 635 ATpGCKTCGHASFCTEC 651
|
|
| Peptidases_S53_like |
cd05562 |
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ... |
383-455 |
1.93e-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: 1.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958641647 383 NHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIvrTSRAGHLNANDWktnaagfkvSHLYGFGLMDAEAMV 455
Cdd:cd05562 212 NFFGTSAAAPHAAGVAALVLSANPGLTPADIRDAL--RSTALDMGEPGY---------DNASGSGLVDADRAV 273
|
|
| FU |
smart00261 |
Furin-like repeats; |
1128-1163 |
2.02e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 43.27 E-value: 2.02e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1958641647 1128 GECKPCHRACETCTGLGYNQCSSCPEGLQLWHGTCI 1163
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCV 37
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
936-981 |
2.54e-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: 2.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958641647 936 PCHHTCQGCQGSGPSNCTSCKADkhgqeYFLYKGECLENCPMGHYP 981
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHG-----FYLDGGTCVSECPEGTYA 41
|
|
| FU |
smart00261 |
Furin-like repeats; |
1035-1078 |
3.18e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 42.88 E-value: 3.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958641647 1035 GECMPCEEGCVGCTVDDPGACTSCATGYYMFERHCYKACPEKTF 1078
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
786-906 |
4.74e-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: 45.06 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 786 PCHRFC--ATCAGAGADGCINCTegYVMEEGRCVQSCSVSYYLDHSLEGGyKSCKRCDNSCL------TCNGPGFKNC-- 855
Cdd:pfam14843 1 VCDPLCssEGCWGPGPDQCLSCR--NFSRGGTCVESCNILQGEPREYVVN-STCVPCHPECLpqngtaTCSGPGADNCtk 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958641647 856 -----------SSCPSGYlldlgmcqMGAICKDGEYIDEQGHCQICDASCAK-CWGPTQDDCI 906
Cdd:pfam14843 78 cahfrdgphcvSSCPSGV--------LGENDLIWKYADANGVCQPCHPNCTQgCTGPGLTGCP 132
|
|
| FU |
smart00261 |
Furin-like repeats; |
1210-1247 |
4.75e-05 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 42.50 E-value: 4.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958641647 1210 QPCHSSCKTCNGSL---CTSCPAGTYLWLQACVPSCPQGTW 1247
Cdd:smart00261 5 KPCHPECATCTGPGpddCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| Furin-like |
pfam00757 |
Furin-like cysteine rich region; |
1350-1438 |
9.63e-05 |
|
Furin-like cysteine rich region;
Pssm-ID: 395614 [Multi-domain] Cd Length: 143 Bit Score: 44.35 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1350 CKHCPERCQDCIHEKTCKECmpdfFLYND---MCHHSCPKNFYPDmRQCvpCHKNCLG-CNGPKEDDCKACadtSKVLHN 1425
Cdd:pfam00757 5 GDVCPGTMEKCHSCCNNGYC----WGPGHcqkVCPEQCKKRCTKP-GEC--CHEQCLGgCTGPNDSDCLAC---RHFNDE 74
|
90
....*....|...
gi 1958641647 1426 GLCLDECPKGTYK 1438
Cdd:pfam00757 75 GTCVDQCPPGTYQ 87
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1646-1689 |
9.88e-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: 41.74 E-value: 9.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958641647 1646 CHPTCDKCSGKEAWNCLSCVWSYHLLKGICTPECIVGEYRDGKG 1689
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEG 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
844-1154 |
1.02e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 46.89 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 844 CLTCNGPGFKNCSSCPSGYLLDLGMCQMGAICKDGEYideqgHCQICDASCAKCWGPTQDDCISCpitrvfDDGRCVMNC 923
Cdd:pfam03302 28 CKACSNDKREVCEECNSNNYLTPTSQCIDDCAKIGNY-----YYTTNANNKKICKECTVANCKTC------EDQGQCQAC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 924 PSWKFELKKQCHPCHHTCQGCQGSGPSNCTSC---KADKHGQEYflYKGECLENCPMGHYPAKGHACLPCPDNCELCynp 1000
Cdd:pfam03302 97 NDGFYKSGDACSPCHESCKTCSGGTASDCTECltgKALRYGNDG--TKGTCGEGCTTGTGAGACKTCGLTIDGTSYC--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1001 hvcSRCmSGYVIVPTNHTCQKLECRQGEFqdseygecmpceegCVGCTVDDpGACTSCATGYYMFERHCYKA-------- 1072
Cdd:pfam03302 172 ---SEC-ATETEYPQNGVCTSTAARATAT--------------CKASSVAN-GMCSSCANGYFRMNGGCYETtkfpgksv 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1073 CPEKTFGEKWECKACGTNCGSCDQHECywCEEGFFLSSGSCVQDCDPGFYGDQelGECKPCHRACETCTGlGYNQCSSCP 1152
Cdd:pfam03302 233 CEEANSGGTCQKEAPGYKLNNGDLVTC--SPGCKTCTSNTVCTTCMDGYVKTS--DSCTKCDSSCETCTG-ATTTCKTCA 307
|
..
gi 1958641647 1153 EG 1154
Cdd:pfam03302 308 TG 309
|
|
| FU |
smart00261 |
Furin-like repeats; |
835-880 |
1.46e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 40.96 E-value: 1.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958641647 835 KSCKRCDNSCLTCNGPGFKNCSSCPSGYLLDLGMCQmgAICKDGEY 880
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCV--SECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
637-681 |
2.20e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 40.57 E-value: 2.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 637 PCDPECSevGCDGPGPDHCTDCLHYHYKLKNntrICVSSCPPGHF 681
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 ... |
637-687 |
2.83e-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: 2.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958641647 637 PCDPECSevGCDGPGPDHCTDCLHYHYklkNNTRICVSSCPPGHFHADKKR 687
Cdd:cd00064 1 PCHPSCA--TCTGPGPDQCTSCRHGFY---LDGGTCVSECPEGTYADTEGG 46
|
|
| FU |
smart00261 |
Furin-like repeats; |
1301-1343 |
3.60e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 39.80 E-value: 3.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958641647 1301 DGVCEHCSSPCKTCKG-NATSCHSCEGDFVLDHGVCWETCPEKH 1343
Cdd:smart00261 1 DGECKPCHPECATCTGpGPDDCTSCKHGFFLDGGKCVSECPPGT 44
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
1595-1712 |
3.74e-04 |
|
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).
Pssm-ID: 464344 [Multi-domain] Cd Length: 132 Bit Score: 42.36 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1595 CDKSCKT--CRGPQPTDCQSCDTFFFllrsKGQCHLACPEHYYAD---QHAQTCERCHPTCDK------CSGKEAWNCLS 1663
Cdd:pfam14843 2 CDPLCSSegCWGPGPDQCLSCRNFSR----GGTCVESCNILQGEPreyVVNSTCVPCHPECLPqngtatCSGPGADNCTK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1664 CVwsyHLLKGI-CTPEC---------IVGEYRDGKGEnfnCKKCHESCME-CKGPGSKNC 1712
Cdd:pfam14843 78 CA---HFRDGPhCVSSCpsgvlgendLIWKYADANGV---CQPCHPNCTQgCTGPGLTGC 131
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1132-1163 |
4.54e-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: 4.54e-04
10 20 30
....*....|....*....|....*....|..
gi 1958641647 1132 PCHRACETCTGLGYNQCSSCPEGLQLWHGTCI 1163
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCV 32
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
890-929 |
5.16e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 39.42 E-value: 5.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958641647 890 CDASCAKCWGPTQDDCISCPITRVFDDGRCVMNCPSWKFE 929
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYA 41
|
|
| Furin-like |
pfam00757 |
Furin-like cysteine rich region; |
638-746 |
5.64e-04 |
|
Furin-like cysteine rich region;
Pssm-ID: 395614 [Multi-domain] Cd Length: 143 Bit Score: 42.04 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 638 CDPECSEvGCDGPGPDHCTDCLHYhyklkNNTRICVSSCPPGHFHADkkrcRKCApNCESCFGSHADQClsckygYFLNE 717
Cdd:pfam00757 49 CHEQCLG-GCTGPNDSDCLACRHF-----NDEGTCVDQCPPGTYQFG----WRCV-TFKECPKSHLPGY------NPLVI 111
|
90 100 110
....*....|....*....|....*....|
gi 1958641647 718 ETSSCVAQCPEGSYQDIKKNI-CGKCSENC 746
Cdd:pfam00757 112 HNGECVRECPSGYTEVENNSRkCEPCEGLC 141
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1039-1085 |
7.00e-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: 7.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958641647 1039 PCEEGCVGCTVDDPGACTSCATGYYMFERHCYKACPEKTFG--EKWECK 1085
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAdtEGGVCL 49
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
840-886 |
7.35e-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: 39.04 E-value: 7.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958641647 840 CDNSCLTCNGPGFKNCSSCPSGYLLDLGMCQmgAICKDGEYIDEQGH 886
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCV--SECPEGTYADTEGG 46
|
|
| FU |
smart00261 |
Furin-like repeats; |
1694-1737 |
8.82e-04 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 38.64 E-value: 8.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958641647 1694 CKKCHESCMECKGPGSKNCTGCSAGLLLqmDDSRCLRCCNASHP 1737
Cdd:smart00261 4 CKPCHPECATCTGPGPDDCTSCKHGFFL--DGGKCVSECPPGTY 45
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
687-822 |
9.99e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 43.86 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 687 RCRKCAPNCESCFGSHADQCLSCKYGYFLNEETSSCVAQCPEGSYQDIKKNICGKCSENCKTCTGFHNCTECKGGLSLQG 766
Cdd:COG4624 2 LLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958641647 767 SRCSVTCEDGqffSGHDCQPCHRFCATCAGAGADG--------CINCtegyvmeeGRCVQSCSV 822
Cdd:COG4624 82 RGPSIIRDKE---KCKNCYPCVRACPVKAIKVDDGkaeideekCISC--------GQCVAVCPF 134
|
|
| FU |
smart00261 |
Furin-like repeats; |
736-778 |
2.06e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 37.87 E-value: 2.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 736 KNICGKCSENCKTCTG--FHNCTECKGGLSLQGSRCSVTCEDGQF 778
Cdd:smart00261 1 DGECKPCHPECATCTGpgPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
1214-1590 |
2.21e-03 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 42.98 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1214 SSCKTCN----GSLCTSCPAGtylwlqacvpscpqgtWLSVRSSSCEKcaegcaSCSGDD--LCQRCLSQPSNTlllhEG 1287
Cdd:PTZ00214 362 SGCATCGynsgAVTCTRCSAG----------------YLGVDGKSCSE------SCSGDTrgVCTKVAEGSEST----EV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1288 RCYHSCPEGFYAKDGVCEHCSSPCKTCK-GNATSCHSCEGDFVLDHGVcwetcpekhvavegVCKHCPERCQDCIHEKTC 1366
Cdd:PTZ00214 416 SCRCVCKPTFYNSSGTCTPCTDSCAVCKdGTPTGCQQCSPGKILEFSI--------------VSSESADCVDQCSVGSEC 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1367 KECmpdfflyndmchhscpknfypdmrqcvpchknclGCNGPKEDDCKACADTSKVLHNGLCLDECPKGTY-KDEVNDEC 1445
Cdd:PTZ00214 482 AEC----------------------------------GITIDGSRYCTRCKDASTYPFNGVCIPNTQRDAYcTSTANGAC 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1446 RDCPESCLICSSAWTCLTCREGFTVVQDVCTAPKECAAIEYWDVGSHRCQPCHRKCSRCSGPSENQCYTCPRETFLLNTT 1525
Cdd:PTZ00214 528 TTCSGAAFLMNGGCYTTEHYPGSTICDKQSNGKCTTTKKGYGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKLLKRAS 607
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958641647 1526 ------CVK--ECPEGYHTDKDShqCVPCHS-SCRTCegPHSMQCLSCRPGWFQL--GKECLLQCR-DGYYGESTSG 1590
Cdd:PTZ00214 608 gaatgsCVDpgACVDGYYADGDA--CLPCATpGCKTC--GHASFCTECAGELFVSldGQSCLEECTgDKVVGEVSGG 680
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
695-776 |
3.93e-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: 38.57 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 695 CESCfgSHADQCLSCKYGYFL------NEETSSCVAQCPEGSY----QDIKKniCGKC-SENCKTCTGFHNCTECKGGLS 763
Cdd:pfam15913 4 CVLC--SEENGCLTCQPRLFLllerngIRQYGVCLHSCPPGYFgirgQEVNR--CTKCkAENCESCFSKDFCTKCKEGFY 79
|
90
....*....|...
gi 1958641647 764 LQGSRCSVTCEDG 776
Cdd:pfam15913 80 LHKGKCLDTCPEG 92
|
|
| FU |
smart00261 |
Furin-like repeats; |
1081-1122 |
7.06e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 36.33 E-value: 7.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 1081 KWECKACGTNCGSC---DQHECYWCEEGFFLSSGSCVQDCDPGFY 1122
Cdd:smart00261 1 DGECKPCHPECATCtgpGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1347-1389 |
9.03e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 35.95 E-value: 9.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958641647 1347 EGVCKHCPERCQDCIH--EKTCKECMPDFFLYNDMCHHSCPKNFY 1389
Cdd:smart00261 1 DGECKPCHPECATCTGpgPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| Furin-like |
pfam00757 |
Furin-like cysteine rich region; |
1206-1311 |
9.46e-03 |
|
Furin-like cysteine rich region;
Pssm-ID: 395614 [Multi-domain] Cd Length: 143 Bit Score: 38.57 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958641647 1206 TRQYQPCHSSC-KTCNGSLCTSCPAGTYLWLQ-ACVPSCPQGTWlsvrssscekcaEGCASCSGDDLCQRCLSQPSNTLL 1283
Cdd:pfam00757 43 TKPGECCHEQClGGCTGPNDSDCLACRHFNDEgTCVDQCPPGTY------------QFGWRCVTFKECPKSHLPGYNPLV 110
|
90 100 110
....*....|....*....|....*....|.
gi 1958641647 1284 LHEGRCYHSCPEGFYAKDGV---CEHCSSPC 1311
Cdd:pfam00757 111 IHNGECVRECPSGYTEVENNsrkCEPCEGLC 141
|
|
| |
