|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidases_S8_Protein_convertases_Kexins_Furin-lik |
cd04059 |
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ... |
128-422 |
1.61e-164 |
|
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: 490.53 E-value: 1.61e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 128 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 206
Cdd:cd04059 1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 207 DasNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGP 286
Cdd:cd04059 81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 287 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 365
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006568 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 |
5.33e-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: 5.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNG----NDLDPMPRYDASNENKHGTRCAGEVAATANNSHCTVGIAFNA 239
Cdd:pfam00082 1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEAsvdfNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 240 KIGGVRML-DGDVTDMVEAKSVSYN-PQHVHIYSASWGPDddgKTVDGPAPLTRQAFENGvrmGRRGLGSVFVWASGNGG 317
Cdd:pfam00082 81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 318 RSKDHCSCDGY-TNSIYTISISSTaesgkkpwylEECSSTLATTYSS----------------GESY-------DKKIIT 373
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAV----------DEASEGNLASFSSygptldgrlkpdivapGGNItggnissTLLTTT 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 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 |
6.42e-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: 6.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 507 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 586
Cdd:pfam01483 1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75
|
90
....*....|.
gi 569006568 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 |
4.25e-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: 4.25e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006568 40 HWAVKIAGGFAEADRIASKYGFINVGQIGALKDYYHFYHSRTIKRSVLSSRGTHSFISMEPKVEWIQQQVVKKRTKR 116
Cdd:pfam16470 1 EWAVHLEGGPEEADRIAEKHGFINLGQIGGLEDYYHFRHRRVSKRSKRSLRHKHSRLKKDPKVKWAEQQRGKKRVKR 77
|
|
| AprE |
COG1404 |
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
156-422 |
2.09e-34 |
|
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 138.31 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 156 GAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCdVNGNDldpmpryDASNENKHGTRCAGEVAATANNSHCTVGI 235
Cdd:COG1404 100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDF-VDGDG-------DPSDDNGHGTHVAGIIAANGNNGGGVAGV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 236 AFNAKIGGVRMLD----GDVTDMVEA--KSVSynpQHVHIYSASWGPDDDGKTvdgpaPLTRQAFENGvrmgrRGLGSVF 309
Cdd:COG1404 172 APGAKLLPVRVLDdngsGTTSDIAAAidWAAD---NGADVINLSLGGPADGYS-----DALAAAVDYA-----VDKGVLV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 310 VWASGNGGRSkdhCSCDGYTNSIY-TISISSTAESGKKPWYleecSSTlattyssGESYD-----KKIITTDLRQRcTDN 383
Cdd:COG1404 239 VAAAGNSGSD---DATVSYPAAYPnVIAVGAVDANGQLASF----SNY-------GPKVDvaapgVDILSTYPGGG-YAT 303
|
250 260 270
....*....|....*....|....*....|....*....
gi 569006568 384 HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:COG1404 304 LSGTSMAAPHVAGAAALLLSANPDLTPAQVRAILLNTAT 342
|
|
| COG4935 |
COG4935 |
Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ... |
508-599 |
3.65e-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: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 508 EHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLfdHSMEGFkNWEFMTIHCWGERAAGDWVLEVYDTPSQlrnfkTP 587
Cdd:COG4935 558 EDVTVTVDITHTYRGDLVITLISPDGTTVVLKNRSG--GSADNI-NATFDVANFSGESANGTWTLRVVDTAGG-----DT 629
|
90
....*....|..
gi 569006568 588 GKLKEWSLVLYG 599
Cdd:COG4935 630 GTLNSWSLTFTG 641
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
637-746 |
6.18e-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: 64.32 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 637 PCDPECSEVGCDGPGPDHCSDCLHYyyklkNNTRICVSSCP-----PGHYhADKKRCRKCAPNCE------SCFGSHGNQ 705
Cdd:pfam14843 1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNilqgePREY-VVNSTCVPCHPECLpqngtaTCSGPGADN 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 569006568 706 CLSCKYgyflNEETSSCVTQCPDGSYEDI--------KKNVCGKCSENC 746
Cdd:pfam14843 75 CTKCAH----FRDGPHCVSSCPSGVLGENdliwkyadANGVCQPCHPNC 119
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
706-1063 |
5.23e-11 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 66.15 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 706 CLSCKYGYFLNEETSSCVTQcpdgsyedikknvcGKC-SENCKACI--GFHNCTECKGGLSL-QGSRCSVTCEDGQFFNG 781
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSS--------------APCkTENCKACSndKREVCEECNSNNYLtPTSQCIDDCAKIGNYYY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 782 HDCQPCHRFCATCSGAGADGCinctegyvmEEGRCVQSCSVSYYLDHsseggyKSCKRCDNSCLTCNGPGFKNCSSCPSG 861
Cdd:pfam03302 67 TTNANNKKICKECTVANCKTC---------EDQGQCQACNDGFYKSG------DACSPCHESCKTCSGGTASDCTECLTG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 862 YLLDLGT--------------CQMGAICKDGEYIDDQGHCQTCEAS--------CAKCWGPTQEDCISCPVTrvldDGRC 919
Cdd:pfam03302 132 KALRYGNdgtkgtcgegcttgTGAGACKTCGLTIDGTSYCSECATEteypqngvCTSTAARATATCKASSVA----NGMC 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 920 vMNCPSWKFEFKKQCHpchytcQGCQGSGPSNCTSCRADKHGQErflyhgeclencPVGHYPAKGHACLPCPDNCELCYN 999
Cdd:pfam03302 208 -SSCANGYFRMNGGCY------ETTKFPGKSVCEEANSGGTCQK------------EAPGYKLNNGDLVTCSPGCKTCTS 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 1000 PHVCSRCMSGYViiPPNHTCQKlecrqgefqdseyeecmpCEEGCLGCTeDDPGACTSCATGYY 1063
Cdd:pfam03302 269 NTVCTTCMDGYV--KTSDSCTK------------------CDSSCETCT-GATTTCKTCATGYY 311
|
|
| PTZ00262 |
PTZ00262 |
subtilisin-like protease; Provisional |
169-413 |
1.94e-09 |
|
subtilisin-like protease; Provisional
Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 61.91 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 169 VTILDDGIERTHPDLMQNY---------------------DALASCDVNGNDLDPMprydasNENKHGTRCAGEVAATAN 227
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM------DDNYHGTHVSGIISAIGN 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 228 NSHCTVGIAFNAKIGGVRMLD----GDVTDMVeaKSVSY-NPQHVHIYSASWGPDDDGKTvdgpapltrqaFENGVRMGR 302
Cdd:PTZ00262 394 NNIGIVGVDKRSKLIICKALDshklGRLGDMF--KCFDYcISREAHMINGSFSFDEYSGI-----------FNESVKYLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 303 RgLGSVFVWASGN----GGRSKDHCSCDGYTNSIYTISISSTAES---------GKKPWYLEECSSTLATTYSSGESYDK 369
Cdd:PTZ00262 461 E-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYPPILSKKLRNvitvsnlikDKNNQYSLSPNSFYSAKYCQLAAPGT 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 569006568 370 KIITTDLRQRCTDNhTGTSASAPMAAGIIALALEANPFLTWRDV 413
Cdd:PTZ00262 540 NIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
|
|
| FU |
smart00261 |
Furin-like repeats; |
781-825 |
8.10e-09 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 52.51 E-value: 8.10e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 569006568 781 GHDCQPCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYY 825
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
690-739 |
4.73e-08 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 50.60 E-value: 4.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569006568 690 KCAPNCESCFGSHGNQCLSCKYGYFLNEETssCVTQCPDGSYEDIKKNVC 739
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGT--CVSECPEGTYADTEGGVC 48
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
712-1114 |
5.97e-08 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 57.23 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 712 GYFLNEETSSCVTQCPDGSYEDiKKNVCGKCSENC---------KACIGFHN--CTECKGGLSLQGSRCSVTCEDGQFFN 780
Cdd:PTZ00214 350 GYLCGDATNGGVSGCATCGYNS-GAVTCTRCSAGYlgvdgkscsESCSGDTRgvCTKVAEGSESTEVSCRCVCKPTFYNS 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 781 GHDCQPCHRFCATCSGAGADGCINCTEGYVM-------EEGRCVQSCSVSyylDHSSE-----GGYKSCKRC-DNSCLTC 847
Cdd:PTZ00214 429 SGTCTPCTDSCAVCKDGTPTGCQQCSPGKILefsivssESADCVDQCSVG---SECAEcgitiDGSRYCTRCkDASTYPF 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 848 NGPGFKNcsscpsgylldlgtCQMGAICKDGEyiddQGHCQTCEASCAKCWGP--TQEDCISCPVTRVLDDGRCVMNCPS 925
Cdd:PTZ00214 506 NGVCIPN--------------TQRDAYCTSTA----NGACTTCSGAAFLMNGGcyTTEHYPGSTICDKQSNGKCTTTKKG 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 926 WKFEFKKQCHPCHYTCQGCQGSGPSNCTSCRADK-HGQERFLYHGECLE-NCPVGHYPAKGHACLPCPD-NCELCYNPHV 1002
Cdd:PTZ00214 568 YGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKlLKRASGAATGSCVDpGACVDGYYADGDACLPCATpGCKTCGHASF 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1003 CSRCMSGYVIIPPNHTC-----------------QKLECRQGEFQDSEYEECMPCEE------GCLGCteDDPGACTSCA 1059
Cdd:PTZ00214 648 CTECAGELFVSLDGQSCleectgdkvvgevsggvRRCWCERGFLPALDRSGCVLPTEcppdmpSCAAC--DESGRCLLCV 725
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 569006568 1060 TGYYmferhcykacpektfGVKWECRACGTNCG---SCDQHECYwCEEGFFLSGGSCV 1114
Cdd:PTZ00214 726 TSGH---------------NVQVDQRTCAEGCGaraSSNQGVCM-CELDAVLTKGVCV 767
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
786-827 |
7.43e-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: 49.82 E-value: 7.43e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 569006568 786 PCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYYLD 827
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
|
|
| FU |
smart00261 |
Furin-like repeats; |
685-731 |
5.01e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 47.50 E-value: 5.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 569006568 685 KKRCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETssCVTQCPDGSY 731
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGK--CVSECPPGTY 45
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1003-1161 |
6.28e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 49.97 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1003 CSRCMSGYVIIPPNHTCQKLEcrqgefqdseyeecmPCE-EGCLGCTEDDPGACTSCATGYYMFE-RHCYKACPE----- 1075
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSA---------------PCKtENCKACSNDKREVCEECNSNNYLTPtSQCIDDCAKignyy 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1076 --KTFGVKWECRACGT-NCGSC-DQHECYWCEEGFFLSGGscvqdcgpgfhgdqelgECKPCHRACENCTGSGYNQCSSC 1151
Cdd:pfam03302 66 ytTNANNKKICKECTVaNCKTCeDQGQCQACNDGFYKSGD-----------------ACSPCHESCKTCSGGTASDCTEC 128
|
170
....*....|
gi 569006568 1152 QEGLQLWHGT 1161
Cdd:pfam03302 129 LTGKALRYGN 138
|
|
| FU |
smart00261 |
Furin-like repeats; |
1128-1165 |
6.82e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.04 E-value: 6.82e-06
10 20 30
....*....|....*....|....*....|....*...
gi 569006568 1128 GECKPCHRACENCTGSGYNQCSSCQEGLQLWHGTCLWS 1165
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSE 39
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
687-822 |
3.65e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 47.71 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 687 RCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETSSCVTQCPDGSYEDIKKNVCGKCSENCKACIGFHNCTECKGGLSLQG 766
Cdd:COG4624 2 LLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 767 SRCSVTCEDGqffNGHDCQPCHRFCATCSGAGADG--------CINCtegyvmeeGRCVQSCSV 822
Cdd:COG4624 82 RGPSIIRDKE---KCKNCYPCVRACPVKAIKVDDGkaeideekCISC--------GQCVAVCPF 134
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1132-1163 |
1.07e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 40.97 E-value: 1.07e-04
10 20 30
....*....|....*....|....*....|..
gi 569006568 1132 PCHRACENCTGSGYNQCSSCQEGLQLWHGTCL 1163
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCV 32
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidases_S8_Protein_convertases_Kexins_Furin-lik |
cd04059 |
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ... |
128-422 |
1.61e-164 |
|
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: 490.53 E-value: 1.61e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 128 FNDPKWPSMWYMHCSD-NTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRY 206
Cdd:cd04059 1 PNDPLFPYQWYLKNTGqAGGTPGLDLNVTPAWEQGITGKGVTVAVVDDGLEITHPDLKDNYDPEASYDFNDNDPDPTPRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 207 DasNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGP 286
Cdd:cd04059 81 D--DDNSHGTRCAGEIAAVGNNGICGVGVAPGAKLGGIRMLDGDVTDVVEAESLGLNPDYIDIYSNSWGPDDDGKTVDGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 287 APLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGE- 365
Cdd:cd04059 159 GPLAQRALENGVTNGRNGKGSIFVWAAGNGGNLGDNCNCDGYNNSIYTISVSAVTANGVRASYSEVGSSVLASAPSGGSg 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006568 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 |
5.33e-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: 5.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNG----NDLDPMPRYDASNENKHGTRCAGEVAATANNSHCTVGIAFNA 239
Cdd:pfam00082 1 GKGVVVAVLDTGIDPNHPDLSGNLDNDPSDDPEAsvdfNNEWDDPRDDIDDKNGHGTHVAGIIAAGGNNSIGVSGVAPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 240 KIGGVRML-DGDVTDMVEAKSVSYN-PQHVHIYSASWGPDddgKTVDGPAPLTRQAFENGvrmGRRGLGSVFVWASGNGG 317
Cdd:pfam00082 81 KILGVRVFgDGGGTDAITAQAISWAiPQGADVINMSWGSD---KTDGGPGSWSAAVDQLG---GAEAAGSLFVWAAGNGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 318 RSKDHCSCDGY-TNSIYTISISSTaesgkkpwylEECSSTLATTYSS----------------GESY-------DKKIIT 373
Cdd:pfam00082 155 PGGNNGSSVGYpAQYKNVIAVGAV----------DEASEGNLASFSSygptldgrlkpdivapGGNItggnissTLLTTT 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 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 |
6.42e-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: 6.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 507 LEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTpsqlrNFKT 586
Cdd:pfam01483 1 LEHVQVSVNITHTRRGDLRITLTSPSGTRSVLLNRRGGDTSSAGFLDWTFMSVHHWGERAEGTWTLEVTDT-----APGD 75
|
90
....*....|.
gi 569006568 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 |
4.25e-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: 4.25e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569006568 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 |
8.56e-36 |
|
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: 8.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 167 IVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPmprydaSNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRM 246
Cdd:cd07498 1 VVVAIIDTGVDLNHPDLSGKPKLVPGWNFVSNNDPT------SDIDGHGTACAGVAAAVGNNGLGVAGVAPGAKLMPVRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 247 LDGD--VTDMVEAKSVSYNPQH-VHIYSASWGPDDdgktvdgPAPLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDhc 323
Cdd:cd07498 75 ADSLgyAYWSDIAQAITWAADNgADVISNSWGGSD-------STESISSAIDNAATYGRNGKGGVVLFAAGNSGRSVS-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 324 scDGYTNSIYTISISSTAESGKKPWY--------LEECSSTLATTYSSGESydkkiiTTDLRQRCTDNHTGTSASAPMAA 395
Cdd:cd07498 146 --SGYAANPSVIAVAATDSNDARASYsnygnyvdLVAPGVGIWTTGTGRGS------AGDYPGGGYGSFSGTSFASPVAA 217
|
250 260
....*....|....*....|....*
gi 569006568 396 GIIALALEANPFLTWRDVQHVIVRT 420
Cdd:cd07498 218 GVAALILSANPNLTPAEVEDILTST 242
|
|
| AprE |
COG1404 |
Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
156-422 |
2.09e-34 |
|
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 138.31 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 156 GAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCdVNGNDldpmpryDASNENKHGTRCAGEVAATANNSHCTVGI 235
Cdd:COG1404 100 GSSAAGLTGAGVTVAVIDTGVDADHPDLAGRVVGGYDF-VDGDG-------DPSDDNGHGTHVAGIIAANGNNGGGVAGV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 236 AFNAKIGGVRMLD----GDVTDMVEA--KSVSynpQHVHIYSASWGPDDDGKTvdgpaPLTRQAFENGvrmgrRGLGSVF 309
Cdd:COG1404 172 APGAKLLPVRVLDdngsGTTSDIAAAidWAAD---NGADVINLSLGGPADGYS-----DALAAAVDYA-----VDKGVLV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 310 VWASGNGGRSkdhCSCDGYTNSIY-TISISSTAESGKKPWYleecSSTlattyssGESYD-----KKIITTDLRQRcTDN 383
Cdd:COG1404 239 VAAAGNSGSD---DATVSYPAAYPnVIAVGAVDANGQLASF----SNY-------GPKVDvaapgVDILSTYPGGG-YAT 303
|
250 260 270
....*....|....*....|....*....|....*....
gi 569006568 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 |
4.75e-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: 4.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 167 IVVTILDDGIERTHPDLmqnyDALASCDVNGNDLDPMPRY--DASNENKHGTRCAGEVAATANNSHCtVGIAFNAKIGGV 244
Cdd:cd00306 1 VTVAVIDTGVDPDHPDL----DGLFGGGDGGNDDDDNENGptDPDDGNGHGTHVAGIIAASANNGGG-VGVAPGAKLIPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 245 RMLD----GDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGktvdgPAPLTRQAFENGVRMgrrgLGSVFVWASGNGGRSK 320
Cdd:cd00306 76 KVLDgdgsGSSSDIAAAIDYAAADQGADVINLSLGGPGSP-----PSSALSEAIDYALAK----LGVLVVAAAGNDGPDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 321 DHCScDGYTNSIYTISISSTAESGKKPWYLEeCSSTLATTYSSGESYdkkIITTDLRQRCTDNHTGTSASAPMAAGIIAL 400
Cdd:cd00306 147 GTNI-GYPAASPNVIAVGAVDRDGTPASPSS-NGGAGVDIAAPGGDI---LSSPTTGGGGYATLSGTSMAAPIVAGVAAL 221
|
250 260
....*....|....*....|
gi 569006568 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 |
5.62e-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: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 165 KNIVVTILDDGIERTHPDLMQNY--DALASC-------------DVNG-----NDLDPMPrydasnENKHGTRCAGEVAA 224
Cdd:cd07473 2 GDVVVAVIDTGVDYNHPDLKDNMwvNPGEIPgngidddgngyvdDIYGwnfvnNDNDPMD------DNGHGTHVAGIIGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 225 TANNSHCTVGIAFNAKIGGVRMLD----GDVTDMVEA--KSVSYNpqhVHIYSASWGPdddgktvDGPAPLTRQAFEngv 298
Cdd:cd07473 76 VGNNGIGIAGVAWNVKIMPLKFLGadgsGTTSDAIKAidYAVDMG---AKIINNSWGG-------GGPSQALRDAIA--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 299 RMGRRGLgsVFVWASGNGGRSKDH-----CScdgYTNSiYTISISSTAESGKKPWYleecSSTLATT---YSSGESydkk 370
Cdd:cd07473 143 RAIDAGI--LFVAAAGNDGTNNDKtptypAS---YDLD-NIISVAATDSNDALASF----SNYGKKTvdlAAPGVD---- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 569006568 371 IITTDLRQRcTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07473 209 ILSTSPGGG-YGYMSGTSMATPHVAGAAALLLSLNPNLTAAQIKDAILSSAD 259
|
|
| Peptidases_S8_Thermitase_like |
cd07484 |
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ... |
129-422 |
1.31e-21 |
|
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173810 [Multi-domain] Cd Length: 260 Bit Score: 95.79 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 129 NDPKWPSMWYMHcsdnthpcqsDMNIEGAWKRGyTGKNIVVTILDDGIERTHPDLM-----QNYDAlascdVNGNDldpm 203
Cdd:cd07484 3 NDPYYSYQWNLD----------QIGAPKAWDIT-GGSGVTVAVVDTGVDPTHPDLLkvkfvLGYDF-----VDNDS---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 204 pryDASNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLD----GDVTDMVEAksvsynpqhvhIYsasWGPDDD 279
Cdd:cd07484 63 ---DAMDDNGHGTHVAGIIAAATNNGTGVAGVAPKAKIMPVKVLDangsGSLADIANG-----------IR---YAADKG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 280 GKTVD---GpAPLTRQAFENGVRMGRRGlGSVFVWASGNGGRSKdhCScdgYTNSI-YTISISSTAESGKKPWYleecss 355
Cdd:cd07484 126 AKVINlslG-GGLGSTALQEAINYAWNK-GVVVVAAAGNEGVSS--VS---YPAAYpGAIAVAATDQDDKRASF------ 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 356 tlaTTYSS-------GESydkkIITTDLRQRcTDNHTGTSASAPMAAGIIALALEANPfLTWRDVQHVIVRTSR 422
Cdd:cd07484 193 ---SNYGKwvdvsapGGG----ILSTTPDGD-YAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDALKKTAD 257
|
|
| Peptidases_S8_Autotransporter_serine_protease_like |
cd04848 |
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ... |
163-422 |
1.78e-21 |
|
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.
Pssm-ID: 173794 [Multi-domain] Cd Length: 267 Bit Score: 95.47 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 163 TGKNIVVTILDDGIERTHPDLMQNYDALAScdvNGNDLDPMPRYDASNENkHGTRCAGEVAATANNSHcTVGIAFNAKIG 242
Cdd:cd04848 1 TGAGVKVGVIDSGIDLSHPEFAGRVSEASY---YVAVNDAGYASNGDGDS-HGTHVAGVIAAARDGGG-MHGVAPDATLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 243 GVRMLDGDVTdmveAKSVSYNPQH--------VHIYSASWGPDDDGKTVDGPAPL---TRQAFENGVRMGRRGLGSVFVW 311
Cdd:cd04848 76 SARASASAGS----TFSDADIAAAydflaasgVRIINNSWGGNPAIDTVSTTYKGsaaTQGNTLLAALARAANAGGLFVF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 312 ASGNGGRSKDhcscDGYTNSIY--------------------TISISSTAESGK--KPWYLeecsST-----LATTYSSG 364
Cdd:cd04848 152 AAGNDGQANP----SLAAAALPylepeleggwiavvavdpngTIASYSYSNRCGvaANWCL----AApgeniYSTDPDGG 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 569006568 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 |
5.43e-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: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 166 NIVVTILDDGIeRTHPDLMQN-----YD----ALASCDVNGNDLDP----------------MPRYDASNENKHGTRCAG 220
Cdd:cd07496 1 GVVVAVLDTGV-LFHHPDLAGvllpgYDfisdPAIANDGDGRDSDPtdpgdwvtgddvppggFCGSGVSPSSWHGTHVAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 221 EVAATANNSHCTVGIAFNAKIGGVRML---DGDVTDMVEA---------KSVSYNPQHVHIYSASWGPDddgktvdGPAP 288
Cdd:cd07496 80 TIAAVTNNGVGVAGVAWGARILPVRVLgkcGGTLSDIVDGmrwaaglpvPGVPVNPNPAKVINLSLGGD-------GACS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 289 LTRQAFENGVRmgrrGLGSVFVWASGNGGRSKDH---CSCDGytnsiyTISISSTAESGKKPWYLE------------EC 353
Cdd:cd07496 153 ATMQNAINDVR----ARGVLVVVAAGNEGSSASVdapANCRG------VIAVGATDLRGQRASYSNygpavdvsapggDC 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006568 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 |
4.55e-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: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 157 AWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALA-SCDVNGNDLDPMPRYDA---SNENKHGTRCAGEVAATANNSHCT 232
Cdd:cd07485 2 AWEFGTGGPGIIVAVVDTGVDGTHPDLQGNGDGDGyDPAVNGYNFVPNVGDIDndvSVGGGHGTHVAGTIAAVNNNGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 233 VGIAFN------AKIGGVRMLDGD--VTDMVEAKSVSYNPQH-VHIYSASWGpdddGKTVDGPAPLTRQAFENGVRMGRR 303
Cdd:cd07485 82 GGIAGAggvapgVKIMSIQIFAGRyyVGDDAVAAAIVYAADNgAVILQNSWG----GTGGGIYSPLLKDAFDYFIENAGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 304 GL--GSVFVWASGNGGRSKDH--CSCDGytnsiyTISISSTAESGKKPWYleecsSTLATTYSSGESYDKKIITTDLRQR 379
Cdd:cd07485 158 SPldGGIVVFSAGNSYTDEHRfpAAYPG------VIAVAALDTNDNKASF-----SNYGRWVDIAAPGVGTILSTVPKLD 226
|
250 260 270
....*....|....*....|....*....|..
gi 569006568 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 |
2.04e-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: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 164 GKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMprYDasnENKHGTRCAGEVAATANNSHCTV-GIAFNAKIG 242
Cdd:cd07487 1 GKGITVAVLDTGIDAPHPDFDGRIIRFADFVNTVNGRTTP--YD---DNGHGTHVAGIIAGSGRASNGKYkGVAPGANLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 243 GVRMLD----GDVTDMVEAksVSY-----NPQHVHIYSASWG-PDDDGktvDGPAPLtRQAFENGVRMgrrglGSVFVWA 312
Cdd:cd07487 76 GVKVLDdsgsGSESDIIAG--IDWvvennEKYNIRVVNLSLGaPPDPS---YGEDPL-CQAVERLWDA-----GIVVVVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 313 SGNGGRSKDHCSCDGytNSIYTISISSTAESGKKPWYLEECSS---TL-----------ATTYSSGESYDKKIITTDLRQ 378
Cdd:cd07487 145 AGNSGPGPGTITSPG--NSPKVITVGAVDDNGPHDDGISYFSSrgpTGdgrikpdvvapGENIVSCRSPGGNPGAGVGSG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 569006568 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 |
3.65e-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: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 508 EHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLfdHSMEGFkNWEFMTIHCWGERAAGDWVLEVYDTPSQlrnfkTP 587
Cdd:COG4935 558 EDVTVTVDITHTYRGDLVITLISPDGTTVVLKNRSG--GSADNI-NATFDVANFSGESANGTWTLRVVDTAGG-----DT 629
|
90
....*....|..
gi 569006568 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 |
6.60e-18 |
|
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173803 [Multi-domain] Cd Length: 229 Bit Score: 84.12 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 166 NIVVTILDDGIERTHPDLMQNYdalascdVNGNDLDPMPRYDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKIGGVR 245
Cdd:cd07477 1 GVKVAVIDTGIDSSHPDLKLNI-------VGGANFTGDDNNDYQDGNGHGTHVAGIIAALDNGVG-VVGVAPEADLYAVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 246 MLD----GDVTDMVEAKSVSYNpQHVHIYSASWGpdddgktVDGPAPLTRQAFENGVrmgRRGLgsVFVWASGNggrskd 321
Cdd:cd07477 73 VLNddgsGTYSDIIAGIEWAIE-NGMDIINMSLG-------GPSDSPALREAIKKAY---AAGI--LVVAAAGN------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 322 hcscDGYTNSIYT--------ISISSTAESGKKpwyleecsstlaTTYSS----------GESydkkIITTDLRQRCTDN 383
Cdd:cd07477 134 ----SGNGDSSYDypakypsvIAVGAVDSNNNR------------ASFSStgpevelaapGVD----ILSTYPNNDYAYL 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 569006568 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 |
8.02e-15 |
|
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases
Pssm-ID: 173791 [Multi-domain] Cd Length: 293 Bit Score: 76.60 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 159 KRGYTGKNIVVTILDDGIERTHPDLMqnydalascDVNGNDLDPMPR----YDASNENK-----HGTRCAGEVAATANNS 229
Cdd:cd04842 1 GLGLTGKGQIVGVADTGLDTNHCFFY---------DPNFNKTNLFHRkivrYDSLSDTKddvdgHGTHVAGIIAGKGNDS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 230 HCTV---GIAFNAKIGGVRM------------LDGDVTDMVEAKSvsynpqhvHIYSASWGPDDDG------KTVDgpap 288
Cdd:cd04842 72 SSISlykGVAPKAKLYFQDIgdtsgnlssppdLNKLFSPMYDAGA--------RISSNSWGSPVNNgytllaRAYD---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 289 ltRQAFENgvrmgrRGLgsVFVWASGNGGrskdhcscDGYTNSIYTISIS-----------STAESGKKPWYLEECSSTL 357
Cdd:cd04842 140 --QFAYNN------PDI--LFVFSAGNDG--------NDGSNTIGSPATAknvltvgasnnPSVSNGEGGLGQSDNSDTV 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006568 358 ATTYSSGESYD--KK---------IITTDLRQR----CTDNH----TGTSASAPMAAGIIALALEA 404
Cdd:cd04842 202 ASFSSRGPTYDgrIKpdlvapgtgILSARSGGGgigdTSDSAytskSGTSMATPLVAGAAALLRQY 267
|
|
| Peptidases_S8_subtilisin_Vpr-like |
cd07474 |
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ... |
164-430 |
1.90e-14 |
|
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173800 [Multi-domain] Cd Length: 295 Bit Score: 75.44 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 164 GKNIVVTILDDGIERTHPDLMQNYDALASC----DVNGNDLDPMPR---------YDASNENKHGTRCAGEVAATANNSH 230
Cdd:cd07474 1 GKGVKVAVIDTGIDYTHPDLGGPGFPNDKVkggyDFVDDDYDPMDTrpypsplgdASAGDATGHGTHVAGIIAGNGVNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 231 CTVGIAFNAKIGGVRMLDGD---VTDMVEA---KSVSynpQHVHIYSASWG-----PDDDGKtvdgpapltrQAFENGVR 299
Cdd:cd07474 81 TIKGVAPKADLYAYKVLGPGgsgTTDVIIAaieQAVD---DGMDVINLSLGssvngPDDPDA----------IAINNAVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 300 mgrrgLGSVFVWASGNGGrskDHCSCDGyTNSIYTISISSTAESGKKPWYleecSSTLATTYSSGESYDKKIITTDL--- 376
Cdd:cd07474 148 -----AGVVVVAAAGNSG---PAPYTIG-SPATAPSAITVGASTVADVAE----ADTVGPSSSRGPPTSDSAIKPDIvap 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 377 -------RQRCTDN---HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTsrAGHLNAND 430
Cdd:cd07474 215 gvdimstAPGSGTGyarMSGTSMAAPHVAGAAALLKQAHPDWSPAQIKAALMNT--AKPLYDSD 276
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
637-746 |
6.18e-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: 64.32 E-value: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 637 PCDPECSEVGCDGPGPDHCSDCLHYyyklkNNTRICVSSCP-----PGHYhADKKRCRKCAPNCE------SCFGSHGNQ 705
Cdd:pfam14843 1 VCDPLCSSEGCWGPGPDQCLSCRNF-----SRGGTCVESCNilqgePREY-VVNSTCVPCHPECLpqngtaTCSGPGADN 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 569006568 706 CLSCKYgyflNEETSSCVTQCPDGSYEDI--------KKNVCGKCSENC 746
Cdd:pfam14843 75 CTKCAH----FRDGPHCVSSCPSGVLGENdliwkyadANGVCQPCHPNC 119
|
|
| Peptidases_S8_PCSK9_ProteinaseK_like |
cd04077 |
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ... |
162-421 |
3.15e-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: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 162 YTGKNIVVTILDDGIERTHPDLMQNydALASCDVNGNDldpmpryDASNENKHGTRCAGEVAATannshcTVGIAFNAKI 241
Cdd:cd04077 22 STGSGVDVYVLDTGIRTTHVEFGGR--AIWGADFVGGD-------PDSDCNGHGTHVAGTVGGK------TYGVAKKANL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 242 GGVRMLD----GDVTDMVEAksvsYNpqhvhiYSASWGPDDDGKTV-----DGPAPltrQAFENGV-RMGRRGLgsVFVW 311
Cdd:cd04077 87 VAVKVLDcngsGTLSGIIAG----LE------WVANDATKRGKPAVanmslGGGAS---TALDAAVaAAVNAGV--VVVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 312 ASGNGGRskDHCscdGYT--NSIYTISISSTAESGKKPWYLE--ECSSTLAttysSGESYDKKIITTDlrqRCTDNHTGT 387
Cdd:cd04077 152 AAGNSNQ--DAC---NYSpaSAPEAITVGATDSDDARASFSNygSCVDIFA----PGVDILSAWIGSD---TATATLSGT 219
|
250 260 270
....*....|....*....|....*....|....
gi 569006568 388 SASAPMAAGIIALALEANPFLTWRDVQHVIVRTS 421
Cdd:cd04077 220 SMAAPHVAGLAAYLLSLGPDLSPAEVKARLLNLA 253
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
706-1063 |
5.23e-11 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 66.15 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 706 CLSCKYGYFLNEETSSCVTQcpdgsyedikknvcGKC-SENCKACI--GFHNCTECKGGLSL-QGSRCSVTCEDGQFFNG 781
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSS--------------APCkTENCKACSndKREVCEECNSNNYLtPTSQCIDDCAKIGNYYY 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 782 HDCQPCHRFCATCSGAGADGCinctegyvmEEGRCVQSCSVSYYLDHsseggyKSCKRCDNSCLTCNGPGFKNCSSCPSG 861
Cdd:pfam03302 67 TTNANNKKICKECTVANCKTC---------EDQGQCQACNDGFYKSG------DACSPCHESCKTCSGGTASDCTECLTG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 862 YLLDLGT--------------CQMGAICKDGEYIDDQGHCQTCEAS--------CAKCWGPTQEDCISCPVTrvldDGRC 919
Cdd:pfam03302 132 KALRYGNdgtkgtcgegcttgTGAGACKTCGLTIDGTSYCSECATEteypqngvCTSTAARATATCKASSVA----NGMC 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 920 vMNCPSWKFEFKKQCHpchytcQGCQGSGPSNCTSCRADKHGQErflyhgeclencPVGHYPAKGHACLPCPDNCELCYN 999
Cdd:pfam03302 208 -SSCANGYFRMNGGCY------ETTKFPGKSVCEEANSGGTCQK------------EAPGYKLNNGDLVTCSPGCKTCTS 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 1000 PHVCSRCMSGYViiPPNHTCQKlecrqgefqdseyeecmpCEEGCLGCTeDDPGACTSCATGYY 1063
Cdd:pfam03302 269 NTVCTTCMDGYV--KTSDSCTK------------------CDSSCETCT-GATTTCKTCATGYY 311
|
|
| Peptidases_S8_5 |
cd07489 |
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ... |
160-423 |
3.49e-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: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 160 RGYTGKNIVVTILDDGIERTHPDL----MQNYDALASCDVNGNDLD----PMPRYDASNENKHGTRCAGEVAATANNSHC 231
Cdd:cd07489 8 EGITGKGVKVAVVDTGIDYTHPALggcfGPGCKVAGGYDFVGDDYDgtnpPVPDDDPMDCQGHGTHVAGIIAANPNAYGF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 232 TvGIAFNAKIGGVRMLD--GDVTD--MVEAKSVSYNpQHVHIYSASWGpDDDGKTVDGPAPLTRQAFENGVRM------- 300
Cdd:cd07489 88 T-GVAPEATLGAYRVFGcsGSTTEdtIIAAFLRAYE-DGADVITASLG-GPSGWSEDPWAVVASRIVDAGVVVtiaagnd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 301 GRRGLgsvfvWASGNGGRSKDHCSCdGYTNSIYTiSISSTAESGKKPWYLEECSSTLATTYSSGESYDkkIIttdlrqrc 380
Cdd:cd07489 165 GERGP-----FYASSPASGRGVIAV-ASVDSYFS-SWGPTNELYLKPDVAAPGGNILSTYPLAGGGYA--VL-------- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 569006568 381 tdnhTGTSASAPMAAGIIALALEA-NPFLTWRDVQHVIVRTSRA 423
Cdd:cd07489 228 ----SGTSMATPYVAGAAALLIQArHGKLSPAELRDLLASTAKP 267
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
889-995 |
5.45e-10 |
|
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).
Pssm-ID: 464344 [Multi-domain] Cd Length: 132 Bit Score: 58.54 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 889 TCEASCAK--CWGPTQEDCISCpvTRVLDDGRCVMNCPSWKFEFK-----KQCHPCHYTCQG------CQGSGPSNCTSC 955
Cdd:pfam14843 1 VCDPLCSSegCWGPGPDQCLSC--RNFSRGGTCVESCNILQGEPReyvvnSTCVPCHPECLPqngtatCSGPGADNCTKC 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 569006568 956 RADKHGQErflyhgeCLENCP---------VGHYPAKGHACLPCPDNCE 995
Cdd:pfam14843 79 AHFRDGPH-------CVSSCPsgvlgendlIWKYADANGVCQPCHPNCT 120
|
|
| Peptidases_S8_10 |
cd07494 |
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ... |
152-430 |
7.78e-10 |
|
Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173819 [Multi-domain] Cd Length: 298 Bit Score: 61.72 E-value: 7.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 152 MNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALAScdvngndLDPMPRYDASNENKHGTrcaGEVAAtannshc 231
Cdd:cd07494 8 LNATRVHQRGITGRGVRVAMVDTGFYAHPFFESRGYQVRVV-------LAPGATDPACDENGHGT---GESAN------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 232 TVGIAFNAKIGGVRMLDGDVTDMVEA--KSVSYNPQhvhIYSASWGPD--DDGKTVDGPAPLTRQAFE----NGVrmgRR 303
Cdd:cd07494 71 LFAIAPGAQFIGVKLGGPDLVNSVGAfkKAISLSPD---IISNSWGYDlrSPGTSWSRSLPNALKALAatlqDAV---AR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 304 GLgsVFVWASGNGGRS-----KDHCSCDG-YTNSIYTISISSTAESGKKPWY-------------LEECSSTLATTYSSG 364
Cdd:cd07494 145 GI--VVVFSAGNGGWSfpaqhPEVIAAGGvFVDEDGARRASSYASGFRSKIYpgrqvpdvcglvgMLPHAAYLMLPVPPG 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006568 365 ESYDKKIITTDLRQRCTDN---HTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRA---GHLNAND 430
Cdd:cd07494 223 SQLDRSCAAFPDGTPPNDGwgvFSGTSAAAPQVAGVCALMLQANPGLSPERARSLLNKTARDvtkGASAQGT 294
|
|
| Peptidases_S8_6 |
cd07490 |
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ... |
169-422 |
1.74e-09 |
|
Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173815 [Multi-domain] Cd Length: 254 Bit Score: 59.87 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 169 VTILDDGIERTHPDLMQNYDALASCDVNGNDLDPmpryDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKiggvrMLD 248
Cdd:cd07490 4 VAVLDTGVDADHPDLAGRVAQWADFDENRRISAT----EVFDAGGHGTHVSGTIGGGGAKGV-YIGVAPEAD-----LLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 249 GDVTDMVEAksvsynPQHVHIYSASWGPDDDGKTV-------DGPAPLTRQAFEngvrMGRRGLGSVFVWASGNGGRSKD 321
Cdd:cd07490 74 GKVLDDGGG------SLSQIIAGMEWAVEKDADVVsmslggtYYSEDPLEEAVE----ALSNQTGALFVVSAGNEGHGTS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 322 HCSCDGYTnsiyTISISSTAESGKKPWYlEECSSTLATTYSSGESYDKKIITTDL-----------RQRCTDNH----TG 386
Cdd:cd07490 144 GSPGSAYA----ALSVGAVDRDDEDAWF-SSFGSSGASLVSAPDSPPDEYTKPDVaapgvdvysarQGANGDGQytrlSG 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 569006568 387 TSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07490 219 TSMAAPHVAGVAALLAAAHPDLSPEQIKDALTETAY 254
|
|
| PTZ00262 |
PTZ00262 |
subtilisin-like protease; Provisional |
169-413 |
1.94e-09 |
|
subtilisin-like protease; Provisional
Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 61.91 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 169 VTILDDGIERTHPDLMQNY---------------------DALASCDVNGNDLDPMprydasNENKHGTRCAGEVAATAN 227
Cdd:PTZ00262 320 ICVIDSGIDYNHPDLHDNIdvnvkelhgrkgidddnngnvDDEYGANFVNNDGGPM------DDNYHGTHVSGIISAIGN 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 228 NSHCTVGIAFNAKIGGVRMLD----GDVTDMVeaKSVSY-NPQHVHIYSASWGPDDDGKTvdgpapltrqaFENGVRMGR 302
Cdd:PTZ00262 394 NNIGIVGVDKRSKLIICKALDshklGRLGDMF--KCFDYcISREAHMINGSFSFDEYSGI-----------FNESVKYLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 303 RgLGSVFVWASGN----GGRSKDHCSCDGYTNSIYTISISSTAES---------GKKPWYLEECSSTLATTYSSGESYDK 369
Cdd:PTZ00262 461 E-KGILFVVSASNcshtKESKPDIPKCDLDVNKVYPPILSKKLRNvitvsnlikDKNNQYSLSPNSFYSAKYCQLAAPGT 539
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 569006568 370 KIITTDLRQRCTDNhTGTSASAPMAAGIIALALEANPFLTWRDV 413
Cdd:PTZ00262 540 NIYSTFPKNSYRKL-NGTSMAAPHVAAIASLILSINPSLSYEEV 582
|
|
| FU |
smart00261 |
Furin-like repeats; |
781-825 |
8.10e-09 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 52.51 E-value: 8.10e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 569006568 781 GHDCQPCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYY 825
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| Peptidases_S8_12 |
cd07480 |
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ... |
162-315 |
2.59e-08 |
|
Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173806 [Multi-domain] Cd Length: 297 Bit Score: 57.00 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 162 YTGKNIVVTILDDGIERTHPDLMqnydalascDVNGNDLDPMPRYDASNENKHGTRCAGEVAATANNSHcTVGIAFNAKI 241
Cdd:cd07480 5 FTGAGVRVAVLDTGIDLTHPAFA---------GRDITTKSFVGGEDVQDGHGHGTHCAGTIFGRDVPGP-RYGVARGAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 242 --GGVRMLDGDVTDMVEAKSVSYNPQH-VHIYSASWGPDDDGKTVDG--PAPLTRQAFE----------NGVRMGRR--- 303
Cdd:cd07480 75 alIGKVLGDGGGGDGGILAGIQWAVANgADVISMSLGADFPGLVDQGwpPGLAFSRALEayrqrarlfdALMTLVAAqaa 154
|
170
....*....|...
gi 569006568 304 -GLGSVFVWASGN 315
Cdd:cd07480 155 lARGTLIVAAAGN 167
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
690-739 |
4.73e-08 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 50.60 E-value: 4.73e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569006568 690 KCAPNCESCFGSHGNQCLSCKYGYFLNEETssCVTQCPDGSYEDIKKNVC 739
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGT--CVSECPEGTYADTEGGVC 48
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
712-1114 |
5.97e-08 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 57.23 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 712 GYFLNEETSSCVTQCPDGSYEDiKKNVCGKCSENC---------KACIGFHN--CTECKGGLSLQGSRCSVTCEDGQFFN 780
Cdd:PTZ00214 350 GYLCGDATNGGVSGCATCGYNS-GAVTCTRCSAGYlgvdgkscsESCSGDTRgvCTKVAEGSESTEVSCRCVCKPTFYNS 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 781 GHDCQPCHRFCATCSGAGADGCINCTEGYVM-------EEGRCVQSCSVSyylDHSSE-----GGYKSCKRC-DNSCLTC 847
Cdd:PTZ00214 429 SGTCTPCTDSCAVCKDGTPTGCQQCSPGKILefsivssESADCVDQCSVG---SECAEcgitiDGSRYCTRCkDASTYPF 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 848 NGPGFKNcsscpsgylldlgtCQMGAICKDGEyiddQGHCQTCEASCAKCWGP--TQEDCISCPVTRVLDDGRCVMNCPS 925
Cdd:PTZ00214 506 NGVCIPN--------------TQRDAYCTSTA----NGACTTCSGAAFLMNGGcyTTEHYPGSTICDKQSNGKCTTTKKG 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 926 WKFEFKKQCHPCHYTCQGCQGSGPSNCTSCRADK-HGQERFLYHGECLE-NCPVGHYPAKGHACLPCPD-NCELCYNPHV 1002
Cdd:PTZ00214 568 YGISPDGKLLECDPTCLACTAPGPGRCTRCPSDKlLKRASGAATGSCVDpGACVDGYYADGDACLPCATpGCKTCGHASF 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1003 CSRCMSGYVIIPPNHTC-----------------QKLECRQGEFQDSEYEECMPCEE------GCLGCteDDPGACTSCA 1059
Cdd:PTZ00214 648 CTECAGELFVSLDGQSCleectgdkvvgevsggvRRCWCERGFLPALDRSGCVLPTEcppdmpSCAAC--DESGRCLLCV 725
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 569006568 1060 TGYYmferhcykacpektfGVKWECRACGTNCG---SCDQHECYwCEEGFFLSGGSCV 1114
Cdd:PTZ00214 726 TSGH---------------NVQVDQRTCAEGCGaraSSNQGVCM-CELDAVLTKGVCV 767
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
786-827 |
7.43e-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: 49.82 E-value: 7.43e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 569006568 786 PCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYYLD 827
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYAD 42
|
|
| Furin-like |
pfam00757 |
Furin-like cysteine rich region; |
638-746 |
2.94e-07 |
|
Furin-like cysteine rich region;
Pssm-ID: 395614 [Multi-domain] Cd Length: 143 Bit Score: 50.90 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 638 CDPECSEvGCDGPGPDHCSDCLHYYYklknnTRICVSSCPPGHYHADkkrcRKCApNCESCFGSHGNQClsckygYFLNE 717
Cdd:pfam00757 49 CHEQCLG-GCTGPNDSDCLACRHFND-----EGTCVDQCPPGTYQFG----WRCV-TFKECPKSHLPGY------NPLVI 111
|
90 100 110
....*....|....*....|....*....|
gi 569006568 718 ETSSCVTQCPDGSYEDIKKNV-CGKCSENC 746
Cdd:pfam00757 112 HNGECVRECPSGYTEVENNSRkCEPCEGLC 141
|
|
| FU |
smart00261 |
Furin-like repeats; |
885-928 |
3.96e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 47.50 E-value: 3.96e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 569006568 885 GHCQTCEASCAKCWGPTQEDCISCPVTRVLDDGRCVMNCPSWKF 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 ... |
671-729 |
4.86e-07 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 49.35 E-value: 4.86e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006568 671 ICVSSCPPGHY---HADKKRCRKC-APNCESCFGShgNQCLSCKYGYFLNEetSSCVTQCPDG 729
Cdd:pfam15913 34 VCLHSCPPGYFgirGQEVNRCTKCkAENCESCFSK--DFCTKCKEGFYLHK--GKCLDTCPEG 92
|
|
| FU |
smart00261 |
Furin-like repeats; |
685-731 |
5.01e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 47.50 E-value: 5.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 569006568 685 KKRCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETssCVTQCPDGSY 731
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHGFFLDGGK--CVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
1036-1078 |
6.53e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 47.12 E-value: 6.53e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 569006568 1036 ECMPCEEGCLGCTEDDPGACTSCATGYYMFERHCYKACPEKTF 1078
Cdd:smart00261 3 ECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| FU |
smart00261 |
Furin-like repeats; |
931-980 |
8.68e-07 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 46.73 E-value: 8.68e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 569006568 931 KKQCHPCHYTCQGCQGSGPSNCTSCRADkhgqeRFLYHGECLENCPVGHY 980
Cdd:smart00261 1 DGECKPCHPECATCTGPGPDDCTSCKHG-----FFLDGGKCVSECPPGTY 45
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
786-906 |
9.79e-07 |
|
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).
Pssm-ID: 464344 [Multi-domain] Cd Length: 132 Bit Score: 49.29 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 786 PCHRFC--ATCSGAGADGCINCTegYVMEEGRCVQSCSVSYYLDHSSEGGyKSCKRCDNSCL------TCNGPGFKNC-- 855
Cdd:pfam14843 1 VCDPLCssEGCWGPGPDQCLSCR--NFSRGGTCVESCNILQGEPREYVVN-STCVPCHPECLpqngtaTCSGPGADNCtk 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006568 856 -----------SSCPSGYlldlgtcqMGAICKDGEYIDDQGHCQTCEASCAK-CWGPTQEDCI 906
Cdd:pfam14843 78 cahfrdgphcvSSCPSGV--------LGENDLIWKYADANGVCQPCHPNCTQgCTGPGLTGCP 132
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
653-908 |
1.60e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 51.89 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 653 DHCSDCLHYYYKLKNNtricvsscppghyhaDKKRCRKCAP-NCESCfgSHGNQCLSCKYGYFLNEETSSCVTQ----CP 727
Cdd:pfam03302 56 DDCAKIGNYYYTTNAN---------------NKKICKECTVaNCKTC--EDQGQCQACNDGFYKSGDACSPCHEscktCS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 728 DGSYEDIKKNVCGK------------CSENCKACIGFHNCTECkgGLSLQG----SRCSVTCEDGQffNGHDCQPCHRFC 791
Cdd:pfam03302 119 GGTASDCTECLTGKalrygndgtkgtCGEGCTTGTGAGACKTC--GLTIDGtsycSECATETEYPQ--NGVCTSTAARAT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 792 ATC-SGAGADG-CINCTEGYVMEEGRCVQSCSVSYYLDHSSEGGYKSCK------RCDNSCLTCNGPGFKNCSSCPsgyl 863
Cdd:pfam03302 195 ATCkASSVANGmCSSCANGYFRMNGGCYETTKFPGKSVCEEANSGGTCQkeapgyKLNNGDLVTCSPGCKTCTSNT---- 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 569006568 864 ldlgTCQMgaiCKDGeYIDDQGHCQTCEASCAKCWGPTQEdCISC 908
Cdd:pfam03302 271 ----VCTT---CMDG-YVKTSDSCTKCDSSCETCTGATTT-CKTC 306
|
|
| Peptidases_S8_8 |
cd07492 |
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ... |
169-422 |
1.64e-06 |
|
Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173817 [Multi-domain] Cd Length: 222 Bit Score: 50.41 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 169 VTILDDGIERTHPDLmqnyDALASCDVNGNDLDPMPRYD-ASNENKHGTRCAGEVAATANnshctvgiafNAKIGGVRML 247
Cdd:cd07492 4 VAVIDSGVDTDHPDL----GNLALDGEVTIDLEIIVVSAeGGDKDGHGTACAGIIKKYAP----------EAEIGSIKIL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 248 DGDVTDMVE--AKSVSY-NPQHVHIYSASWgpdddGKTVDGPAPLTRQAFENGVRMGRrglgsVFVWASGNGGRskdhcs 324
Cdd:cd07492 70 GEDGRCNSFvlEKALRAcVENDIRIVNLSL-----GGPGDRDFPLLKELLEYAYKAGG-----IIVAAAPNNND------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 325 cDGYTNSIYTISI---SSTAESGKKPWYLEECSSTlattyssgesyDKKIITTDLRQRCTDNHTGTSASAPMAAGIIALA 401
Cdd:cd07492 134 -IGTPPASFPNVIgvkSDTADDPKSFWYIYVEFSA-----------DGVDIIAPAPHGRYLTVSGNSFAAPHVTGMVALL 201
|
250 260
....*....|....*....|.
gi 569006568 402 LEANPFLTWRDVQHVIVRTSR 422
Cdd:cd07492 202 LSEKPDIDANDLKRLLQRLAV 222
|
|
| FU |
smart00261 |
Furin-like repeats; |
835-880 |
2.87e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 45.19 E-value: 2.87e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 569006568 835 KSCKRCDNSCLTCNGPGFKNCSSCPSGYLLDLGTCQmgAICKDGEY 880
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCV--SECPPGTY 45
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
637-689 |
3.94e-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: 3.94e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 569006568 637 PCDPECSevGCDGPGPDHCSDCLHYYYklkNNTRICVSSCPPGHYH-ADKKRCR 689
Cdd:cd00064 1 PCHPSCA--TCTGPGPDQCTSCRHGFY---LDGGTCVSECPEGTYAdTEGGVCL 49
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
936-981 |
4.02e-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: 4.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 569006568 936 PCHYTCQGCQGSGPSNCTSCRADKHgqerfLYHGECLENCPVGHYP 981
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFY-----LDGGTCVSECPEGTYA 41
|
|
| FU |
smart00261 |
Furin-like repeats; |
637-681 |
4.79e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.81 E-value: 4.79e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 569006568 637 PCDPECSevGCDGPGPDHCSDCLHYYYKLKNntrICVSSCPPGHY 681
Cdd:smart00261 6 PCHPECA--TCTGPGPDDCTSCKHGFFLDGG---KCVSECPPGTY 45
|
|
| Peptidases_S8_Lantibiotic_specific_protease |
cd07482 |
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ... |
166-409 |
4.91e-06 |
|
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173808 [Multi-domain] Cd Length: 294 Bit Score: 49.67 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 166 NIVVTILDDGIERTHPDLMQNYdalascDVNGNDLDPMPRYDASNE------------NKHGTRCAGEVAATANNShctv 233
Cdd:cd07482 1 KVTVAVIDSGIDPDHPDLKNSI------SSYSKNLVPKGGYDGKEAgetgdindivdkLGHGTAVAGQIAANGNIK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 234 GIAFNAKIGGVRMLD----GDVTDMVEAKSVSYNpQHVHIYSASWGPDDDGKTVDGPAPLTRQAFENGVRMGRRGlGSVF 309
Cdd:cd07482 71 GVAPGIGIVSYRVFGscgsAESSWIIKAIIDAAD-DGVDVINLSLGGYLIIGGEYEDDDVEYNAYKKAINYAKSK-GSIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 310 VWASGNGGRS-------KDHCSCDGY--TNSIY---------TISISSTAESGkkpwYLEECSS------TLAT---TYS 362
Cdd:cd07482 149 VAAAGNDGLDvsnkqelLDFLSSGDDfsVNGEVydvpaslpnVITVSATDNNG----NLSSFSNygnsriDLAApggDFL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006568 363 SGESYDK------------KIITTDLRQrCTDNHTGTSASAPMAAGIIALALEANPFLT 409
Cdd:cd07482 225 LLDQYGKekwvnnglmtkeQILTTAPEG-GYAYMYGTSLAAPKVSGALALIIDKNPLKK 282
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1003-1161 |
6.28e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 49.97 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1003 CSRCMSGYVIIPPNHTCQKLEcrqgefqdseyeecmPCE-EGCLGCTEDDPGACTSCATGYYMFE-RHCYKACPE----- 1075
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSA---------------PCKtENCKACSNDKREVCEECNSNNYLTPtSQCIDDCAKignyy 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1076 --KTFGVKWECRACGT-NCGSC-DQHECYWCEEGFFLSGGscvqdcgpgfhgdqelgECKPCHRACENCTGSGYNQCSSC 1151
Cdd:pfam03302 66 ytTNANNKKICKECTVaNCKTCeDQGQCQACNDGFYKSGD-----------------ACSPCHESCKTCSGGTASDCTEC 128
|
170
....*....|
gi 569006568 1152 QEGLQLWHGT 1161
Cdd:pfam03302 129 LTGKALRYGN 138
|
|
| FU |
smart00261 |
Furin-like repeats; |
1128-1165 |
6.82e-06 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 44.04 E-value: 6.82e-06
10 20 30
....*....|....*....|....*....|....*...
gi 569006568 1128 GECKPCHRACENCTGSGYNQCSSCQEGLQLWHGTCLWS 1165
Cdd:smart00261 2 GECKPCHPECATCTGPGPDDCTSCKHGFFLDGGKCVSE 39
|
|
| Peptidases_S8_11 |
cd04843 |
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ... |
152-402 |
8.47e-06 |
|
Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173792 Cd Length: 277 Bit Score: 48.85 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 152 MNIEGAWKR-GYTGKNIVVTILDDGIERTHPDLMQNydaLAScdvngndldPMPRYDASNENKHGTRCAGEVAATANNSH 230
Cdd:cd04843 2 INARYAWTKpGGSGQGVTFVDIEQGWNLNHEDLVGN---GIT---------LISGLTDQADSDHGTAVLGIIVAKDNGIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 231 CTvGIAFNAKIGGV-----------------RMLDGDVTdMVEAK----SVSYNPQHVHIYSASWGPdddgktvdgpapl 289
Cdd:cd04843 70 VT-GIAHGAQAAVVsstrvsntadaildaadYLSPGDVI-LLEMQtggpNNGYPPLPVEYEQANFDA------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 290 TRQAFENGVrmgrrglgsVFVWASGNGGRSKDHCS-CDGYTNSIYTISIS---------STAESGKKPWyleeCSSTLAT 359
Cdd:cd04843 135 IRTATDLGI---------IVVEAAGNGGQDLDAPVyNRGPILNRFSPDFRdsgaimvgaGSSTTGHTRL----AFSNYGS 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 569006568 360 ---TYSSGE-----SYDKKIITTDLRQRCTDNHTGTSASAPMAAGiiALAL 402
Cdd:cd04843 202 rvdVYGWGEnvtttGYGDLQDLGGENQDYTDSFSGTSSASPIVAG--AAAS 250
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
844-1154 |
1.09e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 49.20 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 844 CLTCNGPGFKNCSSCPSGYLLDLGTCQMGAICKDGEYiddqgHCQTCEASCAKCWGPTQEDCISCpvtrvlDDGRCVMNC 923
Cdd:pfam03302 28 CKACSNDKREVCEECNSNNYLTPTSQCIDDCAKIGNY-----YYTTNANNKKICKECTVANCKTC------EDQGQCQAC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 924 PSWKFEFKKQCHPCHYTCQGCQGSGPSNCTSC---RADKHGQERflYHGECLENCPVGHYPAKGHACLPCPDNCELCynp 1000
Cdd:pfam03302 97 NDGFYKSGDACSPCHESCKTCSGGTASDCTECltgKALRYGNDG--TKGTCGEGCTTGTGAGACKTCGLTIDGTSYC--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1001 hvcSRCmSGYVIIPPNHTCQKLECRQGEFqdseyeecmpceegCLGCTEDDpGACTSCATGYYMFERHCYKA-------- 1072
Cdd:pfam03302 172 ---SEC-ATETEYPQNGVCTSTAARATAT--------------CKASSVAN-GMCSSCANGYFRMNGGCYETtkfpgksv 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1073 CPEKTFGVKWECRACGTNCGSCDQHECywCEEGFFLSGGSCVQDCGPGFHGDQelGECKPCHRACENCTGSGyNQCSSCQ 1152
Cdd:pfam03302 233 CEEANSGGTCQKEAPGYKLNNGDLVTC--SPGCKTCTSNTVCTTCMDGYVKTS--DSCTKCDSSCETCTGAT-TTCKTCA 307
|
..
gi 569006568 1153 EG 1154
Cdd:pfam03302 308 TG 309
|
|
| Peptidases_S53_like |
cd05562 |
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ... |
383-455 |
1.21e-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: 1.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006568 383 NHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIvrTSRAGHLNANDWktnaagfkvSHLYGFGLMDAEAMV 455
Cdd:cd05562 212 NFFGTSAAAPHAAGVAALVLSANPGLTPADIRDAL--RSTALDMGEPGY---------DNASGSGLVDADRAV 273
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1039-1079 |
1.23e-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: 43.66 E-value: 1.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 569006568 1039 PCEEGCLGCTEDDPGACTSCATGYYMFERHCYKACPEKTFG 1079
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYA 41
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
840-886 |
1.92e-05 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 42.89 E-value: 1.92e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 569006568 840 CDNSCLTCNGPGFKNCSSCPSGYLLDLGTCQmgAICKDGEYIDDQGH 886
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCV--SECPEGTYADTEGG 46
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
890-929 |
1.94e-05 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 42.89 E-value: 1.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 569006568 890 CEASCAKCWGPTQEDCISCPVTRVLDDGRCVMNCPSWKFE 929
Cdd:cd00064 2 CHPSCATCTGPGPDQCTSCRHGFYLDGGTCVSECPEGTYA 41
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
687-822 |
3.65e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 47.71 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 687 RCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETSSCVTQCPDGSYEDIKKNVCGKCSENCKACIGFHNCTECKGGLSLQG 766
Cdd:COG4624 2 LLLLRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 767 SRCSVTCEDGqffNGHDCQPCHRFCATCSGAGADG--------CINCtegyvmeeGRCVQSCSV 822
Cdd:COG4624 82 RGPSIIRDKE---KCKNCYPCVRACPVKAIKVDDGkaeideekCISC--------GQCVAVCPF 134
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
695-782 |
7.91e-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: 42.80 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 695 CESCfgSHGNQCLSCKYGYFL------NEETSSCVTQCPDGSY--EDIKKNVCGKC-SENCKACIGFHNCTECKGGLSLQ 765
Cdd:pfam15913 4 CVLC--SEENGCLTCQPRLFLllerngIRQYGVCLHSCPPGYFgiRGQEVNRCTKCkAENCESCFSKDFCTKCKEGFYLH 81
|
90
....*....|....*..
gi 569006568 766 GSRCSVTCEDGQFFNGH 782
Cdd:pfam15913 82 KGKCLDTCPEGTAAQNS 98
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1132-1163 |
1.07e-04 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 40.97 E-value: 1.07e-04
10 20 30
....*....|....*....|....*....|..
gi 569006568 1132 PCHRACENCTGSGYNQCSSCQEGLQLWHGTCL 1163
Cdd:cd00064 1 PCHPSCATCTGPGPDQCTSCRHGFYLDGGTCV 32
|
|
| Furin-like_2 |
pfam15913 |
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a ... |
1043-1130 |
2.72e-04 |
|
Furin-like repeat, cysteine-rich; The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation.
Pssm-ID: 464939 [Multi-domain] Cd Length: 102 Bit Score: 41.26 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 1043 GCLGCTEDDpgACTSCATGYYMFERH--------CYKACPEKTFGVKWE----CRACGT-NCGSC-DQHECYWCEEGFFL 1108
Cdd:pfam15913 3 GCVLCSEEN--GCLTCQPRLFLLLERngirqygvCLHSCPPGYFGIRGQevnrCTKCKAeNCESCfSKDFCTKCKEGFYL 80
|
90 100
....*....|....*....|..
gi 569006568 1109 SGGSCVQDCGPGFHGDQELGEC 1130
Cdd:pfam15913 81 HKGKCLDTCPEGTAAQNSTMEC 102
|
|
| Furin-like |
pfam00757 |
Furin-like cysteine rich region; |
847-994 |
1.08e-03 |
|
Furin-like cysteine rich region;
Pssm-ID: 395614 [Multi-domain] Cd Length: 143 Bit Score: 40.88 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 847 CNGPGFKNCSSCPSGYLLDLGTCQMGAICKDGEYIDDQGHCqtCEASCA-KCWGPTQEDCISCpvTRVLDDGRCVMNCPS 925
Cdd:pfam00757 8 CPGTMEKCHSCCNNGYCWGPGHCQKVCPEQCKKRCTKPGEC--CHEQCLgGCTGPNDSDCLAC--RHFNDEGTCVDQCPP 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006568 926 WKFEFKKQChpchYTCQGCQGSGPSNCTscradkhgqERFLYHGECLENCPVGHYPAKGH--ACLPCPDNC 994
Cdd:pfam00757 84 GTYQFGWRC----VTFKECPKSHLPGYN---------PLVIHNGECVRECPSGYTEVENNsrKCEPCEGLC 141
|
|
| FU |
cd00064 |
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ... |
1086-1131 |
1.08e-03 |
|
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Pssm-ID: 238021 [Multi-domain] Cd Length: 49 Bit Score: 38.27 E-value: 1.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 569006568 1086 ACGTNCGSC---DQHECYWCEEGFFLSGGSCVQDCGPGFHGDQELGECK 1131
Cdd:cd00064 1 PCHPSCATCtgpGPDQCTSCRHGFYLDGGTCVSECPEGTYADTEGGVCL 49
|
|
| Furin-like |
pfam00757 |
Furin-like cysteine rich region; |
990-1137 |
1.31e-03 |
|
Furin-like cysteine rich region;
Pssm-ID: 395614 [Multi-domain] Cd Length: 143 Bit Score: 40.50 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 990 CPDNCELCYNPHVCSRCMSgyviipPNHtCQKL---ECRQGEFQDSEyeeCmpCEEGCLG-CTEDDPGACTSCAtgYYMF 1065
Cdd:pfam00757 8 CPGTMEKCHSCCNNGYCWG------PGH-CQKVcpeQCKKRCTKPGE---C--CHEQCLGgCTGPNDSDCLACR--HFND 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006568 1066 ERHCYKACPEKTFGVKWECrACGTNCGSCDQHECYWceegFFLSGGSCVQDCGPGFH-GDQELGECKPCHRAC 1137
Cdd:pfam00757 74 EGTCVDQCPPGTYQFGWRC-VTFKECPKSHLPGYNP----LVIHNGECVRECPSGYTeVENNSRKCEPCEGLC 141
|
|
| FU |
smart00261 |
Furin-like repeats; |
736-778 |
1.34e-03 |
|
Furin-like repeats;
Pssm-ID: 214589 [Multi-domain] Cd Length: 45 Bit Score: 37.87 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 569006568 736 KNVCGKCSENCKACIG--FHNCTECKGGLSLQGSRCSVTCEDGQF 778
Cdd:smart00261 1 DGECKPCHPECATCTGpgPDDCTSCKHGFFLDGGKCVSECPPGTY 45
|
|
| Peptidases_S8_14 |
cd07497 |
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ... |
164-404 |
1.71e-03 |
|
Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173821 [Multi-domain] Cd Length: 311 Bit Score: 42.07 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 164 GKNIVVTILDDGIERTHPDLMQ--NYDALASCDVNGN---DLDPMPRYDA--SNENKHGTRCAgEVAATANNSHCT---- 232
Cdd:cd07497 1 GEGVVIAIVDTGVDYSHPDLDIygNFSWKLKFDYKAYllpGMDKWGGFYVimYDFFSHGTSCA-SVAAGRGKMEYNlygy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 233 ------VGIAFNAKIGGVRMLD-GDVT---------DMVEAKSV-SYNPQH-VHIYSASWGPDDDGKTVDGPAPLTRQAF 294
Cdd:cd07497 80 tgkfliRGIAPDAKIAAVKALWfGDVIyawlwtagfDPVDRKLSwIYTGGPrVDVISNSWGISNFAYTGYAPGLDISSLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 295 ENGVRMGRrglGSVFVWASGNGGRSKDHCSCDGytNSIYTISISSTAESGKKPWYLeecssTLATTYSSGEsydkkIITT 374
Cdd:cd07497 160 IDALVTYT---GVPIVSAAGNGGPGYGTITAPG--AASLAISVGAATNFDYRPFYL-----FGYLPGGSGD-----VVSW 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006568 375 DLR----------------------QRCTDNHT------------GTSASAPMAAGIIALALEA 404
Cdd:cd07497 225 SSRgpsiagdpkpdlaaigafawapGRVLDSGGaldgneafdlfgGTSMATPMTAGSAALVISA 288
|
|
| GF_recep_IV |
pfam14843 |
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine ... |
742-855 |
4.67e-03 |
|
Growth factor receptor domain IV; This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain (pfam00757) regulates the binding of ligands to the receptor L domains (pfam01030).
Pssm-ID: 464344 [Multi-domain] Cd Length: 132 Bit Score: 38.51 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006568 742 CSENCKA--CIGF--HNCTECKGglSLQGSRCSVTC-----EDGQFFNGHDCQPCHRFC------ATCSGAGADGCINCT 806
Cdd:pfam14843 2 CDPLCSSegCWGPgpDQCLSCRN--FSRGGTCVESCnilqgEPREYVVNSTCVPCHPEClpqngtATCSGPGADNCTKCA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 569006568 807 egYVMEEGRCVQSCSVSYYLDHSSEGGY----KSCKRCDNSC-LTCNGPGFKNC 855
Cdd:pfam14843 80 --HFRDGPHCVSSCPSGVLGENDLIWKYadanGVCQPCHPNCtQGCTGPGLTGC 131
|
|
| |
