|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
211-408 |
2.88e-80 |
|
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
:
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 255.62 E-value: 2.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPEGC-CvqadaE 368
Cdd:cd04269 81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 341940607 369 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 408
Cdd:cd04269 156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
503-645 |
1.08e-44 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 157.14 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 503 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 582
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940607 583 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 645
Cdd:smart00608 80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
427-501 |
2.02e-34 |
|
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
:
Pssm-ID: 214490 Cd Length: 75 Bit Score: 125.88 E-value: 2.02e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940607 427 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 501
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
39-153 |
6.10e-28 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
:
Pssm-ID: 460254 Cd Length: 128 Bit Score: 109.33 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562 1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78
|
90 100 110
....*....|....*....|....*....|....*
gi 341940607 119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562 79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
211-408 |
2.88e-80 |
|
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 255.62 E-value: 2.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPEGC-CvqadaE 368
Cdd:cd04269 81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 341940607 369 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 408
Cdd:cd04269 156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
211-408 |
4.95e-78 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 249.91 E-value: 4.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWR-RG 289
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 290 VWARRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPE--GCCVQada 367
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 341940607 368 EQGGCVMEAATGHPFPRVFSACSRRQLRTFFRKGGGPCLSN 408
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFN 198
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
503-645 |
1.08e-44 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 157.14 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 503 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 582
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940607 583 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 645
Cdd:smart00608 80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
504-612 |
1.99e-36 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 132.35 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 504 DGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQdHKGSFLPCAQRDALCGKLLCQGGE 583
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79
|
90 100
....*....|....*....|....*....
gi 341940607 584 PNPLVPHIVTMDSTILlegREVVCRGAFV 612
Cdd:pfam08516 80 ELPLLGEHATVIYTNI---NGVTCWGTDY 105
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
427-501 |
2.02e-34 |
|
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
Pssm-ID: 214490 Cd Length: 75 Bit Score: 125.88 E-value: 2.02e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940607 427 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 501
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
427-499 |
3.33e-32 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 119.27 E-value: 3.33e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940607 427 EAGEECDCGSGQKC-PDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPAD 499
Cdd:pfam00200 1 EEGEECDCGSLEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
39-153 |
6.10e-28 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 109.33 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562 1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78
|
90 100 110
....*....|....*....|....*....|....*
gi 341940607 119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562 79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
211-408 |
2.88e-80 |
|
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 255.62 E-value: 2.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGV 290
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 291 WA-RRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPEGC-CvqadaE 368
Cdd:cd04269 81 LLpRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 341940607 369 QGGCVMEAATGHPfPRVFSACSRRQLRTFFRKGGGPCLSN 408
Cdd:cd04269 156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
211-408 |
4.95e-78 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 249.91 E-value: 4.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWR-RG 289
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 290 VWARRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPE--GCCVQada 367
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 341940607 368 EQGGCVMEAATGHPFPRVFSACSRRQLRTFFRKGGGPCLSN 408
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFN 198
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
503-645 |
1.08e-44 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 157.14 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 503 LDGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQDHkGSFLPCAQRDALCGKLLCQGG 582
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940607 583 EPNPLV-PHIVTMDSTIllegREVVCRGAFVLPDSHldqLDLGLVEPGTGCGPRMVCQDRHCQN 645
Cdd:smart00608 80 SELPLLgEHATVIYSNI----GGLVCWSLDYHLGTD---PDIGMVKDGTKCGPGKVCINGQCVD 136
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
504-612 |
1.99e-36 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 132.35 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 504 DGSPCAEGRGYCLDGWCPTLEQQCQQLWGPGSKPAPEPCFQQMNSMGNSQGNCGQdHKGSFLPCAQRDALCGKLLCQGGE 583
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79
|
90 100
....*....|....*....|....*....
gi 341940607 584 PNPLVPHIVTMDSTILlegREVVCRGAFV 612
Cdd:pfam08516 80 ELPLLGEHATVIYTNI---NGVTCWGTDY 105
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
211-399 |
5.58e-35 |
|
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239795 Cd Length: 192 Bit Score: 131.77 E-value: 5.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 211 RYLELYIVADHTLFLLQHQNLNHTRQRLLEVANCVDQILRTLD----IQLVLTGLEVW-TEQDLSRITQDANETLWAFLQ 285
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 286 WRRGVWARrpHDSTQLLTGRTF-QGTTVGLAPVEGICRAESSGGVSTDHSELPIgTAATMAHEIGHSLGLHHDPEGCCVQ 364
Cdd:cd04267 81 WRAEGPIR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGGDELAF 157
|
170 180 190
....*....|....*....|....*....|....*
gi 341940607 365 ADAEQGGCVMEAATGHPFPRVFSACSRRQLRTFFR 399
Cdd:cd04267 158 ECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
427-501 |
2.02e-34 |
|
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
Pssm-ID: 214490 Cd Length: 75 Bit Score: 125.88 E-value: 2.02e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341940607 427 EAGEECDCGSGQKCPDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPADVY 501
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
427-499 |
3.33e-32 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 119.27 E-value: 3.33e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940607 427 EAGEECDCGSGQKC-PDPCCFAHNCSLRAGAQCAHGDCCARCLLKSAGTPCRPAATDCDLPEFCTGTSPYCPAD 499
Cdd:pfam00200 1 EEGEECDCGSLEECtNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
211-406 |
1.72e-29 |
|
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.
Pssm-ID: 239801 Cd Length: 207 Bit Score: 116.57 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 211 RYLELYIVADHTLFLLQHQNlnHTRQRLLEVANCVDQILR--TL--DIQLVLTGLEVWT-EQDLSRITQDANETLWAFLQ 285
Cdd:cd04273 1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEdEESGLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 286 WRRGVWARRP-----HDSTQLLTGRTFQG-----TTVGLAPVEGICRAESSGGVSTDHselPIGTAATMAHEIGHSLGLH 355
Cdd:cd04273 79 WQKKLNPPNDsdpehHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSINEDT---GLSSAFTIAHELGHVLGMP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 341940607 356 HDPEG--CcvqADAEQGGCVMEAATGHPFPRVF-SACSRRQLRTFFRKGGGPCL 406
Cdd:cd04273 156 HDGDGnsC---GPEGKDGHIMSPTLGANTGPFTwSKCSRRYLTSFLDTGDGNCL 206
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
39-153 |
6.10e-28 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 109.33 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 39 ELVTPHWILEGRLwlKVTLEEPILKPDSVLVALEAEGQDLLLELEKKHKLLAPGYTETHYRPDGHPVVLSPNHTDHCQYH 118
Cdd:pfam01562 1 EVVIPVRLDPSRR--RRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78
|
90 100 110
....*....|....*....|....*....|....*
gi 341940607 119 GRVRGFRESWVVLSTCSGMSGLIVLSSKVsYYLQP 153
Cdd:pfam01562 79 GHVEGHPDSSVALSTCSGLRGFIRTENEE-YLIEP 112
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
215-379 |
5.91e-15 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 73.99 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 215 LYIVADHTlFLLQHQNlNHTRQRLLEVANCVDQIL-RTLDIQLVLTGLEVWTEQDLS----RITQDANETLWAFlQWRRG 289
Cdd:pfam13688 7 LLVAADCS-YVAAFGG-DAAQANIINMVNTASNVYeRDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEF-QDFSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 290 VWARRPHDSTQLLTGRTFQGTtvGLAPVEGICRAESSGGVSTDHSE--LPIGTAA---TMAHEIGHSLGLHHDPegccvQ 364
Cdd:pfam13688 84 WRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGnnVVVSTATewqVFAHEIGHNFGAVHDC-----D 156
|
170
....*....|....*
gi 341940607 365 ADAEQGGCVMEAATG 379
Cdd:pfam13688 157 SSTSSQCCPPSNSTC 171
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
243-357 |
6.85e-15 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 463926 [Multi-domain] Cd Length: 122 Bit Score: 71.63 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 243 NCVDQILRT-LDIQLVLTGLEVWTEQDLSRITQDANETLWAFLQWRRGVWARRPHDSTQLLTGRTFQGTTvGLAPVEGIC 321
Cdd:pfam13582 8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGG-GIAYVGGVC 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 341940607 322 RAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHD 357
Cdd:pfam13582 87 NSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
211-397 |
4.55e-14 |
|
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.
Pssm-ID: 238124 [Multi-domain] Cd Length: 167 Bit Score: 70.63 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 211 RYLELYIVADHtlfllQHQNLNHTRQRLLEVANCVDQILRT-LDIQLVLTGLEVwteqdlsritqdanetlwaflqwrrg 289
Cdd:cd00203 1 KVIPYVVVADD-----RDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEI-------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 290 vwarRPHDSTQLLTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATMAHEIGHSLGLHHDPEGCCVQADAE- 368
Cdd:cd00203 50 ----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTi 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 341940607 369 ---------QGGCVMEAATG---HPFPRVFSACSRRQLRTF 397
Cdd:cd00203 126 ddtlnaeddDYYSVMSYTKGsfsDGQRKDFSQCDIDQINKL 166
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
212-406 |
2.80e-11 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 63.91 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 212 YLELYIVADHtlfllQHQNLNHTRQRLLE----VANCVDQILRTL---DIQLVLTGLEVWTEQD-------LSRITQDAN 277
Cdd:cd04272 2 YPELFVVVDY-----DHQSEFFSNEQLIRylavMVNAANLRYRDLkspRIRLLLVGITISKDPDfepyihpINYGYIDAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 278 ETLWAFLQWRRGVWARRPHDSTQLLTGR---TFQG-----TTVGLAPVEGICrAESSGGVSTDHSELPIGtAATMAHEIG 349
Cdd:cd04272 77 ETLENFNEYVKKKRDYFNPDVVFLVTGLdmsTYSGgslqtGTGGYAYVGGAC-TENRVAMGEDTPGSYYG-VYTMTHELA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940607 350 HSLGLHHDPEGCC--VQADAEQGGC----------VMEAATGHPfprvFSACSRRQLRTFFRKGGGPCL 406
Cdd:cd04272 155 HLLGAPHDGSPPPswVKGHPGSLDCpwddgyimsyVVNGERQYR----FSQCSQRQIRNVFRRLGASCL 219
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
215-412 |
4.77e-10 |
|
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.
Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 60.85 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 215 LYIVADHTLFllQH---QNLNHTRQRLLEVANCVDQILRTLD--------IQLVLTGLEVWTEQDlsRITQDANETLWAF 283
Cdd:cd04270 5 LLLVADHRFY--KYmgrGEEETTINYLISHIDRVDDIYRNTDwdgggfkgIGFQIKRIRIHTTPD--EVDPGNKFYNKSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 284 LQWRRGVWARRpHDSTQ---------LLTGRTFQGTTVGLAPVeGICRAESSGGVSTDHSELPIGTAA------------ 342
Cdd:cd04270 81 PNWGVEKFLVK-LLLEQfsddvclahLFTYRDFDMGTLGLAYV-GSPRDNSAGGICEKAYYYSNGKKKylntgltttvny 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 343 -----------TMAHEIGHSLGLHHDPEGC-CVQADAEQGGCVM--EAATG-HPFPRVFSACSRRQLRTFFRKGGGPCLS 407
Cdd:cd04270 159 gkrvptkesdlVTAHELGHNFGSPHDPDIAeCAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSCFV 238
|
....*
gi 341940607 408 NTSAP 412
Cdd:cd04270 239 ERSQS 243
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
234-396 |
5.05e-07 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 372637 Cd Length: 193 Bit Score: 50.71 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 234 TRQRLLEVANCVDQILRTLDI----QLVLTG-LEVWTE-------QDLSRITQDANETLwaFLQWRrgvwARRPHDSTQL 301
Cdd:pfam13574 3 VTENLVNVVNRVNQIYEPDDIningGLVNPGeIPATTSasdsgnnYCNSPTTIVRRLNF--LSQWR----GEQDYCLAHL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 302 LTGRTFQGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAATM---------AHEIGHSLGLHHDPEG-----CCVQADA 367
Cdd:pfam13574 77 VTMGTFSGGELGLAYVGQICQKGASSPKTNTGLSTTTNYGSFNyptqewdvvAHEVGHNFGATHDCDGsqyasSGCERNA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 341940607 368 EQGGC------VMeAATGHPFPRVFSACSRRQLRT 396
Cdd:pfam13574 157 ATSVCsangsfIM-NPASKSNNDLFSPCSISLICD 190
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
275-407 |
4.38e-05 |
|
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.
Pssm-ID: 239799 [Multi-domain] Cd Length: 228 Bit Score: 45.49 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940607 275 DANETLWAFLQWRrgvwARRPHDSTQLLTGRTF--QGTTVGLAPVEGICRAESSGGVSTDHSELPIGTAAT-----MAHE 347
Cdd:cd04271 77 DIDDRLSIFSQWR----GQQPDDGNAFWTLMTAcpSGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHE 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341940607 348 IGHSLGLHHD-PEGCCVQADAEQGGC--------------VMEAATGHPFPRvFSACSRRQLRTFFRKGG--GPCLS 407
Cdd:cd04271 153 IGHTFGAVHDcTSGTCSDGSVGSQQCcplststcdangqyIMNPSSSSGITE-FSPCTIGNICSLLGRNPvrTSCLS 228
|
|
| ZnMc_pappalysin_like |
cd04275 |
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ... |
306-366 |
7.81e-05 |
|
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.
Pssm-ID: 239802 [Multi-domain] Cd Length: 225 Bit Score: 44.64 E-value: 7.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940607 306 TFQGTTVGLAPVEGIC--RAESSGGVSTDhselPIGTAATMAHEIGHSLGLHH---DPEGCCVQAD 366
Cdd:cd04275 105 TFPDSLVSLAFITDGVviNPSSLPGGSAA----PYNLGDTATHEVGHWLGLYHtfqGGSPCCTTGD 166
|
|
| |
