|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
211-409 |
8.47e-86 |
|
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: 273.02 E-value: 8.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 289
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 290 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHD--SAHCCSASAa 367
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6752966 368 dGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMP 409
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
502-650 |
2.96e-50 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 173.32 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 502 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGlNGQYRKCSPRDAKCGKIQCQST 581
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 582 QARP-LESNAVSIDTTItlngRRIHCRGTHVYRGPEEeegegdmlDPGLVMTGTKCGHNHICFEGQCRNT 650
Cdd:smart00608 80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP--------DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
45-163 |
1.17e-27 |
|
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: 108.56 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 45 ELIIPQW-------RTSESPGRGKHPLraELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYH 117
Cdd:pfam01562 1 EVVIPVRldpsrrrRSLASESTYLDTL--SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6752966 118 GTVRDVDESSVTLSTCRGIRGLIIVrSNLSYIIEPVPNSDS-----QHRIY 163
Cdd:pfam01562 79 GHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSReegghPHVVY 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
440-500 |
3.58e-27 |
|
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: 105.08 E-value: 3.58e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6752966 440 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYY 500
Cdd:smart00050 15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
211-409 |
8.47e-86 |
|
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: 273.02 E-value: 8.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 289
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 290 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHD--SAHCCSASAa 367
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6752966 368 dGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMP 409
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
211-407 |
2.29e-83 |
|
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: 266.40 E-value: 2.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 289
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 290 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHC-CSASaad 368
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtCGRS--- 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 6752966 369 gGCIMAAATGHPfPKVFSWCNRKELDRYLQTGGGMCLSN 407
Cdd:cd04269 158 -TCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
502-650 |
2.96e-50 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 173.32 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 502 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGlNGQYRKCSPRDAKCGKIQCQST 581
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 582 QARP-LESNAVSIDTTItlngRRIHCRGTHVYRGPEEeegegdmlDPGLVMTGTKCGHNHICFEGQCRNT 650
Cdd:smart00608 80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP--------DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
503-611 |
3.64e-39 |
|
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: 140.44 E-value: 3.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 503 DGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKgLNGQYRKCSPRDAKCGKIQCQSTQ 582
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 6752966 583 ARP-LESNAVSIDTTItlngRRIHCRGTHV 611
Cdd:pfam08516 80 ELPlLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
45-163 |
1.17e-27 |
|
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: 108.56 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 45 ELIIPQW-------RTSESPGRGKHPLraELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYH 117
Cdd:pfam01562 1 EVVIPVRldpsrrrRSLASESTYLDTL--SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6752966 118 GTVRDVDESSVTLSTCRGIRGLIIVrSNLSYIIEPVPNSDS-----QHRIY 163
Cdd:pfam01562 79 GHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSReegghPHVVY 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
440-500 |
3.58e-27 |
|
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: 105.08 E-value: 3.58e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6752966 440 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYY 500
Cdd:smart00050 15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
440-498 |
2.48e-25 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 100.01 E-value: 2.48e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6752966 440 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTN 498
Cdd:pfam00200 16 NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
211-409 |
8.47e-86 |
|
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: 273.02 E-value: 8.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 289
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 290 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHD--SAHCCSASAa 367
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6752966 368 dGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMP 409
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
211-407 |
2.29e-83 |
|
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: 266.40 E-value: 2.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRK- 289
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 290 LLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHC-CSASaad 368
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtCGRS--- 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 6752966 369 gGCIMAAATGHPfPKVFSWCNRKELDRYLQTGGGMCLSN 407
Cdd:cd04269 158 -TCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
502-650 |
2.96e-50 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 173.32 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 502 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGlNGQYRKCSPRDAKCGKIQCQST 581
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 582 QARP-LESNAVSIDTTItlngRRIHCRGTHVYRGPEEeegegdmlDPGLVMTGTKCGHNHICFEGQCRNT 650
Cdd:smart00608 80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP--------DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
503-611 |
3.64e-39 |
|
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: 140.44 E-value: 3.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 503 DGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKgLNGQYRKCSPRDAKCGKIQCQSTQ 582
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 6752966 583 ARP-LESNAVSIDTTItlngRRIHCRGTHV 611
Cdd:pfam08516 80 ELPlLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
211-405 |
3.80e-33 |
|
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: 126.97 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADyAEFQKNRHDQDaTKRKLMEIANYVDKFYR--SL--NIRIALVGLEVWTHGDK-CEVSENPYSTLWSFLS 285
Cdd:cd04273 1 RYVETLVVAD-SKMVEFHHGED-LEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 286 WRRKLLAQ-----KSHDNAQLITGRSFQG-----TTIGLAPLMAMCSVYQSGGVSMDhseNAIGVASTVAHEIGHNFGMS 355
Cdd:cd04273 79 WQKKLNPPndsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSINED---TGLSSAFTIAHELGHVLGMP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6752966 356 HD-SAHCCSASAADgGCIMAAATGHPFPKvFSW--CNRKELDRYLQTGGGMCL 405
Cdd:cd04273 156 HDgDGNSCGPEGKD-GHIMSPTLGANTGP-FTWskCSRRYLTSFLDTGDGNCL 206
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
211-397 |
5.39e-33 |
|
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: 126.00 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRS----LNIRIALVGLEVWtHGdKCEVSENPYS---TLWSF 283
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQIL-KG-EQFAPPIDSDasnTLNSF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 284 LSWRRKLLAqkSHDNAQLITGRSF-QGTTIGLAPLMAMCSVYQSGGVSMDHSENAIgVASTVAHEIGHNFGMSHDSAHCC 362
Cdd:cd04267 79 SFWRAEGPI--RHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGGDEL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 6752966 363 SASA-ADGGCIMAAATGHPFPKVFSWCNRKELDRYL 397
Cdd:cd04267 156 AFECdGGGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
45-163 |
1.17e-27 |
|
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: 108.56 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 45 ELIIPQW-------RTSESPGRGKHPLraELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYH 117
Cdd:pfam01562 1 EVVIPVRldpsrrrRSLASESTYLDTL--SYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6752966 118 GTVRDVDESSVTLSTCRGIRGLIIVrSNLSYIIEPVPNSDS-----QHRIY 163
Cdd:pfam01562 79 GHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSReegghPHVVY 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
440-500 |
3.58e-27 |
|
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: 105.08 E-value: 3.58e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6752966 440 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYY 500
Cdd:smart00050 15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
440-498 |
2.48e-25 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 100.01 E-value: 2.48e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6752966 440 KNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTN 498
Cdd:pfam00200 16 NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
213-379 |
1.87e-20 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 90.17 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 213 VELYLVADYaEFQKNrHDQDATKRKLMEIANYVD-KFYRSLNIRIALVGLEVWTHGD----KCEVSENPYSTLWSFLSwR 287
Cdd:pfam13688 5 VALLVAADC-SYVAA-FGGDAAQANIINMVNTASnVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQD-F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 288 RKLLAQKSHDNAQLITGRSFQGTtiGLAPLMAMCSVYQSGGVSMDHSENAIGVAS-----TVAHEIGHNFGMSHDSA--- 359
Cdd:pfam13688 82 SAWRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCDsst 159
|
170 180
....*....|....*....|....*.
gi 6752966 360 --HCCSASA----ADGGCIMAAATGH 379
Cdd:pfam13688 160 ssQCCPPSNstcpAGGRYIMNPSSSP 185
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
211-396 |
4.76e-18 |
|
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: 82.57 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADyaefqKNRHDQDATKRKLMEIANYVDKFYRS-LNIRIALVGLEVwthgdkcevsenpystlwsflswrrk 289
Cdd:cd00203 1 KVIPYVVVAD-----DRDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEI-------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 290 llaqKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHCC------- 362
Cdd:cd00203 50 ----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDrddypti 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 6752966 363 ----SASAADGGCIMaaatgHPFPKVFSWCNRKELDRY 396
Cdd:cd00203 126 ddtlNAEDDDYYSVM-----SYTKGSFSDGQRKDFSQC 158
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
243-357 |
2.29e-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: 73.17 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 243 NYVDKFYRS-LNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRKLLAQKSHDNAQLITGRSFQGTTiGLAPLMAMC 321
Cdd:pfam13582 8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGG-GIAYVGGVC 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 6752966 322 SVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHD 357
Cdd:pfam13582 87 NSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
233-377 |
4.10e-12 |
|
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: 66.11 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 233 ATKRKLMEIANYVDKFYR--SLNIRIALVGLevwthgDKCEV------SENPYSTLWSFLSWRRKLLAQ----KSHDNAQ 300
Cdd:pfam13574 2 NVTENLVNVVNRVNQIYEpdDININGGLVNP------GEIPAttsasdSGNNYCNSPTTIVRRLNFLSQwrgeQDYCLAH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 301 LITGRSFQGTTIGLAPLMAMC-----SVYQSGGVSMDHSENAIGVAST----VAHEIGHNFGMSHDsahCCSASAADGGC 371
Cdd:pfam13574 76 LVTMGTFSGGELGLAYVGQICqkgasSPKTNTGLSTTTNYGSFNYPTQewdvVAHEVGHNFGATHD---CDGSQYASSGC 152
|
....*.
gi 6752966 372 IMAAAT 377
Cdd:pfam13574 153 ERNAAT 158
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
215-404 |
1.01e-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: 63.16 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 215 LYLVADYAEFQK-NRHDQDATKRKLMEIANYVDKFYRSL--------NIRIALVGLEVWTHGDKCEVSENPY---STLWS 282
Cdd:cd04270 5 LLLVADHRFYKYmGRGEEETTINYLISHIDRVDDIYRNTdwdgggfkGIGFQIKRIRIHTTPDEVDPGNKFYnksFPNWG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 283 FLSWRRKLLAQKSHDN---AQLITGRSFQGTTIGLAPLMA--------MCSVYQSGGVSMDHSENAiGVASTV------- 344
Cdd:cd04270 85 VEKFLVKLLLEQFSDDvclAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAYYYSNGKKKYLNT-GLTTTVnygkrvp 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6752966 345 --------AHEIGHNFGMSHDS--AHCCSASAADGGCIM--AAATG-HPFPKVFSWCNRKELDRYLQTGGGMC 404
Cdd:cd04270 164 tkesdlvtAHELGHNFGSPHDPdiAECAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSC 236
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
231-378 |
8.15e-10 |
|
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: 60.13 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 231 QDATKRKLMEIANYVDKFYR-SLNIRIALVGLEVwthGDKCEVSENPYSTLWS---------------FLSWRrkllAQK 294
Cdd:cd04271 20 VEEARRNILNNVNSASQLYEsSFNISLGLRNLTI---SDASCPSTAVDSAPWNlpcnsrididdrlsiFSQWR----GQQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 295 SHDNAQLITGRSF--QGTTIGLAPLMAMC-SVYQSGGVSMDHSENAIGVAST----VAHEIGHNFGMSHD---------- 357
Cdd:cd04271 93 PDDGNAFWTLMTAcpSGSEVGVAWLGQLCrTGASDQGNETVAGTNVVVRTSNewqvFAHEIGHTFGAVHDctsgtcsdgs 172
|
170 180
....*....|....*....|....*..
gi 6752966 358 --SAHCCSASA----ADGGCIMAAATG 378
Cdd:cd04271 173 vgSQQCCPLSTstcdANGQYIMNPSSS 199
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
211-376 |
3.48e-08 |
|
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: 404471 Cd Length: 203 Bit Score: 54.55 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 211 KYVELYLVADYaEFQKNRHDQDATKRKLMEIANYVDKFY-RSLNIRIALvglevwtHGDKCEVSENPYSTLW-------- 281
Cdd:pfam13583 3 RVYRVAVATDC-TYSASFGSVDELRANINATVTTANEVYgRDFNVSLAL-------ISDRDVIYTDSSTDSFnadcsggd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 282 -------SFLSWRrkllAQKSHDNAQLITGRSFQGTTIGLAPLMAMC-SVYQS---GGVSMDHSEnaigvASTVAHEIGH 350
Cdd:pfam13583 75 lgnwrlaTLTSWR----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQNakaSGVARSRDE-----WDIFAHEIGH 145
|
170 180 190
....*....|....*....|....*....|.
gi 6752966 351 NFGMSHD-SAHCCSASAA----DGGCIMAAA 376
Cdd:pfam13583 146 TFGAVHDcSSQGEGLSSStedgSGQTIMSYA 176
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
212-405 |
5.60e-08 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 54.28 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 212 YVELYLVADYaEFQKNRHDQDATKRKLMEIANYVDKFYRSLN---IRIALVGLEVWTHGDKCEVSENP-------YSTLW 281
Cdd:cd04272 2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHPInygyidaAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6752966 282 SFLSWRRKLLAQKSHDNAQLITGR--------SFQGTTIGLAPLMAMCSVYqsgGVSMdhSENAIGV---ASTVAHEIGH 350
Cdd:cd04272 81 NFNEYVKKKRDYFNPDVVFLVTGLdmstysggSLQTGTGGYAYVGGACTEN---RVAM--GEDTPGSyygVYTMTHELAH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6752966 351 NFGMSHDSAHCCS---------ASAADGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCL 405
Cdd:cd04272 156 LLGAPHDGSPPPSwvkghpgslDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| |
