|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
198-396 |
8.70e-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: 258.31 E-value: 8.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVQKYQ-DFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 276
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 277 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 356
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966920715 357 paKTCIMEASTDFLPgLNFSNCSRQALEKALLDGMGSCLF 396
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
493-625 |
9.50e-40 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 142.11 E-value: 9.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 493 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGGYVSCTPRDAICGQLQCQTGR 572
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 966920715 573 TQPLLGSIQDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLV 625
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKV 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
415-488 |
2.78e-35 |
|
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: 127.42 E-value: 2.78e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966920715 415 EPGEQCDCGFPDDCADPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 488
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| Pep_M12B_propep super family |
cl03265 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
72-130 |
1.40e-08 |
|
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.
The actual alignment was detected with superfamily member pfam01562:
Pssm-ID: 460254 Cd Length: 128 Bit Score: 53.47 E-value: 1.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 966920715 72 RELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVQGYAASWVSVCTCSGLRGLVVLS 130
Cdd:pfam01562 46 RLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
198-396 |
8.70e-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: 258.31 E-value: 8.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVQKYQ-DFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 276
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 277 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 356
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966920715 357 paKTCIMEASTDFLPgLNFSNCSRQALEKALLDGMGSCLF 396
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
198-403 |
2.75e-74 |
|
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: 236.43 E-value: 2.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVQKY-QDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 276
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 277 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPgpa 356
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966920715 357 PAKTCIMEASTDFLPGLNFSNCSRQALEKALLDGMGSCLFerlpNLP 403
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLF----NKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
493-625 |
9.50e-40 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 142.11 E-value: 9.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 493 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGGYVSCTPRDAICGQLQCQTGR 572
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 966920715 573 TQPLLGSIQDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLV 625
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKV 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
415-488 |
2.78e-35 |
|
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: 127.42 E-value: 2.78e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966920715 415 EPGEQCDCGFPDDCADPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 488
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
415-488 |
2.62e-34 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 124.66 E-value: 2.62e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966920715 415 EPGEQCDCGFPDDCA-DPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 488
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
493-602 |
2.10e-33 |
|
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: 123.49 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 493 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPsGGYVSCTPRDAICGQLQCQTGR 572
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 966920715 573 TQPLLGSIQDLLWETIdvngTELNCSWVHL 602
Cdd:pfam08516 80 ELPLLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
72-130 |
1.40e-08 |
|
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: 53.47 E-value: 1.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 966920715 72 RELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVQGYAASWVSVCTCSGLRGLVVLS 130
Cdd:pfam01562 46 RLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 104
|
|
| COG1913 |
COG1913 |
Predicted Zn-dependent protease [General function prediction only]; |
331-377 |
6.07e-03 |
|
Predicted Zn-dependent protease [General function prediction only];
Pssm-ID: 441517 Cd Length: 175 Bit Score: 38.01 E-value: 6.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966920715 331 IAHELGHSLGLDHdlpgnsCPCPGpapaktCIMeastdflpglNFSN 377
Cdd:COG1913 127 AVHELGHLFGLGH------CPNPR------CVM----------HFSN 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
198-396 |
8.70e-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: 258.31 E-value: 8.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVQKYQ-DFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 276
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 277 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 356
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966920715 357 paKTCIMEASTDFLPgLNFSNCSRQALEKALLDGMGSCLF 396
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
198-403 |
2.75e-74 |
|
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: 236.43 E-value: 2.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVQKY-QDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 276
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 277 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPgpa 356
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966920715 357 PAKTCIMEASTDFLPGLNFSNCSRQALEKALLDGMGSCLFerlpNLP 403
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLF----NKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
493-625 |
9.50e-40 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 142.11 E-value: 9.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 493 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGGYVSCTPRDAICGQLQCQTGR 572
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 966920715 573 TQPLLGSIQDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLV 625
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKV 128
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
415-488 |
2.78e-35 |
|
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: 127.42 E-value: 2.78e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966920715 415 EPGEQCDCGFPDDCADPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 488
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
415-488 |
2.62e-34 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 124.66 E-value: 2.62e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966920715 415 EPGEQCDCGFPDDCA-DPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 488
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
493-602 |
2.10e-33 |
|
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: 123.49 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 493 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPsGGYVSCTPRDAICGQLQCQTGR 572
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 966920715 573 TQPLLGSIQDLLWETIdvngTELNCSWVHL 602
Cdd:pfam08516 80 ELPLLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
198-387 |
1.43e-29 |
|
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: 115.60 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVQKYQ-DFQHLLNRTLEVALLLDTFFR----PLNVRVALVGLEAW-TQRDLVEISPNPAVTLENFLH 271
Cdd:cd04267 1 REIELVVVADHRMVSYFNsDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 272 WRRAHLlPRlpHDSAQLVTGTSF-SGPMVGMAIQNSICSPDFSGGVNMDHSTSILgVASSIAHELGHSLGLDHDlPGNSC 350
Cdd:cd04267 81 WRAEGP-IR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHD-GGDEL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 966920715 351 PCPGPApAKTCIMEASTDFLPGLNFSNCSRQALEKAL 387
Cdd:cd04267 156 AFECDG-GGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
198-396 |
6.85e-27 |
|
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: 108.48 E-value: 6.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVQKY--QDFQH----LLNrtlEVALLL-DTFFRPlNVRVALVGLEAWTQR-DLVEISPNPAVTLENF 269
Cdd:cd04273 1 RYVETLVVADSKMVEFHhgEDLEHyiltLMN---IVASLYkDPSLGN-SINIVVVRLIVLEDEeSGLLISGNAQKSLKSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 270 LHWRRAHLLPR----LPHDSAQLVTGTSFSGP-----MVGMAIQNSICSPDFSGGVNMDHStsiLGVASSIAHELGHSLG 340
Cdd:cd04273 77 CRWQKKLNPPNdsdpEHHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELGHVLG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 966920715 341 LDHDLPGNSCpcpGPAPAKTCIMEASTDFLPG-LNFSNCSRQALEKALLDGMGSCLF 396
Cdd:cd04273 154 MPHDGDGNSC---GPEGKDGHIMSPTLGANTGpFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
197-363 |
8.43e-14 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 70.14 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 197 TKTVELVIVADHSEVQKY-----QDF-QHLLNRTLEVallldtFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFL 270
Cdd:pfam13688 2 TRTVALLVAADCSYVAAFggdaaQANiINMVNTASNV------YERDFNISLGLVNLTISDSTCPYTPPACSTGDSSDRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 271 H-------WRRAHllprlPHDSAQLVTGTSFSGPmvGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHS 338
Cdd:pfam13688 76 SefqdfsaWRGTQ-----NDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHN 148
|
170 180 190
....*....|....*....|....*....|....
gi 966920715 339 LGLDHD----LPGNSCP-----CPGPApakTCIM 363
Cdd:pfam13688 149 FGAVHDcdssTSSQCCPpsnstCPAGG---RYIM 179
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
198-387 |
6.90e-11 |
|
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: 61.38 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVqKYQDFQHllnRTLEVALLLDTFFR-PLNVRVALVGLEawtqrdlveispnpavtlenflhwrrah 276
Cdd:cd00203 1 KVIPYVVVADDRDV-EEENLSA---QIQSLILIAMQIWRdYLNIRFVLVGVE---------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 277 llpRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlPGNSCPCPGPA 356
Cdd:cd00203 49 ---IDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHD-HDRKDRDDYPT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 966920715 357 PAKT---------CIMEASTDFLPGLN---FSNCSRQALEKAL 387
Cdd:cd00203 125 IDDTlnaedddyySVMSYTKGSFSDGQrkdFSQCDIDQINKLY 167
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
236-344 |
2.12e-10 |
|
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: 58.54 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 236 RPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAhllpRLPH---DSAQLVTGTSFSGpMVGMAIQNSICSPDF 312
Cdd:pfam13582 16 RDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQygyDLGHLFTGRDGGG-GGGIAYVGGVCNSGS 90
|
90 100 110
....*....|....*....|....*....|..
gi 966920715 313 SGGVNMDHSTSILGVASSIAHELGHSLGLDHD 344
Cdd:pfam13582 91 KFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
72-130 |
1.40e-08 |
|
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: 53.47 E-value: 1.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 966920715 72 RELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVQGYAASWVSVCTCSGLRGLVVLS 130
Cdd:pfam01562 46 RLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 104
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
199-381 |
1.90e-07 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 52.35 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 199 TVELVIVADhsevqkyQDFQHLLNRTLEVALLLDTFFRPLN----------VRVALVGLE----AWTQRDLVEISP---N 261
Cdd:cd04272 2 YPELFVVVD-------YDHQSEFFSNEQLIRYLAVMVNAANlryrdlksprIRLLLVGITiskdPDFEPYIHPINYgyiD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 262 PAVTLENF-LHWRRAHLLPRlpHDSAQLVTG----TSFSGPM----VGMAIQNSICSpDFSGGVNMDHSTSILGVaSSIA 332
Cdd:cd04272 75 AAETLENFnEYVKKKRDYFN--PDVVFLVTGldmsTYSGGSLqtgtGGYAYVGGACT-ENRVAMGEDTPGSYYGV-YTMT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966920715 333 HELGHSLGLDHD-LPGNSCPCPGPApAKTC------IMeaSTDF--LPGLNFSNCSRQ 381
Cdd:cd04272 151 HELAHLLGAPHDgSPPPSWVKGHPG-SLDCpwddgyIM--SYVVngERQYRFSQCSQR 205
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
284-380 |
2.03e-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: 51.86 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 284 DSAQLVTGTSFSGPMVGMAIQNSIC-------------SPDFSGGVNMDHSTSILgvasSIAHELGHSLGLDHDLPGNSC 350
Cdd:pfam13574 72 CLAHLVTMGTFSGGELGLAYVGQICqkgasspktntglSTTTNYGSFNYPTQEWD----VVAHEVGHNFGATHDCDGSQY 147
|
90 100 110
....*....|....*....|....*....|....*...
gi 966920715 351 PCPG-PAPAKTCIMEASTDFL----PGLN---FSNCSR 380
Cdd:pfam13574 148 ASSGcERNAATSVCSANGSFImnpaSKSNndlFSPCSI 185
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
198-381 |
4.38e-06 |
|
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: 48.00 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 198 KTVELVIVADHSEVQKYQDFQHLLNRTLE-VALLLDTFFRPLNVRVALVGleawtQRDLVEISPNPA-----VTLENFLH 271
Cdd:pfam13583 3 RVYRVAVATDCTYSASFGSVDELRANINAtVTTANEVYGRDFNVSLALIS-----DRDVIYTDSSTDsfnadCSGGDLGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 272 WRRAHL---LPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSggvNMDHStsilGVASS------IAHELGHSLGLD 342
Cdd:pfam13583 78 WRLATLtswRDSLNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQ---NAKAS----GVARSrdewdiFAHEIGHTFGAV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 966920715 343 HDLpGNSCPcpgPAPAKTC------IME-ASTDFLPglNFSNCSRQ 381
Cdd:pfam13583 151 HDC-SSQGE---GLSSSTEdgsgqtIMSyASTASQT--AFSPCTIR 190
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
286-398 |
5.26e-06 |
|
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: 48.14 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920715 286 AQLVTGTSFSGPMVGMAIQNS--------ICSPD--FSGGVN----------MDHSTSILGVASSI--AHELGHSLGLDH 343
Cdd:cd04270 104 AHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAyyYSNGKKkylntgltttVNYGKRVPTKESDLvtAHELGHNFGSPH 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 966920715 344 DLPGNSCpCPGPAPAKTCIMEA---STDFLPGLNFSNCSRQALEKALLDGMGSCLFER 398
Cdd:cd04270 184 DPDIAEC-APGESQGGNYIMYAratSGDKENNKKFSPCSKKSISKVLEVKSNSCFVER 240
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
295-367 |
9.49e-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: 44.33 E-value: 9.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966920715 295 SGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEAST 367
Cdd:cd04271 108 SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHTFGAVHDCTSGTCSDGSVGSQQCCPLSTST 185
|
|
| Peptidase_M10 |
pfam00413 |
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
315-343 |
3.79e-03 |
|
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.
Pssm-ID: 425668 [Multi-domain] Cd Length: 159 Bit Score: 38.37 E-value: 3.79e-03
10 20
....*....|....*....|....*....
gi 966920715 315 GVNMDHSTSILGVAssiAHELGHSLGLDH 343
Cdd:pfam00413 99 GSDPPHGINLFLVA---AHEIGHALGLGH 124
|
|
| COG1913 |
COG1913 |
Predicted Zn-dependent protease [General function prediction only]; |
331-377 |
6.07e-03 |
|
Predicted Zn-dependent protease [General function prediction only];
Pssm-ID: 441517 Cd Length: 175 Bit Score: 38.01 E-value: 6.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966920715 331 IAHELGHSLGLDHdlpgnsCPCPGpapaktCIMeastdflpglNFSN 377
Cdd:COG1913 127 AVHELGHLFGLGH------CPNPR------CVM----------HFSN 151
|
|
| |
