|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
214-412 |
8.36e-78 |
|
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: 250.23 E-value: 8.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:cd04269 1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGhsCPCPGpa 372
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 109148517 373 paKSCIMEASTDFLPgLNFSNCSRQALEKALLEGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
509-650 |
1.61e-45 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 159.83 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 509 DGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRsPGGSYMPCAPRDVMCGQLQCQWGR 588
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR-ENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109148517 589 SQPLLGSVQDrlseVLEANGTQLNCSWVDLDLGNDVaQPLLALPGTACGPGLVCIGHRCQPV 650
Cdd:smart00608 81 ELPLLGEHAT----VIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
431-504 |
3.12e-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: 125.11 E-value: 3.12e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148517 431 DPGEQCDCGFPDECTDPCCDHFTCQLRPGAQCASdGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSD 504
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 ... |
74-147 |
1.61e-12 |
|
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: 65.03 E-value: 1.61e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148517 74 LELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLS 147
Cdd:pfam01562 31 LAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 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 ... |
214-412 |
8.36e-78 |
|
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: 250.23 E-value: 8.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:cd04269 1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGhsCPCPGpa 372
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 109148517 373 paKSCIMEASTDFLPgLNFSNCSRQALEKALLEGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
214-414 |
5.94e-67 |
|
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: 221.41 E-value: 5.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGHSCPCPgpa 372
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 109148517 373 PAKSCIMEASTDFLPGLNFSNCSRQALEKALLEGMGSCLFER 414
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNK 199
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
509-650 |
1.61e-45 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 159.83 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 509 DGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRsPGGSYMPCAPRDVMCGQLQCQWGR 588
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR-ENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109148517 589 SQPLLGSVQDrlseVLEANGTQLNCSWVDLDLGNDVaQPLLALPGTACGPGLVCIGHRCQPV 650
Cdd:smart00608 81 ELPLLGEHAT----VIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
509-618 |
2.00e-34 |
|
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: 126.96 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 509 DGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPGGsYMPCAPRDVMCGQLQCQWGR 588
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGG-YVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 109148517 589 SQPLLGSvqdrLSEVLEANGTQLNCSWVDL 618
Cdd:pfam08516 80 ELPLLGE----HATVIYTNINGVTCWGTDY 105
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
431-504 |
3.12e-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: 125.11 E-value: 3.12e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148517 431 DPGEQCDCGFPDECTDPCCDHFTCQLRPGAQCASdGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSD 504
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
431-504 |
2.56e-33 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 122.73 E-value: 2.56e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109148517 431 DPGEQCDCGFPDECT-DPCCDHFTCQLRPGAQCASdGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSD 504
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
74-147 |
1.61e-12 |
|
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: 65.03 E-value: 1.61e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148517 74 LELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLS 147
Cdd:pfam01562 31 LAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 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 ... |
214-412 |
8.36e-78 |
|
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: 250.23 E-value: 8.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:cd04269 1 KYVELVVVVDNSLYKKYgSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGhsCPCPGpa 372
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGG--CTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 109148517 373 paKSCIMEASTDFLPgLNFSNCSRQALEKALLEGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
214-414 |
5.94e-67 |
|
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: 221.41 E-value: 5.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 214 KIVELVIVADNSEVRKY-PDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTD 292
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 293 LLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGHSCPCPgpa 372
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 109148517 373 PAKSCIMEASTDFLPGLNFSNCSRQALEKALLEGMGSCLFER 414
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNK 199
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
509-650 |
1.61e-45 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 159.83 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 509 DGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRsPGGSYMPCAPRDVMCGQLQCQWGR 588
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGR-ENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109148517 589 SQPLLGSVQDrlseVLEANGTQLNCSWVDLDLGNDVaQPLLALPGTACGPGLVCIGHRCQPV 650
Cdd:smart00608 81 ELPLLGEHAT----VIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
509-618 |
2.00e-34 |
|
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: 126.96 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 509 DGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPGGsYMPCAPRDVMCGQLQCQWGR 588
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGG-YVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 109148517 589 SQPLLGSvqdrLSEVLEANGTQLNCSWVDL 618
Cdd:pfam08516 80 ELPLLGE----HATVIYTNINGVTCWGTDY 105
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
431-504 |
3.12e-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: 125.11 E-value: 3.12e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148517 431 DPGEQCDCGFPDECTDPCCDHFTCQLRPGAQCASdGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSD 504
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
431-504 |
2.56e-33 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 122.73 E-value: 2.56e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109148517 431 DPGEQCDCGFPDECT-DPCCDHFTCQLRPGAQCASdGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSD 504
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
216-403 |
5.70e-25 |
|
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: 102.88 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 216 VELVIVADNSEVRKYP-DFQQLLNRTLEAALLLDTFFQ----PLNVRVALVGLEAWTQHNLI-EMSSNPAVLLDNFLRWR 289
Cdd:cd04267 3 IELVVVADHRMVSYFNsDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKGEQFApPIDSDASNTLNSFSFWR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 290 RTDLlPRlpHDSAQLVTVTSF-SGPMVGMAIQNSICSPDFSGGVNMDHSTSILgVASSIAHELGHSLGLDHDsPGHSCPC 368
Cdd:cd04267 83 AEGP-IR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHD-GGDELAF 157
|
170 180 190
....*....|....*....|....*....|....*
gi 109148517 369 PGPApAKSCIMEASTDFLPGLNFSNCSRQALEKAL 403
Cdd:cd04267 158 ECDG-GGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
214-412 |
2.06e-22 |
|
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: 96.15 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 214 KIVELVIVADNSEVRKY--PDFQQ----LLNRtleAALLldtFFQPL---NVRVALVGLEAWT--QHNLiEMSSNPAVLL 282
Cdd:cd04273 1 RYVETLVVADSKMVEFHhgEDLEHyiltLMNI---VASL---YKDPSlgnSINIVVVRLIVLEdeESGL-LISGNAQKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 283 DNFLRWRRTdLLPRLP-----HDSAQLVTVTSFSGP-----MVGMAIQNSICSPDFSGGVNMDHStsiLGVASSIAHELG 352
Cdd:cd04273 74 KSFCRWQKK-LNPPNDsdpehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109148517 353 HSLGLDHDSPGHSCpcpGPAPAKSCIMEASTDFLPG-LNFSNCSRQALEKALLEGMGSCLF 412
Cdd:cd04273 150 HVLGMPHDGDGNSC---GPEGKDGHIMSPTLGANTGpFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
213-379 |
1.43e-12 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 67.06 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 213 TKIVELVIVADNSEVRKYP-DF-QQLLNRTLEAALllDTFFQPLNVRVALVGLEAWTQHNLI----EMSSNPAVLLDNFL 286
Cdd:pfam13688 2 TRTVALLVAADCSYVAAFGgDAaQANIINMVNTAS--NVYERDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 287 R---WRRTDllprlPHDSAQLVTVTSFSGPmvGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHSLGLD 358
Cdd:pfam13688 80 DfsaWRGTQ-----NDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHNFGAV 152
|
170 180 190
....*....|....*....|....*....|
gi 109148517 359 HD----SPGHSCP-----CPGPApakSCIM 379
Cdd:pfam13688 153 HDcdssTSSQCCPpsnstCPAGG---RYIM 179
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
74-147 |
1.61e-12 |
|
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: 65.03 E-value: 1.61e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109148517 74 LELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLS 147
Cdd:pfam01562 31 LAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTE 104
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
254-360 |
9.90e-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: 463926 [Multi-domain] Cd Length: 122 Bit Score: 62.77 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 254 LNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTdllpRLPHDSAQLVTV--TSFSGPMVGMAIQNSICSPDFSGG 331
Cdd:pfam13582 18 LGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYDLGHLftGRDGGGGGGIAYVGGVCNSGSKFG 93
|
90 100
....*....|....*....|....*....
gi 109148517 332 VNMDHSTSILGVASSIAHELGHSLGLDHD 360
Cdd:pfam13582 94 VNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
214-403 |
2.15e-09 |
|
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: 57.53 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 214 KIVELVIVADNSEVrkypDFQQLLNRTLEAALLLDTFF-QPLNVRVALVGLEawtqhnliemssnpavlldnflrwrrtd 292
Cdd:cd00203 1 KVIPYVVVADDRDV----EEENLSAQIQSLILIAMQIWrDYLNIRFVLVGVE---------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 293 llpRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDS--------PGH 364
Cdd:cd00203 49 ---IDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHdrkdrddyPTI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 109148517 365 SCPCPGPAPAKSCIMEASTDFLPGLN---FSNCSRQALEKAL 403
Cdd:cd00203 126 DDTLNAEDDDYYSVMSYTKGSFSDGQrkdFSQCDIDQINKLY 167
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
300-396 |
1.80e-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: 52.25 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 300 DSAQLVTVTSFSGPMVGMAIQNSIC-------------SPDFSGGVNMDHSTSILgvasSIAHELGHSLGLDHDSPGHSC 366
Cdd:pfam13574 72 CLAHLVTMGTFSGGELGLAYVGQICqkgasspktntglSTTTNYGSFNYPTQEWD----VVAHEVGHNFGATHDCDGSQY 147
|
90 100 110
....*....|....*....|....*....|....*...
gi 109148517 367 PCPG-PAPAKSCIMEASTDFL----PGLN---FSNCSR 396
Cdd:pfam13574 148 ASSGcERNAATSVCSANGSFImnpaSKSNndlFSPCSI 185
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
302-418 |
2.60e-07 |
|
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: 52.76 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 302 AQLVTVTSFSGPMVGMAIQNS--------ICSPD--FSGGVN----------MDHSTSILGVASSI--AHELGHSLGLDH 359
Cdd:cd04270 104 AHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAyyYSNGKKkylntgltttVNYGKRVPTKESDLvtAHELGHNFGSPH 183
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109148517 360 DSPGHSCpCPGPAPAKSCIMEA---STDFLPGLNFSNCSRQALEKALLEGMGSCLFERQPSL 418
Cdd:cd04270 184 DPDIAEC-APGESQGGNYIMYAratSGDKENNKKFSPCSKKSISKVLEVKSNSCFVERSQSF 244
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
311-383 |
8.88e-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: 44.72 E-value: 8.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109148517 311 SGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHSLGLDHDSPGHSCPCPGPAPAKSCIMEAST 383
Cdd:cd04271 108 SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHTFGAVHDCTSGTCSDGSVGSQQCCPLSTST 185
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
316-397 |
3.07e-04 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 43.11 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 316 GMAIQNSICSpDFSGGVNMDHSTSILGVaSSIAHELGHSLGLDHDSPGHSCPCPGPAPAKSC------IMeaSTDF--LP 387
Cdd:cd04272 120 GYAYVGGACT-ENRVAMGEDTPGSYYGV-YTMTHELAHLLGAPHDGSPPPSWVKGHPGSLDCpwddgyIM--SYVVngER 195
|
90
....*....|
gi 109148517 388 GLNFSNCSRQ 397
Cdd:cd04272 196 QYRFSQCSQR 205
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
254-397 |
8.09e-04 |
|
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: 41.45 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 254 LNVRVALVGLeawTQHNLIEMSSNPAVLLDN-----------FLRWRRTdllprLPHDSAQLVTVTSFSGPMVGMAIQNS 322
Cdd:pfam13583 44 FNVSLALISD---RDVIYTDSSTDSFNADCSggdlgnwrlatLTSWRDS-----LNYDLAYLTLMTGPSGQNVGVAWVGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 323 ICSPDFSggvNMDHStsilGVASS------IAHELGHSLGLDHDSPGHSCP-----CPGPApakSCIME-ASTDFLPglN 390
Cdd:pfam13583 116 LCSSARQ---NAKAS----GVARSrdewdiFAHEIGHTFGAVHDCSSQGEGlssstEDGSG---QTIMSyASTASQT--A 183
|
....*..
gi 109148517 391 FSNCSRQ 397
Cdd:pfam13583 184 FSPCTIR 190
|
|
| Peptidase_M10 |
pfam00413 |
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
331-361 |
4.29e-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: 38.75 E-value: 4.29e-03
10 20 30
....*....|....*....|....*....|.
gi 109148517 331 GVNMDHSTSILGVAssiAHELGHSLGLDHDS 361
Cdd:pfam00413 99 GSDPPHGINLFLVA---AHEIGHALGLGHSS 126
|
|
| Peptidase_M54 |
cd11375 |
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ... |
280-393 |
5.91e-03 |
|
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.
Pssm-ID: 213029 Cd Length: 173 Bit Score: 38.43 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109148517 280 VLLDNFLRWrrtdLLPRLPHDSAQLVTVTSFSGPM------VGMAIQNS---ICS-----PDFSGGVNmDHSTSILGVAS 345
Cdd:cd11375 51 YLADDILDA----LLKLKPPDADCVLGVTDVDLYEpglnfvFGLADGGSgvaVVStarlrPEFYGLPP-DEGLFLERLLK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 109148517 346 SIAHELGHSLGLDHdspghscpCPGPApaksCIMeastdflpglNFSN 393
Cdd:cd11375 126 EAVHELGHLFGLDH--------CPYYA----CVM----------NFSN 151
|
|
| |
