|
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 |
5.03e-81 |
|
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: 258.70 E-value: 5.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVQKYQ-DFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 292
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 293 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 372
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966920697 373 paKTCIMEASTDFLPgLNFSNCSRQALEKALLDGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
509-650 |
2.68e-45 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 159.06 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 509 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGGYVSCTPRDAICGQLQCQTGR 588
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966920697 589 TQPLLGSIQDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLVCIDHRCQRV 650
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
431-504 |
2.89e-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: 128.19 E-value: 2.89e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966920697 431 EPGEQCDCGFPDDCADPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 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 ... |
62-146 |
4.12e-14 |
|
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: 69.65 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 62 QTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVQGYAASWVSVCTCSGLRG 141
Cdd:pfam01562 20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99
|
....*
gi 966920697 142 LVVLS 146
Cdd:pfam01562 100 FIRTE 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 |
5.03e-81 |
|
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: 258.70 E-value: 5.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVQKYQ-DFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 292
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 293 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 372
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966920697 373 paKTCIMEASTDFLPgLNFSNCSRQALEKALLDGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
214-419 |
8.23e-73 |
|
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: 236.81 E-value: 8.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVQKY-QDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 292
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 293 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPgpa 372
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966920697 373 PAKTCIMEASTDFLPGLNFSNCSRQALEKALLDGMGSCLFerlpNLP 419
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLF----NKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
509-650 |
2.68e-45 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 159.06 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 509 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGGYVSCTPRDAICGQLQCQTGR 588
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966920697 589 TQPLLGSIQDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLVCIDHRCQRV 650
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
431-504 |
2.89e-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: 128.19 E-value: 2.89e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966920697 431 EPGEQCDCGFPDDCADPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 504
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
431-504 |
2.20e-34 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 125.82 E-value: 2.20e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966920697 431 EPGEQCDCGFPDDCA-DPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 504
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
509-618 |
1.43e-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: 124.26 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 509 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPsGGYVSCTPRDAICGQLQCQTGR 588
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 966920697 589 TQPLLGSIQDLLWETIdvngTELNCSWVHL 618
Cdd:pfam08516 80 ELPLLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
62-146 |
4.12e-14 |
|
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: 69.65 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 62 QTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVQGYAASWVSVCTCSGLRG 141
Cdd:pfam01562 20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99
|
....*
gi 966920697 142 LVVLS 146
Cdd:pfam01562 100 FIRTE 104
|
|
| COG1913 |
COG1913 |
Predicted Zn-dependent protease [General function prediction only]; |
347-393 |
8.60e-03 |
|
Predicted Zn-dependent protease [General function prediction only];
Pssm-ID: 441517 Cd Length: 175 Bit Score: 38.01 E-value: 8.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966920697 347 IAHELGHSLGLDHdlpgnsCPCPGpapaktCIMeastdflpglNFSN 393
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 ... |
214-412 |
5.03e-81 |
|
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: 258.70 E-value: 5.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVQKYQ-DFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 292
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 293 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlpGNSCPCPGpa 372
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHD--DGGCTCGR-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966920697 373 paKTCIMEASTDFLPgLNFSNCSRQALEKALLDGMGSCLF 412
Cdd:cd04269 157 --STCIMAPSPSSLT-DAFSNCSYEDYQKFLSRGGGQCLL 193
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
214-419 |
8.23e-73 |
|
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: 236.81 E-value: 8.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVQKY-QDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAH 292
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMgSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 293 LLPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPgpa 372
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 966920697 373 PAKTCIMEASTDFLPGLNFSNCSRQALEKALLDGMGSCLFerlpNLP 419
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLF----NKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
509-650 |
2.68e-45 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 159.06 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 509 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNpSGGYVSCTPRDAICGQLQCQTGR 588
Cdd:smart00608 2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966920697 589 TQPLLGSIQDLLWETIdvngTELNCSWVHLDLGSDVaQPLLTLPGTACGPGLVCIDHRCQRV 650
Cdd:smart00608 81 ELPLLGEHATVIYSNI----GGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
431-504 |
2.89e-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: 128.19 E-value: 2.89e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966920697 431 EPGEQCDCGFPDDCADPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 504
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCAS-GPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
431-504 |
2.20e-34 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 125.82 E-value: 2.20e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966920697 431 EPGEQCDCGFPDDCA-DPCCDSSTCQLRPGAQCASdGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPD 504
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSS-GPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
509-618 |
1.43e-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: 124.26 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 509 DGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPsGGYVSCTPRDAICGQLQCQTGR 588
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79
|
90 100 110
....*....|....*....|....*....|
gi 966920697 589 TQPLLGSIQDLLWETIdvngTELNCSWVHL 618
Cdd:pfam08516 80 ELPLLGEHATVIYTNI----NGVTCWGTDY 105
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
214-403 |
2.24e-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: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVQKYQ-DFQHLLNRTLEVALLLDTFFR----PLNVRVALVGLEAW-TQRDLVEISPNPAVTLENFLH 287
Cdd:cd04267 1 REIELVVVADHRMVSYFNsDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 288 WRRAHLlPRlpHDSAQLVTGTSF-SGPMVGMAIQNSICSPDFSGGVNMDHSTSILgVASSIAHELGHSLGLDHDlPGNSC 366
Cdd:cd04267 81 WRAEGP-IR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHD-GGDEL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 966920697 367 PCPGPApAKTCIMEASTDFLPGLNFSNCSRQALEKAL 403
Cdd:cd04267 156 AFECDG-GGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
214-412 |
5.21e-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: 109.25 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVQKY--QDFQH----LLNrtlEVALLL-DTFFRPlNVRVALVGLEAWTQR-DLVEISPNPAVTLENF 285
Cdd:cd04273 1 RYVETLVVADSKMVEFHhgEDLEHyiltLMN---IVASLYkDPSLGN-SINIVVVRLIVLEDEeSGLLISGNAQKSLKSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 286 LHWRRAHLLPR----LPHDSAQLVTGTSFSGP-----MVGMAIQNSICSPDFSGGVNMDHStsiLGVASSIAHELGHSLG 356
Cdd:cd04273 77 CRWQKKLNPPNdsdpEHHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELGHVLG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 966920697 357 LDHDLPGNSCpcpGPAPAKTCIMEASTDFLPG-LNFSNCSRQALEKALLDGMGSCLF 412
Cdd:cd04273 154 MPHDGDGNSC---GPEGKDGHIMSPTLGANTGpFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
62-146 |
4.12e-14 |
|
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: 69.65 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 62 QTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVQGYAASWVSVCTCSGLRG 141
Cdd:pfam01562 20 ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRG 99
|
....*
gi 966920697 142 LVVLS 146
Cdd:pfam01562 100 FIRTE 104
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
213-379 |
4.13e-14 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 71.68 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 213 TKTVELVIVADHSEVQKY-----QDF-QHLLNRTLEVallldtFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFL 286
Cdd:pfam13688 2 TRTVALLVAADCSYVAAFggdaaQANiINMVNTASNV------YERDFNISLGLVNLTISDSTCPYTPPACSTGDSSDRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 287 H-------WRRAHllprlPHDSAQLVTGTSFSGPmvGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHS 354
Cdd:pfam13688 76 SefqdfsaWRGTQ-----NDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHN 148
|
170 180 190
....*....|....*....|....*....|....
gi 966920697 355 LGLDHD----LPGNSCP-----CPGPApakTCIM 379
Cdd:pfam13688 149 FGAVHDcdssTSSQCCPpsnstCPAGG---RYIM 179
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
214-403 |
9.55e-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: 9.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVqKYQDFQHllnRTLEVALLLDTFFR-PLNVRVALVGLEawtqrdlveispnpavtlenflhwrrah 292
Cdd:cd00203 1 KVIPYVVVADDRDV-EEENLSA---QIQSLILIAMQIWRdYLNIRFVLVGVE---------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 293 llpRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDlPGNSCPCPGPA 372
Cdd:cd00203 49 ---IDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHD-HDRKDRDDYPT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 966920697 373 PAKT---------CIMEASTDFLPGLN---FSNCSRQALEKAL 403
Cdd:cd00203 125 IDDTlnaedddyySVMSYTKGSFSDGQrkdFSQCDIDQINKLY 167
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
252-360 |
2.88e-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: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 252 RPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAhllpRLPH---DSAQLVTGTSFSGpMVGMAIQNSICSPDF 328
Cdd:pfam13582 16 RDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQygyDLGHLFTGRDGGG-GGGIAYVGGVCNSGS 90
|
90 100 110
....*....|....*....|....*....|..
gi 966920697 329 SGGVNMDHSTSILGVASSIAHELGHSLGLDHD 360
Cdd:pfam13582 91 KFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
283-396 |
9.68e-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: 372637 Cd Length: 193 Bit Score: 53.02 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 283 ENFLH-WRRAHllprlPHDSAQLVTGTSFSGPMVGMAIQNSIC-------------SPDFSGGVNMDHSTSILgvasSIA 348
Cdd:pfam13574 59 LNFLSqWRGEQ-----DYCLAHLVTMGTFSGGELGLAYVGQICqkgasspktntglSTTTNYGSFNYPTQEWD----VVA 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 966920697 349 HELGHSLGLDHDLPGNSCPCPG-PAPAKTCIMEASTDFL----PGLN---FSNCSR 396
Cdd:pfam13574 130 HEVGHNFGATHDCDGSQYASSGcERNAATSVCSANGSFImnpaSKSNndlFSPCSI 185
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
215-397 |
2.68e-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: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 215 TVELVIVADhsevqkyQDFQHLLNRTLEVALLLDTFFRPLN----------VRVALVGLE----AWTQRDLVEISP---N 277
Cdd:cd04272 2 YPELFVVVD-------YDHQSEFFSNEQLIRYLAVMVNAANlryrdlksprIRLLLVGITiskdPDFEPYIHPINYgyiD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 278 PAVTLENF-LHWRRAHLLPRlpHDSAQLVTG----TSFSGPM----VGMAIQNSICSpDFSGGVNMDHSTSILGVaSSIA 348
Cdd:cd04272 75 AAETLENFnEYVKKKRDYFN--PDVVFLVTGldmsTYSGGSLqtgtGGYAYVGGACT-ENRVAMGEDTPGSYYGV-YTMT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966920697 349 HELGHSLGLDHD-LPGNSCPCPGPApAKTC------IMeaSTDF--LPGLNFSNCSRQ 397
Cdd:cd04272 151 HELAHLLGAPHDgSPPPSWVKGHPG-SLDCpwddgyIM--SYVVngERQYRFSQCSQR 205
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
214-397 |
6.11e-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: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 214 KTVELVIVADHSEVQKYQDFQHLLNRTLE-VALLLDTFFRPLNVRVALVGleawtQRDLVEISPNPA-----VTLENFLH 287
Cdd:pfam13583 3 RVYRVAVATDCTYSASFGSVDELRANINAtVTTANEVYGRDFNVSLALIS-----DRDVIYTDSSTDsfnadCSGGDLGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 288 WRRAHL---LPRLPHDSAQLVTGTSFSGPMVGMAIQNSICSPDFSggvNMDHStsilGVASS------IAHELGHSLGLD 358
Cdd:pfam13583 78 WRLATLtswRDSLNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQ---NAKAS----GVARSrdewdiFAHEIGHTFGAV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 966920697 359 HDLpGNSCPcpgPAPAKTC------IME-ASTDFLPglNFSNCSRQ 397
Cdd:pfam13583 151 HDC-SSQGE---GLSSSTEdgsgqtIMSyASTASQT--AFSPCTIR 190
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
302-414 |
7.42e-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: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966920697 302 AQLVTGTSFSGPMVGMAIQNS--------ICSPD--FSGGVN----------MDHSTSILGVASSI--AHELGHSLGLDH 359
Cdd:cd04270 104 AHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAyyYSNGKKkylntgltttVNYGKRVPTKESDLvtAHELGHNFGSPH 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 966920697 360 DLPGNSCpCPGPAPAKTCIMEA---STDFLPGLNFSNCSRQALEKALLDGMGSCLFER 414
Cdd:cd04270 184 DPDIAEC-APGESQGGNYIMYAratSGDKENNKKFSPCSKKSISKVLEVKSNSCFVER 240
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
311-383 |
6.58e-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: 45.10 E-value: 6.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966920697 311 SGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASS-----IAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEAST 383
Cdd:cd04271 108 SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHTFGAVHDCTSGTCSDGSVGSQQCCPLSTST 185
|
|
| Peptidase_M10 |
pfam00413 |
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ... |
331-359 |
5.20e-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: 5.20e-03
10 20
....*....|....*....|....*....
gi 966920697 331 GVNMDHSTSILGVAssiAHELGHSLGLDH 359
Cdd:pfam00413 99 GSDPPHGINLFLVA---AHEIGHALGLGH 124
|
|
| COG1913 |
COG1913 |
Predicted Zn-dependent protease [General function prediction only]; |
347-393 |
8.60e-03 |
|
Predicted Zn-dependent protease [General function prediction only];
Pssm-ID: 441517 Cd Length: 175 Bit Score: 38.01 E-value: 8.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 966920697 347 IAHELGHSLGLDHdlpgnsCPCPGpapaktCIMeastdflpglNFSN 393
Cdd:COG1913 127 AVHELGHLFGLGH------CPNPR------CVM----------HFSN 151
|
|
| |
