|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
199-393 |
1.28e-93 |
|
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: 290.74 E-value: 1.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 199 KFIELFVVADEFVYRRNSKPQNKLRKRIWGMVNFVNMIYKALNIRVTLTGMEIWSAGDEIEIVSNLESTLLHFSTWQETV 278
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHDDF--PCTC-PLG 355
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937369500 356 KCVMG--AGSIPAIKFSKCSQTQYQQFLKNQKPACILNNP 393
Cdd:pfam01421 161 GCIMNpsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
486-623 |
2.05e-49 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 170.23 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 486 ANGFPCKNGEGYCFMGLCPTRDDQCAELFSGGAEESHSLCY-RMNQKGNRFGYCKNKDNTFVPCEEKDLKCGKIYCTGGR 564
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 565 RSAHLGEDKTYNLKNVKqniSIKCKTMFLYHNSR-DMGLVNSGTKCGEGMVCSNGECIEM 623
Cdd:smart00608 81 ELPLLGEHATVIYSNIG---GLVCWSLDYHLGTDpDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
28-156 |
1.22e-33 |
|
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: 125.50 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 28 ELVHPKKLSLLQKRDlerihDSDTPEEYEEELLYEIKLGRKTLTLHLLKAREFLALNYSETYYNIKREMVTRHPQILDHC 107
Cdd:pfam01562 1 EVVIPVRLDPSRRRR-----SLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHC 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1937369500 108 FYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDEGD----HLVF 156
Cdd:pfam01562 76 YYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEgghpHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
410-482 |
6.50e-32 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 118.50 E-value: 6.50e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369500 410 DEGEECDCGPVQECT-NPCCDAHKCVLKPGFTCVEGECCESCQMKKEGVICRPAKNECDISEVCTGYSPECPKD 482
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
199-393 |
1.28e-93 |
|
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: 290.74 E-value: 1.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 199 KFIELFVVADEFVYRRNSKPQNKLRKRIWGMVNFVNMIYKALNIRVTLTGMEIWSAGDEIEIVSNLESTLLHFSTWQETV 278
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHDDF--PCTC-PLG 355
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937369500 356 KCVMG--AGSIPAIKFSKCSQTQYQQFLKNQKPACILNNP 393
Cdd:pfam01421 161 GCIMNpsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
199-391 |
1.42e-66 |
|
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: 219.02 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 199 KFIELFVVADEFVYRRNSKPQNKLRKRIWGMVNFVNMIYKALNIRVTLTGMEIWSAGDEIEIVSNLESTLLHFSTWQETV 278
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHDDFPCTCPLGKCV 358
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
|
170 180 190
....*....|....*....|....*....|....
gi 1937369500 359 MGAG-SIPAIKFSKCSQTQYQQFLKNQKPACILN 391
Cdd:cd04269 161 MAPSpSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
486-623 |
2.05e-49 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 170.23 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 486 ANGFPCKNGEGYCFMGLCPTRDDQCAELFSGGAEESHSLCY-RMNQKGNRFGYCKNKDNTFVPCEEKDLKCGKIYCTGGR 564
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 565 RSAHLGEDKTYNLKNVKqniSIKCKTMFLYHNSR-DMGLVNSGTKCGEGMVCSNGECIEM 623
Cdd:smart00608 81 ELPLLGEHATVIYSNIG---GLVCWSLDYHLGTDpDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
28-156 |
1.22e-33 |
|
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: 125.50 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 28 ELVHPKKLSLLQKRDlerihDSDTPEEYEEELLYEIKLGRKTLTLHLLKAREFLALNYSETYYNIKREMVTRHPQILDHC 107
Cdd:pfam01562 1 EVVIPVRLDPSRRRR-----SLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHC 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1937369500 108 FYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDEGD----HLVF 156
Cdd:pfam01562 76 YYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEgghpHVVY 128
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
487-593 |
1.98e-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: 123.88 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 487 NGFPCKNGEGYCFMGLCPTRDDQCAELFSGGAEESHSLCYR-MNQKGNRFGYCKNKDNTFVPCEEKDLKCGKIYCTGGRR 565
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEeVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*...
gi 1937369500 566 SAHLGEDKTYNLKNVKQNIsikCKTMFL 593
Cdd:pfam08516 81 LPLLGEHATVIYTNINGVT---CWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
410-482 |
6.50e-32 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 118.50 E-value: 6.50e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369500 410 DEGEECDCGPVQECT-NPCCDAHKCVLKPGFTCVEGECCESCQMKKEGVICRPAKNECDISEVCTGYSPECPKD 482
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
410-482 |
9.91e-32 |
|
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: 118.18 E-value: 9.91e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937369500 410 DEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGVICRPAKNECDISEVCTGYSPECPKD 482
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
199-393 |
1.28e-93 |
|
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: 290.74 E-value: 1.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 199 KFIELFVVADEFVYRRNSKPQNKLRKRIWGMVNFVNMIYKALNIRVTLTGMEIWSAGDEIEIVSNLESTLLHFSTWQETV 278
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHDDF--PCTC-PLG 355
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937369500 356 KCVMG--AGSIPAIKFSKCSQTQYQQFLKNQKPACILNNP 393
Cdd:pfam01421 161 GCIMNpsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
199-391 |
1.42e-66 |
|
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: 219.02 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 199 KFIELFVVADEFVYRRNSKPQNKLRKRIWGMVNFVNMIYKALNIRVTLTGMEIWSAGDEIEIVSNLESTLLHFSTWQETV 278
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHDDFPCTCPLGKCV 358
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
|
170 180 190
....*....|....*....|....*....|....
gi 1937369500 359 MGAG-SIPAIKFSKCSQTQYQQFLKNQKPACILN 391
Cdd:cd04269 161 MAPSpSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
486-623 |
2.05e-49 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 170.23 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 486 ANGFPCKNGEGYCFMGLCPTRDDQCAELFSGGAEESHSLCY-RMNQKGNRFGYCKNKDNTFVPCEEKDLKCGKIYCTGGR 564
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 565 RSAHLGEDKTYNLKNVKqniSIKCKTMFLYHNSR-DMGLVNSGTKCGEGMVCSNGECIEM 623
Cdd:smart00608 81 ELPLLGEHATVIYSNIG---GLVCWSLDYHLGTDpDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
28-156 |
1.22e-33 |
|
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: 125.50 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 28 ELVHPKKLSLLQKRDlerihDSDTPEEYEEELLYEIKLGRKTLTLHLLKAREFLALNYSETYYNIKREMVTRHPQILDHC 107
Cdd:pfam01562 1 EVVIPVRLDPSRRRR-----SLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHC 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1937369500 108 FYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDEGD----HLVF 156
Cdd:pfam01562 76 YYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEgghpHVVY 128
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
487-593 |
1.98e-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: 123.88 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 487 NGFPCKNGEGYCFMGLCPTRDDQCAELFSGGAEESHSLCYR-MNQKGNRFGYCKNKDNTFVPCEEKDLKCGKIYCTGGRR 565
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEeVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*...
gi 1937369500 566 SAHLGEDKTYNLKNVKQNIsikCKTMFL 593
Cdd:pfam08516 81 LPLLGEHATVIYTNINGVT---CWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
410-482 |
6.50e-32 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 118.50 E-value: 6.50e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369500 410 DEGEECDCGPVQECT-NPCCDAHKCVLKPGFTCVEGECCESCQMKKEGVICRPAKNECDISEVCTGYSPECPKD 482
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
410-482 |
9.91e-32 |
|
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: 118.18 E-value: 9.91e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937369500 410 DEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGVICRPAKNECDISEVCTGYSPECPKD 482
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPD 73
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
199-390 |
2.80e-28 |
|
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: 112.72 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 199 KFIELFVVADEFVYRRNSKpqNKLRKRIWGMVNFVNMIYK----ALNIRVTLTGMEIWSAGDE-IEIVSNLESTLLHFST 273
Cdd:cd04273 1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdpslGNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 274 WQETVLKKRKD----FDHVILLSGKWLYTS-----MQGIAYPGGICQTLRSCSVVKDL-LPDVNIIgnrmAHQLGHSLGM 343
Cdd:cd04273 79 WQKKLNPPNDSdpehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTgLSSAFTI----AHELGHVLGM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937369500 344 RHDDFPCTCP---LGKCVMGA-GSIPAIKF--SKCSQTQYQQFLKNQKPACIL 390
Cdd:cd04273 155 PHDGDGNSCGpegKDGHIMSPtLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
199-382 |
2.11e-26 |
|
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: 107.12 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 199 KFIELFVVADEFVYRRNSKPQNKLRKRIWGMVNFVNMIYK----ALNIRVTLTGMEIWSAGDEI-EIVSNLESTLLHFST 273
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKGEQFApPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 274 WQETVLKKRkdfDHVILLSGKWLYT-SMQGIAYPGGICQTLRSCSVVKD--LLPDVNIIgnrMAHQLGHSLGMRHDDFPC 350
Cdd:cd04267 81 WRAEGPIRH---DNAVLLTAQDFIEgDILGLAYVGSMCNPYSSVGVVEDtgFTLLTALT---MAHELGHNLGAEHDGGDE 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1937369500 351 TCPL----GKCVM--GAGSIPAIKFSKCSQTQYQQFLK 382
Cdd:cd04267 155 LAFEcdggGNYIMapVDSGLNSYRFSQCSIGSIREFLD 192
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
200-389 |
1.15e-16 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 79.70 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 200 FIELFVVADEFVYRRNSKPQNKLRKRIwGMVNFVNMIYKALN---IRVTLTGMEIW-SAGDEIEIVSNL------ESTLL 269
Cdd:cd04272 2 YPELFVVVDYDHQSEFFSNEQLIRYLA-VMVNAANLRYRDLKsprIRLLLVGITISkDPDFEPYIHPINygyidaAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 270 HFSTWqetvLKKRKDF---DHVILLSGKWLY--------TSMQGIAYPGGICqTLRSCSVVKDLLPDVNIIgNRMAHQLG 338
Cdd:cd04272 81 NFNEY----VKKKRDYfnpDVVFLVTGLDMStysggslqTGTGGYAYVGGAC-TENRVAMGEDTPGSYYGV-YTMTHELA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369500 339 HSLGMRHD-DFPCTCPLGKcvMGAGSIPA---------------IKFSKCSQTQYQQFLKNQKPACI 389
Cdd:cd04272 155 HLLGAPHDgSPPPSWVKGH--PGSLDCPWddgyimsyvvngerqYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
199-381 |
5.44e-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: 55.99 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 199 KFIELFVVADEFVYRRNSKPQNklrkrIWGMVNFVNMIY-KALNIRVTLTGMEIWSAgdeieivsnlestllhfstwQET 277
Cdd:cd00203 1 KVIPYVVVADDRDVEEENLSAQ-----IQSLILIAMQIWrDYLNIRFVLVGVEIDKA--------------------DIA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 278 VLKKRKDFDHVILlsgkwlytsmqGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHD----------D 347
Cdd:cd00203 56 ILVTRQDFDGGTG-----------GWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDhdrkdrddypT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937369500 348 FPCTCPL----GKCVM----GAGSIPAIK-FSKCSQTQYQQFL 381
Cdd:cd00203 125 IDDTLNAedddYYSVMsytkGSFSDGQRKdFSQCDIDQINKLY 167
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
230-346 |
1.17e-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: 463926 [Multi-domain] Cd Length: 122 Bit Score: 53.91 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 230 VNFVNMIYKA-LNIRVTLTGMEIWSAGDEIEIVSNLESTLLHFSTWQETVLKKRK-DFDHVILLSGkwlYTSMQGIAYPG 307
Cdd:pfam13582 7 VNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGyDLGHLFTGRD---GGGGGGIAYVG 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1937369500 308 GICQTLRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMRHD 346
Cdd:pfam13582 84 GVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
203-370 |
3.17e-08 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 54.35 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 203 LFVVAD-EFvyrRNSKPQNKLRKRIWGMVNFV-NMIYKALNIRVTLTGMEIWSAGDEIEIVSNLE---STLLH----FST 273
Cdd:pfam13688 7 LLVAADcSY---VAAFGGDAAQANIINMVNTAsNVYERDFNISLGLVNLTISDSTCPYTPPACSTgdsSDRLSefqdFSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 274 WqetvlKKRKDFDHVILLSGKwlYTSMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNR-----MAHQLGHSLGMRHDdf 348
Cdd:pfam13688 84 W-----RGTQNDDLAYLFLMT--NCSGGGLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHNFGAVHD-- 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1937369500 349 pCT-------CPL--------GKCVMGAGSIPAI-KFS 370
Cdd:pfam13688 155 -CDsstssqcCPPsnstcpagGRYIMNPSSSPNStDFS 191
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
229-381 |
1.70e-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: 372637 Cd Length: 193 Bit Score: 43.39 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 229 MVNFVNMIYK--ALNIRVTLTG----MEIWSAGDEIEIVSNLEST----LLHFSTWqetvlKKRKDFDHVILLSGKWLYT 298
Cdd:pfam13574 10 VVNRVNQIYEpdDININGGLVNpgeiPATTSASDSGNNYCNSPTTivrrLNFLSQW-----RGEQDYCLAHLVTMGTFSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 299 SMQGIAYPGGICQTLRSCSVVKDLLPDVNIIGNRM---------AHQLGHSLGMRHDD----FPCT-CPL---------- 354
Cdd:pfam13574 85 GELGLAYVGQICQKGASSPKTNTGLSTTTNYGSFNyptqewdvvAHEVGHNFGATHDCdgsqYASSgCERnaatsvcsan 164
|
170 180
....*....|....*....|....*...
gi 1937369500 355 GKCVMGAGSIPAI-KFSKCSQTQYQQFL 381
Cdd:pfam13574 165 GSFIMNPASKSNNdLFSPCSISLICDVL 192
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
206-377 |
7.92e-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: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 206 VADEFVYRRNSKPQNKLRKRIWGMVNFVNMIY-KALNIRVTLTG----------MEIWSAGDEIEIVSNleSTLLHFSTW 274
Cdd:pfam13583 9 VATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISdrdviytdssTDSFNADCSGGDLGN--WRLATLTSW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369500 275 QETvlkkrKDFDHVILLSGKWLYTSMQGIAYPGGICQTLRS---CSVVKDLLPDVNIIgnrmAHQLGHSLGMRHDDFPCT 351
Cdd:pfam13583 87 RDS-----LNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQnakASGVARSRDEWDIF----AHEIGHTFGAVHDCSSQG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937369500 352 CPL--------GKCVMGAGSIPA-----------IKFSKCSQTQY 377
Cdd:pfam13583 158 EGLssstedgsGQTIMSYASTASqtafspctirnINGNPCSQANY 202
|
|
| |
