|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
199-393 |
2.32e-90 |
|
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: 282.27 E-value: 2.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 199 KFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETV 278
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDGF--PCTC-PLG 355
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110347491 356 KCVMGD--GSIPAIKFSKCSQTQYQQFLQDQKPACILNNP 393
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
486-623 |
8.55e-49 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 168.31 E-value: 8.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 486 ANGFPCRNGEGYCFMGLCPTRNEQCSELFIGGAEESHSLCY-RMNKKGNRFGYCKNKGNTFVPCEEKDLKCGKIYCSGGR 564
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 565 PSSRLGEDKAYNLKNVKQNVtikCRTMFLHHNSR-DMGLVNSGTKCGDGMVCSNGECIEM 623
Cdd:smart00608 81 ELPLLGEHATVIYSNIGGLV---CWSLDYHLGTDpDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
28-156 |
1.46e-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: 125.12 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 28 ELVHPKKL-PLLHKRDLERihdsdiPEEYEEELLYEIKLGKKTLILHLLKAREFLSSNYSETYYNVKREVFTKHPQILDH 106
Cdd:pfam01562 1 EVVIPVRLdPSRRRRSLAS------ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 110347491 107 CFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDDGE----HLVY 156
Cdd:pfam01562 75 CYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEgghpHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
410-482 |
5.16e-31 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 115.80 E-value: 5.16e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110347491 410 DEGEECDCGPVQECT-NPCCDAHKCVLKPGFTCVEGECCESCQMKKEGAVCRLAKNECDISEVCTGYSPECPKD 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 |
2.32e-90 |
|
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: 282.27 E-value: 2.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 199 KFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETV 278
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDGF--PCTC-PLG 355
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110347491 356 KCVMGD--GSIPAIKFSKCSQTQYQQFLQDQKPACILNNP 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 |
1.58e-65 |
|
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: 216.33 E-value: 1.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 199 KFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETV 278
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDGFPCTCPLGKCV 358
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
|
170 180 190
....*....|....*....|....*....|....
gi 110347491 359 MGDG-SIPAIKFSKCSQTQYQQFLQDQKPACILN 391
Cdd:cd04269 161 MAPSpSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
486-623 |
8.55e-49 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 168.31 E-value: 8.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 486 ANGFPCRNGEGYCFMGLCPTRNEQCSELFIGGAEESHSLCY-RMNKKGNRFGYCKNKGNTFVPCEEKDLKCGKIYCSGGR 564
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 565 PSSRLGEDKAYNLKNVKQNVtikCRTMFLHHNSR-DMGLVNSGTKCGDGMVCSNGECIEM 623
Cdd:smart00608 81 ELPLLGEHATVIYSNIGGLV---CWSLDYHLGTDpDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
28-156 |
1.46e-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: 125.12 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 28 ELVHPKKL-PLLHKRDLERihdsdiPEEYEEELLYEIKLGKKTLILHLLKAREFLSSNYSETYYNVKREVFTKHPQILDH 106
Cdd:pfam01562 1 EVVIPVRLdPSRRRRSLAS------ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 110347491 107 CFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDDGE----HLVY 156
Cdd:pfam01562 75 CYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEgghpHVVY 128
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
487-593 |
2.71e-31 |
|
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: 117.72 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 487 NGFPCRNGEGYCFMGLCPTRNEQCSELFIGGAEESHSLCYR-MNKKGNRFGYCKNKGNTFVPCEEKDLKCGKIYCSGGRP 565
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEeVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*...
gi 110347491 566 SSRLGEDKAYNLKNVKQNVtikCRTMFL 593
Cdd:pfam08516 81 LPLLGEHATVIYTNINGVT---CWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
410-482 |
5.16e-31 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 115.80 E-value: 5.16e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110347491 410 DEGEECDCGPVQECT-NPCCDAHKCVLKPGFTCVEGECCESCQMKKEGAVCRLAKNECDISEVCTGYSPECPKD 482
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
410-484 |
1.28e-30 |
|
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: 114.71 E-value: 1.28e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347491 410 DEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGAVCRLAKNECDISEVCTGYSPECPKDEF 484
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
199-393 |
2.32e-90 |
|
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: 282.27 E-value: 2.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 199 KFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETV 278
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDGF--PCTC-PLG 355
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCpPGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110347491 356 KCVMGD--GSIPAIKFSKCSQTQYQQFLQDQKPACILNNP 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 |
1.58e-65 |
|
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: 216.33 E-value: 1.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 199 KFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETV 278
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 279 LKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDGFPCTCPLGKCV 358
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
|
170 180 190
....*....|....*....|....*....|....
gi 110347491 359 MGDG-SIPAIKFSKCSQTQYQQFLQDQKPACILN 391
Cdd:cd04269 161 MAPSpSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
486-623 |
8.55e-49 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 168.31 E-value: 8.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 486 ANGFPCRNGEGYCFMGLCPTRNEQCSELFIGGAEESHSLCY-RMNKKGNRFGYCKNKGNTFVPCEEKDLKCGKIYCSGGR 564
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 565 PSSRLGEDKAYNLKNVKQNVtikCRTMFLHHNSR-DMGLVNSGTKCGDGMVCSNGECIEM 623
Cdd:smart00608 81 ELPLLGEHATVIYSNIGGLV---CWSLDYHLGTDpDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
28-156 |
1.46e-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: 125.12 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 28 ELVHPKKL-PLLHKRDLERihdsdiPEEYEEELLYEIKLGKKTLILHLLKAREFLSSNYSETYYNVKREVFTKHPQILDH 106
Cdd:pfam01562 1 EVVIPVRLdPSRRRRSLAS------ESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDH 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 110347491 107 CFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDDGE----HLVY 156
Cdd:pfam01562 75 CYYQGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEgghpHVVY 128
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
487-593 |
2.71e-31 |
|
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: 117.72 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 487 NGFPCRNGEGYCFMGLCPTRNEQCSELFIGGAEESHSLCYR-MNKKGNRFGYCKNKGNTFVPCEEKDLKCGKIYCSGGRP 565
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEeVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*...
gi 110347491 566 SSRLGEDKAYNLKNVKQNVtikCRTMFL 593
Cdd:pfam08516 81 LPLLGEHATVIYTNINGVT---CWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
410-482 |
5.16e-31 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 115.80 E-value: 5.16e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110347491 410 DEGEECDCGPVQECT-NPCCDAHKCVLKPGFTCVEGECCESCQMKKEGAVCRLAKNECDISEVCTGYSPECPKD 482
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
410-484 |
1.28e-30 |
|
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: 114.71 E-value: 1.28e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347491 410 DEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGAVCRLAKNECDISEVCTGYSPECPKDEF 484
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
199-390 |
2.01e-26 |
|
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: 107.71 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 199 KFIELFVVADEYVYRRNNKpqNKLRKRIWGMVNFVNMIYK------TLNIHVTlaGFEIWSAGDK-IEIVSNLESTLLHF 271
Cdd:cd04273 1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdpslgnSINIVVV--RLIVLEDEESgLLISGNAQKSLKSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 272 STWQETVLKKRKD----FDHVILLSGKWLYTS-----MQGIAYPGGICQILRSCSVVKDL-LPDVNIIgnrmAHQLGHSL 341
Cdd:cd04273 77 CRWQKKLNPPNDSdpehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTgLSSAFTI----AHELGHVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110347491 342 GMQHDGFPCTCP---LGKCVMG-DGSIPAIKF--SKCSQTQYQQFLQDQKPACIL 390
Cdd:cd04273 153 GMPHDGDGNSCGpegKDGHIMSpTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
199-381 |
6.58e-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: 105.58 E-value: 6.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 199 KFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYK----TLNIHVTLAGFEIWSAGDKI-EIVSNLESTLLHFST 273
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKGEQFApPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 274 WQETVLKKRkdfDHVILLSGKWLYT-SMQGIAYPGGICQILRSCSVVKD--LLPDVNIIgnrMAHQLGHSLGMQHDGFPC 350
Cdd:cd04267 81 WRAEGPIRH---DNAVLLTAQDFIEgDILGLAYVGSMCNPYSSVGVVEDtgFTLLTALT---MAHELGHNLGAEHDGGDE 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 110347491 351 TCPL----GKCVM--GDGSIPAIKFSKCSQTQYQQFL 381
Cdd:cd04267 155 LAFEcdggGNYIMapVDSGLNSYRFSQCSIGSIREFL 191
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
200-389 |
7.36e-16 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 77.39 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 200 FIELFVVADEYVYRRNNKPQNKLRKRIwGMVNFVNMIYKTLN---IHVTLAGFEIwSAGDKIEIVS--------NLESTL 268
Cdd:cd04272 2 YPELFVVVDYDHQSEFFSNEQLIRYLA-VMVNAANLRYRDLKsprIRLLLVGITI-SKDPDFEPYIhpinygyiDAAETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 269 LHFSTWqetvLKKRKDF---DHVILLSGKWLY--------TSMQGIAYPGGICQILRsCSVVKDLLPDVNIIgNRMAHQL 337
Cdd:cd04272 80 ENFNEY----VKKKRDYfnpDVVFLVTGLDMStysggslqTGTGGYAYVGGACTENR-VAMGEDTPGSYYGV-YTMTHEL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347491 338 GHSLGMQHDGF-PCTCPLGK-----C------VM--GDGSIPAIKFSKCSQTQYQQFLQDQKPACI 389
Cdd:cd04272 154 AHLLGAPHDGSpPPSWVKGHpgsldCpwddgyIMsyVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
199-381 |
1.87e-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: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 199 KFIELFVVADEYVYRRNNKPQNklrkrIWGMVNFVNMIY-KTLNIHVTLAGFEIWSAgdkieivsnlestllhfstwQET 277
Cdd:cd00203 1 KVIPYVVVADDRDVEEENLSAQ-----IQSLILIAMQIWrDYLNIRFVLVGVEIDKA--------------------DIA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 278 VLKKRKDFDHVILlsgkwlytsmqGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDG---------- 347
Cdd:cd00203 56 ILVTRQDFDGGTG-----------GWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHdrkdrddypt 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110347491 348 FPCTCPL----GKCVM----GDGSIPAIK-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 |
2.64e-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: 52.76 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 230 VNFVNMIYKT-LNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETVLKKRK-DFDHVILLSGkwlYTSMQGIAYPG 307
Cdd:pfam13582 7 VNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGyDLGHLFTGRD---GGGGGGIAYVG 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 110347491 308 GICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHD 346
Cdd:pfam13582 84 GVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
203-359 |
1.22e-07 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 52.81 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 203 LFVVADEYVYRRNNkpQNKLRKRIWGMVNFV-NMIYKTLNIHVTLAGFEIWSAGD---KIEIVSNLESTLLH----FSTW 274
Cdd:pfam13688 7 LLVAADCSYVAAFG--GDAAQANIINMVNTAsNVYERDFNISLGLVNLTISDSTCpytPPACSTGDSSDRLSefqdFSAW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 275 qetvlKKRKDFDHVILLSGKwlYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNR-----MAHQLGHSLGMQHDgfp 349
Cdd:pfam13688 85 -----RGTQNDDLAYLFLMT--NCSGGGLAWLGQLCNSGSAGSVSTRVSGNNVVVSTAtewqvFAHEIGHNFGAVHD--- 154
|
170 180
....*....|....*....|....*
gi 110347491 350 CT-------CPL--------GKCVM 359
Cdd:pfam13688 155 CDsstssqcCPPsnstcpagGRYIM 179
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
206-377 |
5.69e-05 |
|
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: 44.92 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 206 VADEYVYRRNNKPQNKLRKRIWGMVNFVNMIY-KTLNIHVTLAGFE----------IWSAGDKIEIVSNleSTLLHFSTW 274
Cdd:pfam13583 9 VATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDRdviytdsstdSFNADCSGGDLGN--WRLATLTSW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347491 275 QETvlkkrKDFDHVILLSGKWLYTSMQGIAYPGGICQILRS---CSVVKDLLPDVNIIgnrmAHQLGHSLGMQHDGFPCT 351
Cdd:pfam13583 87 RDS-----LNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQnakASGVARSRDEWDIF----AHEIGHTFGAVHDCSSQG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110347491 352 CPL--------GKCVMGDGSIPA-----------IKFSKCSQTQY 377
Cdd:pfam13583 158 EGLssstedgsGQTIMSYASTASqtafspctirnINGNPCSQANY 202
|
|
| |
