|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
193-382 |
9.02e-57 |
|
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: 192.83 E-value: 9.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 193 IIMDKAMFDHMGSEVGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQDKIETNGDADEVLQRFLLWKSKEISQ-KA 271
Cdd:cd04269 7 VVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSNLLPrKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 272 QDITYLLLYKDH-PDYVGATYHGMACNPNFTAGIALHPKTlAVEGFAIVLSQLLGINLGLAYDDVYnCFCPGSTCIMNPS 350
Cdd:cd04269 87 HDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSR-NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRSTCIMAPS 164
|
170 180 190
....*....|....*....|....*....|..
gi 121949804 351 AirSQGIKVFSSCSVDEFKQLASQPELDCLRN 382
Cdd:cd04269 165 P--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
483-614 |
4.15e-43 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 152.90 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 483 ADLEPCNNETAYCFGGVCRDPDRQCTDLFGKYAKGPNYVCAQEVNLQNDKFGNCHGR------CNYSAIFCGKAVCYWNF 556
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREngtyipCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 121949804 557 AEVIQTEKYDVQYTYLGGQVCVSAHLRSQTGTrDDTYVHDGTVCGSGQVCFRGDCLRV 614
Cdd:smart00608 81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
404-479 |
1.15e-29 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 112.33 E-value: 1.15e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121949804 404 EVPEQCDCGPPETCTHKKCCNPKDCTLIDAAQCGTGPCCDKrtCTIAERGRLCRKSKDQCDFPEFCNGETEGCAPD 479
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
27-144 |
6.84e-24 |
|
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: 97.77 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 27 QITVPEKIDTNIQ-----DAKEAETQVTYVVRIEGKAYTLQLEKQS-FLHPLFGTYLRDKLGTLQPYFSLVKTHCFYQGH 100
Cdd:pfam01562 1 EVVIPVRLDPSRRrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRlLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 121949804 101 AAEIPVSTVTLSTCSGLRGLLQLENITYGIEPLE----SSATFEHILY 144
Cdd:pfam01562 81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
|
|
| EB |
pfam01683 |
EB module; This domain has no known function. It is found in several C. elegans proteins. The ... |
600-649 |
1.55e-03 |
|
EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.
:
Pssm-ID: 460294 Cd Length: 52 Bit Score: 37.41 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 121949804 600 CGSGQVCFRGDCLRVHVLRGTreCEADDKCQGHGICNNlNNCQCESGFAP 649
Cdd:pfam01683 1 CPPGQVLVNGQCVPKVAPGES--CEADEQCPGGSVCVN-GVCQCPPGFTP 47
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
193-382 |
9.02e-57 |
|
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: 192.83 E-value: 9.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 193 IIMDKAMFDHMGSEVGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQDKIETNGDADEVLQRFLLWKSKEISQ-KA 271
Cdd:cd04269 7 VVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSNLLPrKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 272 QDITYLLLYKDH-PDYVGATYHGMACNPNFTAGIALHPKTlAVEGFAIVLSQLLGINLGLAYDDVYnCFCPGSTCIMNPS 350
Cdd:cd04269 87 HDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSR-NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRSTCIMAPS 164
|
170 180 190
....*....|....*....|....*....|..
gi 121949804 351 AirSQGIKVFSSCSVDEFKQLASQPELDCLRN 382
Cdd:cd04269 165 P--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
193-382 |
1.67e-56 |
|
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: 192.52 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 193 IIMDKAMFDHMGSEVGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQDKIETNGDADEVLQRFLLWKSKEISQKA- 271
Cdd:pfam01421 7 IVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEYLKKRKp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 272 QDITYLLLYKDHPD-YVGATYHGMACNPNFTAGIALHPKtLAVEGFAIVLSQLLGINLGLAYDD-VYNCFC-PGSTCIMN 348
Cdd:pfam01421 87 HDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHS-KNLESFAVTMAHELGHNLGMQHDDfNGGCKCpPGGGCIMN 165
|
170 180 190
....*....|....*....|....*....|....
gi 121949804 349 PSAIRSQGIKvFSSCSVDEFKQLASQPELDCLRN 382
Cdd:pfam01421 166 PSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFN 198
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
483-614 |
4.15e-43 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 152.90 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 483 ADLEPCNNETAYCFGGVCRDPDRQCTDLFGKYAKGPNYVCAQEVNLQNDKFGNCHGR------CNYSAIFCGKAVCYWNF 556
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREngtyipCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 121949804 557 AEVIQTEKYDVQYTYLGGQVCVSAHLRSQTGTrDDTYVHDGTVCGSGQVCFRGDCLRV 614
Cdd:smart00608 81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
404-479 |
1.15e-29 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 112.33 E-value: 1.15e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121949804 404 EVPEQCDCGPPETCTHKKCCNPKDCTLIDAAQCGTGPCCDKrtCTIAERGRLCRKSKDQCDFPEFCNGETEGCAPD 479
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
484-582 |
2.06e-28 |
|
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: 109.63 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 484 DLEPCNNETAYCFGGVCRDPDRQCTDLFGKYAKGPNYVCAQEVNLQNDKFGNC------HGRCNYSAIFCGKAVCYWNFA 557
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCgrtnggYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*
gi 121949804 558 EVIQTEKYDVQYTYLGGQVCVSAHL 582
Cdd:pfam08516 81 LPLLGEHATVIYTNINGVTCWGTDY 105
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
404-480 |
4.31e-28 |
|
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: 107.78 E-value: 4.31e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121949804 404 EVPEQCDCGPPETCtHKKCCNPKDCTLIDAAQCGTGPCCDkrTCTIAERGRLCRKSKDQCDFPEFCNGETEGCAPDT 480
Cdd:smart00050 1 EEGEECDCGSPKEC-TDPCCDPATCKLKPGAQCASGPCCD--NCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDP 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
27-144 |
6.84e-24 |
|
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: 97.77 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 27 QITVPEKIDTNIQ-----DAKEAETQVTYVVRIEGKAYTLQLEKQS-FLHPLFGTYLRDKLGTLQPYFSLVKTHCFYQGH 100
Cdd:pfam01562 1 EVVIPVRLDPSRRrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRlLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 121949804 101 AAEIPVSTVTLSTCSGLRGLLQLENITYGIEPLE----SSATFEHILY 144
Cdd:pfam01562 81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
|
|
| EB |
pfam01683 |
EB module; This domain has no known function. It is found in several C. elegans proteins. The ... |
600-649 |
1.55e-03 |
|
EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.
Pssm-ID: 460294 Cd Length: 52 Bit Score: 37.41 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 121949804 600 CGSGQVCFRGDCLRVHVLRGTreCEADDKCQGHGICNNlNNCQCESGFAP 649
Cdd:pfam01683 1 CPPGQVLVNGQCVPKVAPGES--CEADEQCPGGSVCVN-GVCQCPPGFTP 47
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
193-382 |
9.02e-57 |
|
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: 192.83 E-value: 9.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 193 IIMDKAMFDHMGSEVGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQDKIETNGDADEVLQRFLLWKSKEISQ-KA 271
Cdd:cd04269 7 VVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSNLLPrKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 272 QDITYLLLYKDH-PDYVGATYHGMACNPNFTAGIALHPKTlAVEGFAIVLSQLLGINLGLAYDDVYnCFCPGSTCIMNPS 350
Cdd:cd04269 87 HDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSR-NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRSTCIMAPS 164
|
170 180 190
....*....|....*....|....*....|..
gi 121949804 351 AirSQGIKVFSSCSVDEFKQLASQPELDCLRN 382
Cdd:cd04269 165 P--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
193-382 |
1.67e-56 |
|
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: 192.52 E-value: 1.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 193 IIMDKAMFDHMGSEVGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQDKIETNGDADEVLQRFLLWKSKEISQKA- 271
Cdd:pfam01421 7 IVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEYLKKRKp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 272 QDITYLLLYKDHPD-YVGATYHGMACNPNFTAGIALHPKtLAVEGFAIVLSQLLGINLGLAYDD-VYNCFC-PGSTCIMN 348
Cdd:pfam01421 87 HDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHS-KNLESFAVTMAHELGHNLGMQHDDfNGGCKCpPGGGCIMN 165
|
170 180 190
....*....|....*....|....*....|....
gi 121949804 349 PSAIRSQGIKvFSSCSVDEFKQLASQPELDCLRN 382
Cdd:pfam01421 166 PSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFN 198
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
483-614 |
4.15e-43 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 152.90 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 483 ADLEPCNNETAYCFGGVCRDPDRQCTDLFGKYAKGPNYVCAQEVNLQNDKFGNCHGR------CNYSAIFCGKAVCYWNF 556
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREngtyipCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 121949804 557 AEVIQTEKYDVQYTYLGGQVCVSAHLRSQTGTrDDTYVHDGTVCGSGQVCFRGDCLRV 614
Cdd:smart00608 81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
404-479 |
1.15e-29 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 112.33 E-value: 1.15e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121949804 404 EVPEQCDCGPPETCTHKKCCNPKDCTLIDAAQCGTGPCCDKrtCTIAERGRLCRKSKDQCDFPEFCNGETEGCAPD 479
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
484-582 |
2.06e-28 |
|
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: 109.63 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 484 DLEPCNNETAYCFGGVCRDPDRQCTDLFGKYAKGPNYVCAQEVNLQNDKFGNC------HGRCNYSAIFCGKAVCYWNFA 557
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCgrtnggYVKCEKRDVLCGKLQCTNVKE 80
|
90 100
....*....|....*....|....*
gi 121949804 558 EVIQTEKYDVQYTYLGGQVCVSAHL 582
Cdd:pfam08516 81 LPLLGEHATVIYTNINGVTCWGTDY 105
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
404-480 |
4.31e-28 |
|
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: 107.78 E-value: 4.31e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 121949804 404 EVPEQCDCGPPETCtHKKCCNPKDCTLIDAAQCGTGPCCDkrTCTIAERGRLCRKSKDQCDFPEFCNGETEGCAPDT 480
Cdd:smart00050 1 EEGEECDCGSPKEC-TDPCCDPATCKLKPGAQCASGPCCD--NCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDP 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
27-144 |
6.84e-24 |
|
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: 97.77 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 27 QITVPEKIDTNIQ-----DAKEAETQVTYVVRIEGKAYTLQLEKQS-FLHPLFGTYLRDKLGTLQPYFSLVKTHCFYQGH 100
Cdd:pfam01562 1 EVVIPVRLDPSRRrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRlLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 121949804 101 AAEIPVSTVTLSTCSGLRGLLQLENITYGIEPLE----SSATFEHILY 144
Cdd:pfam01562 81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
196-381 |
1.14e-05 |
|
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: 47.23 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 196 DKAMFDHMGSEvgvatqKVVH-IFGLINT---MFSQ----LKMTVMLNSLEIW-SEQDKIETNGDADEVLQRFLLWKSKE 266
Cdd:cd04273 10 DSKMVEFHHGE------DLEHyILTLMNIvasLYKDpslgNSINIVVVRLIVLeDEESGLLISGNAQKSLKSFCRWQKKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 267 ISQKAQDITY----LLL------YKDHP-DYVGATYHGMACNPNFTAGIalhpktlaVE--GF--AIVLSQLLGINLGLA 331
Cdd:cd04273 84 NPPNDSDPEHhdhaILLtrqdicRSNGNcDTLGLAPVGGMCSPSRSCSI--------NEdtGLssAFTIAHELGHVLGMP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 121949804 332 YDDVYNcFCPGST---CIMNPSAIRSQGIKVFSSCSVDEFKQLASQPELDCLR 381
Cdd:cd04273 156 HDGDGN-SCGPEGkdgHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
185-361 |
1.76e-04 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 43.18 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 185 TKRILRIKIIMDKAMFDHMGSEvGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQD----KIETNGDADEVLQRFL 260
Cdd:pfam13688 1 STRTVALLVAADCSYVAAFGGD-AAQANIINMVNTASNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121949804 261 LwKSKEISQKAQDITYLLLYKDHpDYVGATYHGMACNPNFTAGIALHPKTLAVE----GFAIVLSQLLGINLGLAYD--- 333
Cdd:pfam13688 80 D-FSAWRGTQNDDLAYLFLMTNC-SGGGLAWLGQLCNSGSAGSVSTRVSGNNVVvstaTEWQVFAHEIGHNFGAVHDcds 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 121949804 334 DVYNCFCPGS--------TCIMNPSAirSQGIKVFS 361
Cdd:pfam13688 158 STSSQCCPPSnstcpaggRYIMNPSS--SPNSTDFS 191
|
|
| EB |
pfam01683 |
EB module; This domain has no known function. It is found in several C. elegans proteins. The ... |
600-649 |
1.55e-03 |
|
EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.
Pssm-ID: 460294 Cd Length: 52 Bit Score: 37.41 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 121949804 600 CGSGQVCFRGDCLRVHVLRGTreCEADDKCQGHGICNNlNNCQCESGFAP 649
Cdd:pfam01683 1 CPPGQVLVNGQCVPKVAPGES--CEADEQCPGGSVCVN-GVCQCPPGFTP 47
|
|
| EGF_2 |
pfam07974 |
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins. |
629-652 |
5.64e-03 |
|
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
Pssm-ID: 400365 Cd Length: 26 Bit Score: 35.02 E-value: 5.64e-03
|
| |
