|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
203-391 |
1.03e-61 |
|
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: 205.93 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 203 KYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRMRIHLKALEVWTDFNKIRVgYPELAEVLGRFVIYKKS 282
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISV-SGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 283 VLNARLSSDWAHLYLQRKY--NDALAWSFGKVCSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHDEQYCQCrGRLN 360
Cdd:cd04269 80 NLLPRKPHDNAQLLTGRDFdgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTC-GRST 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 31881770 361 CIMGSGRT----GFSNCSYISFFKHISSG-ATCLNN 391
Cdd:cd04269 159 CIMAPSPSsltdAFSNCSYEDYQKFLSRGgGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
484-626 |
9.23e-49 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 168.31 E-value: 9.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 484 QDGTPCKYE-GRCFRKGCRSRYMQCQSIFGPDAMEAPSECYDAVNLIGDQFGNCEITGIRnFKKCESANSICGRLQCINV 562
Cdd:smart00608 1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGT-YIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31881770 563 ETIPDLPEHTTIISTHLQaeNLMCWGTGYHLSMKpmgiPDLGMINDGTSCGEGRVCFKKNCVNS 626
Cdd:smart00608 80 SELPLLGEHATVIYSNIG--GLVCWSLDYHLGTD----PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
408-480 |
2.67e-35 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 128.13 E-value: 2.67e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31881770 408 EDNEECDCGSTEECQKDRCCQ-SNCKLQPGANCSIGLCCHDCRFRPSGYVCRQEGNECDLAEYCDGNSSSCPND 480
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
42-160 |
3.54e-32 |
|
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: 121.27 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 42 EVTIPEKLSFR------GEVQGVVSPVSYLLQLKGKKHVLHLWPKRLLLPRHLRVFSFTEHGELLEDHPYIPKDCNYMGS 115
Cdd:pfam01562 1 EVVIPVRLDPSrrrrslASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 31881770 116 VKESLDSKATISTCMgGLRGVFNIDAKHYQIEPLKASP----SFEHVVY 160
Cdd:pfam01562 81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKYSreegGHPHVVY 128
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
203-391 |
1.03e-61 |
|
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: 205.93 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 203 KYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRMRIHLKALEVWTDFNKIRVgYPELAEVLGRFVIYKKS 282
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISV-SGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 283 VLNARLSSDWAHLYLQRKY--NDALAWSFGKVCSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHDEQYCQCrGRLN 360
Cdd:cd04269 80 NLLPRKPHDNAQLLTGRDFdgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTC-GRST 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 31881770 361 CIMGSGRT----GFSNCSYISFFKHISSG-ATCLNN 391
Cdd:cd04269 159 CIMAPSPSsltdAFSNCSYEDYQKFLSRGgGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
484-626 |
9.23e-49 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 168.31 E-value: 9.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 484 QDGTPCKYE-GRCFRKGCRSRYMQCQSIFGPDAMEAPSECYDAVNLIGDQFGNCEITGIRnFKKCESANSICGRLQCINV 562
Cdd:smart00608 1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGT-YIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31881770 563 ETIPDLPEHTTIISTHLQaeNLMCWGTGYHLSMKpmgiPDLGMINDGTSCGEGRVCFKKNCVNS 626
Cdd:smart00608 80 SELPLLGEHATVIYSNIG--GLVCWSLDYHLGTD----PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
485-591 |
6.42e-38 |
|
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: 136.59 E-value: 6.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 485 DGTPCKY-EGRCFRKGCRSRYMQCQSIFGPDAMEAPSECYDAVNLIGDQFGNCEITGiRNFKKCESANSICGRLQCINVE 563
Cdd:pfam08516 1 DGTPCNNgQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79
|
90 100
....*....|....*....|....*...
gi 31881770 564 TIPDLPEHTTIISTHLQaeNLMCWGTGY 591
Cdd:pfam08516 80 ELPLLGEHATVIYTNIN--GVTCWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
408-480 |
2.67e-35 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 128.13 E-value: 2.67e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31881770 408 EDNEECDCGSTEECQKDRCCQ-SNCKLQPGANCSIGLCCHDCRFRPSGYVCRQEGNECDLAEYCDGNSSSCPND 480
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
42-160 |
3.54e-32 |
|
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: 121.27 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 42 EVTIPEKLSFR------GEVQGVVSPVSYLLQLKGKKHVLHLWPKRLLLPRHLRVFSFTEHGELLEDHPYIPKDCNYMGS 115
Cdd:pfam01562 1 EVVIPVRLDPSrrrrslASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 31881770 116 VKESLDSKATISTCMgGLRGVFNIDAKHYQIEPLKASP----SFEHVVY 160
Cdd:pfam01562 81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKYSreegGHPHVVY 128
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
203-393 |
5.56e-32 |
|
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: 123.18 E-value: 5.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 203 KYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRMRIHLKALEVWTDFNKIRVgYPELAEVLGRFVIYKKS 282
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDV-SGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 283 VLNARLSSDWAHLYLQRKYNDA---LAWsFGKVCSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHDE--QYCQCRG 357
Cdd:pfam01421 80 YLKKRKPHDVAQLLSGVEFGGTtvgAAY-VGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 31881770 358 RLNCIMG------SGRTgFSNCSYISFFKHISS-GATCLNNIP 393
Cdd:pfam01421 159 GGGCIMNpsagssFPRK-FSNCSQEDFEQFLTKqKGACLFNKP 200
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
408-482 |
2.76e-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: 113.94 E-value: 2.76e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31881770 408 EDNEECDCGSTEECQkDRCCQSN-CKLQPGANCSIGLCCHDCRFRPSGYVCRQEGNECDLAEYCDGNSSSCPNDVY 482
Cdd:smart00050 1 EEGEECDCGSPKECT-DPCCDPAtCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
203-391 |
1.03e-61 |
|
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: 205.93 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 203 KYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRMRIHLKALEVWTDFNKIRVgYPELAEVLGRFVIYKKS 282
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISV-SGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 283 VLNARLSSDWAHLYLQRKY--NDALAWSFGKVCSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHDEQYCQCrGRLN 360
Cdd:cd04269 80 NLLPRKPHDNAQLLTGRDFdgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTC-GRST 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 31881770 361 CIMGSGRT----GFSNCSYISFFKHISSG-ATCLNN 391
Cdd:cd04269 159 CIMAPSPSsltdAFSNCSYEDYQKFLSRGgGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
484-626 |
9.23e-49 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 168.31 E-value: 9.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 484 QDGTPCKYE-GRCFRKGCRSRYMQCQSIFGPDAMEAPSECYDAVNLIGDQFGNCEITGIRnFKKCESANSICGRLQCINV 562
Cdd:smart00608 1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGT-YIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31881770 563 ETIPDLPEHTTIISTHLQaeNLMCWGTGYHLSMKpmgiPDLGMINDGTSCGEGRVCFKKNCVNS 626
Cdd:smart00608 80 SELPLLGEHATVIYSNIG--GLVCWSLDYHLGTD----PDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
485-591 |
6.42e-38 |
|
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: 136.59 E-value: 6.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 485 DGTPCKY-EGRCFRKGCRSRYMQCQSIFGPDAMEAPSECYDAVNLIGDQFGNCEITGiRNFKKCESANSICGRLQCINVE 563
Cdd:pfam08516 1 DGTPCNNgQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTN-GGYVKCEKRDVLCGKLQCTNVK 79
|
90 100
....*....|....*....|....*...
gi 31881770 564 TIPDLPEHTTIISTHLQaeNLMCWGTGY 591
Cdd:pfam08516 80 ELPLLGEHATVIYTNIN--GVTCWGTDY 105
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
408-480 |
2.67e-35 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 128.13 E-value: 2.67e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31881770 408 EDNEECDCGSTEECQKDRCCQ-SNCKLQPGANCSIGLCCHDCRFRPSGYVCRQEGNECDLAEYCDGNSSSCPND 480
Cdd:pfam00200 1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
42-160 |
3.54e-32 |
|
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: 121.27 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 42 EVTIPEKLSFR------GEVQGVVSPVSYLLQLKGKKHVLHLWPKRLLLPRHLRVFSFTEHGELLEDHPYIPKDCNYMGS 115
Cdd:pfam01562 1 EVVIPVRLDPSrrrrslASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 31881770 116 VKESLDSKATISTCMgGLRGVFNIDAKHYQIEPLKASP----SFEHVVY 160
Cdd:pfam01562 81 VEGHPDSSVALSTCS-GLRGFIRTENEEYLIEPLEKYSreegGHPHVVY 128
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
203-393 |
5.56e-32 |
|
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: 123.18 E-value: 5.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 203 KYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRMRIHLKALEVWTDFNKIRVgYPELAEVLGRFVIYKKS 282
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDV-SGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 283 VLNARLSSDWAHLYLQRKYNDA---LAWsFGKVCSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHDE--QYCQCRG 357
Cdd:pfam01421 80 YLKKRKPHDVAQLLSGVEFGGTtvgAAY-VGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 31881770 358 RLNCIMG------SGRTgFSNCSYISFFKHISS-GATCLNNIP 393
Cdd:pfam01421 159 GGGCIMNpsagssFPRK-FSNCSQEDFEQFLTKqKGACLFNKP 200
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
408-482 |
2.76e-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: 113.94 E-value: 2.76e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31881770 408 EDNEECDCGSTEECQkDRCCQSN-CKLQPGANCSIGLCCHDCRFRPSGYVCRQEGNECDLAEYCDGNSSSCPNDVY 482
Cdd:smart00050 1 EEGEECDCGSPKECT-DPCCDPAtCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
207-371 |
1.82e-09 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 57.81 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 207 LILLFDQSryrFVNNNLSQVIHDAI--LLTGIMDTYFQDVRMRIHLKALEVWTDFN---KIRVGYPELAEVLGRFVIYkk 281
Cdd:pfam13688 7 LLVAADCS---YVAAFGGDAAQANIinMVNTASNVYERDFNISLGLVNLTISDSTCpytPPACSTGDSSDRLSEFQDF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 282 SVLNARLSSDWAHLYLQRKY-NDALAWSfGKVCSLEYAGSVSTLLDTNILAPATWS-----AHELGHAVGMSHD------ 349
Cdd:pfam13688 82 SAWRGTQNDDLAYLFLMTNCsGGGLAWL-GQLCNSGSAGSVSTRVSGNNVVVSTATewqvfAHEIGHNFGAVHDcdssts 160
|
170 180 190
....*....|....*....|....*....|.
gi 31881770 350 EQYC-----QCRGRLNCIM----GSGRTGFS 371
Cdd:pfam13688 161 SQCCppsnsTCPAGGRYIMnpssSPNSTDFS 191
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
203-390 |
2.74e-09 |
|
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: 57.63 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 203 KYLELILLFDQSRYRFVNnnlSQVIHDAIL-LTGIMDTYFQD----VRMRIHLKALEVWTDFNKIRVGYPELAEVLGRFV 277
Cdd:cd04273 1 RYVETLVVADSKMVEFHH---GEDLEHYILtLMNIVASLYKDpslgNSINIVVVRLIVLEDEESGLLISGNAQKSLKSFC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 278 IYKKSvLNARLSSDWAH----LYLQRKynDALAWS----------FGKVCSLEYAGSVSTLLDtniLAPATWSAHELGHA 343
Cdd:cd04273 78 RWQKK-LNPPNDSDPEHhdhaILLTRQ--DICRSNgncdtlglapVGGMCSPSRSCSINEDTG---LSSAFTIAHELGHV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 31881770 344 VGMSHDEQ--YCQCRGRLNCIM------GSGRTGFSNCS--YI-SFFKhiSSGATCLN 390
Cdd:cd04273 152 LGMPHDGDgnSCGPEGKDGHIMsptlgaNTGPFTWSKCSrrYLtSFLD--TGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
203-383 |
3.28e-08 |
|
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: 54.35 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 203 KYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRM----RIHLKALEVWTDFNKIRVGYPELAEVLGRFVI 278
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAPPIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 279 YKKSVLNARlssDWAHLYLQRKYND----ALAWsFGKVCSLEYAGSVSTLLDTNILAPATwSAHELGHAVGMSHDEQYC- 353
Cdd:cd04267 81 WRAEGPIRH---DNAVLLTAQDFIEgdilGLAY-VGSMCNPYSSVGVVEDTGFTLLTALT-MAHELGHNLGAEHDGGDEl 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 31881770 354 --QCRGRLNCIM-----GSGRTGFSNCSYISFFKHIS 383
Cdd:cd04267 156 afECDGGGNYIMapvdsGLNSYRFSQCSIGSIREFLD 192
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
250-377 |
1.51e-04 |
|
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: 42.89 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 250 LKALEVWTDFNKIRvgypelaevlgrFVIYKKSVLNArlssDWAHL-YLQRKYNDALAWSF-GKVCSLEyaGSVSTLLDT 327
Cdd:cd00203 28 LIAMQIWRDYLNIR------------FVLVGVEIDKA----DIAILvTRQDFDGGTGGWAYlGRVCDSL--RGVGVLQDN 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31881770 328 ---NILAPATwSAHELGHAVGMSHDEQYC-------------QCRGRLNCIM--------GSGRTGFSNCSYIS 377
Cdd:cd00203 90 qsgTKEGAQT-IAHELGHALGFYHDHDRKdrddyptiddtlnAEDDDYYSVMsytkgsfsDGQRKDFSQCDIDQ 162
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
240-349 |
3.14e-03 |
|
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: 38.12 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 240 YFQDVRMRIHLKALEVWTDFNKIRVGYPELaevlgrfVIYKKSVLNARLSS-----DWAHLYLQRKYNDA--LAWsFGKV 312
Cdd:pfam13582 14 YERDLGIRLQLAAIIITTSADTPYTSSDAL-------EILDELQEVNDTRIgqygyDLGHLFTGRDGGGGggIAY-VGGV 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 31881770 313 CSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHD 349
Cdd:pfam13582 86 CNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ZnMc_MMP_like_1 |
cd04279 |
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ... |
250-348 |
8.34e-03 |
|
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.
Pssm-ID: 239806 [Multi-domain] Cd Length: 156 Bit Score: 37.82 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31881770 250 LKALEVWTDFNKIRVGYPELAEVLGRFVIYKKSVLNARLSSDW---AHLYLQRKYNDALAWSFgkvcsLEYAGSVSTLLD 326
Cdd:cd04279 27 KQAAAEWENVGPLKFVYNPEEDNDADIVIFFDRPPPVGGAGGGlarAGFPLISDGNRKLFNRT-----DINLGPGQPRGA 101
|
90 100
....*....|....*....|..
gi 31881770 327 TNILAPATwsaHELGHAVGMSH 348
Cdd:cd04279 102 ENLQAIAL---HELGHALGLWH 120
|
|
| |
