|
Name |
Accession |
Description |
Interval |
E-value |
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
227-429 |
7.39e-44 |
|
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: 157.39 E-value: 7.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 227 KYVEVALIADYEFMKARGLHDLDAISYMLESLNIADSMLsRDLNIRLSAVYVELWTDVQRIDLWEDIERTLSGVVDYASG 306
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIY-RPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 307 HIYH-IQKDASILFTAGSFANQEVSNAAIRSICTARSAVivkGVEQF---ATHWNGELLAQSIGHLLGLEHDTTACSCeP 382
Cdd:cd04269 80 NLLPrKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSG---GVVQDhsrNLLLFAVTMAHELGHNLGMEHDDGGCTC-G 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17551722 383 SPECVMRQQPGRvgggggspFSWQFSKCSVARMHGIWQDGNIQCLLN 429
Cdd:cd04269 156 RSTCIMAPSPSS--------LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
524-657 |
2.42e-36 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 134.02 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 524 DGTVCGTD-GQCWRGNCSDSHQQCQKLWGREARVAEPVCFEQ-NTKGAEYANCGQRQadGTYHPCQIEDTRCGTLHCHSG 601
Cdd:smart00608 2 DGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGREN--GTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17551722 602 SITPIDSSLkaFTFHFTeNSHQIQCKSIAS-----AAVGLTSDGTNCASGRVCVAGSCVEM 657
Cdd:smart00608 80 SELPLLGEH--ATVIYS-NIGGLVCWSLDYhlgtdPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
446-521 |
2.88e-33 |
|
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: 122.80 E-value: 2.88e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17551722 446 DGSEECDCGSRENCQDPCCDPLTCTLRPHAQCaAHHKCCHRCELRKAGDTCRSSKSPCDVAEQCDGKSGDCPPDGH 521
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQC-ASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
46-179 |
4.90e-22 |
|
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: 92.76 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 46 EVVHPFQIRDKNER-------IGIDTRNYFLKAQEHYshvtivirsnqlgrLKLVLERN-NFIFLNQTAFHKLDADGERV 117
Cdd:pfam01562 1 EVVIPVRLDPSRRRrslasesTYLDTLSYRLAAFGKK--------------FHLHLTPNrLLLAPGFTVTYYLDGGTGVE 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17551722 118 IQ-NRVENCYYQGTVGGEESSFVALSSCNGLRGVISFANGtTFGIWPLDGGDRNSRRHPHILY 179
Cdd:pfam01562 67 SPpVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLEKYSREEGGHPHVVY 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 ... |
227-429 |
7.39e-44 |
|
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: 157.39 E-value: 7.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 227 KYVEVALIADYEFMKARGLHDLDAISYMLESLNIADSMLsRDLNIRLSAVYVELWTDVQRIDLWEDIERTLSGVVDYASG 306
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIY-RPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 307 HIYH-IQKDASILFTAGSFANQEVSNAAIRSICTARSAVivkGVEQF---ATHWNGELLAQSIGHLLGLEHDTTACSCeP 382
Cdd:cd04269 80 NLLPrKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSG---GVVQDhsrNLLLFAVTMAHELGHNLGMEHDDGGCTC-G 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17551722 383 SPECVMRQQPGRvgggggspFSWQFSKCSVARMHGIWQDGNIQCLLN 429
Cdd:cd04269 156 RSTCIMAPSPSS--------LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
524-657 |
2.42e-36 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 134.02 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 524 DGTVCGTD-GQCWRGNCSDSHQQCQKLWGREARVAEPVCFEQ-NTKGAEYANCGQRQadGTYHPCQIEDTRCGTLHCHSG 601
Cdd:smart00608 2 DGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGREN--GTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17551722 602 SITPIDSSLkaFTFHFTeNSHQIQCKSIAS-----AAVGLTSDGTNCASGRVCVAGSCVEM 657
Cdd:smart00608 80 SELPLLGEH--ATVIYS-NIGGLVCWSLDYhlgtdPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
446-521 |
2.88e-33 |
|
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: 122.80 E-value: 2.88e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17551722 446 DGSEECDCGSRENCQDPCCDPLTCTLRPHAQCaAHHKCCHRCELRKAGDTCRSSKSPCDVAEQCDGKSGDCPPDGH 521
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQC-ASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
446-519 |
6.32e-29 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 110.41 E-value: 6.32e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17551722 446 DGSEECDCGSRENCQ-DPCCDPLTCTLRPHAQCAaHHKCCHRCELRKAGDTCRSSKSPCDVAEQCDGKSGDCPPD 519
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCS-SGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
227-431 |
6.85e-26 |
|
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: 106.23 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 227 KYVEVALIADYEFMKARGlHDLDAI-SYMLESLNIADSMLsRDLNIRLSAVYVELWTDVQRIDLWEDIERTLSGVVDY-A 304
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMG-SDTTVVrQRVFQVVNLVNSIY-KELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWrQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 305 SGHIYHIQKDASILFTAGSFANQEVSNAAIRSICTARSAVivkGVEQFAtHWNGEL----LAQSIGHLLGLEHDT--TAC 378
Cdd:pfam01421 79 EYLKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSG---GVNEDH-SKNLESfavtMAHELGHNLGMQHDDfnGGC 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17551722 379 SCEPSPECVMRQQPGrvgggggSPFSWQFSKCSVARMHGIWQDGNIQCLLNKP 431
Cdd:pfam01421 155 KCPPGGGCIMNPSAG-------SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
524-629 |
4.82e-24 |
|
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: 97.69 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 524 DGTVC-GTDGQCWRGNCSDSHQQCQKLWGREARVAEPVCFEQ-NTKGAEYANCGQRQadGTYHPCQIEDTRCGTLHCHSG 601
Cdd:pfam08516 1 DGTPCnNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTN--GGYVKCEKRDVLCGKLQCTNV 78
|
90 100
....*....|....*....|....*...
gi 17551722 602 SITPIDSSLKafTFHFTeNSHQIQCKSI 629
Cdd:pfam08516 79 KELPLLGEHA--TVIYT-NINGVTCWGT 103
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
46-179 |
4.90e-22 |
|
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: 92.76 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 46 EVVHPFQIRDKNER-------IGIDTRNYFLKAQEHYshvtivirsnqlgrLKLVLERN-NFIFLNQTAFHKLDADGERV 117
Cdd:pfam01562 1 EVVIPVRLDPSRRRrslasesTYLDTLSYRLAAFGKK--------------FHLHLTPNrLLLAPGFTVTYYLDGGTGVE 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17551722 118 IQ-NRVENCYYQGTVGGEESSFVALSSCNGLRGVISFANGtTFGIWPLDGGDRNSRRHPHILY 179
Cdd:pfam01562 67 SPpVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLEKYSREEGGHPHVVY 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 ... |
227-429 |
7.39e-44 |
|
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: 157.39 E-value: 7.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 227 KYVEVALIADYEFMKARGLHDLDAISYMLESLNIADSMLsRDLNIRLSAVYVELWTDVQRIDLWEDIERTLSGVVDYASG 306
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIY-RPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 307 HIYH-IQKDASILFTAGSFANQEVSNAAIRSICTARSAVivkGVEQF---ATHWNGELLAQSIGHLLGLEHDTTACSCeP 382
Cdd:cd04269 80 NLLPrKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSG---GVVQDhsrNLLLFAVTMAHELGHNLGMEHDDGGCTC-G 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17551722 383 SPECVMRQQPGRvgggggspFSWQFSKCSVARMHGIWQDGNIQCLLN 429
Cdd:cd04269 156 RSTCIMAPSPSS--------LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
524-657 |
2.42e-36 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 134.02 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 524 DGTVCGTD-GQCWRGNCSDSHQQCQKLWGREARVAEPVCFEQ-NTKGAEYANCGQRQadGTYHPCQIEDTRCGTLHCHSG 601
Cdd:smart00608 2 DGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGREN--GTYIPCAPEDVKCGKLQCTNV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17551722 602 SITPIDSSLkaFTFHFTeNSHQIQCKSIAS-----AAVGLTSDGTNCASGRVCVAGSCVEM 657
Cdd:smart00608 80 SELPLLGEH--ATVIYS-NIGGLVCWSLDYhlgtdPDIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
446-521 |
2.88e-33 |
|
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: 122.80 E-value: 2.88e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17551722 446 DGSEECDCGSRENCQDPCCDPLTCTLRPHAQCaAHHKCCHRCELRKAGDTCRSSKSPCDVAEQCDGKSGDCPPDGH 521
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQC-ASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
446-519 |
6.32e-29 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 110.41 E-value: 6.32e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17551722 446 DGSEECDCGSRENCQ-DPCCDPLTCTLRPHAQCAaHHKCCHRCELRKAGDTCRSSKSPCDVAEQCDGKSGDCPPD 519
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCS-SGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
227-431 |
6.85e-26 |
|
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: 106.23 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 227 KYVEVALIADYEFMKARGlHDLDAI-SYMLESLNIADSMLsRDLNIRLSAVYVELWTDVQRIDLWEDIERTLSGVVDY-A 304
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMG-SDTTVVrQRVFQVVNLVNSIY-KELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWrQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 305 SGHIYHIQKDASILFTAGSFANQEVSNAAIRSICTARSAVivkGVEQFAtHWNGEL----LAQSIGHLLGLEHDT--TAC 378
Cdd:pfam01421 79 EYLKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSG---GVNEDH-SKNLESfavtMAHELGHNLGMQHDDfnGGC 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17551722 379 SCEPSPECVMRQQPGrvgggggSPFSWQFSKCSVARMHGIWQDGNIQCLLNKP 431
Cdd:pfam01421 155 KCPPGGGCIMNPSAG-------SSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
524-629 |
4.82e-24 |
|
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: 97.69 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 524 DGTVC-GTDGQCWRGNCSDSHQQCQKLWGREARVAEPVCFEQ-NTKGAEYANCGQRQadGTYHPCQIEDTRCGTLHCHSG 601
Cdd:pfam08516 1 DGTPCnNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTN--GGYVKCEKRDVLCGKLQCTNV 78
|
90 100
....*....|....*....|....*...
gi 17551722 602 SITPIDSSLKafTFHFTeNSHQIQCKSI 629
Cdd:pfam08516 79 KELPLLGEHA--TVIYT-NINGVTCWGT 103
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
46-179 |
4.90e-22 |
|
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: 92.76 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 46 EVVHPFQIRDKNER-------IGIDTRNYFLKAQEHYshvtivirsnqlgrLKLVLERN-NFIFLNQTAFHKLDADGERV 117
Cdd:pfam01562 1 EVVIPVRLDPSRRRrslasesTYLDTLSYRLAAFGKK--------------FHLHLTPNrLLLAPGFTVTYYLDGGTGVE 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17551722 118 IQ-NRVENCYYQGTVGGEESSFVALSSCNGLRGVISFANGtTFGIWPLDGGDRNSRRHPHILY 179
Cdd:pfam01562 67 SPpVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLEKYSREEGGHPHVVY 128
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
227-428 |
1.55e-10 |
|
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: 61.87 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 227 KYVEVALIAD---YEFMKARGLHDldaisYMLESLNIADSMLsRD----LNIRLSAVYVELWTDVQR-IDLWEDIERTL- 297
Cdd:cd04273 1 RYVETLVVADskmVEFHHGEDLEH-----YILTLMNIVASLY-KDpslgNSINIVVVRLIVLEDEESgLLISGNAQKSLk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 298 ------SGVVDYASGHIYHIqkDASILFT----AGSFANQEVSN-AAIRSICTA-RSAVIVKGvEQFAThwnGELLAQSI 365
Cdd:cd04273 75 sfcrwqKKLNPPNDSDPEHH--DHAILLTrqdiCRSNGNCDTLGlAPVGGMCSPsRSCSINED-TGLSS---AFTIAHEL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17551722 366 GHLLGLEHDTTACSCEPSPE--CVMrqqpGRVGGGGGSPFSWqfSKCSVARMHGIWQDGNIQCLL 428
Cdd:cd04273 149 GHVLGMPHDGDGNSCGPEGKdgHIM----SPTLGANTGPFTW--SKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
227-414 |
4.80e-10 |
|
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: 60.13 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 227 KYVEVALIADYEFMKARGLHDLDAISYMLESLNIADSM---LSRDLNIRLSAVYVELWTDVQRIDLWE-DIERTLSGV-V 301
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIyrsTNLRLGIRISLEGLQILKGEQFAPPIDsDASNTLNSFsF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 302 DYASGHIYHiqkDASILFTAGSFANQ-EVSNAAIRSICTARSAVIVkgVEQFATHWNGEL-LAQSIGHLLGLEHDT---T 376
Cdd:cd04267 81 WRAEGPIRH---DNAVLLTAQDFIEGdILGLAYVGSMCNPYSSVGV--VEDTGFTLLTALtMAHELGHNLGAEHDGgdeL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 17551722 377 ACSCEPSPECVMRQQPGRVGggggspfSWQFSKCSVAR 414
Cdd:cd04267 156 AFECDGGGNYIMAPVDSGLN-------SYRFSQCSIGS 186
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
228-427 |
4.69e-04 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 42.72 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 228 YVEVALIADYEFMKArGLHDLDAISYMLESLNIADSMLS--RDLNIRLSAVYVELWTD-----VQRIDLWEDIE--RTLS 298
Cdd:cd04272 2 YPELFVVVDYDHQSE-FFSNEQLIRYLAVMVNAANLRYRdlKSPRIRLLLVGITISKDpdfepYIHPINYGYIDaaETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 299 GVVDYASGHIYHIQKDASILFTA--------GSFANQEVSNAAIRSICTARSaviVKGVEQFATHWNGEL-LAQSIGHLL 369
Cdd:cd04272 81 NFNEYVKKKRDYFNPDVVFLVTGldmstysgGSLQTGTGGYAYVGGACTENR---VAMGEDTPGSYYGVYtMTHELAHLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17551722 370 GLEHDTTACSCEPSPECVMRQQPGR----VGGGGGSPFSWQFSKCSVARMHGIWQDGNIQCL 427
Cdd:cd04272 158 GAPHDGSPPPSWVKGHPGSLDCPWDdgyiMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
314-414 |
7.68e-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: 41.35 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551722 314 DASILFTAGSFANQEVSNAAIRSICTARSAVIVKGVEQFATHWNGELLAQSIGHLLGLEHDTTACSCEPSP--------- 384
Cdd:cd00203 53 DIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPtiddtlnae 132
|
90 100 110
....*....|....*....|....*....|....
gi 17551722 385 ----ECVMRQQPGRVGGGGgspfSWQFSKCSVAR 414
Cdd:cd00203 133 dddyYSVMSYTKGSFSDGQ----RKDFSQCDIDQ 162
|
|
| |
