|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
299-496 |
6.12e-86 |
|
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: 271.48 E-value: 6.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 379 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSsrKPKCDCT 453
Cdd:pfam01421 80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDF--NGGCKCP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530371121 454 EsWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 496
Cdd:pfam01421 158 P-GGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
587-726 |
1.84e-51 |
|
ADAM Cysteine-Rich Domain; :
Pssm-ID: 214743 Cd Length: 137 Bit Score: 176.01 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 587 QDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLT 666
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 667 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 726
Cdd:smart00608 81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
147-249 |
8.50e-29 |
|
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: 111.64 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 147 HLAQASFQIEAFGSKFILDLILNNGLLSSDY-VEIHYENGKP--QYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFE 223
Cdd:pfam01562 23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGveSPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
|
90 100
....*....|....*....|....*.
gi 530371121 224 DDTFVYMIEPLElVHDEKSTGRPHII 249
Cdd:pfam01562 103 TENEEYLIEPLE-KYSREEGGHPHVV 127
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
511-583 |
8.66e-29 |
|
Disintegrin; :
Pssm-ID: 459709 Cd Length: 74 Bit Score: 109.64 E-value: 8.66e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530371121 511 EAGEECDCGFHVECY-GLCC--KKCSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPN 583
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCdaKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
299-496 |
6.12e-86 |
|
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: 271.48 E-value: 6.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 379 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSsrKPKCDCT 453
Cdd:pfam01421 80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDF--NGGCKCP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530371121 454 EsWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 496
Cdd:pfam01421 158 P-GGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
299-494 |
2.12e-64 |
|
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: 214.02 E-value: 2.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKeQLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 379 I----KQHaDAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSrkpkCDC 452
Cdd:cd04269 80 NllprKPH-DNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnLLLFAVTMAHELGHNLGMEHDDGG----CTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530371121 453 TESwgGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFN 494
Cdd:cd04269 155 GRS--TCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
587-726 |
1.84e-51 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 176.01 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 587 QDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLT 666
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 667 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 726
Cdd:smart00608 81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
588-697 |
2.11e-33 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 123.88 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 588 DGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLTR 667
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 530371121 668 APRIGQLQgeiipTSFYHQGRVIDCSGAHV 697
Cdd:pfam08516 81 LPLLGEHA-----TVIYTNINGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
147-249 |
8.50e-29 |
|
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: 111.64 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 147 HLAQASFQIEAFGSKFILDLILNNGLLSSDY-VEIHYENGKP--QYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFE 223
Cdd:pfam01562 23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGveSPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
|
90 100
....*....|....*....|....*.
gi 530371121 224 DDTFVYMIEPLElVHDEKSTGRPHII 249
Cdd:pfam01562 103 TENEEYLIEPLE-KYSREEGGHPHVV 127
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
511-583 |
8.66e-29 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 109.64 E-value: 8.66e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530371121 511 EAGEECDCGFHVECY-GLCC--KKCSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPN 583
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCdaKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
511-585 |
1.20e-27 |
|
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: 106.62 E-value: 1.20e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530371121 511 EAGEECDCGFHVECYGLCCKK--CSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPNLH 585
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPatCKLKPGAQCASGPCCDN--CKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
299-496 |
6.12e-86 |
|
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: 271.48 E-value: 6.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 379 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSsrKPKCDCT 453
Cdd:pfam01421 80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDF--NGGCKCP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530371121 454 EsWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 496
Cdd:pfam01421 158 P-GGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
299-494 |
2.12e-64 |
|
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: 214.02 E-value: 2.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKeQLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 379 I----KQHaDAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSrkpkCDC 452
Cdd:cd04269 80 NllprKPH-DNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnLLLFAVTMAHELGHNLGMEHDDGG----CTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530371121 453 TESwgGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFN 494
Cdd:cd04269 155 GRS--TCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
587-726 |
1.84e-51 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 176.01 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 587 QDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLT 666
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 667 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 726
Cdd:smart00608 81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
588-697 |
2.11e-33 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 123.88 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 588 DGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLTR 667
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 530371121 668 APRIGQLQgeiipTSFYHQGRVIDCSGAHV 697
Cdd:pfam08516 81 LPLLGEHA-----TVIYTNINGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
147-249 |
8.50e-29 |
|
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: 111.64 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 147 HLAQASFQIEAFGSKFILDLILNNGLLSSDY-VEIHYENGKP--QYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFE 223
Cdd:pfam01562 23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGveSPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
|
90 100
....*....|....*....|....*.
gi 530371121 224 DDTFVYMIEPLElVHDEKSTGRPHII 249
Cdd:pfam01562 103 TENEEYLIEPLE-KYSREEGGHPHVV 127
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
511-583 |
8.66e-29 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 109.64 E-value: 8.66e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530371121 511 EAGEECDCGFHVECY-GLCC--KKCSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPN 583
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCdaKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
511-585 |
1.20e-27 |
|
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: 106.62 E-value: 1.20e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530371121 511 EAGEECDCGFHVECYGLCCKK--CSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPNLH 585
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPatCKLKPGAQCASGPCCDN--CKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
299-484 |
6.42e-20 |
|
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: 88.25 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKE---QLNTRVVLVAVETWTEKDQIDITTNPVQM-LHEFSK 374
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKGEQFAPPIDSDASNtLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 375 YRQRIKQHADAVHLISRVTFHYKRS-SLSYFGGVCSRTRGVGVNE-YGLPMAVAQVLSQSLAQNLGIQWEPSSRkpkCDC 452
Cdd:cd04267 81 WRAEGPIRHDNAVLLTAQDFIEGDIlGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAEHDGGDE---LAF 157
|
170 180 190
....*....|....*....|....*....|....
gi 530371121 453 TESWGG-CIMEETGVSH-SRKFSKCSILEYRDFL 484
Cdd:cd04267 158 ECDGGGnYIMAPVDSGLnSYRFSQCSIGSIREFL 191
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
299-493 |
3.60e-19 |
|
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: 86.52 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 299 KYLELMIVNDHKTYKKHrsSHAHTNNFAKSVVNLVDSIYKEQL---NTRVVLVAVETWT-EKDQIDITTNPVQMLHEFSK 374
Cdd:cd04273 1 RYVETLVVADSKMVEFH--HGEDLEHYILTLMNIVASLYKDPSlgnSINIVVVRLIVLEdEESGLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 375 YRQRIK-------QHADAVHLISRVTFHYKRSS-----LSYFGGVCSRTRGVGVNE-YGLPMAVaqVLSQSLAQNLGIQW 441
Cdd:cd04273 79 WQKKLNppndsdpEHHDHAILLTRQDICRSNGNcdtlgLAPVGGMCSPSRSCSINEdTGLSSAF--TIAHELGHVLGMPH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530371121 442 EPSSrkPKCDcTESWGGCIMEETGVSHSRKF--SKCSILEYRDFLQRGGGACLF 493
Cdd:cd04273 157 DGDG--NSCG-PEGKDGHIMSPTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
303-473 |
1.04e-05 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 47.03 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 303 LMIVNDHKTYKKHRSSHAHTNnfAKSVVNLVDSIYKEQLNTRVVLVAVETWTEKD----QIDITTNPVQMLHEFSKYRQR 378
Cdd:pfam13688 7 LLVAADCSYVAAFGGDAAQAN--IINMVNTASNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQDFSAW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 379 I-KQHADAVHLISRVTFHYkrSSLSYFGGVCSRTRGVGVNEYGLPMAVAQ---VLSQSLAQNLGIQW------EPSSRKP 448
Cdd:pfam13688 85 RgTQNDDLAYLFLMTNCSG--GGLAWLGQLCNSGSAGSVSTRVSGNNVVVstaTEWQVFAHEIGHNFgavhdcDSSTSSQ 162
|
170 180
....*....|....*....|....*....
gi 530371121 449 KCDCTESW----GGCIMEETGVSHSRKFS 473
Cdd:pfam13688 163 CCPPSNSTcpagGRYIMNPSSSPNSTDFS 191
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
299-484 |
1.45e-05 |
|
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: 45.98 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 299 KYLELMIVNDHKTYKKHRSSHAHtnnfaKSVVNLVDSIYKEQLNTRVVLVAVETwtekdqidittnpvqmlhefskyrqr 378
Cdd:cd00203 1 KVIPYVVVADDRDVEEENLSAQI-----QSLILIAMQIWRDYLNIRFVLVGVEI-------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 379 ikQHADAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGV---NEYGlPMAVAQVLSQSLAQNLGIqWEPSSRKPKCDCTES 455
Cdd:cd00203 50 --DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVlqdNQSG-TKEGAQTIAHELGHALGF-YHDHDRKDRDDYPTI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530371121 456 W---------GGCIM--EETGVSHSRK--FSKCSILEYRDFL 484
Cdd:cd00203 126 DdtlnaedddYYSVMsyTKGSFSDGQRkdFSQCDIDQINKLY 167
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
300-492 |
1.77e-04 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 43.88 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 300 YLELMIVNDHKTYKKHRSSHAHTNNFAkSVVNLVDSIYKEQLNTRV--VLVAVETWTEKD-------QIDITTNPVQMLH 370
Cdd:cd04272 2 YPELFVVVDYDHQSEFFSNEQLIRYLA-VMVNAANLRYRDLKSPRIrlLLVGITISKDPDfepyihpINYGYIDAAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371121 371 EFSKY--RQRIKQHADAVHLISR---VTFHYKR-----SSLSYFGGVCSRTRgVGVNEY--GLPMAVaQVLSQSLAQNLG 438
Cdd:cd04272 81 NFNEYvkKKRDYFNPDVVFLVTGldmSTYSGGSlqtgtGGYAYVGGACTENR-VAMGEDtpGSYYGV-YTMTHELAHLLG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530371121 439 IQWEPSSRKPKCDCTESWGGC------IME--ETGVSHSRkFSKCSILEYRDFLQRGGGACL 492
Cdd:cd04272 159 APHDGSPPPSWVKGHPGSLDCpwddgyIMSyvVNGERQYR-FSQCSQRQIRNVFRRLGASCL 219
|
|
|