|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
296-493 |
2.17e-83 |
|
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: 264.93 E-value: 2.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 296 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDHIDITINPVQMLHDFSKYRQR 375
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 376 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRIRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSRKPKCeci 450
Cdd:pfam01421 80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDFNGGCKC--- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568906339 451 ESWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 493
Cdd:pfam01421 157 PPGGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
584-723 |
2.34e-51 |
|
ADAM Cysteine-Rich Domain;
:
Pssm-ID: 214743 Cd Length: 137 Bit Score: 176.01 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 584 QDGYSCNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIPCSKHDVFCGFLLCTNLT 663
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 664 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 723
Cdd:smart00608 81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
144-246 |
6.07e-31 |
|
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: 117.80 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 144 HLAQASFQIEAFGSKFILDLTLNNGLLSSDY-VEIHYEDGKQM--YSKGGEHCYYHGSIRGVKDSRVALSTCNGLHGMFE 220
Cdd:pfam01562 23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGVesPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
|
90 100
....*....|....*....|....*.
gi 568906339 221 DDTFVYMIEPLELTDDEkSTGRPHII 246
Cdd:pfam01562 103 TENEEYLIEPLEKYSRE-EGGHPHVV 127
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
508-580 |
1.10e-27 |
|
Disintegrin;
:
Pssm-ID: 459709 Cd Length: 74 Bit Score: 106.56 E-value: 1.10e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568906339 508 EAGEECDCGFHVECY-GVCC--KKCSLSNGAHCSDGPCCNNtsCLFQSRGYECRDAVNSCDITEYCTGDSGQCPPN 580
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 ... |
296-493 |
2.17e-83 |
|
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: 264.93 E-value: 2.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 296 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDHIDITINPVQMLHDFSKYRQR 375
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 376 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRIRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSRKPKCeci 450
Cdd:pfam01421 80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDFNGGCKC--- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568906339 451 ESWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 493
Cdd:pfam01421 157 PPGGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
296-491 |
7.34e-62 |
|
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: 207.08 E-value: 7.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 296 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKeQLNTRVVLVAVETWTEKDHIDITINPVQMLHDFSKYRQR 375
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 376 I----KQHaDAVHLISRVTFHYKRSSLSYFGGVCSRIRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSrkpkCEC 449
Cdd:cd04269 80 NllprKPH-DNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnLLLFAVTMAHELGHNLGMEHDDGG----CTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568906339 450 IESwgGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFN 491
Cdd:cd04269 155 GRS--TCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
584-723 |
2.34e-51 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 176.01 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 584 QDGYSCNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIPCSKHDVFCGFLLCTNLT 663
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 664 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 723
Cdd:smart00608 81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
585-694 |
9.20e-34 |
|
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: 125.04 E-value: 9.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 585 DGYSCNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIPCSKHDVFCGFLLCTNLTR 664
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 568906339 665 APRIGQLQgeiipTSFYHQGRVIDCSGAHV 694
Cdd:pfam08516 81 LPLLGEHA-----TVIYTNINGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
144-246 |
6.07e-31 |
|
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: 117.80 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 144 HLAQASFQIEAFGSKFILDLTLNNGLLSSDY-VEIHYEDGKQM--YSKGGEHCYYHGSIRGVKDSRVALSTCNGLHGMFE 220
Cdd:pfam01562 23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGVesPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
|
90 100
....*....|....*....|....*.
gi 568906339 221 DDTFVYMIEPLELTDDEkSTGRPHII 246
Cdd:pfam01562 103 TENEEYLIEPLEKYSRE-EGGHPHVV 127
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
508-580 |
1.10e-27 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 106.56 E-value: 1.10e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568906339 508 EAGEECDCGFHVECY-GVCC--KKCSLSNGAHCSDGPCCNNtsCLFQSRGYECRDAVNSCDITEYCTGDSGQCPPN 580
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCdaKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
508-582 |
7.45e-26 |
|
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: 101.23 E-value: 7.45e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568906339 508 EAGEECDCGFHVECYGVCCKK--CSLSNGAHCSDGPCCNNtsCLFQSRGYECRDAVNSCDITEYCTGDSGQCPPNLH 582
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 ... |
296-493 |
2.17e-83 |
|
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: 264.93 E-value: 2.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 296 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDHIDITINPVQMLHDFSKYRQR 375
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 376 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRIRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSRKPKCeci 450
Cdd:pfam01421 80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDFNGGCKC--- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568906339 451 ESWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 493
Cdd:pfam01421 157 PPGGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
296-491 |
7.34e-62 |
|
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: 207.08 E-value: 7.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 296 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKeQLNTRVVLVAVETWTEKDHIDITINPVQMLHDFSKYRQR 375
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 376 I----KQHaDAVHLISRVTFHYKRSSLSYFGGVCSRIRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSrkpkCEC 449
Cdd:cd04269 80 NllprKPH-DNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnLLLFAVTMAHELGHNLGMEHDDGG----CTC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568906339 450 IESwgGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFN 491
Cdd:cd04269 155 GRS--TCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
584-723 |
2.34e-51 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 176.01 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 584 QDGYSCNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIPCSKHDVFCGFLLCTNLT 663
Cdd:smart00608 1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 664 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 723
Cdd:smart00608 81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
585-694 |
9.20e-34 |
|
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: 125.04 E-value: 9.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 585 DGYSCNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIPCSKHDVFCGFLLCTNLTR 664
Cdd:pfam08516 1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
|
90 100 110
....*....|....*....|....*....|
gi 568906339 665 APRIGQLQgeiipTSFYHQGRVIDCSGAHV 694
Cdd:pfam08516 81 LPLLGEHA-----TVIYTNINGVTCWGTDY 105
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
144-246 |
6.07e-31 |
|
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: 117.80 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 144 HLAQASFQIEAFGSKFILDLTLNNGLLSSDY-VEIHYEDGKQM--YSKGGEHCYYHGSIRGVKDSRVALSTCNGLHGMFE 220
Cdd:pfam01562 23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGVesPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
|
90 100
....*....|....*....|....*.
gi 568906339 221 DDTFVYMIEPLELTDDEkSTGRPHII 246
Cdd:pfam01562 103 TENEEYLIEPLEKYSRE-EGGHPHVV 127
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
508-580 |
1.10e-27 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 106.56 E-value: 1.10e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568906339 508 EAGEECDCGFHVECY-GVCC--KKCSLSNGAHCSDGPCCNNtsCLFQSRGYECRDAVNSCDITEYCTGDSGQCPPN 580
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCdaKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
508-582 |
7.45e-26 |
|
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: 101.23 E-value: 7.45e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568906339 508 EAGEECDCGFHVECYGVCCKK--CSLSNGAHCSDGPCCNNtsCLFQSRGYECRDAVNSCDITEYCTGDSGQCPPNLH 582
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPatCKLKPGAQCASGPCCDN--CKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
296-481 |
8.37e-19 |
|
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: 85.16 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 296 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKE---QLNTRVVLVAVETWTEKDHIDITINPVQM-LHDFSK 371
Cdd:cd04267 1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKGEQFAPPIDSDASNtLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 372 YRQRIKQHADAVHLISRVTFHYKRS-SLSYFGGVCSRIRGVGVNE-YGLPMAVAQVLSQSLAQNLGIQWEPSSRkpkCEC 449
Cdd:cd04267 81 WRAEGPIRHDNAVLLTAQDFIEGDIlGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAEHDGGDE---LAF 157
|
170 180 190
....*....|....*....|....*....|....
gi 568906339 450 IESWGG-CIMEETGVSH-SRKFSKCSILEYRDFL 481
Cdd:cd04267 158 ECDGGGnYIMAPVDSGLnSYRFSQCSIGSIREFL 191
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
296-490 |
3.92e-18 |
|
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: 83.83 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 296 KYLELMIVNDHKTYKKHrsSHAHTNNFAKSVVNLVDSIYKEQL---NTRVVLVAVETWTEKDH-IDITINPVQMLHDFSK 371
Cdd:cd04273 1 RYVETLVVADSKMVEFH--HGEDLEHYILTLMNIVASLYKDPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 372 YRQRIK-------QHADAVHLISRVTFHYKRSS-----LSYFGGVCSRIRGVGVNE-YGLPMAVaqVLSQSLAQNLGIQW 438
Cdd:cd04273 79 WQKKLNppndsdpEHHDHAILLTRQDICRSNGNcdtlgLAPVGGMCSPSRSCSINEdTGLSSAF--TIAHELGHVLGMPH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568906339 439 EPSSrkPKCECiESWGGCIMEETGVSHSRKF--SKCSILEYRDFLQRGGGACLF 490
Cdd:cd04273 157 DGDG--NSCGP-EGKDGHIMSPTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
296-481 |
7.45e-06 |
|
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: 47.13 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 296 KYLELMIVNDHKTYKKHRSSHAHtnnfaKSVVNLVDSIYKEQLNTRVVLVAVETwtekdhiditinpvqmlhdfskyrqr 375
Cdd:cd00203 1 KVIPYVVVADDRDVEEENLSAQI-----QSLILIAMQIWRDYLNIRFVLVGVEI-------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 376 ikQHADAVHLISRVTFHYKRSSLSYFGGVCSRIRGVGV---NEYGlPMAVAQVLSQSLAQNLGIqWEPSSRKPKCECIES 452
Cdd:cd00203 50 --DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVlqdNQSG-TKEGAQTIAHELGHALGF-YHDHDRKDRDDYPTI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568906339 453 W---------GGCIM--EETGVSHSRK--FSKCSILEYRDFL 481
Cdd:cd00203 126 DdtlnaedddYYSVMsyTKGSFSDGQRkdFSQCDIDQINKLY 167
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
297-489 |
1.95e-05 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 46.58 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 297 YLELMIVNDHKTYKKHRSSHAHTNNFAkSVVNLVDSIYKEQLNTRV--VLVAVETWTEKD-------HIDITINPVQMLH 367
Cdd:cd04272 2 YPELFVVVDYDHQSEFFSNEQLIRYLA-VMVNAANLRYRDLKSPRIrlLLVGITISKDPDfepyihpINYGYIDAAETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 368 DFSKY--RQRIKQHADAVHLISR---VTFHYKR-----SSLSYFGGVCSRiRGVGVNEY--GLPMAVaQVLSQSLAQNLG 435
Cdd:cd04272 81 NFNEYvkKKRDYFNPDVVFLVTGldmSTYSGGSlqtgtGGYAYVGGACTE-NRVAMGEDtpGSYYGV-YTMTHELAHLLG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568906339 436 IQWEPSSRKPKCECIESWGGC------IME--ETGVSHSRkFSKCSILEYRDFLQRGGGACL 489
Cdd:cd04272 159 APHDGSPPPSWVKGHPGSLDCpwddgyIMSyvVNGERQYR-FSQCSQRQIRNVFRRLGASCL 219
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
300-470 |
3.85e-05 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 45.49 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 300 LMIVNDHKTYKKHRSSHAHTNnfAKSVVNLVDSIYKEQLNTRVVLVAVETWTEKD----HIDITINPVQMLHDFSKYRQR 375
Cdd:pfam13688 7 LLVAADCSYVAAFGGDAAQAN--IINMVNTASNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQDFSAW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906339 376 I-KQHADAVHLISRVTFHYkrSSLSYFGGVCSRIRGVGVNEYGLPMAVA-------QVLSQSLAQNLG------IQWEPS 441
Cdd:pfam13688 85 RgTQNDDLAYLFLMTNCSG--GGLAWLGQLCNSGSAGSVSTRVSGNNVVvstatewQVFAHEIGHNFGavhdcdSSTSSQ 162
|
170 180
....*....|....*....|....*....
gi 568906339 442 SRKPKCECIESWGGCIMEETGVSHSRKFS 470
Cdd:pfam13688 163 CCPPSNSTCPAGGRYIMNPSSSPNSTDFS 191
|
|
| |
