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Conserved domains on  [gi|497239341|ref|NP_001265043|]
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disintegrin and metalloproteinase domain-containing protein 2 isoform 3 precursor [Homo sapiens]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 12023311)

disintegrin and metalloproteinase domain-containing protein, also called metalloproteinase-disintegrin (ADAM), is a membrane-spanning multi-domain protein which may serve as an integrin ligand

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 178-375 5.05e-92

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: 283.81  E-value: 5.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341  178 KYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVSFNITIILSSLELWIDENKIATTGEANELLHTFLRWKTSY 257
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341  258 LV-LRPHDVAFLLVYREKSN-YVGATFQGKMCDANYAGGVVLHPRtISLESLAVILAQLLSLSMGITYDDINK-CQC-SG 333
Cdd:pfam01421  81 LKkRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCpPG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 497239341  334 AVCIMNPEAIHFSGVKiFSNCSFEDFAHFISKQKSQCLHNQP 375
Cdd:pfam01421 160 GGCIMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 393-470 3.53e-34

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: 124.73  E-value: 3.53e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497239341   393 EAGEECDCGTEQDCaliGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHY 470
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 26-141 3.66e-27

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: 106.63  E-value: 3.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341   26 QITVPEKIRSIIK-------EGIESQASYKIVIEGKPYTVNLMQ-KNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGY 97
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslaseSTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 497239341   98 IEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLE----SSVGFEHVIY 141
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
ACR smart00608
ADAM Cysteine-Rich Domain;
472-536 9.76e-22

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 91.65  E-value: 9.76e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497239341   472 QTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCE 536
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCA 65
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 178-375 5.05e-92

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: 283.81  E-value: 5.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341  178 KYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVSFNITIILSSLELWIDENKIATTGEANELLHTFLRWKTSY 257
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341  258 LV-LRPHDVAFLLVYREKSN-YVGATFQGKMCDANYAGGVVLHPRtISLESLAVILAQLLSLSMGITYDDINK-CQC-SG 333
Cdd:pfam01421  81 LKkRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCpPG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 497239341  334 AVCIMNPEAIHFSGVKiFSNCSFEDFAHFISKQKSQCLHNQP 375
Cdd:pfam01421 160 GGCIMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 178-373 8.87e-72

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: 230.58  E-value: 8.87e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341 178 KYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVSFNITIILSSLELWIDENKIATTGEANELLHTFLRWKTSY 257
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341 258 LVLR-PHDVAFLLVYRE-KSNYVGATFQGKMCDANYAGGVVLHPRTiSLESLAVILAQLLSLSMGITYDDINkCQCSGAV 335
Cdd:cd04269   81 LLPRkPHDNAQLLTGRDfDGNTVGLAYVGGMCSPKYSGGVVQDHSR-NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRST 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 497239341 336 CIMNPEAIHFSgvKIFSNCSFEDFAHFISKQKSQCLHN 373
Cdd:cd04269  159 CIMAPSPSSLT--DAFSNCSYEDYQKFLSRGGGQCLLN 194
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 393-470 3.53e-34

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: 124.73  E-value: 3.53e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497239341   393 EAGEECDCGTEQDCaliGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHY 470
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
393-468 9.81e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 120.42  E-value: 9.81e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497239341  393 EAGEECDCGTEQDCALigETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPEN 468
Cdd:pfam00200   1 EEGEECDCGSLEECTN--DPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 26-141 3.66e-27

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: 106.63  E-value: 3.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341   26 QITVPEKIRSIIK-------EGIESQASYKIVIEGKPYTVNLMQ-KNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGY 97
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslaseSTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 497239341   98 IEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLE----SSVGFEHVIY 141
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
ACR smart00608
ADAM Cysteine-Rich Domain;
472-536 9.76e-22

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 91.65  E-value: 9.76e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497239341   472 QTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCE 536
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCA 65
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 474-543 2.39e-21

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: 89.21  E-value: 2.39e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341  474 GHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEVcRNQRC 543
Cdd:pfam08516   2 GTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEK-RDVLC 70
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 178-375 5.05e-92

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: 283.81  E-value: 5.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341  178 KYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVSFNITIILSSLELWIDENKIATTGEANELLHTFLRWKTSY 257
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341  258 LV-LRPHDVAFLLVYREKSN-YVGATFQGKMCDANYAGGVVLHPRtISLESLAVILAQLLSLSMGITYDDINK-CQC-SG 333
Cdd:pfam01421  81 LKkRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCpPG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 497239341  334 AVCIMNPEAIHFSGVKiFSNCSFEDFAHFISKQKSQCLHNQP 375
Cdd:pfam01421 160 GGCIMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 178-373 8.87e-72

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: 230.58  E-value: 8.87e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341 178 KYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVSFNITIILSSLELWIDENKIATTGEANELLHTFLRWKTSY 257
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341 258 LVLR-PHDVAFLLVYRE-KSNYVGATFQGKMCDANYAGGVVLHPRTiSLESLAVILAQLLSLSMGITYDDINkCQCSGAV 335
Cdd:cd04269   81 LLPRkPHDNAQLLTGRDfDGNTVGLAYVGGMCSPKYSGGVVQDHSR-NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRST 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 497239341 336 CIMNPEAIHFSgvKIFSNCSFEDFAHFISKQKSQCLHN 373
Cdd:cd04269  159 CIMAPSPSSLT--DAFSNCSYEDYQKFLSRGGGQCLLN 194
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 393-470 3.53e-34

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: 124.73  E-value: 3.53e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497239341   393 EAGEECDCGTEQDCaliGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHY 470
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
393-468 9.81e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 120.42  E-value: 9.81e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497239341  393 EAGEECDCGTEQDCALigETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPEN 468
Cdd:pfam00200   1 EEGEECDCGSLEECTN--DPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 26-141 3.66e-27

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: 106.63  E-value: 3.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341   26 QITVPEKIRSIIK-------EGIESQASYKIVIEGKPYTVNLMQ-KNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGY 97
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslaseSTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 497239341   98 IEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLE----SSVGFEHVIY 141
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
ACR smart00608
ADAM Cysteine-Rich Domain;
472-536 9.76e-22

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 91.65  E-value: 9.76e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497239341   472 QTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCE 536
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCA 65
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 474-543 2.39e-21

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: 89.21  E-value: 2.39e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341  474 GHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEVcRNQRC 543
Cdd:pfam08516   2 GTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEK-RDVLC 70
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 178-372 7.28e-08

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: 53.40  E-value: 7.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341 178 KYIEMHVIVEKQLYNHMGSDTTV--------VAQKVFQLIGLTNaifvsfNITIILSSLELWIDENK-IATTGEANELLH 248
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEhyiltlmnIVASLYKDPSLGN------SINIVVVRLIVLEDEESgLLISGNAQKSLK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341 249 TFLRWKTSYLVLRP-----HDVAFLL------VYREKSNYVGATFQGKMCDANYAGGVVlhprtislE----SLAVILAQ 313
Cdd:cd04273   75 SFCRWQKKLNPPNDsdpehHDHAILLtrqdicRSNGNCDTLGLAPVGGMCSPSRSCSIN--------EdtglSSAFTIAH 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497239341 314 LLSLSMGITYDD-INKCQCSGAVC-IMNPEAIHFSGVKIFSNCSFEDFAHFISKQKSQCLH 372
Cdd:cd04273  147 ELGHVLGMPHDGdGNSCGPEGKDGhIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 178-355 4.84e-07

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: 50.50  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341 178 KYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVS----FNITIILSSLELWiDENKIATTGEAN--ELLHTFL 251
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQIL-KGEQFAPPIDSDasNTLNSFS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497239341 252 RWKTSylVLRPHDVAFLLVYREKSN--YVGATFQGKMCDANYAGGVVLhpRTISLESLAVILAQLLSLSMGITYDDINKC 329
Cdd:cd04267   80 FWRAE--GPIRHDNAVLLTAQDFIEgdILGLAYVGSMCNPYSSVGVVE--DTGFTLLTALTMAHELGHNLGAEHDGGDEL 155

                        170       180
                 ....*....|....*....|....*....
gi 497239341 330 QC---SGAVCIMNPeAIHFSGVKIFSNCS 355
Cdd:cd04267  156 AFecdGGGNYIMAP-VDSGLNSYRFSQCS 183
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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