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Conserved domains on  [gi|14423640|sp|Q9XSL6|]
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RecName: Full=Disintegrin and metalloproteinase domain-containing protein 28; Short=ADAM 28; AltName: Full=Epididymal metalloproteinase-like, disintegrin-like, and cysteine-rich protein II; Short=eMDC II; Flags: Precursor

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 10480592)

disintegrin and metalloproteinase domain-containing protein also contains an ADAM domain and belongs to the ADAM family of membrane-anchored metalloproteases; ADAMs (A Disintegrin And Metalloprotease) are glycoproteins that play roles in cell signaling, cell fusion, and cell-cell interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 204-398 3.07e-94

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: 291.83  E-value: 3.07e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 204 KYIEYYLVLDNGEFKKYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDEDKINITPNASFTLENFSKWRGSV 283
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 284 LPRRKRHDIAQLITATEFAGMTVGLAFMSTMCSPYHSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDNYSCKCPSTICV 363
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 14423640 364 MDKALSfYIPTDFSSCSRVSYDKFFEDKLSNCLFN 398
Cdd:cd04269 161 MAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
493-621 2.23e-45

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 159.06  E-value: 2.23e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640    493 ANGFPCHHGKGYCLMGACPTLQEQCTELWGPGTKVADQSCYNR-NEGGSKYGYCRRVDDTLIPCKTNDTMCGKLFCQGGS 571
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 14423640    572 dNLPWKGRIVTF-------LTCKTFD-PEDTSEEIGMVANGTKCGHNKVCINAECVDI 621
Cdd:smart00608  81 -ELPLLGEHATViysniggLVCWSLDyHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 30-157 1.57e-39

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: 142.07  E-value: 1.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640    30 EVVYPIRLHP-LHKREVKEPEQQEQfetELKYKMTVNGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYY 108
Cdd:pfam01562   1 EVVIPVRLDPsRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14423640   109 QGHIINEKDSDASISTCRGLRGYFSQGNQRYFIEPLSPIHRD--GQEHALF 157
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
417-489 1.19e-36

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.19e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14423640   417 EMGEDCDCGTSEECT-NICCDAKTCKIKAGFQCTSGECCEKCQFKKAGMVCRPAKDECDLPEMCDGKSGNCPDD 489
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 204-398 3.07e-94

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: 291.83  E-value: 3.07e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 204 KYIEYYLVLDNGEFKKYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDEDKINITPNASFTLENFSKWRGSV 283
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 284 LPRRKRHDIAQLITATEFAGMTVGLAFMSTMCSPYHSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDNYSCKCPSTICV 363
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 14423640 364 MDKALSfYIPTDFSSCSRVSYDKFFEDKLSNCLFN 398
Cdd:cd04269 161 MAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 204-400 3.74e-84

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: 265.70  E-value: 3.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   204 KYIEYYLVLDNGEFKKYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDEDKINITPNASFTLENFSKWRGSV 283
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   284 LPRRKRHDIAQLITATEFAGMTVGLAFMSTMCSPYHSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHD--NYSCKC-PST 360
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 14423640   361 ICVMDKALSFYIPTDFSSCSRVSYDKFFEDKLSNCLFNAP 400
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
493-621 2.23e-45

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 159.06  E-value: 2.23e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640    493 ANGFPCHHGKGYCLMGACPTLQEQCTELWGPGTKVADQSCYNR-NEGGSKYGYCRRVDDTLIPCKTNDTMCGKLFCQGGS 571
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 14423640    572 dNLPWKGRIVTF-------LTCKTFD-PEDTSEEIGMVANGTKCGHNKVCINAECVDI 621
Cdd:smart00608  81 -ELPLLGEHATViysniggLVCWSLDyHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 30-157 1.57e-39

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: 142.07  E-value: 1.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640    30 EVVYPIRLHP-LHKREVKEPEQQEQfetELKYKMTVNGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYY 108
Cdd:pfam01562   1 EVVIPVRLDPsRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14423640   109 QGHIINEKDSDASISTCRGLRGYFSQGNQRYFIEPLSPIHRD--GQEHALF 157
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
417-489 1.19e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.19e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14423640   417 EMGEDCDCGTSEECT-NICCDAKTCKIKAGFQCTSGECCEKCQFKKAGMVCRPAKDECDLPEMCDGKSGNCPDD 489
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 417-491 4.54e-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: 4.54e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14423640    417 EMGEDCDCGTSEECTNICCDAKTCKIKAGFQCTSGECCEKCQFKKAGMVCRPAKDECDLPEMCDGKSGNCPDDRF 491
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 494-590 1.03e-25

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: 101.92  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   494 NGFPCHHGKGYCLMGACPTLQEQCTELWGPGTKVADQSCYNR-NEGGSKYGYCRRVDDTLIPCKTNDTMCGKLFCQGGSD 572
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 14423640   573 nLPWKGRIVTFL-------TCKTFD 590
Cdd:pfam08516  81 -LPLLGEHATVIytningvTCWGTD 104
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 204-398 3.07e-94

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: 291.83  E-value: 3.07e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 204 KYIEYYLVLDNGEFKKYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDEDKINITPNASFTLENFSKWRGSV 283
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 284 LPRRKRHDIAQLITATEFAGMTVGLAFMSTMCSPYHSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDNYSCKCPSTICV 363
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 14423640 364 MDKALSfYIPTDFSSCSRVSYDKFFEDKLSNCLFN 398
Cdd:cd04269 161 MAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 204-400 3.74e-84

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: 265.70  E-value: 3.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   204 KYIEYYLVLDNGEFKKYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDEDKINITPNASFTLENFSKWRGSV 283
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   284 LPRRKRHDIAQLITATEFAGMTVGLAFMSTMCSPYHSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHD--NYSCKC-PST 360
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 14423640   361 ICVMDKALSFYIPTDFSSCSRVSYDKFFEDKLSNCLFNAP 400
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
493-621 2.23e-45

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 159.06  E-value: 2.23e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640    493 ANGFPCHHGKGYCLMGACPTLQEQCTELWGPGTKVADQSCYNR-NEGGSKYGYCRRVDDTLIPCKTNDTMCGKLFCQGGS 571
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 14423640    572 dNLPWKGRIVTF-------LTCKTFD-PEDTSEEIGMVANGTKCGHNKVCINAECVDI 621
Cdd:smart00608  81 -ELPLLGEHATViysniggLVCWSLDyHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 204-389 8.29e-42

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: 151.03  E-value: 8.29e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 204 KYIEYYLVLDNGEFKKYNENQDEIRKRVFEMANYVNMLYKK----LNTHVALVGMEIWTDEDKI-NITPNASFTLENFSK 278
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQILKGEQFApPIDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 279 WRGSVLPRrkrHDIAQLITATEFAGM-TVGLAFMSTMCSPYHSVGVVQDHSDNLLrVAGTMAHEMGHNFGMFHD-NYSCK 356
Cdd:cd04267  81 WRAEGPIR---HDNAVLLTAQDFIEGdILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDgGDELA 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 14423640 357 CP---STICVMDKALSFYIPTDFSSCSRVSYDKFFE 389
Cdd:cd04267 157 FEcdgGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 30-157 1.57e-39

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: 142.07  E-value: 1.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640    30 EVVYPIRLHP-LHKREVKEPEQQEQfetELKYKMTVNGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYY 108
Cdd:pfam01562   1 EVVIPVRLDPsRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14423640   109 QGHIINEKDSDASISTCRGLRGYFSQGNQRYFIEPLSPIHRD--GQEHALF 157
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
417-489 1.19e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.19e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14423640   417 EMGEDCDCGTSEECT-NICCDAKTCKIKAGFQCTSGECCEKCQFKKAGMVCRPAKDECDLPEMCDGKSGNCPDD 489
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 417-491 4.54e-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: 4.54e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14423640    417 EMGEDCDCGTSEECTNICCDAKTCKIKAGFQCTSGECCEKCQFKKAGMVCRPAKDECDLPEMCDGKSGNCPDDRF 491
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 204-397 1.69e-32

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: 125.04  E-value: 1.69e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 204 KYIEYYLVLDNGEFKKYNEnqDEIRKRVFEMANYVNMLYK------KLNthVALVGMEIWTDEDK-INITPNASFTLENF 276
Cdd:cd04273   1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdpslgnSIN--IVVVRLIVLEDEESgLLISGNAQKSLKSF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 277 SKWRGSVLPRR----KRHDIAQLITATEFAGM-----TVGLAFMSTMCSPYHSVGVVQDHSdnlLRVAGTMAHEMGHNFG 347
Cdd:cd04273  77 CRWQKKLNPPNdsdpEHHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDTG---LSSAFTIAHELGHVLG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 14423640 348 MFHDNYSCKCPSTI---CVMDKALSFYI-PTDFSSCSRVSYDKFFEDKLSNCLF 397
Cdd:cd04273 154 MPHDGDGNSCGPEGkdgHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 494-590 1.03e-25

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: 101.92  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   494 NGFPCHHGKGYCLMGACPTLQEQCTELWGPGTKVADQSCYNR-NEGGSKYGYCRRVDDTLIPCKTNDTMCGKLFCQGGSD 572
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 14423640   573 nLPWKGRIVTFL-------TCKTFD 590
Cdd:pfam08516  81 -LPLLGEHATVIytningvTCWGTD 104
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 204-387 5.18e-22

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: 93.74  E-value: 5.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 204 KYIEYYLVLDNGEFKkynenQDEIRKRVFEMANYVnmlykklnthvalvgMEIWtdEDKINITpnasFTLENfskwrgsv 283
Cdd:cd00203   1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIA---------------MQIW--RDYLNIR----FVLVG-------- 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 284 lPRRKRHDIAQLITATEFAGMTVGLAFMSTMCSPYHSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDNYSCKCPSTICV 363
Cdd:cd00203  47 -VEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTI 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 14423640 364 MDKALS-----FYI------------PTDFSSCSRVSYDKF 387
Cdd:cd00203 126 DDTLNAedddyYSVmsytkgsfsdgqRKDFSQCDIDQINKL 166
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 236-351 7.57e-16

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 74.33  E-value: 7.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   236 NYVNMLYKK-LNTHVALVGMEIWTDEDKINITPNASFTLENFSKWRGSVLPRRKrHDIAQLITATEFAGmTVGLAFMSTM 314
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYG-YDLGHLFTGRDGGG-GGGIAYVGGV 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 14423640   315 CSPYHSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHD 351
Cdd:pfam13582  86 CNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 228-381 2.80e-14

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 372637  Cd Length: 193  Bit Score: 71.89  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   228 RKRVFEMANYVNMLYKK--LNTHVALVGmeiwtdEDKINITPNAS--------------FTLENFSKWRGSvlprrKRHD 291
Cdd:pfam13574   4 TENLVNVVNRVNQIYEPddININGGLVN------PGEIPATTSASdsgnnycnspttivRRLNFLSQWRGE-----QDYC 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   292 IAQLITATEFAGMTVGLAFMSTMC-----SPYHSVGVVQDHSDNLLRVAGT----MAHEMGHNFGMFHDNYSCKCPSTIC 362
Cdd:pfam13574  73 LAHLVTMGTFSGGELGLAYVGQICqkgasSPKTNTGLSTTTNYGSFNYPTQewdvVAHEVGHNFGATHDCDGSQYASSGC 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 14423640   363 VMDKALSF------YI--------PTDFSSCSR 381
Cdd:pfam13574 153 ERNAATSVcsangsFImnpasksnNDLFSPCSI 185
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
209-377 4.26e-14

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 71.30  E-value: 4.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   209 YLVLDNGEFKKYNenQDEIRKRVFEMANYV-NMLYKKLNTHVALVGMEIWTDED----KINITPNASFTLENF---SKWR 280
Cdd:pfam13688   8 LVAADCSYVAAFG--GDAAQANIINMVNTAsNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFqdfSAWR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   281 GsvlprRKRHDIAQLITATEFAgmTVGLAFMSTMCSPYHSVGVVQDHSDNLLRV-----AGTMAHEMGHNFGMFHD---- 351
Cdd:pfam13688  86 G-----TQNDDLAYLFLMTNCS--GGGLAWLGQLCNSGSAGSVSTRVSGNNVVVstateWQVFAHEIGHNFGAVHDcdss 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 14423640   352 -NYSCkCPSTI--------CVMDKALSFYIpTDFS 377
Cdd:pfam13688 159 tSSQC-CPPSNstcpaggrYIMNPSSSPNS-TDFS 191
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 214-398 2.72e-11

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 63.41  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   214 NGEFKKYNENQDEIRKRVFEMANYVNMLY-KKLNTHVALVGME--IWTDED----KINITPNASFT--LENFSKWRGSvl 284
Cdd:pfam13583  12 DCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSStdsfNADCSGGDLGNwrLATLTSWRDS-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   285 prrKRHDIAQLITATEFAGMTVGLAFMSTMCSPYHsvgvvQDHSDNLLRVAG----TMAHEMGHNFGMFHDNYSCKCPST 360
Cdd:pfam13583  90 ---LNYDLAYLTLMTGPSGQNVGVAWVGALCSSAR-----QNAKASGVARSRdewdIFAHEIGHTFGAVHDCSSQGEGLS 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 14423640   361 ICVMDKALSfyipTDFSSCSRVSYDKFFEDKLSNCLFN 398
Cdd:pfam13583 162 SSTEDGSGQ----TIMSYASTASQTAFSPCTIRNINGN 195
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 223-380 7.85e-11

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 62.82  E-value: 7.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 223 NQDEIRKRVFEMANYVNMLYKK-LNTHVALVGMEI--------WTDEDKINI--TPNASFT--LENFSKWRGSvlprRKR 289
Cdd:cd04271  19 SVEEARRNILNNVNSASQLYESsFNISLGLRNLTIsdascpstAVDSAPWNLpcNSRIDIDdrLSIFSQWRGQ----QPD 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 290 HDIA--QLITATEfAGMTVGLAFMSTMCSPYHSVGVVQDHSDNLLRVAGT-----MAHEMGHNFGMFHD--NYSCK---- 356
Cdd:cd04271  95 DGNAfwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAHEIGHTFGAVHDctSGTCSdgsv 173

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 14423640 357 -----CP--STIC------VMDKALSFYIpTDFSSCS 380
Cdd:cd04271 174 gsqqcCPlsTSTCdangqyIMNPSSSSGI-TEFSPCT 209
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 205-351 3.04e-10

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 60.83  E-value: 3.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 205 YIEYYLVLDNgEFKKYNENQDEIRKRVFEMANYVNMLYKKLNT---HVALVGMEIWTDED-KINITPN------ASFTLE 274
Cdd:cd04272   2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDLKSpriRLLLVGITISKDPDfEPYIHPInygyidAAETLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 275 NFSKWRgsvlpRRKRH----DIAQLITATEFAGM--------TVGLAFMSTMCSPyHSVGVVQDhSDNLLRVAGTMAHEM 342
Cdd:cd04272  81 NFNEYV-----KKKRDyfnpDVVFLVTGLDMSTYsggslqtgTGGYAYVGGACTE-NRVAMGED-TPGSYYGVYTMTHEL 153


                ....*....
gi 14423640 343 GHNFGMFHD 351
Cdd:cd04272 154 AHLLGAPHD 162
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 209-395 1.45e-04

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 44.29  E-value: 1.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 209 YLVLDNGEFKKYNENQDEIR-KRVFEMANYVNMLYKKLNTHVALV-GMEIWTDEDKINITPNASFTLENF---------- 276
Cdd:cd04270   6 LLVADHRFYKYMGRGEEETTiNYLISHIDRVDDIYRNTDWDGGGFkGIGFQIKRIRIHTTPDEVDPGNKFynksfpnwgv 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640 277 SKWRGSVLPRRKRHD--IAQLITATEFAGMTVGLAFMST--------MCSP--YHSVGV----------VQDHSDNLL-R 333
Cdd:cd04270  86 EKFLVKLLLEQFSDDvcLAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKayYYSNGKkkylntglttTVNYGKRVPtK 165

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14423640 334 VAG-TMAHEMGHNFGMFHDNYSCKCPSTICVMDKALSFYIPTD--------FSSCSRVSYDKFFEDKLSNC 395
Cdd:cd04270 166 ESDlVTAHELGHNFGSPHDPDIAECAPGESQGGNYIMYARATSgdkennkkFSPCSKKSISKVLEVKSNSC 236
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 528-619 9.34e-04

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 38.09  E-value: 9.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423640   528 ADQSCynRNEGGSKYGYCRRVDDTlipcktndtMCGKLFCQGGSDNlpwkgrivtflTCKTFdpedtseeIGMVANGTKC 607
Cdd:pfam17771   7 ADEQC--RLIFGPGSTFCPNGDED---------VCSKLWCSNPGGS-----------TCTTK--------NLPAADGTPC 56

                          90
                  ....*....|..
gi 14423640   608 GHNKVCINAECV 619
Cdd:pfam17771  57 GNKKWCLNGKCV 68
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 322-364 2.24e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 39.59  E-value: 2.24e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 14423640 322 GVVQDHSDNLLRVAGTMAHEMGHNFGMFHdnysckCPSTICVM 364
Cdd:cd11375 111 GLPPDEGLFLERLLKEAVHELGHLFGLDH------CPYYACVM 147
 
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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