NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|578815157|ref|XP_006716337|]
View 

disintegrin and metalloproteinase domain-containing protein 28 isoform X6 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 204-397 2.94e-92

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: 285.66  E-value: 2.94e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 204 KYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSV 283
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 284 LSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTICV 362
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578815157 363 MDKALSfYIPTDFSSCSRLSYDKFFEDKLSNCLFN 397
Cdd:cd04269  161 MAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
493-620 1.58e-42

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 150.59  E-value: 1.58e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157   493 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSd 571
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578815157   572 NLPWKGRIVTF-------LTCKTFDPEDTSQE-IGMVANGTKCGDNKVCINAECVDI 620
Cdd:smart00608  81 ELPLLGEHATViysniggLVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 29-156 9.34e-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: 139.76  E-value: 9.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157   29 EVVYPIRLHP-LHKREAKEPEQQEQfetELKYKMTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYY 107
Cdd:pfam01562   1 EVVIPVRLDPsRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578815157  108 QGHILNEKVSDASISTCRGLRGYFSQGDQRYFIEPLSPIHRD--GQEHALF 156
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
416-488 1.07e-33

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 123.51  E-value: 1.07e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578815157  416 EMGEDCDCGTSEECT-NICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDD 488
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 ...
 204-397 2.94e-92

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: 285.66  E-value: 2.94e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 204 KYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSV 283
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 284 LSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTICV 362
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578815157 363 MDKALSfYIPTDFSSCSRLSYDKFFEDKLSNCLFN 397
Cdd:cd04269  161 MAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 204-399 1.88e-82

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: 260.31  E-value: 1.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  204 KYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSV 283
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  284 LSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYS--CKC-PST 359
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578815157  360 ICVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAP 399
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
493-620 1.58e-42

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 150.59  E-value: 1.58e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157   493 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSd 571
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578815157   572 NLPWKGRIVTF-------LTCKTFDPEDTSQE-IGMVANGTKCGDNKVCINAECVDI 620
Cdd:smart00608  81 ELPLLGEHATViysniggLVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 29-156 9.34e-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: 139.76  E-value: 9.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157   29 EVVYPIRLHP-LHKREAKEPEQQEQfetELKYKMTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYY 107
Cdd:pfam01562   1 EVVIPVRLDPsRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578815157  108 QGHILNEKVSDASISTCRGLRGYFSQGDQRYFIEPLSPIHRD--GQEHALF 156
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
416-488 1.07e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 123.51  E-value: 1.07e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578815157  416 EMGEDCDCGTSEECT-NICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDD 488
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 416-490 5.88e-32

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: 118.56  E-value: 5.88e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578815157   416 EMGEDCDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDDRF 490
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 493-589 8.21e-23

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: 93.45  E-value: 8.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  493 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSD 571
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 578815157  572 nLPWKGRIVTFL-------TCKTFD 589
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 ...
 204-397 2.94e-92

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: 285.66  E-value: 2.94e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 204 KYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSV 283
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 284 LSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTICV 362
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578815157 363 MDKALSfYIPTDFSSCSRLSYDKFFEDKLSNCLFN 397
Cdd:cd04269  161 MAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 204-399 1.88e-82

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: 260.31  E-value: 1.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  204 KYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSV 283
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  284 LSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYS--CKC-PST 359
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578815157  360 ICVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAP 399
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
493-620 1.58e-42

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 150.59  E-value: 1.58e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157   493 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSd 571
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578815157   572 NLPWKGRIVTF-------LTCKTFDPEDTSQE-IGMVANGTKCGDNKVCINAECVDI 620
Cdd:smart00608  81 ELPLLGEHATViysniggLVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 29-156 9.34e-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: 139.76  E-value: 9.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157   29 EVVYPIRLHP-LHKREAKEPEQQEQfetELKYKMTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYY 107
Cdd:pfam01562   1 EVVIPVRLDPsRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578815157  108 QGHILNEKVSDASISTCRGLRGYFSQGDQRYFIEPLSPIHRD--GQEHALF 156
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREegGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 204-388 7.33e-38

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: 139.48  E-value: 7.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 204 KYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKK----LNTHVALVGMEIWTDKDKI-KITPNASFTLENFSK 278
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQILKGEQFApPIDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 279 WRGSVlsrRKRHDIAQLITATELA-GTTVGLAFMSTMCSPY-SVGVVQDHSDNLLrVAGTMAHEMGHNFGMFHD-DYSCK 355
Cdd:cd04267   81 WRAEG---PIRHDNAVLLTAQDFIeGDILGLAYVGSMCNPYsSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDgGDELA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 578815157 356 CP---STICVMDKALSFYIPTDFSSCSRLSYDKFFE 388
Cdd:cd04267  157 FEcdgGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Disintegrin pfam00200
Disintegrin;
416-488 1.07e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 123.51  E-value: 1.07e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578815157  416 EMGEDCDCGTSEECT-NICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDD 488
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 416-490 5.88e-32

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: 118.56  E-value: 5.88e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578815157   416 EMGEDCDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDDRF 490
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 204-396 9.03e-29

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: 114.26  E-value: 9.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 204 KYIEYYLVLDNGEFKRYNEnqDEIRKRVFEMANYVNMLYK------KLNthVALVGMEIWTDKDK-IKITPNASFTLENF 276
Cdd:cd04273    1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYKdpslgnSIN--IVVVRLIVLEDEESgLLISGNAQKSLKSF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 277 SKWRGSVLSRR----KRHDIAQLITATELAG-----TTVGLAFMSTMCSPY-SVGVVQDHSdnlLRVAGTMAHEMGHNFG 346
Cdd:cd04273   77 CRWQKKLNPPNdsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSrSCSINEDTG---LSSAFTIAHELGHVLG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578815157 347 MFHDDYSCKCPSTI---CVMDKALSFYI-PTDFSSCSRLSYDKFFEDKLSNCLF 396
Cdd:cd04273  154 MPHDGDGNSCGPEGkdgHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 493-589 8.21e-23

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: 93.45  E-value: 8.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  493 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSD 571
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 578815157  572 nLPWKGRIVTFL-------TCKTFD 589
Cdd:pfam08516  81 -LPLLGEHATVIytningvTCWGTD 104
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 204-386 3.40e-19

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: 85.27  E-value: 3.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 204 KYIEYYLVLDNGEFKrynenQDEIRKRVFEMANYVnmlykklnthvalvgMEIWTDKDKIKITPnasftlenfskwrgsV 283
Cdd:cd00203    1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIA---------------MQIWRDYLNIRFVL---------------V 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 284 LSRRKRHDIAQLITATELAGTTVGLAFMSTMCSPY-SVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTICV 362
Cdd:cd00203   46 GVEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLrGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTI 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578815157 363 MDKALS-----FYI------------PTDFSSCSRLSYDKF 386
Cdd:cd00203  126 DDTLNAedddyYSVmsytkgsfsdgqRKDFSQCDIDQINKL 166
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 236-350 1.86e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 70.48  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  236 NYVNMLYKK-LNTHVALVGMEIWTDKDKIKITPNASFTLENFSkwrgSVLSRRKRH---DIAQLITATElAGTTVGLAFM 311
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQ----EVNDTRIGQygyDLGHLFTGRD-GGGGGGIAYV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 578815157  312 STMCSP-YSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHD 350
Cdd:pfam13582  83 GGVCNSgSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
209-376 1.17e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 67.06  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  209 YLVLDNGEFKRYNenQDEIRKRVFEMANYV-NMLYKKLNTHVALVGMEIWTDKD----KIKITPNASFTLENF---SKWR 280
Cdd:pfam13688   8 LVAADCSYVAAFG--GDAAQANIINMVNTAsNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFqdfSAWR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  281 GsvlsrRKRHDIAQLITATELAGTtvGLAFMSTMCSPYSVG-VVQDHSDNLLRV-----AGTMAHEMGHNFGMFHD---- 350
Cdd:pfam13688  86 G-----TQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGsVSTRVSGNNVVVstateWQVFAHEIGHNFGAVHDcdss 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 578815157  351 --DYSC-----KCPSTI-CVMDKALSFYIpTDFS 376
Cdd:pfam13688 159 tsSQCCppsnsTCPAGGrYIMNPSSSPNS-TDFS 191
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 205-350 1.51e-11

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 64.68  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 205 YIEYYLVLDNGEFKRYNENQDEIRkRVFEMANYVNMLYKKLNT---HVALVGMEIWTDKD-KIKITPN------ASFTLE 274
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSNEQLIR-YLAVMVNAANLRYRDLKSpriRLLLVGITISKDPDfEPYIHPInygyidAAETLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 275 NFSKWrgsvlSRRKRH----DIAQLITATELAGT--------TVGLAFMSTMCSPYSVGVVQDhSDNLLRVAGTMAHEMG 342
Cdd:cd04272   81 NFNEY-----VKKKRDyfnpDVVFLVTGLDMSTYsggslqtgTGGYAYVGGACTENRVAMGED-TPGSYYGVYTMTHELA 154


                 ....*...
gi 578815157 343 HNFGMFHD 350
Cdd:cd04272  155 HLLGAPHD 162
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 228-380 1.56e-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: 372637  Cd Length: 193  Bit Score: 63.80  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  228 RKRVFEMANYVNMLYKK--LNTHVALVGMeiwtdkDKIKITPNAS--------------FTLENFSKWRGSvlsrrKRHD 291
Cdd:pfam13574   4 TENLVNVVNRVNQIYEPddININGGLVNP------GEIPATTSASdsgnnycnspttivRRLNFLSQWRGE-----QDYC 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  292 IAQLITATELAGTTVGLAFMSTMC-----SPYSVGVVQDHSDNLLRVAGT-----MAHEMGHNFGMFHDDYSCKCPSTIC 361
Cdd:pfam13574  73 LAHLVTMGTFSGGELGLAYVGQICqkgasSPKTNTGLSTTTNYGSFNYPTqewdvVAHEVGHNFGATHDCDGSQYASSGC 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 578815157  362 VMDKALSF------YI--------PTDFSSCSR 380
Cdd:pfam13574 153 ERNAATSVcsangsFImnpasksnNDLFSPCSI 185
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 214-359 3.83e-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: 63.02  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  214 NGEFKRYNENQDEIRKRVFEMANYVNMLY-KKLNTHVALVGME--IWTDKD----KIKITPNASFT--LENFSKWRGSvl 284
Cdd:pfam13583  12 DCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSStdsfNADCSGGDLGNwrLATLTSWRDS-- 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578815157  285 srrKRHDIAQLITATELAGTTVGLAFMSTMCSPYSvgvvQDHSDNLLRVAG----TMAHEMGHNFGMFHDDYSCKCPST 359
Cdd:pfam13583  90 ---LNYDLAYLTLMTGPSGQNVGVAWVGALCSSAR----QNAKASGVARSRdewdIFAHEIGHTFGAVHDCSSQGEGLS 161
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 218-379 4.05e-09

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: 57.43  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 218 KRYNeNQDEIRKRVFEMANYVNMLYKK-LNTHVALVGMEIwTDKD-----------KIKITPNASFT--LENFSKWRGSv 283
Cdd:cd04271   15 KSFG-SVEEARRNILNNVNSASQLYESsFNISLGLRNLTI-SDAScpstavdsapwNLPCNSRIDIDdrLSIFSQWRGQ- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 284 lsrRKRHDIA--QLITATElAGTTVGLAFMSTMCSPysvgvvqDHSD-NLLRVAGT------------MAHEMGHNFGMF 348
Cdd:cd04271   92 ---QPDDGNAfwTLMTACP-SGSEVGVAWLGQLCRT-------GASDqGNETVAGTnvvvrtsnewqvFAHEIGHTFGAV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 578815157 349 HD--DYSCK---------CP--STIC------VMDKALSFYIpTDFSSCS 379
Cdd:cd04271  161 HDctSGTCSdgsvgsqqcCPlsTSTCdangqyIMNPSSSSGI-TEFSPCT 209
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 317-363 1.05e-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: 40.74  E-value: 1.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 578815157 317 PYSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHddysckCPSTICVM 363
Cdd:cd11375  107 PEFYGLPPDEGLFLERLLKEAVHELGHLFGLDH------CPYYACVM 147
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 209-394 1.65e-03

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: 40.82  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 209 YLVLDNGEFKRYNENQDEIR-KRVFEMANYVNMLYKKLNTHVALV-GMEIWTDKDKIKITPNASFTLENF---------- 276
Cdd:cd04270    6 LLVADHRFYKYMGRGEEETTiNYLISHIDRVDDIYRNTDWDGGGFkGIGFQIKRIRIHTTPDEVDPGNKFynksfpnwgv 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157 277 SKWRgSVLSRRKRHD---IAQLITATELAGTTVGLAFMST--------MCSP---YSVGV----------VQDHSDNLL- 331
Cdd:cd04270   86 EKFL-VKLLLEQFSDdvcLAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKayyYSNGKkkylntglttTVNYGKRVPt 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578815157 332 RVAG-TMAHEMGHNFGMFHDDYSCKCPSTICVMDKALSFYIPTD--------FSSCSRLSYDKFFEDKLSNC 394
Cdd:cd04270  165 KESDlVTAHELGHNFGSPHDPDIAECAPGESQGGNYIMYARATSgdkennkkFSPCSKKSISKVLEVKSNSC 236
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 538-618 3.75e-03

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: 36.55  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578815157  538 GSKYGYCRRVDDTlipckandtMCGKLFCQGGSDNlpwkgrivtflTCKTFdpedtsqeIGMVANGTKCGDNKVCINAEC 617
Cdd:pfam17771  16 GPGSTFCPNGDED---------VCSKLWCSNPGGS-----------TCTTK--------NLPAADGTPCGNKKWCLNGKC 67


                  .
gi 578815157  618 V 618
Cdd:pfam17771  68 V 68
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH