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Conserved domains on  [gi|767950497|ref|XP_011542673|]
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disintegrin and metalloproteinase domain-containing protein 28 isoform X12 [Homo sapiens]

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein; disintegrin and metalloproteinase domain-containing protein; disintegrin and metalloproteinase domain-containing protein( domain architecture ID 10136397)

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; disintegrin and metalloproteinase domain-containing protein such as snake venom metalloproteinases that impairs hemostasis in envenomed animals; 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; protein containing domains ZnMc_adamalysin_II_like, DISIN, and ACR; disintegrin and metalloproteinase domain-containing protein such as snake venom metalloproteinases that impairs hemostasis in envenomed animals; 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
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 1-144 5.63e-67

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


:

Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 214.40  E-value: 5.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   1 MEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLR 79
Cdd:cd04269   51 LEIWTDKDKISVSGDAGETLNRFLDWKRSNLLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLL 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767950497  80 VAGTMAHEMGHNFGMFHDDYSCKCPSTICVMDKALSfYIPTDFSSCSRLSYDKFFEDKLSNCLFN 144
Cdd:cd04269  131 FAVTMAHELGHNLGMEHDDGGCTCGRSTCIMAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
240-367 2.79e-42

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 147.51  E-value: 2.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   240 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSd 318
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950497   319 NLPWKGRIVTF-------LTCKTFDPEDTSQE-IGMVANGTKCGDNKVCINAECVDI 367
Cdd:smart00608  81 ELPLLGEHATViysniggLVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
163-235 2.05e-32

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.50  E-value: 2.05e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950497  163 EMGEDCDCGTSEECT-NICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDD 235
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 ...
 1-144 5.63e-67

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 214.40  E-value: 5.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   1 MEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLR 79
Cdd:cd04269   51 LEIWTDKDKISVSGDAGETLNRFLDWKRSNLLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLL 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767950497  80 VAGTMAHEMGHNFGMFHDDYSCKCPSTICVMDKALSfYIPTDFSSCSRLSYDKFFEDKLSNCLFN 144
Cdd:cd04269  131 FAVTMAHELGHNLGMEHDDGGCTCGRSTCIMAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 1-146 6.49e-57

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: 188.28  E-value: 6.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497    1 MEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLR 79
Cdd:pfam01421  51 LEIWTDEDKIDVSGDANDTLRNFLKWRQEYLKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLES 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   80 VAGTMAHEMGHNFGMFHDDYS--CKC-PSTICVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAP 146
Cdd:pfam01421 131 FAVTMAHELGHNLGMQHDDFNggCKCpPGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
240-367 2.79e-42

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 147.51  E-value: 2.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   240 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSd 318
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950497   319 NLPWKGRIVTF-------LTCKTFDPEDTSQE-IGMVANGTKCGDNKVCINAECVDI 367
Cdd:smart00608  81 ELPLLGEHATViysniggLVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
163-235 2.05e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.50  E-value: 2.05e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950497  163 EMGEDCDCGTSEECT-NICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDD 235
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 163-237 7.84e-31

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: 114.32  E-value: 7.84e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767950497   163 EMGEDCDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDDRF 237
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 240-336 1.73e-22

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: 91.91  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497  240 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSD 318
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 767950497  319 nLPWKGRIVTFL-------TCKTFD 336
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 ...
 1-144 5.63e-67

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 214.40  E-value: 5.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   1 MEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLR 79
Cdd:cd04269   51 LEIWTDKDKISVSGDAGETLNRFLDWKRSNLLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLL 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767950497  80 VAGTMAHEMGHNFGMFHDDYSCKCPSTICVMDKALSfYIPTDFSSCSRLSYDKFFEDKLSNCLFN 144
Cdd:cd04269  131 FAVTMAHELGHNLGMEHDDGGCTCGRSTCIMAPSPS-SLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 1-146 6.49e-57

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: 188.28  E-value: 6.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497    1 MEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSP-YSVGVVQDHSDNLLR 79
Cdd:pfam01421  51 LEIWTDEDKIDVSGDANDTLRNFLKWRQEYLKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLES 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   80 VAGTMAHEMGHNFGMFHDDYS--CKC-PSTICVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAP 146
Cdd:pfam01421 131 FAVTMAHELGHNLGMQHDDFNggCKCpPGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
240-367 2.79e-42

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 147.51  E-value: 2.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   240 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSd 318
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS- 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767950497   319 NLPWKGRIVTF-------LTCKTFDPEDTSQE-IGMVANGTKCGDNKVCINAECVDI 367
Cdd:smart00608  81 ELPLLGEHATViysniggLVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
163-235 2.05e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 118.50  E-value: 2.05e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950497  163 EMGEDCDCGTSEECT-NICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDD 235
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 163-237 7.84e-31

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: 114.32  E-value: 7.84e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767950497   163 EMGEDCDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDDRF 237
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 1-135 9.93e-31

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: 117.91  E-value: 9.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   1 MEIWTDKDKI-KITPNASFTLENFSKWRGSVlsrRKRHDIAQLITATELA-GTTVGLAFMSTMCSPY-SVGVVQDHSDNL 77
Cdd:cd04267   55 LQILKGEQFApPIDSDASNTLNSFSFWRAEG---PIRHDNAVLLTAQDFIeGDILGLAYVGSMCNPYsSVGVVEDTGFTL 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950497  78 LrVAGTMAHEMGHNFGMFHD-DYSCKCP---STICVMDKALSFYIPTDFSSCSRLSYDKFFE 135
Cdd:cd04267  132 L-TALTMAHELGHNLGAEHDgGDELAFEcdgGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 1-143 8.78e-26

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: 104.63  E-value: 8.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   1 MEIWTDKDK-IKITPNASFTLENFSKWRGSVLSRR----KRHDIAQLITATELAG-----TTVGLAFMSTMCSPY-SVGV 69
Cdd:cd04273   53 LIVLEDEESgLLISGNAQKSLKSFCRWQKKLNPPNdsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSrSCSI 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950497  70 VQDHSdnlLRVAGTMAHEMGHNFGMFHDDYSCKCPSTI---CVMDKALSFYI-PTDFSSCSRLSYDKFFEDKLSNCLF 143
Cdd:cd04273  133 NEDTG---LSSAFTIAHELGHVLGMPHDGDGNSCGPEGkdgHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 240-336 1.73e-22

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: 91.91  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497  240 NGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNR-NEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSD 318
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 767950497  319 nLPWKGRIVTFL-------TCKTFD 336
Cdd:pfam08516  81 -LPLLGEHATVIytningvTCWGTD 104
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 1-133 5.04e-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: 84.50  E-value: 5.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   1 MEIWTDKDKIKITPnasftlenfskwrgsVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSPY-SVGVVQDHSDNLLR 79
Cdd:cd00203   31 MQIWRDYLNIRFVL---------------VGVEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLrGVGVLQDNQSGTKE 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950497  80 VAGTMAHEMGHNFGMFHDDYSCKCPSTICVMDKALS-----FYI------------PTDFSSCSRLSYDKF 133
Cdd:cd00203   96 GAQTIAHELGHALGFYHDHDRKDRDDYPTIDDTLNAedddyYSVmsytkgsfsdgqRKDFSQCDIDQINKL 166
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 2-97 3.99e-10

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: 57.38  E-value: 3.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497    2 EIWTDKDKIKITPNASFTLENFSkwrgSVLSRRKRH---DIAQLITATElAGTTVGLAFMSTMCSP-YSVGVVQDHSDNL 77
Cdd:pfam13582  28 IITTSADTPYTSSDALEILDELQ----EVNDTRIGQygyDLGHLFTGRD-GGGGGGIAYVGGVCNSgSKFGVNSGSGPVG 102

                          90       100
                  ....*....|....*....|
gi 767950497   78 LRVAGTMAHEMGHNFGMFHD 97
Cdd:pfam13582 103 DTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
13-123 2.83e-09

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 56.66  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   13 TPNASFTLENF---SKWRGsvlsrRKRHDIAQLITATELAGTtvGLAFMSTMCSPYSVG-VVQDHSDNLLRV-----AGT 83
Cdd:pfam13688  68 TGDSSDRLSEFqdfSAWRG-----TQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGsVSTRVSGNNVVVstateWQV 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767950497   84 MAHEMGHNFGMFHD------DYSC-----KCPSTI-CVMDKALSFYIpTDFS 123
Cdd:pfam13688 141 FAHEIGHNFGAVHDcdsstsSQCCppsnsTCPAGGrYIMNPSSSPNS-TDFS 191
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 8-127 4.50e-09

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: 56.10  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497    8 DKIKITPNAS--------------FTLENFSKWRGSvlsrrKRHDIAQLITATELAGTTVGLAFMSTMC-----SPYSVG 68
Cdd:pfam13574  33 GEIPATTSASdsgnnycnspttivRRLNFLSQWRGE-----QDYCLAHLVTMGTFSGGELGLAYVGQICqkgasSPKTNT 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950497   69 VVQDHSDNLLRVAGT-----MAHEMGHNFGMFHDDYSCKCPSTICVMDKALSF------YI--------PTDFSSCSR 127
Cdd:pfam13574 108 GLSTTTNYGSFNYPTqewdvVAHEVGHNFGATHDCDGSQYASSGCERNAATSVcsangsFImnpasksnNDLFSPCSI 185
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 19-97 8.97e-07

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 50.04  E-value: 8.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497  19 TLENFSKWrgsvlSRRKRH----DIAQLITATELAGT--------TVGLAFMSTMCSPYSVGVVQDhSDNLLRVAGTMAH 86
Cdd:cd04272   78 TLENFNEY-----VKKKRDyfnpDVVFLVTGLDMSTYsggslqtgTGGYAYVGGACTENRVAMGED-TPGSYYGVYTMTH 151

                         90
                 ....*....|.
gi 767950497  87 EMGHNFGMFHD 97
Cdd:cd04272  152 ELAHLLGAPHD 162
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 20-126 1.18e-06

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: 49.73  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497  20 LENFSKWRGSvlsrRKRHDIA--QLITATElAGTTVGLAFMSTMCSPYSVGVVQDHSDNLLRVAGT------MAHEMGHN 91
Cdd:cd04271   82 LSIFSQWRGQ----QPDDGNAfwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTsnewqvFAHEIGHT 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767950497  92 FGMFHD--DYSCK---------CP--STIC------VMDKALSFYIpTDFSSCS 126
Cdd:cd04271  157 FGAVHDctSGTCSdgsvgsqqcCPlsTSTCdangqyIMNPSSSSGI-TEFSPCT 209
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 20-106 2.45e-06

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: 48.38  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497   20 LENFSKWRGSvlsrrKRHDIAQLITATELAGTTVGLAFMSTMCSPYSvgvvQDHSDNLLRVAG----TMAHEMGHNFGMF 95
Cdd:pfam13583  80 LATLTSWRDS-----LNYDLAYLTLMTGPSGQNVGVAWVGALCSSAR----QNAKASGVARSRdewdIFAHEIGHTFGAV 150

                          90
                  ....*....|.
gi 767950497   96 HDDYSCKCPST 106
Cdd:pfam13583 151 HDCSSQGEGLS 161
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 64-110 6.90e-04

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: 6.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 767950497  64 PYSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHddysckCPSTICVM 110
Cdd:cd11375  107 PEFYGLPPDEGLFLERLLKEAVHELGHLFGLDH------CPYYACVM 147
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 39-141 2.70e-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: 39.66  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497  39 IAQLITATELAGTTVGLAFMST--------MCSP---YSVGV----------VQDHSDNLL-RVAG-TMAHEMGHNFGMF 95
Cdd:cd04270  103 LAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKayyYSNGKkkylntglttTVNYGKRVPtKESDlVTAHELGHNFGSP 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767950497  96 HDDYSCKCPSTICVMDKALSFYIPTD--------FSSCSRLSYDKFFEDKLSNC 141
Cdd:cd04270  183 HDPDIAECAPGESQGGNYIMYARATSgdkennkkFSPCSKKSISKVLEVKSNSC 236
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 285-365 8.40e-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: 35.01  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950497  285 GSKYGYCRRVDDTlipckandtMCGKLFCQGGSDNlpwkgrivtflTCKTFdpedtsqeIGMVANGTKCGDNKVCINAEC 364
Cdd:pfam17771  16 GPGSTFCPNGDED---------VCSKLWCSNPGGS-----------TCTTK--------NLPAADGTPCGNKKWCLNGKC 67


                  .
gi 767950497  365 V 365
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.
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