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Conserved domains on  [gi|12053591|emb|CAC20585|]
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meltrin-beta/ADAM 19 homologue [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 210-408 2.46e-86

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: 274.18  E-value: 2.46e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   210 KYVELYLVADYLEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHD--SADCCSASAa 366
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 12053591   367 dGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCLSNMP 408
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
501-646 4.85e-52

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 178.32  E-value: 4.85e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591    501 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNMRDAKCGKIQCQSS 580
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12053591    581 EARP-LESNAVPIDTTIimngRQIQCRGTHVYRGPEEegdmlDPGLVMTGTKCGYNHICFEGQCRNT 646
Cdd:smart00608  80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP-----DIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-162 2.06e-29

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: 113.56  E-value: 2.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591    44 ELIIPQW-----KTSESPVREKHPLKAELRVMAEGRELILDLEKNEQLFAPSYTETHYTSSGNPQTTTRKLEDHCFYHGT 118
Cdd:pfam01562   1 EVVIPVRldpsrRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 12053591   119 VRETELSSVTLSTCRGIRGLITVSSNlSYVIEPL-----PDSKGQHLIY 162
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLekysrEEGGHPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 439-499 3.78e-28

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: 108.16  E-value: 3.78e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12053591    439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTNFY 499
Cdd:smart00050  15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 210-408 2.46e-86

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: 274.18  E-value: 2.46e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   210 KYVELYLVADYLEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHD--SADCCSASAa 366
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 12053591   367 dGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCLSNMP 408
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 210-406 9.29e-84

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: 267.17  E-value: 9.29e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 210 KYVELYLVADYLEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHDSADC-CSASaad 367
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtCGRS--- 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 12053591 368 gGCIMAAATGHPfPKVFNGCNRRELDRYLQSGGGMCLSN 406
Cdd:cd04269 158 -TCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
501-646 4.85e-52

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 178.32  E-value: 4.85e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591    501 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNMRDAKCGKIQCQSS 580
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12053591    581 EARP-LESNAVPIDTTIimngRQIQCRGTHVYRGPEEegdmlDPGLVMTGTKCGYNHICFEGQCRNT 646
Cdd:smart00608  80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP-----DIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 502-610 8.85e-42

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: 148.15  E-value: 8.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   502 DGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNMRDAKCGKIQCQSSE 581
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRT-NGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 12053591   582 ARP-LESNAVPIDTTIimngRQIQCRGTHV 610
Cdd:pfam08516  80 ELPlLGEHATVIYTNI----NGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-162 2.06e-29

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: 113.56  E-value: 2.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591    44 ELIIPQW-----KTSESPVREKHPLKAELRVMAEGRELILDLEKNEQLFAPSYTETHYTSSGNPQTTTRKLEDHCFYHGT 118
Cdd:pfam01562   1 EVVIPVRldpsrRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 12053591   119 VRETELSSVTLSTCRGIRGLITVSSNlSYVIEPL-----PDSKGQHLIY 162
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLekysrEEGGHPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 439-499 3.78e-28

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: 108.16  E-value: 3.78e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12053591    439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTNFY 499
Cdd:smart00050  15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
439-497 1.30e-26

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 103.47  E-value: 1.30e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 12053591   439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTN 497
Cdd:pfam00200  16 NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 289-384 3.57e-03

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 40.92  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591  289 LLAQKYHDNAQLITGMSFHGTTIGLAplmAMCSVYQSGGVNMDhsENAIGVAATMAHEMGHNFGMTHDSADccSASAADG 368
Cdd:NF038115 129 NAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVT--LDLYVATQTLAHELGHLFGLYNGHAE--SAECSEG 201

                         90
                 ....*....|....*..
gi 12053591  369 G-CIMAAATGHPFPKVF 384
Cdd:NF038115 202 GyRLMCGSLAENFENLF 218
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 210-408 2.46e-86

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: 274.18  E-value: 2.46e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   210 KYVELYLVADYLEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHD--SADCCSASAa 366
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPPG- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 12053591   367 dGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCLSNMP 408
Cdd:pfam01421 160 -GGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 210-406 9.29e-84

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: 267.17  E-value: 9.29e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 210 KYVELYLVADYLEFQKNRRDQDATKHKLIEIANYVDKFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRK- 288
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 289 LLAQKYHDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHDSADC-CSASaad 367
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtCGRS--- 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 12053591 368 gGCIMAAATGHPfPKVFNGCNRRELDRYLQSGGGMCLSN 406
Cdd:cd04269 158 -TCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
501-646 4.85e-52

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 178.32  E-value: 4.85e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591    501 MDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNMRDAKCGKIQCQSS 580
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12053591    581 EARP-LESNAVPIDTTIimngRQIQCRGTHVYRGPEEegdmlDPGLVMTGTKCGYNHICFEGQCRNT 646
Cdd:smart00608  80 SELPlLGEHATVIYSNI----GGLVCWSLDYHLGTDP-----DIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 502-610 8.85e-42

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: 148.15  E-value: 8.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   502 DGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPAPDLCFEKVNVAGDTFGNCGKDmNGEHRKCNMRDAKCGKIQCQSSE 581
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRT-NGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 12053591   582 ARP-LESNAVPIDTTIimngRQIQCRGTHV 610
Cdd:pfam08516  80 ELPlLGEHATVIYTNI----NGVTCWGTDY 105
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 210-389 2.11e-33

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: 127.54  E-value: 2.11e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 210 KYVELYLVADYLEFQKNRRDQDATKHKLIEIANYVDKFYRS----LNIRIALVGLEVWtHGNmCEVSENPYS---TLWSF 282
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlrLGIRISLEGLQIL-KGE-QFAPPIDSDasnTLNSF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 283 LSWRRKLLAQkyHDNAQLITGMSFH-GTTIGLAPLMAMCSVYQSGGVNMDHSENAIgVAATMAHEMGHNFGMTHDSADCC 361
Cdd:cd04267  79 SFWRAEGPIR--HDNAVLLTAQDFIeGDILGLAYVGSMCNPYSSVGVVEDTGFTLL-TALTMAHELGHNLGAEHDGGDEL 155

                       170       180
                ....*....|....*....|....*....
gi 12053591 362 SASA-ADGGCIMAAATGHPFPKVFNGCNR 389
Cdd:cd04267 156 AFECdGGGNYIMAPVDSGLNSYRFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 210-404 9.94e-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: 123.12  E-value: 9.94e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 210 KYVELYLVADYLEFQKNRRDQdaTKHKLIEIANYVDKFYR--SL--NIRIALVGLEVWTHGN-MCEVSENPYSTLWSFLS 284
Cdd:cd04273   1 RYVETLVVADSKMVEFHHGED--LEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEDEEsGLLISGNAQKSLKSFCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 285 WRRKLLAQ-----KYHDNAQLITGMSFHG-----TTIGLAPLMAMCSVYQSGGVNMDhseNAIGVAATMAHEMGHNFGMT 354
Cdd:cd04273  79 WQKKLNPPndsdpEHHDHAILLTRQDICRsngncDTLGLAPVGGMCSPSRSCSINED---TGLSSAFTIAHELGHVLGMP 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 12053591 355 HD-SADCCSASAADgGCIMAAATGHPF-PKVFNGCNRRELDRYLQSGGGMCL 404
Cdd:cd04273 156 HDgDGNSCGPEGKD-GHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCL 206
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-162 2.06e-29

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: 113.56  E-value: 2.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591    44 ELIIPQW-----KTSESPVREKHPLKAELRVMAEGRELILDLEKNEQLFAPSYTETHYTSSGNPQTTTRKLEDHCFYHGT 118
Cdd:pfam01562   1 EVVIPVRldpsrRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 12053591   119 VRETELSSVTLSTCRGIRGLITVSSNlSYVIEPL-----PDSKGQHLIY 162
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENE-EYLIEPLekysrEEGGHPHVVY 128
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 439-499 3.78e-28

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: 108.16  E-value: 3.78e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12053591    439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTNFY 499
Cdd:smart00050  15 TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
439-497 1.30e-26

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 103.47  E-value: 1.30e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 12053591   439 NNPCCNASNCTLRPGAECAHGSCCHQCKLLAPGTLCREQARQCDLPEFCTGKSPHCPTN 497
Cdd:pfam00200  16 NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
212-378 8.46e-19

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 85.16  E-value: 8.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   212 VELYLVADYlEFQKNRrDQDATKHKLIEIANYVD-KFYRSLNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLS---WRR 287
Cdd:pfam13688   5 VALLVAADC-SYVAAF-GGDAAQANIINMVNTASnVYERDFNISLGLVNLTISDSTCPYTPPACSTGDSSDRLSefqDFS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   288 KLLAQKYHDNAQLITGMSFHGTtiGLAPLMAMCSVYQSGGVNMDHSENAIGVAA-----TMAHEMGHNFGMTHDSA---- 358
Cdd:pfam13688  83 AWRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCDssts 160

                         170       180
                  ....*....|....*....|....*
gi 12053591   359 -DCCSASA----ADGGCIMAAATGH 378
Cdd:pfam13688 161 sQCCPPSNstcpAGGRYIMNPSSSP 185
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 210-395 1.21e-17

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: 81.41  E-value: 1.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 210 KYVELYLVADylefqKNRRDQDATKHKLIEIANYVDKFYRS-LNIRIALVGLEVWTHgnmcevsenpystlwsflswrrk 288
Cdd:cd00203   1 KVIPYVVVAD-----DRDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEIDKA----------------------- 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 289 llaqkyhDNAQLITGMSFHGTTIGLAPLMAMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHDSADCC------- 361
Cdd:cd00203  53 -------DIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDrddypti 125

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 12053591 362 ----SASAADGGCIMaaatgHPFPKVFNGCNRRELDRY 395
Cdd:cd00203 126 ddtlNAEDDDYYSVM-----SYTKGSFSDGQRKDFSQC 158
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 242-356 1.79e-12

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: 65.08  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   242 NYVDKFYRS-LNIRIALVGLEVWTHGNMCEVSENPYSTLWSFLSWRRKllaQKYHDNA---QLITGMSFHGTTiGLAPLM 317
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT---RIGQYGYdlgHLFTGRDGGGGG-GIAYVG 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 12053591   318 AMCSVYQSGGVNMDHSENAIGVAATMAHEMGHNFGMTHD 356
Cdd:pfam13582  84 GVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 214-403 6.73e-11

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: 63.55  E-value: 6.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 214 LYLVADYLEFQKNRRDQ-DATKHKLIEIANYVDKFYRSL--------NIRIALVGLEVWTHGNMCEVSENPY---STLWS 281
Cdd:cd04270   5 LLLVADHRFYKYMGRGEeETTINYLISHIDRVDDIYRNTdwdgggfkGIGFQIKRIRIHTTPDEVDPGNKFYnksFPNWG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 282 FLSWRRKLLAQKYHDN---AQLITGMSFHGTTIGLAPLMA--------MCSVYQ--SGGVN----------MDHSENAIG 338
Cdd:cd04270  85 VEKFLVKLLLEQFSDDvclAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKAYyySNGKKkylntgltttVNYGKRVPT 164

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12053591 339 VAA--TMAHEMGHNFGMTHDS--ADCCSASAADGGCIM--AAATG-HPFPKVFNGCNRRELDRYLQSGGGMC 403
Cdd:cd04270 165 KESdlVTAHELGHNFGSPHDPdiAECAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSC 236
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 211-404 4.62e-09

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 57.75  E-value: 4.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 211 YVELYLVADYlEFQKNRRDQDATKHKLIEIANYVDKFYRSLN---IRIALVGLEVWTH-----GNMCEVSEN--PYSTLW 280
Cdd:cd04272   2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDpdfepYIHPINYGYidAAETLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 281 SFLSWRRKLLAQKYHDNAQLITGM---SFHG-----TTIGLAPLMAMCSVYqsgGVNMdhSENAIGV---AATMAHEMGH 349
Cdd:cd04272  81 NFNEYVKKKRDYFNPDVVFLVTGLdmsTYSGgslqtGTGGYAYVGGACTEN---RVAM--GEDTPGSyygVYTMTHELAH 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12053591 350 NFGMTHDSADCCS---------ASAADGGCIMAAATGHPFPKVFNGCNRRELDRYLQSGGGMCL 404
Cdd:cd04272 156 LLGAPHDGSPPPSwvkghpgslDCPWDDGYIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 232-376 6.96e-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: 56.48  E-value: 6.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   232 ATKHKLIEIANYVDKFYR--SLNIRIALVG---LEVWTHGNmceVSENPYSTLWSFLSWRRKLLAQ----KYHDNAQLIT 302
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEpdDININGGLVNpgeIPATTSAS---DSGNNYCNSPTTIVRRLNFLSQwrgeQDYCLAHLVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   303 GMSFHGTTIGLAPLMAMC-----SVYQSGGVNMDHSENAIGVAAT----MAHEMGHNFGMTHdsaDCCSASAADGGCIMA 373
Cdd:pfam13574  79 MGTFSGGELGLAYVGQICqkgasSPKTNTGLSTTTNYGSFNYPTQewdvVAHEVGHNFGATH---DCDGSQYASSGCERN 155


                  ...
gi 12053591   374 AAT 376
Cdd:pfam13574 156 AAT 158
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 230-377 2.56e-08

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: 55.51  E-value: 2.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 230 QDATKHKLIEIANYVDKFYR-SLNIRIALVGLEVwthGNMCEVSENPYSTLWS---------------FLSWRrkllAQK 293
Cdd:cd04271  20 VEEARRNILNNVNSASQLYEsSFNISLGLRNLTI---SDASCPSTAVDSAPWNlpcnsrididdrlsiFSQWR----GQQ 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591 294 YHDNAQLITGMSF--HGTTIGLAPLMAMCSVYQSGGVNMDHSeNAIGVAAT------MAHEMGHNFGMTHD--------- 356
Cdd:cd04271  93 PDDGNAFWTLMTAcpSGSEVGVAWLGQLCRTGASDQGNETVA-GTNVVVRTsnewqvFAHEIGHTFGAVHDctsgtcsdg 171

                       170       180
                ....*....|....*....|....*...
gi 12053591 357 ---SADCCSASA----ADGGCIMAAATG 377
Cdd:cd04271 172 svgSQQCCPLSTstcdANGQYIMNPSSS 199
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 210-375 3.95e-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: 48.77  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   210 KYVELYLVADYlEFQKNRRDQDATKHKLIEIANYVDKFY-RSLNIRIALVGL--------EVWTHGNMCEVSENPYSTLW 280
Cdd:pfam13583   3 RVYRVAVATDC-TYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDrdviytdsSTDSFNADCSGGDLGNWRLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591   281 SFLSWRrkllAQKYHDNAQLITGMSFHGTTIGLAPLMAMC-SVYQSGGVNmdhsenaiGVAA------TMAHEMGHNFGM 353
Cdd:pfam13583  82 TLTSWR----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCsSARQNAKAS--------GVARsrdewdIFAHEIGHTFGA 149

                         170       180
                  ....*....|....*....|....*..
gi 12053591   354 THDSAD-CCSASAA----DGGCIMAAA 375
Cdd:pfam13583 150 VHDCSSqGEGLSSStedgSGQTIMSYA 176
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 289-384 3.57e-03

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 40.92  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053591  289 LLAQKYHDNAQLITGMSFHGTTIGLAplmAMCSVYQSGGVNMDhsENAIGVAATMAHEMGHNFGMTHDSADccSASAADG 368
Cdd:NF038115 129 NAGYSYGADFWVTIVSGSDGNANGVA---QVGMDLQVKGYNVT--LDLYVATQTLAHELGHLFGLYNGHAE--SAECSEG 201

                         90
                 ....*....|....*..
gi 12053591  369 G-CIMAAATGHPFPKVF 384
Cdd:NF038115 202 GyRLMCGSLAENFENLF 218
 
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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