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Conserved domains on  [gi|1743156891|ref|XP_030682335|]
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disintegrin and metalloproteinase domain-containing protein 33 isoform X3 [Nomascus leucogenys]

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 ...
 210-409 8.42e-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: 259.93  E-value: 8.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 210 KYLELYIVADHALFLTRHRNLNYTKQRLLEVANYVDQLLRTLDIQVVLTGLEVWTERDRSRVTQDANATLWAFLQWR-RG 288
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 289 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPD--GCCVEaaa 366
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1743156891 367 ESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAP 409
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
502-643 1.03e-42

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 151.36  E-value: 1.03e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891  502 LDGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQDSeGHFLPCAGRDALCGKLQCQGG 581
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743156891  582 KPSllaPHMVPVDSIVHLDGHEVTCRGALALPSAQLDllgLGLVEPGTQCGPRMVCnSNHNC 643
Cdd:smart00608  80 SEL---PLLGEHATVIYSNIGGLVCWSLDYHLGTDPD---IGMVKDGTKCGPGKVC-INGQC 134
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 426-500 2.56e-36

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: 130.89  E-value: 2.56e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743156891  426 EAGEECDCGSGQECRDLCCFAHNCSLRPGAQCAHGDCCTHCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPDVY 500
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 83-167 2.18e-22

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: 93.15  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891  83 KNHRLLAPGYIETHYGPDGQPVVLAPNHTDHCHYQGRVRGFPDSWVVLCTCSGMSGLITLsSNASYYLRPWPSQGSKDFS 162
Cdd:pfam01562  44 PNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSREEGG 122


                  ....*.
gi 1743156891 163 -THKIF 167
Cdd:pfam01562 123 hPHVVY 128
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 210-409 8.42e-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: 259.93  E-value: 8.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 210 KYLELYIVADHALFLTRHRNLNYTKQRLLEVANYVDQLLRTLDIQVVLTGLEVWTERDRSRVTQDANATLWAFLQWR-RG 288
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 289 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPD--GCCVEaaa 366
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1743156891 367 ESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAP 409
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 210-407 2.29e-81

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: 258.31  E-value: 2.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 210 KYLELYIVADHALFLTRHRNLNYTKQRLLEVANYVDQLLRTLDIQVVLTGLEVWTERDRSRVTQDANATLWAFLQWRRG- 288
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 289 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGC-CveaaaE 367
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1743156891 368 SGGCVMAAATGHPfPRVFSACSRRQLRAFFRKGGGACLSN 407
Cdd:cd04269   156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
502-643 1.03e-42

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 151.36  E-value: 1.03e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891  502 LDGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQDSeGHFLPCAGRDALCGKLQCQGG 581
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743156891  582 KPSllaPHMVPVDSIVHLDGHEVTCRGALALPSAQLDllgLGLVEPGTQCGPRMVCnSNHNC 643
Cdd:smart00608  80 SEL---PLLGEHATVIYSNIGGLVCWSLDYHLGTDPD---IGMVKDGTKCGPGKVC-INGQC 134
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 426-500 2.56e-36

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: 130.89  E-value: 2.56e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743156891  426 EAGEECDCGSGQECRDLCCFAHNCSLRPGAQCAHGDCCTHCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPDVY 500
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 503-609 6.33e-35

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: 128.12  E-value: 6.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 503 DGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQdSEGHFLPCAGRDALCGKLQCQGGK 582
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100
                  ....*....|....*....|....*..
gi 1743156891 583 PSllaPHMVPVDSIVHLDGHEVTCRGA 609
Cdd:pfam08516  80 EL---PLLGEHATVIYTNINGVTCWGT 103
Disintegrin pfam00200
Disintegrin;
426-498 5.36e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.58  E-value: 5.36e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743156891 426 EAGEECDCGSGQECR-DLCCFAHNCSLRPGAQCAHGDCCTHCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPD 498
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 83-167 2.18e-22

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: 93.15  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891  83 KNHRLLAPGYIETHYGPDGQPVVLAPNHTDHCHYQGRVRGFPDSWVVLCTCSGMSGLITLsSNASYYLRPWPSQGSKDFS 162
Cdd:pfam01562  44 PNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSREEGG 122


                  ....*.
gi 1743156891 163 -THKIF 167
Cdd:pfam01562 123 hPHVVY 128
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 210-409 8.42e-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: 259.93  E-value: 8.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 210 KYLELYIVADHALFLTRHRNLNYTKQRLLEVANYVDQLLRTLDIQVVLTGLEVWTERDRSRVTQDANATLWAFLQWR-RG 288
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRqEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 289 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPD--GCCVEaaa 366
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFngGCKCP--- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1743156891 367 ESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAP 409
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 210-407 2.29e-81

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: 258.31  E-value: 2.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 210 KYLELYIVADHALFLTRHRNLNYTKQRLLEVANYVDQLLRTLDIQVVLTGLEVWTERDRSRVTQDANATLWAFLQWRRG- 288
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 289 LWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGC-CveaaaE 367
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCtC-----G 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1743156891 368 SGGCVMAAATGHPfPRVFSACSRRQLRAFFRKGGGACLSN 407
Cdd:cd04269   156 RSTCIMAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
502-643 1.03e-42

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 151.36  E-value: 1.03e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891  502 LDGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQDSeGHFLPCAGRDALCGKLQCQGG 581
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGREN-GTYIPCAPEDVKCGKLQCTNV 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743156891  582 KPSllaPHMVPVDSIVHLDGHEVTCRGALALPSAQLDllgLGLVEPGTQCGPRMVCnSNHNC 643
Cdd:smart00608  80 SEL---PLLGEHATVIYSNIGGLVCWSLDYHLGTDPD---IGMVKDGTKCGPGKVC-INGQC 134
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 426-500 2.56e-36

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: 130.89  E-value: 2.56e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743156891  426 EAGEECDCGSGQECRDLCCFAHNCSLRPGAQCAHGDCCTHCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPDVY 500
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 503-609 6.33e-35

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: 128.12  E-value: 6.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 503 DGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQdSEGHFLPCAGRDALCGKLQCQGGK 582
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGR-TNGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100
                  ....*....|....*....|....*..
gi 1743156891 583 PSllaPHMVPVDSIVHLDGHEVTCRGA 609
Cdd:pfam08516  80 EL---PLLGEHATVIYTNINGVTCWGT 103
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 210-398 2.65e-34

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: 129.85  E-value: 2.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 210 KYLELYIVADHALFLTRHRNLNYTKQRLLEVANYVDQLLRTLD----IQVVLTGLEVW-TERDRSRVTQDANATLWAFLQ 284
Cdd:cd04267     1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 285 WRRGLWAQrpHDSAQLLTGRAF-QGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAaTMAHEIGHSLGLSHDPDGCCVE 363
Cdd:cd04267    81 WRAEGPIR--HDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLTAL-TMAHELGHNLGAEHDGGDELAF 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1743156891 364 AAAESGGCVMAAATGHPFPRVFSACSRRQLRAFFR 398
Cdd:cd04267   158 ECDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Disintegrin pfam00200
Disintegrin;
426-498 5.36e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.58  E-value: 5.36e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743156891 426 EAGEECDCGSGQECR-DLCCFAHNCSLRPGAQCAHGDCCTHCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPD 498
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 210-405 7.23e-31

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: 120.42  E-value: 7.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 210 KYLELYIVADHALFLTRHRNlnYTKQRLLEVANYVDQLLR--TL--DIQVVLTGLEVWTERDR-SRVTQDANATLWAFLQ 284
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKdpSLgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 285 WRRGLWAQRP-----HDSAQLLTGRAFQGA-----TVGLAPVEGMCRAESSGGVSTDHselPIGAAATMAHEIGHSLGLS 354
Cdd:cd04273    79 WQKKLNPPNDsdpehHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDT---GLSSAFTIAHELGHVLGMP 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1743156891 355 HDPDG--CcveAAAESGGCVMAAATGHPFPRVF-SACSRRQLRAFFRKGGGACL 405
Cdd:cd04273   156 HDGDGnsC---GPEGKDGHIMSPTLGANTGPFTwSKCSRRYLTSFLDTGDGNCL 206
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 83-167 2.18e-22

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: 93.15  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891  83 KNHRLLAPGYIETHYGPDGQPVVLAPNHTDHCHYQGRVRGFPDSWVVLCTCSGMSGLITLsSNASYYLRPWPSQGSKDFS 162
Cdd:pfam01562  44 PNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIRT-ENEEYLIEPLEKYSREEGG 122


                  ....*.
gi 1743156891 163 -THKIF 167
Cdd:pfam01562 123 hPHVVY 128
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 210-396 4.83e-16

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: 76.41  E-value: 4.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 210 KYLELYIVADHalfltRHRNLNYTKQRLLEVANYVDQLLRT-LDIQVVLTGLEVwterdrsrvtqdanatlwaflqwrrg 288
Cdd:cd00203     1 KVIPYVVVADD-----RDVEEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEI-------------------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 289 lwaqRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGCCVEAAAES 368
Cdd:cd00203    50 ----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTI 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1743156891 369 ----------GGCVMAAATG---HPFPRVFSACSRRQLRAF 396
Cdd:cd00203   126 ddtlnaedddYYSVMSYTKGsfsDGQRKDFSQCDIDQINKL 166
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
214-379 1.35e-15

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 75.92  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 214 LYIVADHAlFLTRHRNlNYTKQRLLEVANYVDQLL-RTLDIQVVLTGLEVWTERDRS----RVTQDANATLWAFlQWRRG 288
Cdd:pfam13688   7 LLVAADCS-YVAAFGG-DAAQANIINMVNTASNVYeRDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEF-QDFSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 289 LWAQRPHDSAQLLTGRAFQgaTVGLAPVEGMCRAESSGGVSTDHSELPIGAAA-----TMAHEIGHSLGLSHDPD----- 358
Cdd:pfam13688  84 WRGTQNDDLAYLFLMTNCS--GGGLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDCDsstss 161

                         170       180
                  ....*....|....*....|....
gi 1743156891 359 GCC---VEAAAESGGCVMAAATGH 379
Cdd:pfam13688 162 QCCppsNSTCPAGGRYIMNPSSSP 185
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 242-356 6.86e-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: 68.94  E-value: 6.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 242 NYVDQLLRT-LDIQVVLTGLEVWTERDRSRVTQDANATLWAFLQWRRGLWAQRPHDSAQLLTGRAFQGaTVGLAPVEGMC 320
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGG-GGGIAYVGGVC 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1743156891 321 RAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHD 356
Cdd:pfam13582  87 NSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 211-405 9.32e-12

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 65.45  E-value: 9.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 211 YLELYIVADHALfltrHRNLNYTKQRLLEVANYVDQL-LRTLD-----IQVVLTGLEVWTERDRSRV-------TQDANA 277
Cdd:cd04272     2 YPELFVVVDYDH----QSEFFSNEQLIRYLAVMVNAAnLRYRDlksprIRLLLVGITISKDPDFEPYihpinygYIDAAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 278 TLWAFLQWRRGLWAQRPHDSAQLLTGR--------AFQGATVGLAPVEGMCrAESSGGVSTDHSELPIGAAaTMAHEIGH 349
Cdd:cd04272    78 TLENFNEYVKKKRDYFNPDVVFLVTGLdmstysggSLQTGTGGYAYVGGAC-TENRVAMGEDTPGSYYGVY-TMTHELAH 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743156891 350 SLGLSHDPDGCCVEAAAESGGCVMAAATGHPFPRV--------FSACSRRQLRAFFRKGGGACL 405
Cdd:cd04272   156 LLGAPHDGSPPPSWVKGHPGSLDCPWDDGYIMSYVvngerqyrFSQCSQRQIRNVFRRLGASCL 219
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 214-404 1.09e-10

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: 62.78  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 214 LYIVADHALF-LTRHRNLNYTKQRLLEVANYVDQLLRTLDIQV-VLTGLEVWTER-----DRSRVTQDANATLWAFLQWR 286
Cdd:cd04270     5 LLLVADHRFYkYMGRGEEETTINYLISHIDRVDDIYRNTDWDGgGFKGIGFQIKRirihtTPDEVDPGNKFYNKSFPNWG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 287 RGLW----AQRPHDS----AQLLTGRAFQGATVGLAPVeGMCRAESSGGVSTDHSELPIGAAA----------------- 341
Cdd:cd04270    85 VEKFlvklLLEQFSDdvclAHLFTYRDFDMGTLGLAYV-GSPRDNSAGGICEKAYYYSNGKKKylntgltttvnygkrvp 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743156891 342 ------TMAHEIGHSLGLSHDPDGC-CVEAAAESGGCVM--AAATG-HPFPRVFSACSRRQLRAFFRKGGGAC 404
Cdd:cd04270   164 tkesdlVTAHELGHNFGSPHDPDIAeCAPGESQGGNYIMyaRATSGdKENNKKFSPCSKKSISKVLEVKSNSC 236
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 233-395 1.26e-08

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: 55.71  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 233 TKQRLLEVANYVDQL--LRTLDIQVVLTG---LEVWTERDRSR-VTQDANAT----LWAFLQWRrglwAQRPHDSAQLLT 302
Cdd:pfam13574   3 VTENLVNVVNRVNQIyePDDININGGLVNpgeIPATTSASDSGnNYCNSPTTivrrLNFLSQWR----GEQDYCLAHLVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 303 GRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATM---------AHEIGHSLGLSHDPDG------CCVEAAA- 366
Cdd:pfam13574  79 MGTFSGGELGLAYVGQICQKGASSPKTNTGLSTTTNYGSFNyptqewdvvAHEVGHNFGATHDCDGsqyassGCERNAAt 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1743156891 367 ----ESGGCVMAAATGHpFPRVFSACSRRQLRA 395
Cdd:pfam13574 159 svcsANGSFIMNPASKS-NNDLFSPCSISLICD 190
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 274-406 1.99e-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: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743156891 274 DANATLWAFLQWRrglwAQRPHDSA---QLLTGRAfQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAAT-----MAH 345
Cdd:cd04271    77 DIDDRLSIFSQWR----GQQPDDGNafwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTSnewqvFAH 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743156891 346 EIGHSLGLSHDPD-GCCVEAAAESGGC--------------VMAAATGHPFPRvFSACSRRQLRAFFRKGG--GACLS 406
Cdd:cd04271   152 EIGHTFGAVHDCTsGTCSDGSVGSQQCcplststcdangqyIMNPSSSSGITE-FSPCTIGNICSLLGRNPvrTSCLS 228
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 320-361 3.40e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 39.63  E-value: 3.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1743156891 320 CRAESSGGVSTDhselPIGAAATMAHEIGHSLGLSH---DPDGCC 361
Cdd:cd04275   122 INPSSLPGGSAA----PYNLGDTATHEVGHWLGLYHtfqGGSPCC 162
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 341-358 4.59e-03

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 38.34  E-value: 4.59e-03
                          10
                  ....*....|....*...
gi 1743156891 341 ATMAHEIGHSLGLSHDPD 358
Cdd:cd04278   109 SVAAHEIGHALGLGHSSD 126
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 341-355 7.24e-03

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 38.55  E-value: 7.24e-03
                          10
                  ....*....|....*
gi 1743156891 341 ATMAHEIGHSLGLSH 355
Cdd:cd04277   115 QTIIHEIGHALGLEH 129
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 344-358 9.10e-03

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 37.60  E-value: 9.10e-03
                          10
                  ....*....|....*
gi 1743156891 344 AHEIGHSLGLSHDPD 358
Cdd:pfam00413 113 AHEIGHALGLGHSSD 127
 
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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