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Conserved domains on  [gi|4501915|ref|NP_003807|]
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disintegrin and metalloproteinase domain-containing protein 9 precursor [Homo sapiens]

Protein Classification

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

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

Graphical summary

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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 ...
 212-404 2.91e-92

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


:

Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 287.59  E-value: 2.91e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  212 RYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKF 291
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  292 LITRRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrDCSCGAKSC 370
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4501915  371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGNCLLN 404
Cdd:cd04269 160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 4.25e-61

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 202.59  E-value: 4.25e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915     500 QNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 4501915     580 EIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCGAGKICRNFQCVD 636
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-163 1.32e-45

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: 159.40  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915     44 EIITPWRLT--RERREA--PRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 4501915    120 VEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQN----SSHFEHIIY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.99e-35

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 128.51  E-value: 1.99e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501915    423 DAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPD 496
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 ...
 212-404 2.91e-92

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 287.59  E-value: 2.91e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  212 RYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKF 291
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  292 LITRRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrDCSCGAKSC 370
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4501915  371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGNCLLN 404
Cdd:cd04269 160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 212-406 9.16e-90

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: 281.50  E-value: 9.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    212 RYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    292 LITRRRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RDCSCG-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 4501915    369 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGNCLLNIP 406
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 4.25e-61

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 202.59  E-value: 4.25e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915     500 QNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 4501915     580 EIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCGAGKICRNFQCVD 636
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 501-605 2.17e-48

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: 166.25  E-value: 2.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    501 NGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQE 580
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 4501915    581 IPVFGIVPAIIQTPSRGTKCWGVDF 605
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-163 1.32e-45

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: 159.40  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915     44 EIITPWRLT--RERREA--PRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 4501915    120 VEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQN----SSHFEHIIY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.99e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 128.51  E-value: 1.99e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501915    423 DAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 423-498 3.76e-35

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: 127.81  E-value: 3.76e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4501915     423 DAGEECDCGTPKECeLDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVF 498
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 212-404 2.91e-92

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 287.59  E-value: 2.91e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  212 RYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKF 291
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  292 LITRRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrDCSCGAKSC 370
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4501915  371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGNCLLN 404
Cdd:cd04269 160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 212-406 9.16e-90

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: 281.50  E-value: 9.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    212 RYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    292 LITRRRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RDCSCG-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 4501915    369 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGNCLLNIP 406
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 4.25e-61

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 202.59  E-value: 4.25e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915     500 QNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 4501915     580 EIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCGAGKICRNFQCVD 636
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 501-605 2.17e-48

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: 166.25  E-value: 2.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    501 NGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQE 580
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 4501915    581 IPVFGIVPAIIQTPSRGTKCWGVDF 605
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-163 1.32e-45

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: 159.40  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915     44 EIITPWRLT--RERREA--PRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 4501915    120 VEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQN----SSHFEHIIY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.99e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 128.51  E-value: 1.99e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501915    423 DAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 423-498 3.76e-35

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: 127.81  E-value: 3.76e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4501915     423 DAGEECDCGTPKECeLDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVF 498
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 212-403 2.54e-29

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 115.80  E-value: 2.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  212 RYVELFIVVDKERYDMMGRNQTavrEEMIL-LANYLDSMY----IMLNIRIVLVGLEIWTNGN-LINIVGGAGDVLGNFV 285
Cdd:cd04273   1 RYVETLVVADSKMVEFHHGEDL---EHYILtLMNIVASLYkdpsLGNSINIVVVRLIVLEDEEsGLLISGNAQKSLKSFC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  286 QWREK---------------FLITRRrhdsaQLVLKKGFGGTAGMAFVGTVCSRSHAGGINvfgQITVETFASIVAHELG 350
Cdd:cd04273  78 RWQKKlnppndsdpehhdhaILLTRQ-----DICRSNGNCDTLGLAPVGGMCSPSRSCSIN---EDTGLSSAFTIAHELG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4501915  351 HNLGMNHDD-GRDC-SCGAKSCIMNS-GASGSRNF--SSCSAEDFEKLTLNKGGNCLL 403
Cdd:cd04273 150 HVLGMPHDGdGNSCgPEGKDGHIMSPtLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 212-387 7.35e-28

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: 111.36  E-value: 7.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  212 RYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMY----IMLNIRIVLVGLEIWTNGNLINIVG-GAGDVLGNFVQ 286
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  287 WREKFLItrrRHDSAQLVLKKGF--GGTAGMAFVGTVCSRSHAGGINVFGQITVETfASIVAHELGHNLGMNHDDGRDCS 364
Cdd:cd04267  81 WRAEGPI---RHDNAVLLTAQDFieGDILGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDELA 156

                       170       180
                ....*....|....*....|....*...
gi 4501915  365 C---GAKSCIMNSGASGSRN--FSSCSA 387
Cdd:cd04267 157 FecdGGGNYIMAPVDSGLNSyrFSQCSI 184
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 237-358 8.17e-19

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: 82.80  E-value: 8.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    237 EEMILLANYLDSMY-IMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWrekfLITRRRH---DSAQLVLKKGFGGT 312
Cdd:pfam13582   1 ARIVSLVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEV----NDTRIGQygyDLGHLFTGRDGGGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 4501915    313 AGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHD 358
Cdd:pfam13582  77 GGIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
211-383 3.21e-17

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 80.54  E-value: 3.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    211 TRYVELFIVVDKERYDMMGRNqtAVREEMILLANYLDS-MYIMLNIRIVLVGLEIWTNGNLI----NIVGGAGDVLGNFV 285
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    286 QWREkfLITRRRHDSAQLVLKKGFGGTaGMAFVGTVCSRSHAGGINVFGQITVE-----TFASIVAHELGHNLGMNHDDG 360
Cdd:pfam13688  80 DFSA--WRGTQNDDLAYLFLMTNCSGG-GLAWLGQLCNSGSAGSVSTRVSGNNVvvstaTEWQVFAHEIGHNFGAVHDCD 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 4501915    361 RD-----CSCGAKSC------IMN-SGASGSRNFS 383
Cdd:pfam13688 157 SStssqcCPPSNSTCpaggryIMNpSSSPNSTDFS 191
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 213-402 2.00e-13

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 70.46  E-value: 2.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  213 YVELFIVVDKERYDMMGRNQtAVREEMILLANYLDSMYIML---NIRIVLVGLEIWTN-GNLINIVGGAGDV------LG 282
Cdd:cd04272   2 YPELFVVVDYDHQSEFFSNE-QLIRYLAVMVNAANLRYRDLkspRIRLLLVGITISKDpDFEPYIHPINYGYidaaetLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  283 NFVQW-REK---------FLITRRR-HDSAQLVLKKgfgGTAGMAFVGTVCSRSHAGginvFGQITVETFASI--VAHEL 349
Cdd:cd04272  81 NFNEYvKKKrdyfnpdvvFLVTGLDmSTYSGGSLQT---GTGGYAYVGGACTENRVA----MGEDTPGSYYGVytMTHEL 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4501915  350 GHNLGMNHD-DGRDCSC----GAKSC------IMNSGASGSRN--FSSCSAEDFEKLTLNKGGNCL 402
Cdd:cd04272 154 AHLLGAPHDgSPPPSWVkghpGSLDCpwddgyIMSYVVNGERQyrFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 212-393 1.67e-11

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: 63.31  E-value: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  212 RYVELFIVVDKERYDmmgrnQTAVREEMILLANYLDSMY-IMLNIRIVLVGLEIwtngnlinivggagdvlgnfvqwrek 290
Cdd:cd00203   1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIAMQIWrDYLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  291 flitrRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCG--- 366
Cdd:cd00203  50 -----DKADIAILVTRQDFdGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDypt 124

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4501915  367 ----------AKSCIMNSGAS-----GSRNFSSCSAEDFEKL 393
Cdd:cd00203 125 iddtlnaeddDYYSVMSYTKGsfsdgQRKDFSQCDIDQINKL 166
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 234-386 3.70e-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: 372637  Cd Length: 193  Bit Score: 59.95  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    234 AVREEMILLANYLDSMYIM--LNIRIVLVG---LEIWTNG-----NLINIVGGAGDVLGNFVQWRekfliTRRRHDSAQL 303
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPddININGGLVNpgeIPATTSAsdsgnNYCNSPTTIVRRLNFLSQWR-----GEQDYCLAHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    304 VLKKGF-GGTAGMAFVGTVC-----SRSHAGGINV---FGQITVETFA-SIVAHELGHNLGMNHD---DGRDCSCGAK-- 368
Cdd:pfam13574  77 VTMGTFsGGELGLAYVGQICqkgasSPKTNTGLSTttnYGSFNYPTQEwDVVAHEVGHNFGATHDcdgSQYASSGCERna 156

                         170       180
                  ....*....|....*....|....*...
gi 4501915    369 ---------SCIMN-SGASGSRNFSSCS 386
Cdd:pfam13574 157 atsvcsangSFIMNpASKSNNDLFSPCS 184
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 212-390 2.04e-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: 49.15  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    212 RYVELFIVVDKERYDMMGrNQTAVREEMILLANYLDSMY-IMLNIRIVLVGLE--IWTNG--NLINIVGGAGDvLGNFVQ 286
Cdd:pfam13583   3 RVYRVAVATDCTYSASFG-SVDELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSstDSFNADCSGGD-LGNWRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915    287 WREKFLITRRRHDSAQLVLKKG-FGGTAGMAFVGTVCSRSH--AGGiNVFGQITVETfaSIVAHELGHNLGMNHDDGRDC 363
Cdd:pfam13583  81 ATLTSWRDSLNYDLAYLTLMTGpSGQNVGVAWVGALCSSARqnAKA-SGVARSRDEW--DIFAHEIGHTFGAVHDCSSQG 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 4501915    364 sCGAK--------SCIMNSGASGSR-NFSSCSAEDF 390
Cdd:pfam13583 158 -EGLSsstedgsgQTIMSYASTASQtAFSPCTIRNI 192
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 281-386 2.58e-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: 49.34  E-value: 2.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  281 LGNFVQWREKflitRRRHDSAQLVLKKGF--GGTAGMAFVGTVCSRSHAG-------GINVFGQITVETfaSIVAHELGH 351
Cdd:cd04271  82 LSIFSQWRGQ----QPDDGNAFWTLMTACpsGSEVGVAWLGQLCRTGASDqgnetvaGTNVVVRTSNEW--QVFAHEIGH 155

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4501915  352 NLGMNHD-------DGRD-----CSCGAKSC------IMN-SGASGSRNFSSCS 386
Cdd:cd04271 156 TFGAVHDctsgtcsDGSVgsqqcCPLSTSTCdangqyIMNpSSSSGITEFSPCT 209
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 310-401 7.47e-05

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: 45.06  E-value: 7.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  310 GGTAGMAFVGTVCSRSHaGGI---------------NVfGQITVETFAS---------IVAHELGHNLGMNHD-DGRDCS 364
Cdd:cd04270 114 MGTLGLAYVGSPRDNSA-GGIcekayyysngkkkylNT-GLTTTVNYGKrvptkesdlVTAHELGHNFGSPHDpDIAECA 191

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 4501915  365 CGAK---SCIMNSGA-SGS----RNFSSCSAEDFEKLTLNKGGNC 401
Cdd:cd04270 192 PGESqggNYIMYARAtSGDkennKKFSPCSKKSISKVLEVKSNSC 236
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 287-357 7.17e-04

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 40.94  E-value: 7.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501915  287 WREKFLIT---RRRHDSAQL---VLKKGFGGTAGMAFVGTVcSRSHAGGI--------NVFGQITVETFASIVAHELGHN 352
Cdd:cd04268  27 WNKAFAIGfknANDVDPADIrysVIRWIPYNDGTWSYGPSQ-VDPLTGEIllarvylySSFVEYSGARLRNTAEHELGHA 105


                ....*
gi 4501915  353 LGMNH 357
Cdd:cd04268 106 LGLRH 110
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 345-392 5.72e-03

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


Pssm-ID: 213029  Cd Length: 173  Bit Score: 38.43  E-value: 5.72e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 4501915  345 VAHELGHNLGMNHddgrdcsCGAKSCIMnsgasgsrNFSSCSAEDFEK 392
Cdd:cd11375 127 AVHELGHLFGLDH-------CPYYACVM--------NFSNSLEETDRK 159
 
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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