NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4501913|ref|NP_003803|]
View 

disintegrin and metalloproteinase domain-containing protein 23 isoform 1 preproprotein [Homo sapiens]

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 12023297)

protein containing domains Pep_M12B_propep, ZnMc_adamalysin_II_like, Disintegrin, and ACR

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 299-496 4.11e-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: 272.25  E-value: 4.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    379 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSsrKPKCDCT 453
Cdd:pfam01421  80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDF--NGGCKCP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 4501913    454 EsWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 496
Cdd:pfam01421 158 P-GGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
587-726 4.00e-51

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 4.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913     587 QDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLT 666
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913     667 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 726
Cdd:smart00608  81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 147-249 4.57e-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: 112.41  E-value: 4.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    147 HLAQASFQIEAFGSKFILDLILNNGLLSSDY-VEIHYENGKP--QYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFE 223
Cdd:pfam01562  23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGveSPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102

                          90       100
                  ....*....|....*....|....*.
gi 4501913    224 DDTFVYMIEPLElVHDEKSTGRPHII 249
Cdd:pfam01562 103 TENEEYLIEPLE-KYSREEGGHPHVV 127
Disintegrin pfam00200
Disintegrin;
511-583 8.01e-29

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 109.64  E-value: 8.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4501913    511 EAGEECDCGFHVECY-GLCC--KKCSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPN 583
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCdaKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 299-496 4.11e-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: 272.25  E-value: 4.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    379 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSsrKPKCDCT 453
Cdd:pfam01421  80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDF--NGGCKCP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 4501913    454 EsWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 496
Cdd:pfam01421 158 P-GGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 299-494 1.55e-64

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 214.40  E-value: 1.55e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKeQLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  379 I----KQHaDAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSrkpkCDC 452
Cdd:cd04269  80 NllprKPH-DNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnLLLFAVTMAHELGHNLGMEHDDGG----CTC 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4501913  453 TESwgGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFN 494
Cdd:cd04269 155 GRS--TCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
587-726 4.00e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 4.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913     587 QDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLT 666
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913     667 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 726
Cdd:smart00608  81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 588-697 3.50e-33

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: 123.49  E-value: 3.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    588 DGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLTR 667
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4501913    668 APRIGQLQgeiipTSFYHQGRVIDCSGAHV 697
Cdd:pfam08516  81 LPLLGEHA-----TVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 147-249 4.57e-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: 112.41  E-value: 4.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    147 HLAQASFQIEAFGSKFILDLILNNGLLSSDY-VEIHYENGKP--QYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFE 223
Cdd:pfam01562  23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGveSPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102

                          90       100
                  ....*....|....*....|....*.
gi 4501913    224 DDTFVYMIEPLElVHDEKSTGRPHII 249
Cdd:pfam01562 103 TENEEYLIEPLE-KYSREEGGHPHVV 127
Disintegrin pfam00200
Disintegrin;
511-583 8.01e-29

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 109.64  E-value: 8.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4501913    511 EAGEECDCGFHVECY-GLCC--KKCSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPN 583
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCdaKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 511-585 1.16e-27

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: 106.62  E-value: 1.16e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4501913     511 EAGEECDCGFHVECYGLCCKK--CSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPNLH 585
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPatCKLKPGAQCASGPCCDN--CKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 299-496 4.11e-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: 272.25  E-value: 4.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEqLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    379 -IKQHA--DAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSsrKPKCDCT 453
Cdd:pfam01421  80 yLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSknLESFAVTMAHELGHNLGMQHDDF--NGGCKCP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 4501913    454 EsWGGCIM-EETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRP 496
Cdd:pfam01421 158 P-GGGCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 299-494 1.55e-64

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 214.40  E-value: 1.55e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKeQLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQR 378
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  379 I----KQHaDAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGL--PMAVAQVLSQSLAQNLGIQWEPSSrkpkCDC 452
Cdd:cd04269  80 NllprKPH-DNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSrnLLLFAVTMAHELGHNLGMEHDDGG----CTC 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4501913  453 TESwgGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFN 494
Cdd:cd04269 155 GRS--TCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
587-726 4.00e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 4.00e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913     587 QDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLT 666
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913     667 RAPRIGQLQGEIiptsfYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCL 726
Cdd:smart00608  81 ELPLLGEHATVI-----YSNIGGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCV 135
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 588-697 3.50e-33

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: 123.49  E-value: 3.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    588 DGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLTR 667
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 4501913    668 APRIGQLQgeiipTSFYHQGRVIDCSGAHV 697
Cdd:pfam08516  81 LPLLGEHA-----TVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 147-249 4.57e-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: 112.41  E-value: 4.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    147 HLAQASFQIEAFGSKFILDLILNNGLLSSDY-VEIHYENGKP--QYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFE 223
Cdd:pfam01562  23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFtVTYYLDGGTGveSPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102

                          90       100
                  ....*....|....*....|....*.
gi 4501913    224 DDTFVYMIEPLElVHDEKSTGRPHII 249
Cdd:pfam01562 103 TENEEYLIEPLE-KYSREEGGHPHVV 127
Disintegrin pfam00200
Disintegrin;
511-583 8.01e-29

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 109.64  E-value: 8.01e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4501913    511 EAGEECDCGFHVECY-GLCC--KKCSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPN 583
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCdaKTCKLKPGAQCSSGPCCTN--CQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 511-585 1.16e-27

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: 106.62  E-value: 1.16e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4501913     511 EAGEECDCGFHVECYGLCCKK--CSLSNGAHCSDGPCCNNtsCLFQPRGYECRDAVNECDITEYCTGDSGQCPPNLH 585
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPatCKLKPGAQCASGPCCDN--CKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 299-484 5.50e-20

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: 88.63  E-value: 5.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  299 KYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKE---QLNTRVVLVAVETWTEKDQIDITTNPVQM-LHEFSK 374
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKGEQFAPPIDSDASNtLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  375 YRQRIKQHADAVHLISRVTFHYKRS-SLSYFGGVCSRTRGVGVNE-YGLPMAVAQVLSQSLAQNLGIQWEPSSRkpkCDC 452
Cdd:cd04267  81 WRAEGPIRHDNAVLLTAQDFIEGDIlGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAEHDGGDE---LAF 157

                       170       180       190
                ....*....|....*....|....*....|....
gi 4501913  453 TESWGG-CIMEETGVSH-SRKFSKCSILEYRDFL 484
Cdd:cd04267 158 ECDGGGnYIMAPVDSGLnSYRFSQCSIGSIREFL 191
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 299-493 2.21e-19

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: 87.29  E-value: 2.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  299 KYLELMIVNDHKTYKKHrsSHAHTNNFAKSVVNLVDSIYKEQL---NTRVVLVAVETWT-EKDQIDITTNPVQMLHEFSK 374
Cdd:cd04273   1 RYVETLVVADSKMVEFH--HGEDLEHYILTLMNIVASLYKDPSlgnSINIVVVRLIVLEdEESGLLISGNAQKSLKSFCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  375 YRQRIK-------QHADAVHLISRVTFHYKRSS-----LSYFGGVCSRTRGVGVNE-YGLPMAVaqVLSQSLAQNLGIQW 441
Cdd:cd04273  79 WQKKLNppndsdpEHHDHAILLTRQDICRSNGNcdtlgLAPVGGMCSPSRSCSINEdTGLSSAF--TIAHELGHVLGMPH 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4501913  442 EPSSrkPKCDcTESWGGCIMEETGVSHSRKF--SKCSILEYRDFLQRGGGACLF 493
Cdd:cd04273 157 DGDG--NSCG-PEGKDGHIMSPTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
303-473 1.20e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 46.64  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    303 LMIVNDHKTYKKHRSSHAHTNnfAKSVVNLVDSIYKEQLNTRVVLVAVETWTEKD----QIDITTNPVQMLHEFSKYRQR 378
Cdd:pfam13688   7 LLVAADCSYVAAFGGDAAQAN--IINMVNTASNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQDFSAW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913    379 I-KQHADAVHLISRVTFHYkrSSLSYFGGVCSRTRGVGVNEYGLPMAVAQ---VLSQSLAQNLGIQW------EPSSRKP 448
Cdd:pfam13688  85 RgTQNDDLAYLFLMTNCSG--GGLAWLGQLCNSGSAGSVSTRVSGNNVVVstaTEWQVFAHEIGHNFgavhdcDSSTSSQ 162

                         170       180
                  ....*....|....*....|....*....
gi 4501913    449 KCDCTESW----GGCIMEETGVSHSRKFS 473
Cdd:pfam13688 163 CCPPSNSTcpagGRYIMNPSSSPNSTDFS 191
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 299-484 1.61e-05

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: 45.98  E-value: 1.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  299 KYLELMIVNDHKTYKKHRSSHAHtnnfaKSVVNLVDSIYKEQLNTRVVLVAVETwtekdqidittnpvqmlhefskyrqr 378
Cdd:cd00203   1 KVIPYVVVADDRDVEEENLSAQI-----QSLILIAMQIWRDYLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  379 ikQHADAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGV---NEYGlPMAVAQVLSQSLAQNLGIqWEPSSRKPKCDCTES 455
Cdd:cd00203  50 --DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVlqdNQSG-TKEGAQTIAHELGHALGF-YHDHDRKDRDDYPTI 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4501913  456 W---------GGCIM--EETGVSHSRK--FSKCSILEYRDFL 484
Cdd:cd00203 126 DdtlnaedddYYSVMsyTKGSFSDGQRkdFSQCDIDQINKLY 167
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 300-492 1.59e-04

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 43.88  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  300 YLELMIVNDHKTYKKHRSSHAHTNNFAkSVVNLVDSIYKEQLNTRV--VLVAVETWTEKD-------QIDITTNPVQMLH 370
Cdd:cd04272   2 YPELFVVVDYDHQSEFFSNEQLIRYLA-VMVNAANLRYRDLKSPRIrlLLVGITISKDPDfepyihpINYGYIDAAETLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501913  371 EFSKY--RQRIKQHADAVHLISR---VTFHYKR-----SSLSYFGGVCSRTRgVGVNEY--GLPMAVaQVLSQSLAQNLG 438
Cdd:cd04272  81 NFNEYvkKKRDYFNPDVVFLVTGldmSTYSGGSlqtgtGGYAYVGGACTENR-VAMGEDtpGSYYGV-YTMTHELAHLLG 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4501913  439 IQWEPSSRKPKCDCTESWGGC------IME--ETGVSHSRkFSKCSILEYRDFLQRGGGACL 492
Cdd:cd04272 159 APHDGSPPPSWVKGHPGSLDCpwddgyIMSyvVNGERQYR-FSQCSQRQIRNVFRRLGASCL 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH