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Conserved domains on  [gi|767948064|ref|XP_011514620|]
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disintegrin and metalloproteinase domain-containing protein 22 isoform X2 [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

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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 ...
239-438 1.48e-83

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 and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


:

Pssm-ID: 307535  Cd Length: 199  Bit Score: 267.99  E-value: 1.48e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSDVNVVRQRVFQVVNLVNSIYK-ELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   319 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKrklaSGECKC 394
Cdd:pfam01421   80 YLKKRKphDVAQLLSGRTFGGTTVGAAYPGGMCSPSYSGGVNLDHKINVegFAVTMAHELGHNLGMTHDD----ITGCKC 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 767948064   395 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 438
Cdd:pfam01421  156 P-PGGGCIMNPsAGSSFGRKFSNCSQDDFEQFLLKQKGACLFNKP 199
ACR smart00608
ADAM Cysteine-Rich Domain;
530-671 1.82e-51

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 176.78  E-value: 1.82e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064    530 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 609
Cdd:smart00608    1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948064    610 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 671
Cdd:smart00608   81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
73-188 2.45e-30

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: 334593  Cd Length: 125  Bit Score: 116.13  E-value: 2.45e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064    73 RVRGDLGGPqltHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSFVA 150
Cdd:pfam01562   13 RRRRSLSSE---YPDQLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYGEDGTEVTDQppIQDHCHYQGHVEGHPDSSVA 89
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767948064   151 LSTCHGLHGMFYDGNHTYLIEPEEndTTQEDFHFHSVY 188
Cdd:pfam01562   90 LSTCSGLRGVIRTDNEEYFIEPLE--SSEEEGHPHVVY 125
Disintegrin pfam00200
Disintegrin;
453-526 1.00e-29

Disintegrin;


:

Pssm-ID: 333919  Cd Length: 74  Bit Score: 112.29  E-value: 1.00e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948064   453 ETGEECDCGTPAECvlEGAECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 526
Cdd:pfam00200    1 EEGEECDCGSTEEC--ANDPCCdpKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPAVNECDLPEYCNGTSAECPPD 74
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
239-438 1.48e-83

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 and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 307535  Cd Length: 199  Bit Score: 267.99  E-value: 1.48e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSDVNVVRQRVFQVVNLVNSIYK-ELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   319 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKrklaSGECKC 394
Cdd:pfam01421   80 YLKKRKphDVAQLLSGRTFGGTTVGAAYPGGMCSPSYSGGVNLDHKINVegFAVTMAHELGHNLGMTHDD----ITGCKC 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 767948064   395 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 438
Cdd:pfam01421  156 P-PGGGCIMNPsAGSSFGRKFSNCSQDDFEQFLLKQKGACLFNKP 199
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
239-436 7.03e-62

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  Cd Length: 194  Bit Score: 208.24  E-value: 7.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  319 FIKE--KSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTD--LMAVTLAQSLAHNIGIISDKrklasGECKC 394
Cdd:cd04269    80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNllLFAVTMAHELGHNLGMEHDD-----GGCTC 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767948064  395 EDtwSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFN 436
Cdd:cd04269   155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
530-671 1.82e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 176.78  E-value: 1.82e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064    530 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 609
Cdd:smart00608    1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948064    610 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 671
Cdd:smart00608   81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
531-649 2.78e-37

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: 337086  Cd Length: 115  Bit Score: 135.43  E-value: 2.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   531 DGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGN 610
Cdd:pfam08516    1 DGTPCSNGTAYCYNGRCRDRDRQCQEIFGKGAKSAPDACYEEVNTKGDRFGNCGRTNGGYVKCNKRDVLCGKLQCTNVTE 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 767948064   611 IPRLGELdgeitSTLVVQQGRTLNCSGGHVKLEEDV-DLG 649
Cdd:pfam08516   81 LPRLGEH-----ATVIYTYINGHTCWGTDYHLGMDVpDPG 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
73-188 2.45e-30

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: 334593  Cd Length: 125  Bit Score: 116.13  E-value: 2.45e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064    73 RVRGDLGGPqltHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSFVA 150
Cdd:pfam01562   13 RRRRSLSSE---YPDQLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYGEDGTEVTDQppIQDHCHYQGHVEGHPDSSVA 89
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767948064   151 LSTCHGLHGMFYDGNHTYLIEPEEndTTQEDFHFHSVY 188
Cdd:pfam01562   90 LSTCSGLRGVIRTDNEEYFIEPLE--SSEEEGHPHVVY 125
Disintegrin pfam00200
Disintegrin;
453-526 1.00e-29

Disintegrin;


Pssm-ID: 333919  Cd Length: 74  Bit Score: 112.29  E-value: 1.00e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948064   453 ETGEECDCGTPAECvlEGAECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 526
Cdd:pfam00200    1 EEGEECDCGSTEEC--ANDPCCdpKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPAVNECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
453-528 5.21e-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: 104.69  E-value: 5.21e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948064    453 ETGEECDCGTPAECvleGAECCKK--CTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIH 528
Cdd:smart00050    1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
239-438 1.48e-83

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 and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 307535  Cd Length: 199  Bit Score: 267.99  E-value: 1.48e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:pfam01421    1 KYIELFIVVDKQLFQKMGSDVNVVRQRVFQVVNLVNSIYK-ELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   319 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKrklaSGECKC 394
Cdd:pfam01421   80 YLKKRKphDVAQLLSGRTFGGTTVGAAYPGGMCSPSYSGGVNLDHKINVegFAVTMAHELGHNLGMTHDD----ITGCKC 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 767948064   395 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 438
Cdd:pfam01421  156 P-PGGGCIMNPsAGSSFGRKFSNCSQDDFEQFLLKQKGACLFNKP 199
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
239-436 7.03e-62

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  Cd Length: 194  Bit Score: 208.24  E-value: 7.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 318
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  319 FIKE--KSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTD--LMAVTLAQSLAHNIGIISDKrklasGECKC 394
Cdd:cd04269    80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNllLFAVTMAHELGHNLGMEHDD-----GGCTC 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767948064  395 EDtwSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFN 436
Cdd:cd04269   155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
530-671 1.82e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 176.78  E-value: 1.82e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064    530 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 609
Cdd:smart00608    1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948064    610 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 671
Cdd:smart00608   81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
531-649 2.78e-37

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: 337086  Cd Length: 115  Bit Score: 135.43  E-value: 2.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   531 DGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGN 610
Cdd:pfam08516    1 DGTPCSNGTAYCYNGRCRDRDRQCQEIFGKGAKSAPDACYEEVNTKGDRFGNCGRTNGGYVKCNKRDVLCGKLQCTNVTE 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 767948064   611 IPRLGELdgeitSTLVVQQGRTLNCSGGHVKLEEDV-DLG 649
Cdd:pfam08516   81 LPRLGEH-----ATVIYTYINGHTCWGTDYHLGMDVpDPG 115
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
73-188 2.45e-30

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: 334593  Cd Length: 125  Bit Score: 116.13  E-value: 2.45e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064    73 RVRGDLGGPqltHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSFVA 150
Cdd:pfam01562   13 RRRRSLSSE---YPDQLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYGEDGTEVTDQppIQDHCHYQGHVEGHPDSSVA 89
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767948064   151 LSTCHGLHGMFYDGNHTYLIEPEEndTTQEDFHFHSVY 188
Cdd:pfam01562   90 LSTCSGLRGVIRTDNEEYFIEPLE--SSEEEGHPHVVY 125
Disintegrin pfam00200
Disintegrin;
453-526 1.00e-29

Disintegrin;


Pssm-ID: 333919  Cd Length: 74  Bit Score: 112.29  E-value: 1.00e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948064   453 ETGEECDCGTPAECvlEGAECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 526
Cdd:pfam00200    1 EEGEECDCGSTEEC--ANDPCCdpKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPAVNECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
453-528 5.21e-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: 104.69  E-value: 5.21e-27
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948064    453 ETGEECDCGTPAECvleGAECCKK--CTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIH 528
Cdd:smart00050    1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
239-435 2.22e-18

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: 84.60  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  239 KYIELMIVNDHLMFKKHRLSvvHTNTYAKSVVNMADLIYKDQL---KTRIVLVAMETWATDNK-FAISENPLITLREFMK 314
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKDPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  315 YRR------DFIKEKSDAVHLFSGSQFESSRS-----GAAYIGGICSLLKGGGVNEfgKTDLM-AVTLAQSLAHNIGIIS 382
Cdd:cd04273    79 WQKklnppnDSDPEHHDHAILLTRQDICRSNGncdtlGLAPVGGMCSPSRSCSINE--DTGLSsAFTIAHELGHVLGMPH 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767948064  383 DKrklASGECKcEDTWSGCIMGDTGYYLPKKFT--QCNIEEYHDFLNSGGGACLF 435
Cdd:cd04273   157 DG---DGNSCG-PEGKDGHIMSPTLGANTGPFTwsKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
239-427 5.18e-17

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: 80.16  E-value: 5.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  239 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKD---QLKTRIVLVAMETWATdNKFA--ISENPLITLREFM 313
Cdd:cd04267     1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKG-EQFAppIDSDASNTLNSFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  314 KYRRDFIKeKSDAVHLFSGSQF-ESSRSGAAYIGGICSLLKGGGVNE-FGKTDLMAVTLAQSLAHNIGIISDkrklASGE 391
Cdd:cd04267    80 FWRAEGPI-RHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAEHD----GGDE 154
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767948064  392 CKCEDTWSG-CIMGDT-GYYLPKKFTQCNIEEYHDFLN 427
Cdd:cd04267   155 LAFECDGGGnYIMAPVdSGLNSYRFSQCSIGSIREFLD 192
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
268-379 2.24e-10

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 316138  Cd Length: 122  Bit Score: 58.90  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   268 SVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRDFIKEKS-DAVHLFSGSQFESSrSGAAYIG 346
Cdd:pfam13582    5 ALVNRANQIYERDSGIRLQLVAIIYTDPASDDYTTSDALEILDELQQVIDTRYRQYGyDLGHLFTGRDVGGG-GGLAYVG 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 767948064   347 GICSLLKGGGVNEFGKT--DLMAVTLAQSLAHNIG 379
Cdd:pfam13582   84 SVCNSGSKAGVNGGSSPygDCGVDTFAHEIGHNFG 118
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
240-434 7.35e-09

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 56.98  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  240 YIELMIVNDHlMFKKHRLSVVHTNTYAKSVVNMADLIYKD--QLKTRIVLVAMETwATDNKFAI-----------SENPL 306
Cdd:cd04272     2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDlkSPRIRLLLVGITI-SKDPDFEPyihpinygyidAAETL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064  307 ITLREFMKYRRDFikEKSDAVHL--------FSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNI 378
Cdd:cd04272    80 ENFNEYVKKKRDY--FNPDVVFLvtgldmstYSGGSLQTGTGGYAYVGGACTENRVAMGEDTPGSYYGVYTMTHELAHLL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948064  379 GIISD--------KRKLASGECKCEDtwsGCIM----GDTGYYlpkKFTQCNIEEYHDFLNSGGGACL 434
Cdd:cd04272   158 GAPHDgspppswvKGHPGSLDCPWDD---GYIMsyvvNGERQY---RFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
238-379 2.93e-04

Metallo-peptidase family M12;


Pssm-ID: 338898  Cd Length: 188  Bit Score: 42.75  E-value: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948064   238 TKYIELMIVNDHLMFKKHRLSVVHTNTYakSVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRR 317
Cdd:pfam13688    2 TRTVALLVAADCSYVAAFGGDAAQANII--NMVNTASNVYERNFNISLGLVNLTITDYTDPYTSPPTSSGNASDRLNRFQ 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948064   318 DFIKEKS----DAVHLFSGSQFESSrsGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNIG 379
Cdd:pfam13688   80 SFSAWRGtqndDLAHLFLDTNCSGG--GLAWLGQLCNSGSAGSVSTSVNVVVGTATEWQVFAHEIG 143
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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