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Conserved domains on  [gi|1965410872|ref|NP_001378910|]
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disintegrin and metalloproteinase domain-containing protein 22 isoform 17 precursor [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 ...
 238-437 8.09e-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: 271.87  E-value: 8.09e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 393
Cdd:pfam01421  80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1965410872 394 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 437
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
529-670 5.13e-51

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 5.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872  529 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 608
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965410872  609 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 670
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 70-187 2.87e-31

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: 118.96  E-value: 2.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872  70 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 147
Cdd:pfam01562  10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1965410872 148 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 187
Cdd:pfam01562  89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
452-525 1.50e-28

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 108.87  E-value: 1.50e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965410872 452 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 525
Cdd:pfam00200   1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 238-437 8.09e-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: 271.87  E-value: 8.09e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 393
Cdd:pfam01421  80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1965410872 394 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 437
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 238-435 7.08e-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 [Multi-domain]  Cd Length: 194  Bit Score: 207.47  E-value: 7.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKE--KSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTD--LMAVTLAQSLAHNIGIISDKrklasGECKC 393
Cdd:cd04269    80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNllLFAVTMAHELGHNLGMEHDD-----GGCTC 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1965410872 394 EDtwSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFN 435
Cdd:cd04269   155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
529-670 5.13e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 5.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872  529 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 608
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965410872  609 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 670
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 530-639 1.06e-34

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: 127.73  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 530 DGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGN 609
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1965410872 610 IPRLGELdgeitSTLVVQQGRTLNCSGGHV 639
Cdd:pfam08516  81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 70-187 2.87e-31

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: 118.96  E-value: 2.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872  70 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 147
Cdd:pfam01562  10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1965410872 148 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 187
Cdd:pfam01562  89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
452-525 1.50e-28

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 108.87  E-value: 1.50e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965410872 452 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 525
Cdd:pfam00200   1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 452-527 2.51e-26

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: 102.77  E-value: 2.51e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1965410872  452 ETGEECDCGTPAECvleGAECCKK--CTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIH 527
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 ...
 238-437 8.09e-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: 271.87  E-value: 8.09e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDqLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKEKS--DAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDL--MAVTLAQSLAHNIGIISDKRKlasGECKC 393
Cdd:pfam01421  80 YLKKRKphDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLesFAVTMAHELGHNLGMQHDDFN---GGCKC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1965410872 394 EdTWSGCIMGD-TGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKP 437
Cdd:pfam01421 157 P-PGGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 238-435 7.08e-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 [Multi-domain]  Cd Length: 194  Bit Score: 207.47  E-value: 7.08e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKdQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRD 317
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 318 FIKE--KSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTD--LMAVTLAQSLAHNIGIISDKrklasGECKC 393
Cdd:cd04269    80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNllLFAVTMAHELGHNLGMEHDD-----GGCTC 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1965410872 394 EDtwSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFN 435
Cdd:cd04269   155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
529-670 5.13e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 5.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872  529 MDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIG 608
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965410872  609 NIPRLGELDGEITSTLvvqqgRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPV 670
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 530-639 1.06e-34

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: 127.73  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 530 DGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGN 609
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1965410872 610 IPRLGELdgeitSTLVVQQGRTLNCSGGHV 639
Cdd:pfam08516  81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 70-187 2.87e-31

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: 118.96  E-value: 2.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872  70 DTRVRGDLGGPQlTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVK--GGEHCYYQGHIRGNPDSF 147
Cdd:pfam01562  10 PSRRRRSLASES-TYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPpvQTDHCYYQGHVEGHPDSS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1965410872 148 VALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVY 187
Cdd:pfam01562  89 VALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
452-525 1.50e-28

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 108.87  E-value: 1.50e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965410872 452 ETGEECDCGTPAECVLEgaECC--KKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPN 525
Cdd:pfam00200   1 EEGEECDCGSLEECTND--PCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 452-527 2.51e-26

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: 102.77  E-value: 2.51e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1965410872  452 ETGEECDCGTPAECvleGAECCKK--CTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIH 527
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 238-434 3.70e-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: 83.83  E-value: 3.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSvvHTNTYAKSVVNMADLIYKDQL---KTRIVLVAMETWATDNK-FAISENPLITLREFMK 313
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGE--DLEHYILTLMNIVASLYKDPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 314 YRR------DFIKEKSDAVHLFSGSQFESSRS-----GAAYIGGICSLLKGGGVNEfgKTDLM-AVTLAQSLAHNIGIIS 381
Cdd:cd04273    79 WQKklnppnDSDPEHHDHAILLTRQDICRSNGncdtlGLAPVGGMCSPSRSCSINE--DTGLSsAFTIAHELGHVLGMPH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1965410872 382 DKrklASGECKcEDTWSGCIMGDTGYYLPKKFT--QCNIEEYHDFLNSGGGACLF 434
Cdd:cd04273   157 DG---DGNSCG-PEGKDGHIMSPTLGANTGPFTwsKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 238-426 6.32e-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: 79.77  E-value: 6.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 238 KYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKD---QLKTRIVLVAMETWATdNKFA--ISENPLITLREFM 312
Cdd:cd04267     1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKG-EQFAppIDSDASNTLNSFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 313 KYRRDFIKeKSDAVHLFSGSQF-ESSRSGAAYIGGICSLLKGGGVNE-FGKTDLMAVTLAQSLAHNIGIISDkrklASGE 390
Cdd:cd04267    80 FWRAEGPI-RHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAEHD----GGDE 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1965410872 391 CKCEDTWSG-CIMGDT-GYYLPKKFTQCNIEEYHDFLN 426
Cdd:cd04267   155 LAFECDGGGnYIMAPVdSGLNSYRFSQCSIGSIREFLD 192
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 267-378 8.80e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 57.38  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 267 SVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMkyrrDFIKEKS-----DAVHLFSGSQFESSrSGA 341
Cdd:pfam13582   5 SLVNRANTIYERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQ----EVNDTRIgqygyDLGHLFTGRDGGGG-GGI 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1965410872 342 AYIGGICSLLKGGGVNE--FGKTDLMAVTLAQSLAHNIG 378
Cdd:pfam13582  80 AYVGGVCNSGSKFGVNSgsGPVGDTGADTFAHEIGHNFG 118
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 239-433 7.52e-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: 7.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 239 YIELMIVNDHlMFKKHRLSVVHTNTYAKSVVNMADLIYKD--QLKTRIVLVAMETwATDNKFAI-----------SENPL 305
Cdd:cd04272     2 YPELFVVVDY-DHQSEFFSNEQLIRYLAVMVNAANLRYRDlkSPRIRLLLVGITI-SKDPDFEPyihpinygyidAAETL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965410872 306 ITLREFMKYRRDFikEKSDAVHL--------FSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNI 377
Cdd:cd04272    80 ENFNEYVKKKRDY--FNPDVVFLvtgldmstYSGGSLQTGTGGYAYVGGACTENRVAMGEDTPGSYYGVYTMTHELAHLL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1965410872 378 GIISD--------KRKLASGECKCEDtwsGCIM----GDTGYYlpkKFTQCNIEEYHDFLNSGGGACL 433
Cdd:cd04272   158 GAPHDgspppswvKGHPGSLDCPWDD---GYIMsyvvNGERQY---RFSQCSQRQIRNVFRRLGASCL 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.
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