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Conserved domains on  [gi|121247243|ref|NP_001073400|]
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a disintegrin and metallopeptidase domain 34-like [Mus musculus]

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 ...
 206-394 1.52e-65

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: 215.17  E-value: 1.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 206 RFIDYFVVIDHKRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEMSKVLGAFCNWKIKT 285
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 286 IGKRVRHDIIHLFVRRSY-GIYLGLAYVGTVClTLNCA--VNSFLSDSLSDMAFIIAHEMGHNFGMMHDGSACTCGLHSC 362
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMC-SPKYSggVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 121247243 363 IMAPHKSNSPK-FSNCSYEEMFSVVTKR--SCLYD 394
Cdd:cd04269  160 IMAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
491-627 1.68e-51

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 1.68e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243   491 ADGIRCSRG-GYCYKMECQRHNRQCREIFGKRSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELTDVLCGRIQCENVI 569
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 121247243   570 QLPQRRNHETVHFTHFSNNTCWTMDYHFGITiDDVGAVSDGTPCAPDHICLDRKCVSK 627
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
415-487 7.03e-36

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 129.67  E-value: 7.03e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121247243  415 EEGEQCDCGNSESCLQDPCC-SSNCVFKPGAKCAFGRCCKNCQFLKAGTVCRQEKNECDLPEWCNGTSGECPGD 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-158 4.68e-24

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: 97.77  E-value: 4.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243   40 EVVIPLRVTVTR------GNNISPGWLSYSLNIGGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEEQPFVQNDCYYHGY 113
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 121247243  114 VDEDPESLVIVNTCFGsLQGTLEINGTTYEIMP----KSSTSTFEHLAY 158
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 206-394 1.52e-65

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: 215.17  E-value: 1.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 206 RFIDYFVVIDHKRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEMSKVLGAFCNWKIKT 285
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 286 IGKRVRHDIIHLFVRRSY-GIYLGLAYVGTVClTLNCA--VNSFLSDSLSDMAFIIAHEMGHNFGMMHDGSACTCGLHSC 362
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMC-SPKYSggVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 121247243 363 IMAPHKSNSPK-FSNCSYEEMFSVVTKR--SCLYD 394
Cdd:cd04269  160 IMAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
491-627 1.68e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 1.68e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243   491 ADGIRCSRG-GYCYKMECQRHNRQCREIFGKRSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELTDVLCGRIQCENVI 569
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 121247243   570 QLPQRRNHETVHFTHFSNNTCWTMDYHFGITiDDVGAVSDGTPCAPDHICLDRKCVSK 627
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 206-396 8.09e-46

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: 162.08  E-value: 8.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  206 RFIDYFVVIDHKRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEMSKVLGAFCNWKIKT 285
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  286 IGKRVRHDIIHLFVRRS-YGIYLGLAYVGTVCLTL-NCAVNSFLSDSLSDMAFIIAHEMGHNFGMMHD--GSACTCG-LH 360
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEfGGTTVGAAYVGGMCSLEySGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 121247243  361 SCIMAPHKSNSP--KFSNCSYEEMFSVVTKR--SCLYDIP 396
Cdd:pfam01421 161 GCIMNPSAGSSFprKFSNCSQEDFEQFLTKQkgACLFNKP 200
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 492-595 9.37e-42

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: 146.99  E-value: 9.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  492 DGIRCSRG-GYCYKMECQRHNRQCREIFGKRSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELTDVLCGRIQCENVIQ 570
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 121247243  571 LPQRRNHETVHFTHFSNNTCWTMDY 595
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
415-487 7.03e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 129.67  E-value: 7.03e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121247243  415 EEGEQCDCGNSESCLQDPCC-SSNCVFKPGAKCAFGRCCKNCQFLKAGTVCRQEKNECDLPEWCNGTSGECPGD 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-489 3.39e-32

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: 119.33  E-value: 3.39e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121247243   415 EEGEQCDCGNSESClQDPCC-SSNCVFKPGAKCAFGRCCKNCQFLKAGTVCRQEKNECDLPEWCNGTSGECPGDVY 489
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-158 4.68e-24

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: 97.77  E-value: 4.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243   40 EVVIPLRVTVTR------GNNISPGWLSYSLNIGGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEEQPFVQNDCYYHGY 113
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 121247243  114 VDEDPESLVIVNTCFGsLQGTLEINGTTYEIMP----KSSTSTFEHLAY 158
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 407-446 6.90e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 34.66  E-value: 6.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 121247243  407 TKCGNNLVEEGEQCDCGNSESclqDPCCSSNCVFKPGAKC 446
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTS---GDGCSATCRLEEGFAC 38
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 206-394 1.52e-65

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: 215.17  E-value: 1.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 206 RFIDYFVVIDHKRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEMSKVLGAFCNWKIKT 285
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 286 IGKRVRHDIIHLFVRRSY-GIYLGLAYVGTVClTLNCA--VNSFLSDSLSDMAFIIAHEMGHNFGMMHDGSACTCGLHSC 362
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMC-SPKYSggVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 121247243 363 IMAPHKSNSPK-FSNCSYEEMFSVVTKR--SCLYD 394
Cdd:cd04269  160 IMAPSPSSLTDaFSNCSYEDYQKFLSRGggQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
491-627 1.68e-51

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 175.24  E-value: 1.68e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243   491 ADGIRCSRG-GYCYKMECQRHNRQCREIFGKRSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELTDVLCGRIQCENVI 569
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 121247243   570 QLPQRRNHETVHFTHFSNNTCWTMDYHFGITiDDVGAVSDGTPCAPDHICLDRKCVSK 627
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 206-396 8.09e-46

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: 162.08  E-value: 8.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  206 RFIDYFVVIDHKRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQTDVVLTKLEVWSQNNLINVEQEMSKVLGAFCNWKIKT 285
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  286 IGKRVRHDIIHLFVRRS-YGIYLGLAYVGTVCLTL-NCAVNSFLSDSLSDMAFIIAHEMGHNFGMMHD--GSACTCG-LH 360
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEfGGTTVGAAYVGGMCSLEySGGVNEDHSKNLESFAVTMAHELGHNLGMQHDdfNGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 121247243  361 SCIMAPHKSNSP--KFSNCSYEEMFSVVTKR--SCLYDIP 396
Cdd:pfam01421 161 GCIMNPSAGSSFprKFSNCSQEDFEQFLTKQkgACLFNKP 200
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 492-595 9.37e-42

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: 146.99  E-value: 9.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  492 DGIRCSRG-GYCYKMECQRHNRQCREIFGKRSRSADEICYMEMNRRGDRFGNCGNDSSKYKICELTDVLCGRIQCENVIQ 570
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 121247243  571 LPQRRNHETVHFTHFSNNTCWTMDY 595
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
415-487 7.03e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 129.67  E-value: 7.03e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121247243  415 EEGEQCDCGNSESCLQDPCC-SSNCVFKPGAKCAFGRCCKNCQFLKAGTVCRQEKNECDLPEWCNGTSGECPGD 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-489 3.39e-32

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: 119.33  E-value: 3.39e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121247243   415 EEGEQCDCGNSESClQDPCC-SSNCVFKPGAKCAFGRCCKNCQFLKAGTVCRQEKNECDLPEWCNGTSGECPGDVY 489
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 40-158 4.68e-24

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: 97.77  E-value: 4.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243   40 EVVIPLRVTVTR------GNNISPGWLSYSLNIGGQRHIITMKPKKNLISRNFLLFTYSDQGDLLEEQPFVQNDCYYHGY 113
Cdd:pfam01562   1 EVVIPVRLDPSRrrrslaSESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 121247243  114 VDEDPESLVIVNTCFGsLQGTLEINGTTYEIMP----KSSTSTFEHLAY 158
Cdd:pfam01562  81 VEGHPDSSVALSTCSG-LRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 206-382 3.34e-22

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: 95.38  E-value: 3.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 206 RFIDYFVVIDHK--RYVHRNNntttcIQDM-LQVVNGINGYY----LQIQTDVVLTKLEVW-SQNNLINVEQEMSKVLGA 277
Cdd:cd04273    1 RYVETLVVADSKmvEFHHGED-----LEHYiLTLMNIVASLYkdpsLGNSINIVVVRLIVLeDEESGLLISGNAQKSLKS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 278 FCNWKiKTIGKRVRHDIIH-----LFVRrsYGIY--------LGLAYVGTVC-LTLNCAVNSflsDSLSDMAFIIAHEMG 343
Cdd:cd04273   76 FCRWQ-KKLNPPNDSDPEHhdhaiLLTR--QDICrsngncdtLGLAPVGGMCsPSRSCSINE---DTGLSSAFTIAHELG 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 121247243 344 HNFGMMHDGSACTCG---LHSCIMAPH-KSNSPKF--SNCSYEEM 382
Cdd:cd04273  150 HVLGMPHDGDGNSCGpegKDGHIMSPTlGANTGPFtwSKCSRRYL 194
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 206-379 6.41e-19

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: 85.16  E-value: 6.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 206 RFIDYFVVIDHKRYVHRNNNTTTCIQDMLQVVNGINGYYLQIQT----DVVLTKLEVWSQNNLINVEQ-EMSKVLGAFCN 280
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 281 WKIKtigKRVRHDIIHLFVRRSY--GIYLGLAYVGTVCltlncavNSFLSDSLS-------DMAFIIAHEMGHNFGMMHD 351
Cdd:cd04267   81 WRAE---GPIRHDNAVLLTAQDFieGDILGLAYVGSMC-------NPYSSVGVVedtgftlLTALTMAHELGHNLGAEHD 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 121247243 352 GSACTC----GLHSCIMAP--HKSNSPKFSNCSY 379
Cdd:cd04267  151 GGDELAfecdGGGNYIMAPvdSGLNSYRFSQCSI 184
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 293-351 2.52e-11

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: 61.23  E-value: 2.52e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  293 DIIHLFVRRSYGIYLGLAYVGTVCL-TLNCAVNSFLSDSLSDMAFIIAHEMGHNFGMMHD 351
Cdd:pfam13582  63 DLGHLFTGRDGGGGGGIAYVGGVCNsGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
205-375 1.10e-10

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 61.28  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  205 HRFIDYFVVIDHkRYV--HRNNNTTTCIQDMLQVVNgiNGYYLQIQTDVVLTKLEVWSQNNLINVEQEM----SKVLGAF 278
Cdd:pfam13688   2 TRTVALLVAADC-SYVaaFGGDAAQANIINMVNTAS--NVYERDFNISLGLVNLTISDSTCPYTPPACStgdsSDRLSEF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  279 CNwkIKTIGKRVRHDIIHLFVRR--SYGiylGLAYVGTVC-------LTLNCAVNSFLSDSLSDmAFIIAHEMGHNFGMM 349
Cdd:pfam13688  79 QD--FSAWRGTQNDDLAYLFLMTncSGG---GLAWLGQLCnsgsagsVSTRVSGNNVVVSTATE-WQVFAHEIGHNFGAV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 121247243  350 HD-----------GSACTCGLH-SCIMAPH-KSNSPKFS 375
Cdd:pfam13688 153 HDcdsstssqccpPSNSTCPAGgRYIMNPSsSPNSTDFS 191
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 225-386 4.54e-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: 59.56  E-value: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  225 NTTTCIqdmLQVVNGINGYYLQ--IQTDVVLTK---LEVW-----SQNNLINVEQEMSKVLGAFCNWkiktIGKRvRHDI 294
Cdd:pfam13574   2 NVTENL---VNVVNRVNQIYEPddININGGLVNpgeIPATtsasdSGNNYCNSPTTIVRRLNFLSQW----RGEQ-DYCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  295 IHLFVRRSY-GIYLGLAYVGTVCLT--LNCAVNSFLSDSLSDMAF--------IIAHEMGHNFGMMHD----GSACTCGL 359
Cdd:pfam13574  74 AHLVTMGTFsGGELGLAYVGQICQKgaSSPKTNTGLSTTTNYGSFnyptqewdVVAHEVGHNFGATHDcdgsQYASSGCE 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 121247243  360 H-----------SCIMAP-HKSNSPKFSNCSYEEMFSVV 386
Cdd:pfam13574 154 RnaatsvcsangSFIMNPaSKSNNDLFSPCSISLICDVL 192
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 291-365 2.78e-08

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: 53.68  E-value: 2.78e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121247243 291 RHDIIHLFVR--RSYGIyLGLAYVGTVCLTLNcAVNSFLSDSL--SDMAFIIAHEMGHNFGMMHDGSACTCGLHSCIMA 365
Cdd:cd00203   51 KADIAILVTRqdFDGGT-GGWAYLGRVCDSLR-GVGVLQDNQSgtKEGAQTIAHELGHALGFYHDHDRKDRDDYPTIDD 127
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 293-378 6.19e-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: 47.61  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243  293 DIIHLFVR-RSYGIYLGLAYVGTVCLTLNCAVNSFLSDSLSDMAFIIAHEMGHNFGMMHDGSACTCGLH--------SCI 363
Cdd:pfam13583  93 DLAYLTLMtGPSGQNVGVAWVGALCSSARQNAKASGVARSRDEWDIFAHEIGHTFGAVHDCSSQGEGLSsstedgsgQTI 172

                          90
                  ....*....|....*.
gi 121247243  364 MAP-HKSNSPKFSNCS 378
Cdd:pfam13583 173 MSYaSTASQTAFSPCT 188
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 296-391 3.32e-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: 45.83  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 296 HLFVRRSY-GIYLGLAYVGT--------VC-----------LTLNCAVNSFLSDS------LSDMAFiiAHEMGHNFGMM 349
Cdd:cd04270  105 HLFTYRDFdMGTLGLAYVGSprdnsaggICekayyysngkkKYLNTGLTTTVNYGkrvptkESDLVT--AHELGHNFGSP 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 121247243 350 HD--GSACTCGLH---SCIMAP-----HKSNSPKFSNCSYEEMFSV--VTKRSC 391
Cdd:cd04270  183 HDpdIAECAPGESqggNYIMYAratsgDKENNKKFSPCSKKSISKVleVKSNSC 236
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 289-392 6.07e-05

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 45.04  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 289 RVRHDIIHLFVRRSYGIY---------LGLAYVGTVCLTLNCAVNSFLSDSLSDMaFIIAHEMGHNFGMMHDGSACT--C 357
Cdd:cd04272   92 YFNPDVVFLVTGLDMSTYsggslqtgtGGYAYVGGACTENRVAMGEDTPGSYYGV-YTMTHELAHLLGAPHDGSPPPswV 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 121247243 358 GLH----SC------IM--APHKSNSPKFSNCSYEEMFSVV--TKRSCL 392
Cdd:cd04272  171 KGHpgslDCpwddgyIMsyVVNGERQYRFSQCSQRQIRNVFrrLGASCL 219
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 271-392 4.30e-04

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: 42.41  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121247243 271 MSKVLGAFCNWKiktiGKRVRHDII--HLFVRRSYGIYLGLAYVGTVCLTL------NCAVNSFLSDSLSDMAFIIAHEM 342
Cdd:cd04271   78 IDDRLSIFSQWR----GQQPDDGNAfwTLMTACPSGSEVGVAWLGQLCRTGasdqgnETVAGTNVVVRTSNEWQVFAHEI 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121247243 343 GHNFGMMHDGSACTCGLHS-----C--------------IMAPHKSNS-PKFSNCSYEEMFSVVTKR----SCL 392
Cdd:cd04271  154 GHTFGAVHDCTSGTCSDGSvgsqqCcplststcdangqyIMNPSSSSGiTEFSPCTIGNICSLLGRNpvrtSCL 227
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 407-446 6.90e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 34.66  E-value: 6.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 121247243  407 TKCGNNLVEEGEQCDCGNSESclqDPCCSSNCVFKPGAKC 446
Cdd:TIGR02232   2 PTCGDGIIEPGEECDDGNTTS---GDGCSATCRLEEGFAC 38
 
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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