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Conserved domains on  [gi|157012013|ref|NP_034216|]
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disintegrin and metalloproteinase domain-containing protein 24 preproprotein [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 ...
 209-395 4.39e-63

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: 209.39  E-value: 4.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 209 YIKLALVIDHEQYLYRKKNTSLVIRDVLSIMQGINLFLLSVDINVVLLGLTIWTNGNPIPVQ-DIYALLPAFCTWKGTNL 287
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 288 DSQIPYDIAHLFVNYTF-SNYFGIAYVGTVCDKTFGCGIDSIAEDDFLTIGHIVAHEIGHNLGMSHDGILCTCGEESCLM 366
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCIM 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 157012013 367 SATMDS-SQKLSNCSYEVLWAHMINK--SCIH 395
Cdd:cd04269  162 APSPSSlTDAFSNCSYEDYQKFLSRGggQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
492-628 2.93e-56

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 188.72  E-value: 2.93e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013   492 QDGTSCPGD-GYCYEKRCNSHDVHCQRVFGQLAMKASDSCYKELNTRGDRFGNCGFINNEYVRCEISDILCGRIQCDKVG 570
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157012013   571 TLPILQNHYTIHWTHFNSVSCWSTDYHLGMKIaDLGDIKDGTNCGPQHVCIARKCVNK 628
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
415-488 4.66e-33

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.58  E-value: 4.66e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157012013  415 EEGEQCDCGSSENCRRNRCCMPS-CTLRSKAKCDTGLCCNrKCQIQPSGTLCRARENECDLPEWCNGTSHECPED 488
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKtCKLKPGAQCSSGPCCT-NCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 42-160 1.60e-17

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: 79.28  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013   42 ETVKPLRVIVSSKDMSLAG------WMSYSLYFGGQRHIISMKSKNFLESRQLPVFTYNDQGVLFEDRPFVQNDCYYLGF 115
Cdd:pfam01562   1 EVVIPVRLDPSRRRRSLASestyldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157012013  116 VDGDLESMAALTTCfGGFQGILQINDTAYEIKP----KSPSSTFEHLLY 160
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPlekySREEGGHPHVVY 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 ...
 209-395 4.39e-63

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: 209.39  E-value: 4.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 209 YIKLALVIDHEQYLYRKKNTSLVIRDVLSIMQGINLFLLSVDINVVLLGLTIWTNGNPIPVQ-DIYALLPAFCTWKGTNL 287
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 288 DSQIPYDIAHLFVNYTF-SNYFGIAYVGTVCDKTFGCGIDSIAEDDFLTIGHIVAHEIGHNLGMSHDGILCTCGEESCLM 366
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCIM 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 157012013 367 SATMDS-SQKLSNCSYEVLWAHMINK--SCIH 395
Cdd:cd04269  162 APSPSSlTDAFSNCSYEDYQKFLSRGggQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
492-628 2.93e-56

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 188.72  E-value: 2.93e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013   492 QDGTSCPGD-GYCYEKRCNSHDVHCQRVFGQLAMKASDSCYKELNTRGDRFGNCGFINNEYVRCEISDILCGRIQCDKVG 570
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157012013   571 TLPILQNHYTIHWTHFNSVSCWSTDYHLGMKIaDLGDIKDGTNCGPQHVCIARKCVNK 628
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 493-596 1.19e-45

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: 158.16  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  493 DGTSCP-GDGYCYEKRCNSHDVHCQRVFGQLAMKASDSCYKELNTRGDRFGNCGFINNEYVRCEISDILCGRIQCDKVGT 571
Cdd:pfam08516   1 DGTPCNnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 157012013  572 LPILQNHYTIHWTHFNSVSCWSTDY 596
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 209-382 1.18e-37

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: 139.36  E-value: 1.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  209 YIKLALVIDHEQYLYRKKNTSLVIRDVLSIMQGINLFLLSVDINVVLLGLTIWTNGNPIPVQ-DIYALLPAFCTWKGTNL 287
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSgDANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  288 DSQIPYDIAHLFVNYTFSN-YFGIAYVGTVCDKTFGCGIDSIAEDDFLTIGHIVAHEIGHNLGMSHDGIL--CTCGE-ES 363
Cdd:pfam01421  82 KKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPgGG 161

                         170       180
                  ....*....|....*....|.
gi 157012013  364 CLM--SATMDSSQKLSNCSYE 382
Cdd:pfam01421 162 CIMnpSAGSSFPRKFSNCSQE 182
Disintegrin pfam00200
Disintegrin;
415-488 4.66e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.58  E-value: 4.66e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157012013  415 EEGEQCDCGSSENCRRNRCCMPS-CTLRSKAKCDTGLCCNrKCQIQPSGTLCRARENECDLPEWCNGTSHECPED 488
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKtCKLKPGAQCSSGPCCT-NCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-490 1.70e-29

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: 111.63  E-value: 1.70e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157012013   415 EEGEQCDCGSSENCRrNRCCMP-SCTLRSKAKCDTGLCCnRKCQIQPSGTLCRARENECDLPEWCNGTSHECPEDLF 490
Cdd:smart00050   1 EEGEECDCGSPKECT-DPCCDPaTCKLKPGAQCASGPCC-DNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 42-160 1.60e-17

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: 79.28  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013   42 ETVKPLRVIVSSKDMSLAG------WMSYSLYFGGQRHIISMKSKNFLESRQLPVFTYNDQGVLFEDRPFVQNDCYYLGF 115
Cdd:pfam01562   1 EVVIPVRLDPSRRRRSLASestyldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157012013  116 VDGDLESMAALTTCfGGFQGILQINDTAYEIKP----KSPSSTFEHLLY 160
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
298-367 9.11e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 9.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 298 LFV-NYTFsnYFGIAYVGtvcdktFGCGIDSIA------------EDDFLT-IGHIVAHEIGHNLGMSHdgilctCGEES 363
Cdd:COG1913   79 LYApGLNF--VFGLAYLG------GRVAVVSTArlrpefyglppdEELFLErVLKEAVHELGHLFGLGH------CPNPR 144


                 ....
gi 157012013 364 CLMS 367
Cdd:COG1913  145 CVMH 148
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 209-395 4.39e-63

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: 209.39  E-value: 4.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 209 YIKLALVIDHEQYLYRKKNTSLVIRDVLSIMQGINLFLLSVDINVVLLGLTIWTNGNPIPVQ-DIYALLPAFCTWKGTNL 287
Cdd:cd04269    2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 288 DSQIPYDIAHLFVNYTF-SNYFGIAYVGTVCDKTFGCGIDSIAEDDFLTIGHIVAHEIGHNLGMSHDGILCTCGEESCLM 366
Cdd:cd04269   82 LPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCIM 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 157012013 367 SATMDS-SQKLSNCSYEVLWAHMINK--SCIH 395
Cdd:cd04269  162 APSPSSlTDAFSNCSYEDYQKFLSRGggQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
492-628 2.93e-56

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 188.72  E-value: 2.93e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013   492 QDGTSCPGD-GYCYEKRCNSHDVHCQRVFGQLAMKASDSCYKELNTRGDRFGNCGFINNEYVRCEISDILCGRIQCDKVG 570
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157012013   571 TLPILQNHYTIHWTHFNSVSCWSTDYHLGMKIaDLGDIKDGTNCGPQHVCIARKCVNK 628
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTDP-DIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 493-596 1.19e-45

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: 158.16  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  493 DGTSCP-GDGYCYEKRCNSHDVHCQRVFGQLAMKASDSCYKELNTRGDRFGNCGFINNEYVRCEISDILCGRIQCDKVGT 571
Cdd:pfam08516   1 DGTPCNnGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 157012013  572 LPILQNHYTIHWTHFNSVSCWSTDY 596
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 209-382 1.18e-37

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: 139.36  E-value: 1.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  209 YIKLALVIDHEQYLYRKKNTSLVIRDVLSIMQGINLFLLSVDINVVLLGLTIWTNGNPIPVQ-DIYALLPAFCTWKGTNL 287
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSgDANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  288 DSQIPYDIAHLFVNYTFSN-YFGIAYVGTVCDKTFGCGIDSIAEDDFLTIGHIVAHEIGHNLGMSHDGIL--CTCGE-ES 363
Cdd:pfam01421  82 KKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPgGG 161

                         170       180
                  ....*....|....*....|.
gi 157012013  364 CLM--SATMDSSQKLSNCSYE 382
Cdd:pfam01421 162 CIMnpSAGSSFPRKFSNCSQE 182
Disintegrin pfam00200
Disintegrin;
415-488 4.66e-33

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 121.58  E-value: 4.66e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157012013  415 EEGEQCDCGSSENCRRNRCCMPS-CTLRSKAKCDTGLCCNrKCQIQPSGTLCRARENECDLPEWCNGTSHECPED 488
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKtCKLKPGAQCSSGPCCT-NCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-490 1.70e-29

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: 111.63  E-value: 1.70e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157012013   415 EEGEQCDCGSSENCRrNRCCMP-SCTLRSKAKCDTGLCCnRKCQIQPSGTLCRARENECDLPEWCNGTSHECPEDLF 490
Cdd:smart00050   1 EEGEECDCGSPKECT-DPCCDPaTCKLKPGAQCASGPCC-DNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 208-380 9.64e-26

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: 105.40  E-value: 9.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 208 LYIKLALVIDHEqyLYRKKNTSLVIRDVLSIMQGIN-LF---LLSVDINVVLLGLTIWTNGNPIP--VQDIYALLPAFCT 281
Cdd:cd04273    1 RYVETLVVADSK--MVEFHHGEDLEHYILTLMNIVAsLYkdpSLGNSINIVVVRLIVLEDEESGLliSGNAQKSLKSFCR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 282 WK---GTNLDSQIP-YDIAHLFVNYTFSNYF------GIAYVGTVCDKTFGCgidSIAEDDFLTIGHIVAHEIGHNLGMS 351
Cdd:cd04273   79 WQkklNPPNDSDPEhHDHAILLTRQDICRSNgncdtlGLAPVGGMCSPSRSC---SINEDTGLSSAFTIAHELGHVLGMP 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 157012013 352 HDGILCTCGEES---CLMSATMDS---SQKLSNCS 380
Cdd:cd04273  156 HDGDGNSCGPEGkdgHIMSPTLGAntgPFTWSKCS 190
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 209-381 1.67e-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: 89.79  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 209 YIKLALVIDHEQYLYRKKNTSLVIRDVLSIMQGINLFLLSVD----INVVLLGLTIWTNGNPIPVQ--DIYALLPAFCTW 282
Cdd:cd04267    2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNlrlgIRISLEGLQILKGEQFAPPIdsDASNTLNSFSFW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 283 KGTNLdsqIPYDIAHLFVNYTFSN--YFGIAYVGTVCDKTFGCGIDSIAEDDFLTiGHIVAHEIGHNLGMSHDGILCTCG 360
Cdd:cd04267   82 RAEGP---IRHDNAVLLTAQDFIEgdILGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDELAF 157

                        170       180
                 ....*....|....*....|....*..
gi 157012013 361 EE----SCLMSATMDS--SQKLSNCSY 381
Cdd:cd04267  158 ECdgggNYIMAPVDSGlnSYRFSQCSI 184
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 42-160 1.60e-17

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: 79.28  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013   42 ETVKPLRVIVSSKDMSLAG------WMSYSLYFGGQRHIISMKSKNFLESRQLPVFTYNDQGVLFEDRPFVQNDCYYLGF 115
Cdd:pfam01562   1 EVVIPVRLDPSRRRRSLASestyldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157012013  116 VDGDLESMAALTTCfGGFQGILQINDTAYEIKP----KSPSSTFEHLLY 160
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
212-353 1.18e-14

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 72.84  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  212 LALVIDHEqylYRKKNTS-LVIRDVLSIMQGI-NLFLLSVDINVVLLGLTIWTNGNPIP--------VQDIYALLPAFCT 281
Cdd:pfam13688   7 LLVAADCS---YVAAFGGdAAQANIINMVNTAsNVYERDFNISLGLVNLTISDSTCPYTppacstgdSSDRLSEFQDFSA 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157012013  282 WKGtnldsQIPYDIAHLFVNYTFSNYfGIAYVGTVCDKTFGCGIDSIAEDDFLTIG-----HIVAHEIGHNLGMSHD 353
Cdd:pfam13688  84 WRG-----TQNDDLAYLFLMTNCSGG-GLAWLGQLCNSGSAGSVSTRVSGNNVVVStatewQVFAHEIGHNFGAVHD 154
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 293-353 5.31e-12

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: 63.54  E-value: 5.31e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157012013  293 YDIAHLFVNYTFSNYFGIAYVGTVCDKTFGCGI--DSIAEDDFLTIghIVAHEIGHNLGMSHD 353
Cdd:pfam13582  62 YDLGHLFTGRDGGGGGGIAYVGGVCNSGSKFGVnsGSGPVGDTGAD--TFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 274-364 1.98e-08

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: 54.94  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  274 ALLPAFC---TWKGTNLD------SQIPYDIAHLFVNYTFSN-YFGIAYVGTVCDKTFGC-----GI-DSIAEDDFLTIG 337
Cdd:pfam13574  43 DSGNNYCnspTTIVRRLNflsqwrGEQDYCLAHLVTMGTFSGgELGLAYVGQICQKGASSpktntGLsTTTNYGSFNYPT 122

                          90       100       110
                  ....*....|....*....|....*....|
gi 157012013  338 H---IVAHEIGHNLGMSHDgilCTCGEESC 364
Cdd:pfam13574 123 QewdVVAHEVGHNFGATHD---CDGSQYAS 149
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 208-354 1.74e-07

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 52.74  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 208 LYIKLALVIDHEQYLYRKKNtSLVIRDVLSIMQGINLFLLSV---DINVVLLGLTIWTNGNPIPVQD--IYALLPAFCTW 282
Cdd:cd04272    1 VYPELFVVVDYDHQSEFFSN-EQLIRYLAVMVNAANLRYRDLkspRIRLLLVGITISKDPDFEPYIHpiNYGYIDAAETL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 283 KGTNL-----DSQIPYDIAHLFVNYTFSNYF---------GIAYVGTVCDKTFgcgiDSIAEDD--FLTIGHIVAHEIGH 346
Cdd:cd04272   80 ENFNEyvkkkRDYFNPDVVFLVTGLDMSTYSggslqtgtgGYAYVGGACTENR----VAMGEDTpgSYYGVYTMTHELAH 155


                 ....*...
gi 157012013 347 NLGMSHDG 354
Cdd:cd04272  156 LLGAPHDG 163
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 294-381 7.34e-07

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: 49.83  E-value: 7.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 294 DIAHLFVNYTFSNYF-GIAYVGTVCDKTFGCGIDSIAEDDFLTIGHIVAHEIGHNLGMSHDG----------ILCTCGEE 362
Cdd:cd00203   53 DIAILVTRQDFDGGTgGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHdrkdrddyptIDDTLNAE 132

                         90       100
                 ....*....|....*....|....*...
gi 157012013 363 ----SCLMSATMDS-----SQKLSNCSY 381
Cdd:cd00203  133 dddyYSVMSYTKGSfsdgqRKDFSQCDI 160
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 276-371 4.10e-05

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: 45.30  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013  276 LPAFCTWKGTnldsqIPYDIAHLFVNYTFSNY-FGIAYVGTVCD---KTFGCGIDSIAEDDFltigHIVAHEIGHNLGMS 351
Cdd:pfam13583  80 LATLTSWRDS-----LNYDLAYLTLMTGPSGQnVGVAWVGALCSsarQNAKASGVARSRDEW----DIFAHEIGHTFGAV 150

                          90       100
                  ....*....|....*....|
gi 157012013  352 HDgilctCGEESCLMSATMD 371
Cdd:pfam13583 151 HD-----CSSQGEGLSSSTE 165
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 233-369 7.88e-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: 41.64  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 233 RDVLSIMQGI-NLFLLSVDINVVLLGLTIWTNGNPIPVQ-------------DIYALLPAFCTWKGTNLDSQIPYdiAHL 298
Cdd:cd04271   25 RNILNNVNSAsQLYESSFNISLGLRNLTISDASCPSTAVdsapwnlpcnsriDIDDRLSIFSQWRGQQPDDGNAF--WTL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 299 FVNYTFSNYFGIAYVGTVCDK---------TFGCGIDSIAEDDFLtighIVAHEIGHNLGMSHDGILCTCG------EES 363
Cdd:cd04271  103 MTACPSGSEVGVAWLGQLCRTgasdqgnetVAGTNVVVRTSNEWQ----VFAHEIGHTFGAVHDCTSGTCSdgsvgsQQC 178


                 ....*.
gi 157012013 364 CLMSAT 369
Cdd:cd04271  179 CPLSTS 184
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
298-367 9.11e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 9.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157012013 298 LFV-NYTFsnYFGIAYVGtvcdktFGCGIDSIA------------EDDFLT-IGHIVAHEIGHNLGMSHdgilctCGEES 363
Cdd:COG1913   79 LYApGLNF--VFGLAYLG------GRVAVVSTArlrpefyglppdEELFLErVLKEAVHELGHLFGLGH------CPNPR 144


                 ....
gi 157012013 364 CLMS 367
Cdd:COG1913  145 CVMH 148
 
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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