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Conserved domains on  [gi|1958679644|ref|XP_038949072|]
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disintegrin and metalloproteinase domain-containing protein 28 isoform X2 [Rattus norvegicus]

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 ...
 206-400 5.55e-88

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: 274.88  E-value: 5.55e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 206 KYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGND 285
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 286 LLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVCV 365
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958679644 366 MEQSLRFHmPTDFSSCSRDNYRRFLEEKLSHCLFN 400
Cdd:cd04269   161 MAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
496-623 1.96e-43

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 153.28  E-value: 1.96e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644  496 NGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQ-NEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGSG 574
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679644  575 ------DLPWKGLTIAFLTCKLFD-PEDINQGVDMVANGTKCGNNKVCINAECVDM 623
Cdd:smart00608  82 lpllgeHATVIYSNIGGLVCWSLDyHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 31-155 2.16e-35

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: 130.13  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644  31 EVVYPIRL-HLLHKRETKEPEPKETfetELRYKMTVNGKVVELYLKKNNKLLAPGYLETYYNSSGNKVTTSPQIMDSCYY 109
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958679644 110 QGHIINEKDSAASISMCQGLRGYFSQADERYFIEPLSSEILDEQAH 155
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
Disintegrin pfam00200
Disintegrin;
419-491 8.71e-35

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 8.71e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679644 419 EMNEDCDCGTPKECT-NKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVD 491
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 206-400 5.55e-88

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: 274.88  E-value: 5.55e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 206 KYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGND 285
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 286 LLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVCV 365
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958679644 366 MEQSLRFHmPTDFSSCSRDNYRRFLEEKLSHCLFN 400
Cdd:cd04269   161 MAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 206-402 1.44e-82

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: 261.08  E-value: 1.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 206 KYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGND 285
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 286 LLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLS--CKC-PSE 362
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958679644 363 VCVMEQSLRFHMPTDFSSCSRDNYRRFLEEKLSHCLFNSP 402
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
496-623 1.96e-43

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 153.28  E-value: 1.96e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644  496 NGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQ-NEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGSG 574
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679644  575 ------DLPWKGLTIAFLTCKLFD-PEDINQGVDMVANGTKCGNNKVCINAECVDM 623
Cdd:smart00608  82 lpllgeHATVIYSNIGGLVCWSLDyHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 31-155 2.16e-35

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: 130.13  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644  31 EVVYPIRL-HLLHKRETKEPEPKETfetELRYKMTVNGKVVELYLKKNNKLLAPGYLETYYNSSGNKVTTSPQIMDSCYY 109
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958679644 110 QGHIINEKDSAASISMCQGLRGYFSQADERYFIEPLSSEILDEQAH 155
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
Disintegrin pfam00200
Disintegrin;
419-491 8.71e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 8.71e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679644 419 EMNEDCDCGTPKECT-NKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVD 491
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 419-493 3.90e-34

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: 124.73  E-value: 3.90e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679644  419 EMNEDCDCGTPKECTNKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVDRF 493
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 496-573 5.67e-26

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: 102.69  E-value: 5.67e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679644 496 NGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQ-NEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGS 573
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVK 79
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
324-394 1.03e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.71  E-value: 1.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679644 324 GIVQDHSNYHLRVAGTMAHEMGHNLGMIHdylsckCPSEVCVME--QSLRfhmPTDFSS---CSRDnyRRFLEEKL 394
Cdd:COG1913   111 GLPPDEELFLERVLKEAVHELGHLFGLGH------CPNPRCVMHfsNSLE---ELDRKPpsfCPSC--RRKLRRKL 175
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 206-400 5.55e-88

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: 274.88  E-value: 5.55e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 206 KYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGND 285
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 286 LLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVCV 365
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958679644 366 MEQSLRFHmPTDFSSCSRDNYRRFLEEKLSHCLFN 400
Cdd:cd04269   161 MAPSPSSL-TDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 206-402 1.44e-82

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: 261.08  E-value: 1.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 206 KYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGND 285
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 286 LLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLS--CKC-PSE 362
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958679644 363 VCVMEQSLRFHMPTDFSSCSRDNYRRFLEEKLSHCLFNSP 402
Cdd:pfam01421 161 GCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
496-623 1.96e-43

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 153.28  E-value: 1.96e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644  496 NGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQ-NEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGSG 574
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679644  575 ------DLPWKGLTIAFLTCKLFD-PEDINQGVDMVANGTKCGNNKVCINAECVDM 623
Cdd:smart00608  82 lpllgeHATVIYSNIGGLVCWSLDyHLGTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 206-391 8.55e-43

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: 153.73  E-value: 8.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 206 KYIEYYVVLDNGEFKKYNKNLDEIRKRVHEMANYVNMLYNKLDAH----VALVGMEIWTDEDKI-KITPDANTTLENFSK 280
Cdd:cd04267     1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTNLRlgirISLEGLQILKGEQFApPIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 281 WRGNDllkRKHHDVAQLISSTDF-SGSTVGLAFMSSMCSPYHSVGIVQDHsNYHLRVAGTMAHEMGHNLGMIHDYLSCKC 359
Cdd:cd04267    81 WRAEG---PIRHDNAVLLTAQDFiEGDILGLAYVGSMCNPYSSVGVVEDT-GFTLLTALTMAHELGHNLGAEHDGGDELA 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958679644 360 PSEV----CVMEQSLRFHMPTDFSSCSRDNYRRFLE 391
Cdd:cd04267   157 FECDgggnYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 31-155 2.16e-35

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: 130.13  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644  31 EVVYPIRL-HLLHKRETKEPEPKETfetELRYKMTVNGKVVELYLKKNNKLLAPGYLETYYNSSGNKVTTSPQIMDSCYY 109
Cdd:pfam01562   1 EVVIPVRLdPSRRRRSLASESTYLD---TLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958679644 110 QGHIINEKDSAASISMCQGLRGYFSQADERYFIEPLSSEILDEQAH 155
Cdd:pfam01562  78 QGHVEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSREEGGH 123
Disintegrin pfam00200
Disintegrin;
419-491 8.71e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 8.71e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679644 419 EMNEDCDCGTPKECT-NKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVD 491
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 419-493 3.90e-34

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: 124.73  E-value: 3.90e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679644  419 EMNEDCDCGTPKECTNKCCDAETCKIKAGFQCALGECCEKCQLKKPGVVCRAAKDECDLPEMCDGKSSHCPVDRF 493
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 206-399 1.80e-32

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: 124.66  E-value: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 206 KYIEYYVVLDNGEFKKYNKnlDEIRKRVHEMANYVNMLYNklDA------HVALVGMEIWTDEDK-IKITPDANTTLENF 278
Cdd:cd04273     1 RYVETLVVADSKMVEFHHG--EDLEHYILTLMNIVASLYK--DPslgnsiNIVVVRLIVLEDEESgLLISGNAQKSLKSF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 279 SKWR----GNDLLKRKHHDVAQLISSTDFSGS-----TVGLAFMSSMCSPYHSVGIVQDHsnyHLRVAGTMAHEMGHNLG 349
Cdd:cd04273    77 CRWQkklnPPNDSDPEHHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINEDT---GLSSAFTIAHELGHVLG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958679644 350 MIHDYLSCKCPSEV---CVMEQSLRFHM-PTDFSSCSRDNYRRFLEEKLSHCLF 399
Cdd:cd04273   154 MPHDGDGNSCGPEGkdgHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCLL 207
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 496-573 5.67e-26

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: 102.69  E-value: 5.67e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679644 496 NGFPCQNGHGYCLKGNCPTLQQQCMDMWGPETKVANKSCYKQ-NEGGSKYGYCHVENGTHMPCKAKDAMCGKLFCEGGS 573
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVK 79
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 206-390 1.51e-22

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: 94.90  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 206 KYIEYYVVLDNGEFKkynknLDEIRKRVHEMANYVnmlynkldahvalvgMEIWTDEDKIKITPdanttlenfSKWRgnd 285
Cdd:cd00203     1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIA---------------MQIWRDYLNIRFVL---------VGVE--- 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 286 llkRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVCV 365
Cdd:cd00203    49 ---IDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTI 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958679644 366 ME------QSLRFHM-----------PTDFSSCSRDNYRRFL 390
Cdd:cd00203   126 DDtlnaedDDYYSVMsytkgsfsdgqRKDFSQCDIDQINKLY 167
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 207-398 3.85e-15

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 75.08  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 207 YIEYYVVLDNGEFKKYNKNLDEIRkRVHEMANYVNMLYNKLDA---HVALVGMEIWTDED-KIKITP------DANTTLE 276
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSNEQLIR-YLAVMVNAANLRYRDLKSpriRLLLVGITISKDPDfEPYIHPinygyiDAAETLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 277 NFskwrgNDLLKRKHH----DVAQLIS----STDFSGS----TVGLAFMSSMCSPyHSVGIVQD--HSNYHLRvagTMAH 342
Cdd:cd04272    81 NF-----NEYVKKKRDyfnpDVVFLVTgldmSTYSGGSlqtgTGGYAYVGGACTE-NRVAMGEDtpGSYYGVY---TMTH 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679644 343 EMGHNLGMIHD-----------YLSCKCP-SEVCVM---EQSLRFHMptdFSSCSRDNYRRFLEEKLSHCL 398
Cdd:cd04272   152 ELAHLLGAPHDgspppswvkghPGSLDCPwDDGYIMsyvVNGERQYR---FSQCSQRQIRNVFRRLGASCL 219
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 238-353 4.96e-15

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: 72.02  E-value: 4.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 238 NYVNMLYNK-LDAHVALVGMEIWTDEDKIKITPDANTTLENFSKWRGNdllkRKHH---DVAQLISSTDFSGsTVGLAFM 313
Cdd:pfam13582   8 NRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQygyDLGHLFTGRDGGG-GGGIAYV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958679644 314 SSMCSPYHSVGIVQDHSNYHLRVAGTMAHEMGHNLGMIHD 353
Cdd:pfam13582  83 GGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
211-353 1.52e-12

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 67.06  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 211 YVVLDNGEFKKYNknLDEIRKRVHEMANYV-NMLYNKLDAHVALVGMEIWTDED----KIKITPDANTTLENF---SKWR 282
Cdd:pfam13688   8 LVAADCSYVAAFG--GDAAQANIINMVNTAsNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFqdfSAWR 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679644 283 GNDllkrkHHDVAQLISSTDFSgsTVGLAFMSSMCSPYHSVGIVQDHSNYHLRV-----AGTMAHEMGHNLGMIHD 353
Cdd:pfam13688  86 GTQ-----NDDLAYLFLMTNCS--GGGLAWLGQLCNSGSAGSVSTRVSGNNVVVstateWQVFAHEIGHNFGAVHD 154
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 235-391 1.48e-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: 372637  Cd Length: 193  Bit Score: 64.19  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 235 EMANYVNMLYNKLDAHVALvgmeIWTDEDKIKITPDAN-----------TTLEN---FSKWRGNdllkrKHHDVAQLISS 300
Cdd:pfam13574   9 NVVNRVNQIYEPDDINING----GLVNPGEIPATTSASdsgnnycnsptTIVRRlnfLSQWRGE-----QDYCLAHLVTM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 301 TDFSGSTVGLAFMSSMC-----SPYHSVGIV----QDHSNYHLRVAGTMAHEMGHNLGMIHDYLSCKCPSEVC------- 364
Cdd:pfam13574  80 GTFSGGELGLAYVGQICqkgasSPKTNTGLStttnYGSFNYPTQEWDVVAHEVGHNFGATHDCDGSQYASSGCernaats 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958679644 365 VMEQSLRFHMP-------TDFSSCSRDNYRRFLE 391
Cdd:pfam13574 160 VCSANGSFIMNpasksnnDLFSPCSISLICDVLG 193
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 268-398 3.17e-11

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: 63.98  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 268 TPDANTTLENFSKWRGNdllkRKHHDVAQLISSTDF-SGSTVGLAFMSSMCSPYHSVGIVQDHS--NYHLRVAG---TMA 341
Cdd:cd04271    75 RIDIDDRLSIFSQWRGQ----QPDDGNAFWTLMTACpSGSEVGVAWLGQLCRTGASDQGNETVAgtNVVVRTSNewqVFA 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679644 342 HEMGHNLGMIHDYLSCKCPS------EVCVMEQSL-----RFHM-P------TDFSSCSRDNYRRFLEEK--LSHCL 398
Cdd:cd04271   151 HEIGHTFGAVHDCTSGTCSDgsvgsqQCCPLSTSTcdangQYIMnPssssgiTEFSPCTIGNICSLLGRNpvRTSCL 227
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 216-385 1.73e-09

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: 58.40  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 216 NGEFKKYNKNLDEIRKRVHEMANYVNMLY-NKLDAHVALVGME--IWTDEDKIKITPD------ANTTLENFSKWRGNdl 286
Cdd:pfam13583  12 DCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSSTDSFNADcsggdlGNWRLATLTSWRDS-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 287 lkrKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHsvgivQDHSNYHLRVAG----TMAHEMGHNLGMIHDYLSCKCPSE 362
Cdd:pfam13583  90 ---LNYDLAYLTLMTGPSGQNVGVAWVGALCSSAR-----QNAKASGVARSRdewdIFAHEIGHTFGAVHDCSSQGEGLS 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958679644 363 VCVMEQSLRFHMP-------TDFSSCSRDN 385
Cdd:pfam13583 162 SSTEDGSGQTIMSyastasqTAFSPCTIRN 191
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 211-397 1.22e-07

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: 53.53  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 211 YVVLDNGEFKKYNKNLDEIR-KRVHEMANYVNMLYNKLDAHVALV-GMEIWTDEDKIKITPDANTTLENF---------- 278
Cdd:cd04270     6 LLVADHRFYKYMGRGEEETTiNYLISHIDRVDDIYRNTDWDGGGFkGIGFQIKRIRIHTTPDEVDPGNKFynksfpnwgv 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 279 SKWRgNDLLKRKHHD---VAQLISSTDFSGSTVGLAFMSS--------MCSP----------YHSVGIVQDhSNYHLRVA 337
Cdd:cd04270    86 EKFL-VKLLLEQFSDdvcLAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKayyysngkkkYLNTGLTTT-VNYGKRVP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679644 338 G-----TMAHEMGHNLGMIHDYLSCKC-PSEvcvmEQSLRFHMPT-----------DFSSCSRDNYRRFLEEKLSHC 397
Cdd:cd04270   164 TkesdlVTAHELGHNFGSPHDPDIAECaPGE----SQGGNYIMYAratsgdkennkKFSPCSKKSISKVLEVKSNSC 236
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
324-394 1.03e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.71  E-value: 1.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679644 324 GIVQDHSNYHLRVAGTMAHEMGHNLGMIHdylsckCPSEVCVME--QSLRfhmPTDFSS---CSRDnyRRFLEEKL 394
Cdd:COG1913   111 GLPPDEELFLERVLKEAVHELGHLFGLGH------CPNPRCVMHfsNSLE---ELDRKPpsfCPSC--RRKLRRKL 175
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 284-366 1.28e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 40.36  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679644 284 NDLLKRKHHDVAQLISSTDFSGSTVGLAFMSSMCSPYHSVGIV-------------QDHSNYHLRVAGTMAHEMGHNLGM 350
Cdd:cd11375    58 DALLKLKPPDADCVLGVTDVDLYEPGLNFVFGLADGGSGVAVVstarlrpefyglpPDEGLFLERLLKEAVHELGHLFGL 137

                          90
                  ....*....|....*.
gi 1958679644 351 IHdylsckCPSEVCVM 366
Cdd:cd11375   138 DH------CPYYACVM 147
 
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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