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Conserved domains on  [gi|290560289|pdb|3K7L|A]
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Chain A, Atragin

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein; disintegrin and metalloproteinase domain-containing protein; disintegrin and metalloproteinase domain-containing protein( domain architecture ID 10136397)

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; disintegrin and metalloproteinase domain-containing protein such as snake venom metalloproteinases that impairs hemostasis in envenomed animals; disintegrin and metalloproteinase domain-containing protein, also called metalloproteinase-disintegrin (ADAM), is a membrane-spanning multi-domain protein which may serve as an integrin ligand; protein containing domains ZnMc_adamalysin_II_like, DISIN, and ACR; disintegrin and metalloproteinase domain-containing protein such as snake venom metalloproteinases that impairs hemostasis in envenomed animals; disintegrin and metalloproteinase domain-containing protein, also called metalloproteinase-disintegrin (ADAM), is a membrane-spanning multi-domain protein which may serve as an integrin ligand

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 ...
 14-207 5.11e-96

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: 286.05  E-value: 5.11e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       14 KYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKK 93
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       94 LLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHDRGFCTCGFNKCV 173
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
3K7L_A      174 MSTRRTKPAYQFSSCSVREHQRYLLRDRPQCILN 207
Cdd:cd04269 161 MAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
302-418 1.08e-43

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 149.05  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         302 RNGLPCQNNQGYCYNGKCPIMTNQCIALRGPGVKVSRDSCF-TLNQRTRGCGLCRMEYGRKIPCAAKDVKCGRLFCK--- 377
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTnvs 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
3K7L_A         378 --------------RRNSMICNCSISPRDPN--YGMVEPGTKCGDGMVCSNRQCVDV 418
Cdd:smart00608  81 elpllgehatviysNIGGLVCWSLDYHLGTDpdIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
226-298 7.79e-29

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 107.71  E-value: 7.79e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3K7L_A        226 EVGEECDCGSPADCQ-SACCNATTCKLQHEAQCDSEECCEKCKFKGARAECRAAKDDCDLPELCTGQSAECPTD 298
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 ...
 14-207 5.11e-96

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: 286.05  E-value: 5.11e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       14 KYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKK 93
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       94 LLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHDRGFCTCGFNKCV 173
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
3K7L_A      174 MSTRRTKPAYQFSSCSVREHQRYLLRDRPQCILN 207
Cdd:cd04269 161 MAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 14-209 3.47e-69

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: 217.55  E-value: 3.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         14 KYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKK 93
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         94 LLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHDR--GFCTCG-FN 170
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
3K7L_A        171 KCVM-STRRTKPAYQFSSCSVREHQRYLLRDRPQCILNKP 209
Cdd:pfam01421 161 GCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
302-418 1.08e-43

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 149.05  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         302 RNGLPCQNNQGYCYNGKCPIMTNQCIALRGPGVKVSRDSCF-TLNQRTRGCGLCRMEYGRKIPCAAKDVKCGRLFCK--- 377
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTnvs 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
3K7L_A         378 --------------RRNSMICNCSISPRDPN--YGMVEPGTKCGDGMVCSNRQCVDV 418
Cdd:smart00608  81 elpllgehatviysNIGGLVCWSLDYHLGTDpdIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
226-298 7.79e-29

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 107.71  E-value: 7.79e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3K7L_A        226 EVGEECDCGSPADCQ-SACCNATTCKLQHEAQCDSEECCEKCKFKGARAECRAAKDDCDLPELCTGQSAECPTD 298
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 226-300 1.97e-28

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: 106.62  E-value: 1.97e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3K7L_A         226 EVGEECDCGSPADCQSACCNATTCKLQHEAQCDSEECCEKCKFKGARAECRAAKDDCDLPELCTGQSAECPTDVF 300
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 303-376 7.37e-18

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: 78.43  E-value: 7.37e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3K7L_A        303 NGLPCQNNQGYCYNGKCPIMTNQCIALRGPGVKVSRDSCFT-LNQRTRGCGLCRMEYGRKIPCAAKDVKCGRLFC 376
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEeVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQC 75
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 14-207 5.11e-96

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: 286.05  E-value: 5.11e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       14 KYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKK 93
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       94 LLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHDRGFCTCGFNKCV 173
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                       170       180       190
                ....*....|....*....|....*....|....
3K7L_A      174 MSTRRTKPAYQFSSCSVREHQRYLLRDRPQCILN 207
Cdd:cd04269 161 MAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 14-209 3.47e-69

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: 217.55  E-value: 3.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         14 KYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKK 93
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         94 LLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHDR--GFCTCG-FN 170
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
3K7L_A        171 KCVM-STRRTKPAYQFSSCSVREHQRYLLRDRPQCILNKP 209
Cdd:pfam01421 161 GCIMnPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
302-418 1.08e-43

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 149.05  E-value: 1.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         302 RNGLPCQNNQGYCYNGKCPIMTNQCIALRGPGVKVSRDSCF-TLNQRTRGCGLCRMEYGRKIPCAAKDVKCGRLFCK--- 377
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYeELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTnvs 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
3K7L_A         378 --------------RRNSMICNCSISPRDPN--YGMVEPGTKCGDGMVCSNRQCVDV 418
Cdd:smart00608  81 elpllgehatviysNIGGLVCWSLDYHLGTDpdIGMVKDGTKCGPGKVCINGQCVDV 137
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 14-190 1.25e-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: 151.03  E-value: 1.25e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       14 KYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYR----RLNFHIALIGLEIWSNINEINV-QSDVRATLNLFGE 88
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILKGEQFAPPiDSDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       89 WREKKllpRKRNDNAQLLTGIDFNGTP-VGLAYIGSICNPKTSAAVVQDySSRTRMVAITMAHEMGHNLGMNHDRGFCTC 167
Cdd:cd04267  81 WRAEG---PIRHDNAVLLTAQDFIEGDiLGLAYVGSMCNPYSSVGVVED-TGFTLLTALTMAHELGHNLGAEHDGGDELA 156

                       170       180
                ....*....|....*....|....*...
3K7L_A      168 GFN----KCVMSTRRTKP-AYQFSSCSV 190
Cdd:cd04267 157 FECdgggNYIMAPVDSGLnSYRFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 14-206 2.54e-29

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: 113.49  E-value: 2.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       14 KYIEFYVVVDNIMYRHYKRDQpvIKRKVYEMINTMNMIYR----RLNFHIALIGLEIWSNINE-INVQSDVRATLNLFGE 88
Cdd:cd04273   1 RYVETLVVADSKMVEFHHGED--LEHYILTLMNIVASLYKdpslGNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       89 WrEKKLLPRKRN-----DNAQLLTGIDF-----NGTPVGLAYIGSICNPKTSAAVVQD--YSSrtrmvAITMAHEMGHNL 156
Cdd:cd04273  79 W-QKKLNPPNDSdpehhDHAILLTRQDIcrsngNCDTLGLAPVGGMCSPSRSCSINEDtgLSS-----AFTIAHELGHVL 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
3K7L_A      157 GMNHDRGFCTCGF---NKCVMSTRRTKPAYQF--SSCSVREHQRYLLRDRPQCIL 206
Cdd:cd04273 153 GMPHDGDGNSCGPegkDGHIMSPTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
Disintegrin pfam00200
Disintegrin;
226-298 7.79e-29

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 107.71  E-value: 7.79e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3K7L_A        226 EVGEECDCGSPADCQ-SACCNATTCKLQHEAQCDSEECCEKCKFKGARAECRAAKDDCDLPELCTGQSAECPTD 298
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 226-300 1.97e-28

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: 106.62  E-value: 1.97e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3K7L_A         226 EVGEECDCGSPADCQSACCNATTCKLQHEAQCDSEECCEKCKFKGARAECRAAKDDCDLPELCTGQSAECPTDVF 300
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 14-187 1.15e-20

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: 88.35  E-value: 1.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       14 KYIEFYVVVDNIMYrhykrDQPVIKRKVYEMINTMNMIYR-RLNFHIALIGLEIwsnineinvqsdvratlnlfgewrek 92
Cdd:cd00203   1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRdYLNIRFVLVGVEI-------------------------- 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       93 kllprKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHDRGFCTCGFNKC 172
Cdd:cd00203  50 -----DKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPT 124

                       170
                ....*....|....*
3K7L_A      173 VMSTRRTKPAYQFSS 187
Cdd:cd00203 125 IDDTLNAEDDDYYSV 139
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 303-376 7.37e-18

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: 78.43  E-value: 7.37e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3K7L_A        303 NGLPCQNNQGYCYNGKCPIMTNQCIALRGPGVKVSRDSCFT-LNQRTRGCGLCRMEYGRKIPCAAKDVKCGRLFC 376
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEeVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQC 75
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 15-205 6.94e-17

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 78.93  E-value: 6.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       15 YIEFYVVVDnimYRHYKRDQPVIKRKVY--EMINTMNMIYRRLN---FHIALIGLEI------WSNINEINVQS-DVRAT 82
Cdd:cd04272   2 YPELFVVVD---YDHQSEFFSNEQLIRYlaVMVNAANLRYRDLKsprIRLLLVGITIskdpdfEPYIHPINYGYiDAAET 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       83 LNLFGEWREKKLLPRkRNDNAQLLTGIDF----NGTP----VGLAYIGSICNpKTSAAVVQDySSRTRMVAITMAHEMGH 154
Cdd:cd04272  79 LENFNEYVKKKRDYF-NPDVVFLVTGLDMstysGGSLqtgtGGYAYVGGACT-ENRVAMGED-TPGSYYGVYTMTHELAH 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3K7L_A      155 NLGMNHD-----------RGFCTC----GFnkcVMSTRRTKP-AYQFSSCSVREHQRYLLRDRPQCI 205
Cdd:cd04272 156 LLGAPHDgspppswvkghPGSLDCpwddGY---IMSYVVNGErQYRFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 45-161 2.19e-16

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: 75.10  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         45 INTMNMIYRR-LNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKkllpRKRNDNA---QLLTGIDFNGTpVGLAY 120
Cdd:pfam13582   7 VNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYdlgHLFTGRDGGGG-GGIAY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
3K7L_A        121 IGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHD 161
Cdd:pfam13582  82 VGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
19-182 6.77e-16

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 75.53  E-value: 6.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         19 YVVVDNIMYRHYKRDqpVIKRKVYEMINT-MNMIYRRLNFHIALIGLEIWSNINEI----NVQSDVRATLNLF---GEWR 90
Cdd:pfam13688   8 LVAADCSYVAAFGGD--AAQANIINMVNTaSNVYERDFNISLGLVNLTISDSTCPYtppaCSTGDSSDRLSEFqdfSAWR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         91 EkkllpRKRNDNAQLLTGIDFNGTpvGLAYIGSICNPKTSAAVVQDYSSRTRMV-----AITMAHEMGHNLGMNHDrgFC 165
Cdd:pfam13688  86 G-----TQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVstateWQVFAHEIGHNFGAVHD--CD 156

                         170
                  ....*....|....*..
3K7L_A        166 TCGFNKCVMSTRRTKPA 182
Cdd:pfam13688 157 SSTSSQCCPPSNSTCPA 173
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 43-190 5.01e-14

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: 70.35  E-value: 5.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         43 EMINTMNMIYRRLNFHIALIgleiWSNINEI----------NVQSDVRAT----LNLFGEWREKKllprkRNDNAQLLTG 108
Cdd:pfam13574   9 NVVNRVNQIYEPDDININGG----LVNPGEIpattsasdsgNNYCNSPTTivrrLNFLSQWRGEQ-----DYCLAHLVTM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A        109 IDFNGTPVGLAYIGSIC-----NPKTSAAVVQDYSSRTRMVAIT----MAHEMGHNLGMNHDrgfCTCGFNKC------- 172
Cdd:pfam13574  80 GTFSGGELGLAYVGQICqkgasSPKTNTGLSTTTNYGSFNYPTQewdvVAHEVGHNFGATHD---CDGSQYASsgcerna 156

                         170       180
                  ....*....|....*....|....*....
3K7L_A        173 -----------VMSTRRTKPAYQFSSCSV 190
Cdd:pfam13574 157 atsvcsangsfIMNPASKSNNDLFSPCSI 185
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 19-204 1.34e-12

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: 67.01  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       19 YVVVDNIMYRHYKRD--QPVIKrKVYEMINTMNMIYRRLNF---HIALIGLEIWSNIneINVQSDVRATLNLF------- 86
Cdd:cd04270   6 LLVADHRFYKYMGRGeeETTIN-YLISHIDRVDDIYRNTDWdggGFKGIGFQIKRIR--IHTTPDEVDPGNKFynksfpn 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       87 ---GEWREKKLLPRKRNDN--AQLLTGIDFNGTPVGLAYIGS--------ICNP------------KTSAAVVQDYSSR- 140
Cdd:cd04270  83 wgvEKFLVKLLLEQFSDDVclAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKayyysngkkkylNTGLTTTVNYGKRv 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3K7L_A      141 -TRMVAITMAHEMGHNLGMNHDRGFCTCGFN-----KCVMSTRRTKPAY----QFSSCSVREHQRYLLRDRPQC 204
Cdd:cd04270 163 pTKESDLVTAHELGHNFGSPHDPDIAECAPGesqggNYIMYARATSGDKennkKFSPCSKKSISKVLEVKSNSC 236
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 27-191 9.44e-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: 404471  Cd Length: 203  Bit Score: 61.10  E-value: 9.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A         27 YRHYKRDQPVIKRKVYEMINTMNMIY-RRLNFHIALIGLEiwsNINEINVQSDVRATLNLFGE---WREKKL---LPRKR 99
Cdd:pfam13583  15 YSASFGSVDELRANINATVTTANEVYgRDFNVSLALISDR---DVIYTDSSTDSFNADCSGGDlgnWRLATLtswRDSLN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A        100 NDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAItMAHEMGHNLGMNHDRGFCTCGFN--------K 171
Cdd:pfam13583  92 YDLAYLTLMTGPSGQNVGVAWVGALCSSARQNAKASGVARSRDEWDI-FAHEIGHTFGAVHDCSSQGEGLSsstedgsgQ 170

                         170       180
                  ....*....|....*....|
3K7L_A        172 CVMSTRRTKPAYQFSSCSVR 191
Cdd:pfam13583 171 TIMSYASTASQTAFSPCTIR 190
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 38-176 1.84e-07

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: 51.65  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A       38 KRKVYEMINTMNMIYRR-LNFHIALIGLEIWSN------------INEINVQSDVRATLNLFGEWREKkllpRKRNDNA- 103
Cdd:cd04271  24 RRNILNNVNSASQLYESsFNISLGLRNLTISDAscpstavdsapwNLPCNSRIDIDDRLSIFSQWRGQ----QPDDGNAf 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K7L_A      104 -QLLTGIDfNGTPVGLAYIGSICNPKTSA-----AVVQDYSSRTRMVAITMAHEMGHNLGMNHDRGFCTCGFNK------ 171
Cdd:cd04271 100 wTLMTACP-SGSEVGVAWLGQLCRTGASDqgnetVAGTNVVVRTSNEWQVFAHEIGHTFGAVHDCTSGTCSDGSvgsqqc 178


                ....*
3K7L_A      172 CVMST 176
Cdd:cd04271 179 CPLST 183
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 111-160 8.74e-06

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 46.16  E-value: 8.74e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
3K7L_A      111 FNGTPVGLAYIGSICNPKTSAAV---VQDYSSRTRMVAITM------------AHEMGHNLGMNH 160
Cdd:cd04276  68 IHSPNGGWAYGPSVVDPRTGEILkadVILYSGFLRQDQLWYedllaaslryllAHEVGHTLGLRH 132
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 354-416 7.13e-04

ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS peptidases (A Disintegrin and Metalloproteinase with Thrombospondin Motifs) which is closely related to the ADAM family (pfam08516). Members of the ADAM-TS family have been implicated in a range of diseases. For instance, members of this family have been found to participate directly in processes in the central nervous system (CNS) such as the regulation of brain plasticity.


Pssm-ID: 465496  Cd Length: 68  Bit Score: 37.71  E-value: 7.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
3K7L_A        354 CRMEYGRK-IPCAAKDVK-CGRLFCKRRNSMICncsisprDPNYGMVEPGTKCGDGMVCSNRQCV 416
Cdd:pfam17771  11 CRLIFGPGsTFCPNGDEDvCSKLWCSNPGGSTC-------TTKNLPAADGTPCGNKKWCLNGKCV 68
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 110-160 5.55e-03

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 37.48  E-value: 5.55e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
3K7L_A      110 DFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAI-------TMAHEMGHNLGMNH 160
Cdd:cd04268  53 WIPYNDGTWSYGPSQVDPLTGEILLARVYLYSSFVEYsgarlrnTAEHELGHALGLRH 110
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 144-175 5.87e-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: 37.66  E-value: 5.87e-03
                        10        20        30
                ....*....|....*....|....*....|..
3K7L_A      144 VAITMAHEMGHNLGMNHdrgfctCGFNKCVMS 175
Cdd:cd11375 123 LLKEAVHELGHLFGLDH------CPYYACVMN 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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