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Conserved domains on  [gi|974576780|ref|NP_001305862|]
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disintegrin and metalloproteinase domain-containing protein 11 isoform 3 [Homo sapiens]

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 12019649)

protein containing domains ZnMc_adamalysin_II_like, Disintegrin, and ACR

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 39-238 3.44e-92

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: 281.11  E-value: 3.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780   39 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEqLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 118
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  119 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSHGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKHrssAGDCKC 194
Cdd:pfam01421  80 YLKKrkPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHskNLESFAVTMAHELGHNLGMQHDDF---NGGCKC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 974576780  195 PDiWLGCIMED-TGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKP 238
Cdd:pfam01421 157 PP-GGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
330-468 2.18e-44

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 154.06  E-value: 2.18e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780   330 LDGYYCDHEQGRCYGGRCKTRDRQCQVLWGHAA--ADRFCYEKLNVEGTERGSCGRKGSGWVQCSKQDVLCGFLLCVNIS 407
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAkvAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576780   408 GAPRLGDLVGDISSVTfyhqgKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLP 468
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVD 136
Disintegrin pfam00200
Disintegrin;
253-326 3.37e-27

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 104.63  E-value: 3.37e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974576780  253 EAGEECDCGSVQECSRagGNCC--KKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPN 326
Cdd:pfam00200   1 EEGEECDCGSLEECTN--DPCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 39-238 3.44e-92

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: 281.11  E-value: 3.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780   39 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEqLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 118
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  119 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSHGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKHrssAGDCKC 194
Cdd:pfam01421  80 YLKKrkPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHskNLESFAVTMAHELGHNLGMQHDDF---NGGCKC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 974576780  195 PDiWLGCIMED-TGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKP 238
Cdd:pfam01421 157 PP-GGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 39-236 3.62e-70

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: 224.03  E-value: 3.62e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  39 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKeQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 118
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780 119 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSHGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKhrssaGDCKC 194
Cdd:cd04269   80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHsrNLLLFAVTMAHELGHNLGMEHDD-----GGCTC 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 974576780 195 PDiwLGCIMEDTGFYLPRKFSRCSIDEYNQFLQEGGGSCLFN 236
Cdd:cd04269  155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
330-468 2.18e-44

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 154.06  E-value: 2.18e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780   330 LDGYYCDHEQGRCYGGRCKTRDRQCQVLWGHAA--ADRFCYEKLNVEGTERGSCGRKGSGWVQCSKQDVLCGFLLCVNIS 407
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAkvAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576780   408 GAPRLGDLVGDISSVTfyhqgKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLP 468
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 331-438 2.00e-28

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: 108.86  E-value: 2.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  331 DGYYCDHEQGRCYGGRCKTRDRQCQVLWGHAA--ADRFCYEKLNVEGTERGSCGRKGSGWVQCSKQDVLCGFLLCVNISG 408
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAksAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 974576780  409 APRLGDLvgdisSVTFYHQGKELDCRGGHV 438
Cdd:pfam08516  81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
253-326 3.37e-27

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 104.63  E-value: 3.37e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974576780  253 EAGEECDCGSVQECSRagGNCC--KKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPN 326
Cdd:pfam00200   1 EEGEECDCGSLEECTN--DPCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 253-328 3.43e-26

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 101.61  E-value: 3.43e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974576780   253 EAGEECDCGSVQECsraGGNCCKK--CTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPNLH 328
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 39-238 3.44e-92

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: 281.11  E-value: 3.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780   39 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEqLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 118
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKE-LNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  119 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSHGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKHrssAGDCKC 194
Cdd:pfam01421  80 YLKKrkPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHskNLESFAVTMAHELGHNLGMQHDDF---NGGCKC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 974576780  195 PDiWLGCIMED-TGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKP 238
Cdd:pfam01421 157 PP-GGGCIMNPsAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 39-236 3.62e-70

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: 224.03  E-value: 3.62e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  39 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKeQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRRE 118
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYR-PLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780 119 GLPE--PSDATHLFSGRTFQSTSSGAAYVGGICSLSHGGGVNEYG--NMGAMAVTLAQTLGQNLGMMWNKhrssaGDCKC 194
Cdd:cd04269   80 NLLPrkPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHsrNLLLFAVTMAHELGHNLGMEHDD-----GGCTC 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 974576780 195 PDiwLGCIMEDTGFYLPRKFSRCSIDEYNQFLQEGGGSCLFN 236
Cdd:cd04269  155 GR--STCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
330-468 2.18e-44

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 154.06  E-value: 2.18e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780   330 LDGYYCDHEQGRCYGGRCKTRDRQCQVLWGHAA--ADRFCYEKLNVEGTERGSCGRKGSGWVQCSKQDVLCGFLLCVNIS 407
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAkvAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576780   408 GAPRLGDLVGDISSVTfyhqgKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLP 468
Cdd:smart00608  81 ELPLLGEHATVIYSNI-----GGLVCWSLDYHLGTDPDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 331-438 2.00e-28

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: 108.86  E-value: 2.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  331 DGYYCDHEQGRCYGGRCKTRDRQCQVLWGHAA--ADRFCYEKLNVEGTERGSCGRKGSGWVQCSKQDVLCGFLLCVNISG 408
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAksAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 974576780  409 APRLGDLvgdisSVTFYHQGKELDCRGGHV 438
Cdd:pfam08516  81 LPLLGEH-----ATVIYTNINGVTCWGTDY 105
Disintegrin pfam00200
Disintegrin;
253-326 3.37e-27

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 104.63  E-value: 3.37e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974576780  253 EAGEECDCGSVQECSRagGNCC--KKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPN 326
Cdd:pfam00200   1 EEGEECDCGSLEECTN--DPCCdaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 253-328 3.43e-26

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 101.61  E-value: 3.43e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974576780   253 EAGEECDCGSVQECsraGGNCCKK--CTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPNLH 328
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPatCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 39-226 1.10e-15

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: 75.53  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  39 KYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKE---QLNTRIVLVAMETWADGDKIQVQD-DLLETLARLMV 114
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRStnlRLGIRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780 115 YRREGLPEpSDATHLFSGRTFQSTSS-GAAYVGGICSLSHGGGVNE-YGNMGAMAVTLAQTLGQNLGMMwnkHrSSAGDC 192
Cdd:cd04267   81 WRAEGPIR-HDNAVLLTAQDFIEGDIlGLAYVGSMCNPYSSVGVVEdTGFTLLTALTMAHELGHNLGAE---H-DGGDEL 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 974576780 193 KCPDIWLG-CIMEDT-GFYLPRKFSRCSIDEYNQFL 226
Cdd:cd04267  156 AFECDGGGnYIMAPVdSGLNSYRFSQCSIGSIREFL 191
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 39-235 1.09e-13

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: 69.96  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  39 KYVELIVINDHQLFEQMRQSVVLTsnFAKSVVNLADVIYKEQL---NTRIVLVAMETWADGDK-IQVQDDLLETLARLMV 114
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDLEH--YILTLMNIVASLYKDPSlgnSINIVVVRLIVLEDEESgLLISGNAQKSLKSFCR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780 115 Y-RREGLPEPSDATH-----LFSGRTFQSTSS-----GAAYVGGICSLSHGGGVNEYGNMGAmAVTLAQTLGQNLGMMwn 183
Cdd:cd04273   79 WqKKLNPPNDSDPEHhdhaiLLTRQDICRSNGncdtlGLAPVGGMCSPSRSCSINEDTGLSS-AFTIAHELGHVLGMP-- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974576780 184 kHRSSAGDCKcPDIWLGCIMEDTGFYLPRKF--SRCSIDEYNQFLQEGGGSCLF 235
Cdd:cd04273  156 -HDGDGNSCG-PEGKDGHIMSPTLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 68-179 7.54e-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: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 53.91  E-value: 7.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780   68 SVVNLADVIYKEQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRREGLPEPS-DATHLFSGRTFqSTSSGAAYVG 146
Cdd:pfam13582   5 SLVNRANTIYERDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRIGQYGyDLGHLFTGRDG-GGGGGIAYVG 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 974576780  147 GICSLSHGGGVNeYGNMGA---MAVTLAQTLGQNLG 179
Cdd:pfam13582  84 GVCNSGSKFGVN-SGSGPVgdtGADTFAHEIGHNFG 118
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 40-234 5.87e-07

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 50.43  E-value: 5.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  40 YVELIVIND---HQLFEQMRQsvvLTSNFAkSVVNLADVIYKEQLNTRI--VLVAMETWADGDKIQVQDDLL-------E 107
Cdd:cd04272    2 YPELFVVVDydhQSEFFSNEQ---LIRYLA-VMVNAANLRYRDLKSPRIrlLLVGITISKDPDFEPYIHPINygyidaaE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780 108 TLARLMVY-RREGLPEPSDATHLFSGRTFQSTSSGA--------AYVGGICSlSHGGGVNE-----YGNMGAMAVTLAQT 173
Cdd:cd04272   78 TLENFNEYvKKKRDYFNPDVVFLVTGLDMSTYSGGSlqtgtggyAYVGGACT-ENRVAMGEdtpgsYYGVYTMTHELAHL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974576780 174 LG----QNLGMMWNKHRSSAGDCKcpdiW-LGCIMEdTGFYLPR--KFSRCSIDEYNQFLQEGGGSCL 234
Cdd:cd04272  157 LGaphdGSPPPSWVKGHPGSLDCP----WdDGYIMS-YVVNGERqyRFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
38-215 1.89e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 45.49  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780   38 TKYVELIVINDHQLFEQMRQSVVLTsnFAKSVVNLADVIYKEQLNTRIVLVAMETWADGD----KIQVQDDLLETLARLM 113
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGDAAQA--NIINMVNTASNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576780  114 VYRREGLPEPSDATHLFSGRTFQSTssGAAYVGGICSLSHGGGVNEYGNMGAMAV-------TLAQTLGQNLG------M 180
Cdd:pfam13688  80 DFSAWRGTQNDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVVstatewqVFAHEIGHNFGavhdcdS 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 974576780  181 MWNKHRSSAGDCKCPDIWlGCIM-EDTGFYLpRKFS 215
Cdd:pfam13688 158 STSSQCCPPSNSTCPAGG-RYIMnPSSSPNS-TDFS 191
 
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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