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Conserved domains on  [gi|28201768|sp|Q60718|]
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RecName: Full=Disintegrin and metalloproteinase domain-containing protein 2; Short=ADAM 2; AltName: Full=Fertilin subunit beta; AltName: Full=PH-30; Short=PH30; AltName: Full=PH30-beta; Flags: Precursor

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 12023297)

protein containing domains Pep_M12B_propep, 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 ...
184-381 5.54e-87

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: 272.25  E-value: 5.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768   184 HYLEIHIVVEKQMFEHIGADTAIVTQKIFQLIGLANAIFAPFNLTVILSSLEFWMDENKILTTGDANKLLYRFLKWKQSY 263
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768   264 LV-LRPHDMAFLLVYRN-TTDYVGATYQGKMCDKNYAGGVALHPKaVTLESLAIILVQLLSLSMGLAYDDVNK-CQCG-V 339
Cdd:pfam01421  81 LKkRKPHDVAQLLSGVEfGGTTVGAAYVGGMCSLEYSGGVNEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCPpG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 28201768   340 PVCVMNPEAPHSSGvRAFSNCSMEDFSKFITSQSSHCLQNQP 381
Cdd:pfam01421 160 GGCIMNPSAGSSFP-RKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
475-610 2.69e-53

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 180.25  E-value: 2.69e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768    475 QNGHPCDNRKWICINGTCQSGEQQCQDLFGIDAGFGSSECFWELNSKSDISGSCGISAGGYKECPPNDRMCGKIICKYQS 554
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 28201768    555 ENILKLRSATVIYANISGHVCVSLEYPQGHNeSQKMWVRDGTVCGSNKVCQNQKCV 610
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCV 135
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
32-147 8.14e-32

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: 120.11  E-value: 8.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768    32 QVTVPEKI------RSVTSNG-YETQVTYNLKIEGKTYTLDLMQKP-FLPPNFRVYSYDNAGIMRSLEQKFQNICYFQGY 103
Cdd:pfam01562   1 EVVIPVRLdpsrrrRSLASEStYLDTLSYRLAAFGKKFHLHLTPNRlLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 28201768   104 IEGYPNSMVIVSTCTGLRGFLQFGNVSYGIEPLE----SSSGFEHVIY 147
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
398-469 7.91e-28

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 106.94  E-value: 7.91e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28201768   398 EEDEICDCG-KKGCAemPPPCCNPDTCKLSDGSECSSGICCNSCKLKRKGEVCRLAQDECDVTEYCNGTSEVC 469
Cdd:pfam00200   1 EEGEECDCGsLEECT--NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAEC 71
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
184-381 5.54e-87

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: 272.25  E-value: 5.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768   184 HYLEIHIVVEKQMFEHIGADTAIVTQKIFQLIGLANAIFAPFNLTVILSSLEFWMDENKILTTGDANKLLYRFLKWKQSY 263
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768   264 LV-LRPHDMAFLLVYRN-TTDYVGATYQGKMCDKNYAGGVALHPKaVTLESLAIILVQLLSLSMGLAYDDVNK-CQCG-V 339
Cdd:pfam01421  81 LKkRKPHDVAQLLSGVEfGGTTVGAAYVGGMCSLEYSGGVNEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCPpG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 28201768   340 PVCVMNPEAPHSSGvRAFSNCSMEDFSKFITSQSSHCLQNQP 381
Cdd:pfam01421 160 GGCIMNPSAGSSFP-RKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
185-379 3.76e-63

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 209.01  E-value: 3.76e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768 185 YLEIHIVVEKQMFEHIGADTAIVTQKIFQLIGLANAIFAPFNLTVILSSLEFWMDENKILTTGDANKLLYRFLKWKQSYL 264
Cdd:cd04269   2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768 265 VLR-PHDMAFLLVYRNTT-DYVGATYQGKMCDKNYAGGVALHPKaVTLESLAIILVQLLSLSMGLAYDDvNKCQCGVPVC 342
Cdd:cd04269  82 LPRkPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHS-RNLLLFAVTMAHELGHNLGMEHDD-GGCTCGRSTC 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 28201768 343 VMNPEAphSSGVRAFSNCSMEDFSKFITSQSSHCLQN 379
Cdd:cd04269 160 IMAPSP--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
475-610 2.69e-53

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 180.25  E-value: 2.69e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768    475 QNGHPCDNRKWICINGTCQSGEQQCQDLFGIDAGFGSSECFWELNSKSDISGSCGISAGGYKECPPNDRMCGKIICKYQS 554
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 28201768    555 ENILKLRSATVIYANISGHVCVSLEYPQGHNeSQKMWVRDGTVCGSNKVCQNQKCV 610
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCV 135
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
476-580 1.61e-35

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: 129.66  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768   476 NGHPCDNRKWICINGTCQSGEQQCQDLFGIDAGFGSSECFWELNSKSDISGSCGISAGGYKECPPNDRMCGKIICKYQSE 555
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
                          90       100
                  ....*....|....*....|....*
gi 28201768   556 NILKLRSATVIYANISGHVCVSLEY 580
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
32-147 8.14e-32

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: 120.11  E-value: 8.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768    32 QVTVPEKI------RSVTSNG-YETQVTYNLKIEGKTYTLDLMQKP-FLPPNFRVYSYDNAGIMRSLEQKFQNICYFQGY 103
Cdd:pfam01562   1 EVVIPVRLdpsrrrRSLASEStYLDTLSYRLAAFGKKFHLHLTPNRlLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 28201768   104 IEGYPNSMVIVSTCTGLRGFLQFGNVSYGIEPLE----SSSGFEHVIY 147
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
398-469 7.91e-28

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 106.94  E-value: 7.91e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28201768   398 EEDEICDCG-KKGCAemPPPCCNPDTCKLSDGSECSSGICCNSCKLKRKGEVCRLAQDECDVTEYCNGTSEVC 469
Cdd:pfam00200   1 EEGEECDCGsLEECT--NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAEC 71
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
398-473 1.60e-27

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: 105.85  E-value: 1.60e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28201768    398 EEDEICDCGKKGcaEMPPPCCNPDTCKLSDGSECSSGICCNSCKLKRKGEVCRLAQDECDVTEYCNGTSEVC-EDFF 473
Cdd:smart00050   1 EEGEECDCGSPK--ECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCpPDPY 75
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
184-381 5.54e-87

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: 272.25  E-value: 5.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768   184 HYLEIHIVVEKQMFEHIGADTAIVTQKIFQLIGLANAIFAPFNLTVILSSLEFWMDENKILTTGDANKLLYRFLKWKQSY 263
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768   264 LV-LRPHDMAFLLVYRN-TTDYVGATYQGKMCDKNYAGGVALHPKaVTLESLAIILVQLLSLSMGLAYDDVNK-CQCG-V 339
Cdd:pfam01421  81 LKkRKPHDVAQLLSGVEfGGTTVGAAYVGGMCSLEYSGGVNEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCPpG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 28201768   340 PVCVMNPEAPHSSGvRAFSNCSMEDFSKFITSQSSHCLQNQP 381
Cdd:pfam01421 160 GGCIMNPSAGSSFP-RKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
185-379 3.76e-63

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 209.01  E-value: 3.76e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768 185 YLEIHIVVEKQMFEHIGADTAIVTQKIFQLIGLANAIFAPFNLTVILSSLEFWMDENKILTTGDANKLLYRFLKWKQSYL 264
Cdd:cd04269   2 YVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSNL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768 265 VLR-PHDMAFLLVYRNTT-DYVGATYQGKMCDKNYAGGVALHPKaVTLESLAIILVQLLSLSMGLAYDDvNKCQCGVPVC 342
Cdd:cd04269  82 LPRkPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHS-RNLLLFAVTMAHELGHNLGMEHDD-GGCTCGRSTC 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 28201768 343 VMNPEAphSSGVRAFSNCSMEDFSKFITSQSSHCLQN 379
Cdd:cd04269 160 IMAPSP--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
475-610 2.69e-53

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 180.25  E-value: 2.69e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768    475 QNGHPCDNRKWICINGTCQSGEQQCQDLFGIDAGFGSSECFWELNSKSDISGSCGISAGGYKECPPNDRMCGKIICKYQS 554
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 28201768    555 ENILKLRSATVIYANISGHVCVSLEYPQGHNeSQKMWVRDGTVCGSNKVCQNQKCV 610
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCV 135
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
476-580 1.61e-35

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: 129.66  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768   476 NGHPCDNRKWICINGTCQSGEQQCQDLFGIDAGFGSSECFWELNSKSDISGSCGISAGGYKECPPNDRMCGKIICKYQSE 555
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80
                          90       100
                  ....*....|....*....|....*
gi 28201768   556 NILKLRSATVIYANISGHVCVSLEY 580
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
32-147 8.14e-32

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: 120.11  E-value: 8.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768    32 QVTVPEKI------RSVTSNG-YETQVTYNLKIEGKTYTLDLMQKP-FLPPNFRVYSYDNAGIMRSLEQKFQNICYFQGY 103
Cdd:pfam01562   1 EVVIPVRLdpsrrrRSLASEStYLDTLSYRLAAFGKKFHLHLTPNRlLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 28201768   104 IEGYPNSMVIVSTCTGLRGFLQFGNVSYGIEPLE----SSSGFEHVIY 147
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
398-469 7.91e-28

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 106.94  E-value: 7.91e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28201768   398 EEDEICDCG-KKGCAemPPPCCNPDTCKLSDGSECSSGICCNSCKLKRKGEVCRLAQDECDVTEYCNGTSEVC 469
Cdd:pfam00200   1 EEGEECDCGsLEECT--NDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAEC 71
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
398-473 1.60e-27

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: 105.85  E-value: 1.60e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28201768    398 EEDEICDCGKKGcaEMPPPCCNPDTCKLSDGSECSSGICCNSCKLKRKGEVCRLAQDECDVTEYCNGTSEVC-EDFF 473
Cdd:smart00050   1 EEGEECDCGSPK--ECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCpPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
184-378 5.51e-11

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: 62.64  E-value: 5.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768 184 HYLEIHIVVEKQMFEHIGADTaiVTQKIFQLIGLANAIF------APFNLTVIlsSLEFWMDENKILT-TGDANKLLYRF 256
Cdd:cd04273   1 RYVETLVVADSKMVEFHHGED--LEHYILTLMNIVASLYkdpslgNSINIVVV--RLIVLEDEESGLLiSGNAQKSLKSF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28201768 257 LKWKQSYLVLRP-----HDMAFLL------VYRNTTDYVGATYQGKMCDKNYAGGVAlhpkavtlE----SLAIILVQLL 321
Cdd:cd04273  77 CRWQKKLNPPNDsdpehHDHAILLtrqdicRSNGNCDTLGLAPVGGMCSPSRSCSIN--------EdtglSSAFTIAHEL 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28201768 322 SLSMGLAYDDV-NKCQCGVPVC-VMNPEAPHSSGVRAFSNCSMEDFSKFITSQSSHCLQ 378
Cdd:cd04273 149 GHVLGMPHDGDgNSCGPEGKDGhIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
 
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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