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Conserved domains on  [gi|255917952]
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Chain A, AAHIV

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 10136411)

protein containing domains ZnMc_adamalysin_II_like, DISIN, and ACR

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 ...
 5-199 1.13e-90

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: 272.18  E-value: 1.13e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   5 KYVETVFVVDKAMVTKYNGDLDKIKTKMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTY 84
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  85 LLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCI 164
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 255917952 165 MGPSISPePSKFFSNCSYIQCWDFIMNHNPECIDN 199
Cdd:cd04269  161 MAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
295-413 2.95e-45

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 153.28  E-value: 2.95e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   295 NGEPCLDNYGYCYNGNCPIMYHQCYALFGADIYEAEDSCFES-NKKGNYYGYCRKENGKKIPCASEDVKCGRLYCKD--- 370
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNvse 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 255917952   371 -----------DSPGQNNPCKMFYSNDDEH--KGMVLPGTKCADGKVCSNGHCVDV 413
Cdd:smart00608  82 lpllgehatviYSNIGGLVCWSLDYHLGTDpdIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 218-292 2.17e-35

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: 125.11  E-value: 2.17e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255917952   218 EVGEECDCGTPENCQNPCCDAATCKLKSGSQCGHGKCCEQCKFRTSGTECRASMSECDPAEHCTGQSSECPADVF 292
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 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 ...
 5-199 1.13e-90

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: 272.18  E-value: 1.13e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   5 KYVETVFVVDKAMVTKYNGDLDKIKTKMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTY 84
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  85 LLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCI 164
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 255917952 165 MGPSISPePSKFFSNCSYIQCWDFIMNHNPECIDN 199
Cdd:cd04269  161 MAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 5-201 8.20e-64

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: 203.69  E-value: 8.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952    5 KYVETVFVVDKAMVTKYNGDLDKIKTKMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTY 84
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   85 LLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDD--GYCYCGGYP 162
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 255917952  163 -CIMGPSISPEPSKFFSNCSYIQCWDFIMNHNPECIDNEP 201
Cdd:pfam01421 161 gCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
295-413 2.95e-45

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 153.28  E-value: 2.95e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   295 NGEPCLDNYGYCYNGNCPIMYHQCYALFGADIYEAEDSCFES-NKKGNYYGYCRKENGKKIPCASEDVKCGRLYCKD--- 370
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNvse 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 255917952   371 -----------DSPGQNNPCKMFYSNDDEH--KGMVLPGTKCADGKVCSNGHCVDV 413
Cdd:smart00608  82 lpllgehatviYSNIGGLVCWSLDYHLGTDpdIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 218-292 2.17e-35

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: 125.11  E-value: 2.17e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255917952   218 EVGEECDCGTPENCQNPCCDAATCKLKSGSQCGHGKCCEQCKFRTSGTECRASMSECDPAEHCTGQSSECPADVF 292
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
218-290 9.26e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 115.42  E-value: 9.26e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255917952  218 EVGEECDCGTPENCQ-NPCCDAATCKLKSGSQCGHGKCCEQCKFRTSGTECRASMSECDPAEHCTGQSSECPAD 290
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 295-368 2.59e-20

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: 85.36  E-value: 2.59e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255917952  295 NGEPCLDNYGYCYNGNCPIMYHQCYALFGADIYEAEDSCFES-NKKGNYYGYCRKENGKKIPCASEDVKCGRLYC 368
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQC 75
metallo_CpaA NF033511
metalloendopeptidase CpaA;
138-179 6.83e-04

metalloendopeptidase CpaA;


Pssm-ID: 411150 [Multi-domain]  Cd Length: 575  Bit Score: 42.00  E-value: 6.83e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 255917952 138 IMAHEMGHNLGIHHDD----GYCYCGGYPC---IMGPSISPepskFFSN 179
Cdd:NF033511 496 VMRHEFGHNMGLYHGDstniGSPYGFGHPLgstIMGGNNIP----YYSS 540
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
135-181 8.84e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.86  E-value: 8.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255917952 135 LAVIMAHEMGHNLGIHHddgycyCGGYPCIMGPSISPE-----PSKFFSNCS 181
Cdd:COG1913  123 VLKEAVHELGHLFGLGH------CPNPRCVMHFSNSLEeldrkPPSFCPSCR 168
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 5-199 1.13e-90

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: 272.18  E-value: 1.13e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   5 KYVETVFVVDKAMVTKYNGDLDKIKTKMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTY 84
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  85 LLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCI 164
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 255917952 165 MGPSISPePSKFFSNCSYIQCWDFIMNHNPECIDN 199
Cdd:cd04269  161 MAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 5-201 8.20e-64

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: 203.69  E-value: 8.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952    5 KYVETVFVVDKAMVTKYNGDLDKIKTKMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTY 84
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   85 LLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDD--GYCYCGGYP 162
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDfnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 255917952  163 -CIMGPSISPEPSKFFSNCSYIQCWDFIMNHNPECIDNEP 201
Cdd:pfam01421 161 gCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 5-189 5.42e-46

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: 157.20  E-value: 5.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   5 KYVETVFVVDKAMVTKYNGDLDKIKTKMYEAANNMNEMYRYM----FFRVVMVGLIIWTEEDKITV-KPDVDYTLNAFAE 79
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTnlrlGIRISLEGLQILKGEQFAPPiDSDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  80 WRKTYLlaeKKHDNAQLITGIDFR-GSIIGYAYIGSMCHPKRSVGIIQDYSPiNLVLAVIMAHEMGHNLGIHHDDGYC-- 156
Cdd:cd04267   81 WRAEGP---IRHDNAVLLTAQDFIeGDILGLAYVGSMCNPYSSVGVVEDTGF-TLLTALTMAHELGHNLGAEHDGGDEla 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 255917952 157 --YCGGYPCIMGPSISPEPSKFFSNCSYIQCWDFI 189
Cdd:cd04267  157 feCDGGGNYIMAPVDSGLNSYRFSQCSIGSIREFL 191
ACR smart00608
ADAM Cysteine-Rich Domain;
295-413 2.95e-45

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 153.28  E-value: 2.95e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   295 NGEPCLDNYGYCYNGNCPIMYHQCYALFGADIYEAEDSCFES-NKKGNYYGYCRKENGKKIPCASEDVKCGRLYCKD--- 370
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEElNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNvse 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 255917952   371 -----------DSPGQNNPCKMFYSNDDEH--KGMVLPGTKCADGKVCSNGHCVDV 413
Cdd:smart00608  82 lpllgehatviYSNIGGLVCWSLDYHLGTDpdIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 218-292 2.17e-35

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: 125.11  E-value: 2.17e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255917952   218 EVGEECDCGTPENCQNPCCDAATCKLKSGSQCGHGKCCEQCKFRTSGTECRASMSECDPAEHCTGQSSECPADVF 292
Cdd:smart00050   1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 5-198 3.24e-34

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: 126.20  E-value: 3.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   5 KYVETVFVVDKAMVTKYNGD--LDKIKTKMyeaaNNMNEMYRY----MFFRVVMVGLIIWTEEDK-ITVKPDVDYTLNAF 77
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEdlEHYILTLM----NIVASLYKDpslgNSINIVVVRLIVLEDEESgLLISGNAQKSLKSF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  78 AEWRKTYL----LAEKKHDNAQLITGIDFRGS-----IIGYAYIGSMCHPKRSVGIIQDyspINLVLAVIMAHEMGHNLG 148
Cdd:cd04273   77 CRWQKKLNppndSDPEHHDHAILLTRQDICRSngncdTLGLAPVGGMCSPSRSCSINED---TGLSSAFTIAHELGHVLG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255917952 149 IHHDDGYCYCGGY---PCIMGPSISPEPSKFF-SNCS--YIQcwDFIMNHNPECID 198
Cdd:cd04273  154 MPHDGDGNSCGPEgkdGHIMSPTLGANTGPFTwSKCSrrYLT--SFLDTGDGNCLL 207
Disintegrin pfam00200
Disintegrin;
218-290 9.26e-32

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 115.42  E-value: 9.26e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255917952  218 EVGEECDCGTPENCQ-NPCCDAATCKLKSGSQCGHGKCCEQCKFRTSGTECRASMSECDPAEHCTGQSSECPAD 290
Cdd:pfam00200   1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 5-189 1.91e-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: 93.36  E-value: 1.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   5 KYVETVFVVDKAMVtkyngDLDKIKTKMYEAANNMNEMYRYMFfrvvmvgliiwteedKITVKPdvdytlnafaewrktY 84
Cdd:cd00203    1 KVIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRDYL---------------NIRFVL---------------V 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  85 LLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCI 164
Cdd:cd00203   46 GVEIDKADIAILVTRQDFDGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTI 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 255917952 165 ----------MGPSISPEPSKF-------FSNCSYIQCWDFI 189
Cdd:cd00203  126 ddtlnaedddYYSVMSYTKGSFsdgqrkdFSQCDIDQINKLY 167
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 295-368 2.59e-20

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: 85.36  E-value: 2.59e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255917952  295 NGEPCLDNYGYCYNGNCPIMYHQCYALFGADIYEAEDSCFES-NKKGNYYGYCRKENGKKIPCASEDVKCGRLYC 368
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEvNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQC 75
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
10-171 6.64e-13

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 67.06  E-value: 6.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   10 VFVVDKAMVTKYNGDldKIKTKMYEAANN-MNEMYRYMFFRVVMVGLIIWTEED----KITVKPDVDYTLNAF---AEWR 81
Cdd:pfam13688   8 LVAADCSYVAAFGGD--AAQANIINMVNTaSNVYERDFNISLGLVNLTISDSTCpytpPACSTGDSSDRLSEFqdfSAWR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   82 KTYllaekKHDNAQLITGIDFRGSiiGYAYIGSMCHPKRSVGIIQDYSPINLV-----LAVIMAHEMGHNLGIHHD---- 152
Cdd:pfam13688  86 GTQ-----NDDLAYLFLMTNCSGG--GLAWLGQLCNSGSAGSVSTRVSGNNVVvstatEWQVFAHEIGHNFGAVHDcdss 158

                         170       180
                  ....*....|....*....|....*..
gi 255917952  153 --DGYC-----YCG-GYPCIMGPSISP 171
Cdd:pfam13688 159 tsSQCCppsnsTCPaGGRYIMNPSSSP 185
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 34-152 6.92e-13

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: 65.08  E-value: 6.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   34 EAANNMNEmyRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTyllaEKKHDNA---QLITGIDFRGSIiGYA 110
Cdd:pfam13582   8 NRANTIYE--RDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDT----RIGQYGYdlgHLFTGRDGGGGG-GIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 255917952  111 YIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHD 152
Cdd:pfam13582  81 YVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 66-209 4.46e-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: 372637  Cd Length: 193  Bit Score: 55.71  E-value: 4.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   66 VKPDVDYTLNAFAEWRktyllAEKKHDNAQLITGIDFRGSIIGYAYIGSMCH-----PKRSVGIIqdySPINLVLAV--- 137
Cdd:pfam13574  51 SPTTIVRRLNFLSQWR-----GEQDYCLAHLVTMGTFSGGELGLAYVGQICQkgassPKTNTGLS---TTTNYGSFNypt 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255917952  138 ----IMAHEMGHNLGIHHDdgyCYCGGYPCIMGPSISPEPSKFFSNcsyiqcwDFIMNHNPECidneplGTDIISP 209
Cdd:pfam13574 123 qewdVVAHEVGHNFGATHD---CDGSQYASSGCERNAATSVCSANG-------SFIMNPASKS------NNDLFSP 182
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 6-197 6.95e-09

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 55.82  E-value: 6.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   6 YVETVFVVDKAMVtKYNGDLDKIKTKMYEAANNMNEMYRYMF---FRVVMVGLIIWTEEDkitVKPDVDY---------- 72
Cdd:cd04272    2 YPELFVVVDYDHQ-SEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPD---FEPYIHPinygyidaae 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  73 TLNAFAEW--RKTYLLaekKHDNAQLITGIDFRG--------SIIGYAYIGSMCHpKRSVGIIQD----YSPINLvlavi 138
Cdd:cd04272   78 TLENFNEYvkKKRDYF---NPDVVFLVTGLDMSTysggslqtGTGGYAYVGGACT-ENRVAMGEDtpgsYYGVYT----- 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255917952 139 MAHEMGHNLGIHHD--DGYCYCGGYP----C------IMGPSISPEPSKFFSNCSYIQCWDFIMNHNPECI 197
Cdd:cd04272  149 MTHELAHLLGAPHDgsPPPSWVKGHPgsldCpwddgyIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCL 219
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 19-181 8.44e-07

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: 49.15  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   19 TKYNGDLDKIKTKMYEAANNMNEMYRYMF---FRVVMVGLIIWTEEDKITVKPD------VDYTLNAFAEWRKTyllaeK 89
Cdd:pfam13583  16 SASFGSVDELRANINATVTTANEVYGRDFnvsLALISDRDVIYTDSSTDSFNADcsggdlGNWRLATLTSWRDS-----L 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952   90 KHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVImAHEMGHNLGIHHDDGYCYC--------GGY 161
Cdd:pfam13583  91 NYDLAYLTLMTGPSGQNVGVAWVGALCSSARQNAKASGVARSRDEWDIF-AHEIGHTFGAVHDCSSQGEglssstedGSG 169

                         170       180
                  ....*....|....*....|
gi 255917952  162 PCIMGPSiSPEPSKFFSNCS 181
Cdd:pfam13583 170 QTIMSYA-STASQTAFSPCT 188
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 68-181 2.54e-04

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 42.02  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  68 PDVDYTLNAFAEWRKTyllaEKKHDNA--QLITGIDfRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAV-----IMA 140
Cdd:cd04271   76 IDIDDRLSIFSQWRGQ----QPDDGNAfwTLMTACP-SGSEVGVAWLGQLCRTGASDQGNETVAGTNVVVRTsnewqVFA 150

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952 141 HEMGHNLGIHHD--DGYCYCGGY---PC--------------IMGPSISpEPSKFFSNCS 181
Cdd:cd04271  151 HEIGHTFGAVHDctSGTCSDGSVgsqQCcplststcdangqyIMNPSSS-SGITEFSPCT 209
metallo_CpaA NF033511
metalloendopeptidase CpaA;
138-179 6.83e-04

metalloendopeptidase CpaA;


Pssm-ID: 411150 [Multi-domain]  Cd Length: 575  Bit Score: 42.00  E-value: 6.83e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 255917952 138 IMAHEMGHNLGIHHDD----GYCYCGGYPC---IMGPSISPepskFFSN 179
Cdd:NF033511 496 VMRHEFGHNMGLYHGDstniGSPYGFGHPLgstIMGGNNIP----YYSS 540
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 85-181 1.42e-03

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: 40.05  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  85 LLAEKKHDN---AQLITGIDFRGSIIGYAYIGS--------MCHP--------KRS--VGII--QDYSP--INLVLAVIM 139
Cdd:cd04270   92 LLLEQFSDDvclAHLFTYRDFDMGTLGLAYVGSprdnsaggICEKayyysngkKKYlnTGLTttVNYGKrvPTKESDLVT 171

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255917952 140 AHEMGHNLGIHHDDGYCYC-------GGYpcIMGP---SISPEPSKFFSNCS 181
Cdd:cd04270  172 AHELGHNFGSPHDPDIAECapgesqgGNY--IMYAratSGDKENNKKFSPCS 221
ADAMTS_CR_2 pfam17771
ADAMTS cysteine-rich domain 2; This cysteine rich domain is found in a variety of ADAMTS ...
 340-411 2.68e-03

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: 36.17  E-value: 2.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255917952  340 GNYYGYCRKEngkkipcaSEDVkCGRLYCKDdspGQNNPCKMfysnddeHKGMVLPGTKCADGKVCSNGHCV 411
Cdd:pfam17771  16 GPGSTFCPNG--------DEDV-CSKLWCSN---PGGSTCTT-------KNLPAADGTPCGNKKWCLNGKCV 68
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
135-181 8.84e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.86  E-value: 8.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 255917952 135 LAVIMAHEMGHNLGIHHddgycyCGGYPCIMGPSISPE-----PSKFFSNCS 181
Cdd:COG1913  123 VLKEAVHELGHLFGLGH------CPNPRCVMHFSNSLEeldrkPPSFCPSCR 168
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 67-151 9.59e-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: 36.71  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255917952  67 KPDVDYTLNAFAEWRKTYLL---AEKKHDNAQLITGiDFRGSII---GYAYIGSMCHPKR---SVGIIQDYSPI-----N 132
Cdd:cd04268   14 DKLRAAILDAIEAWNKAFAIgfkNANDVDPADIRYS-VIRWIPYndgTWSYGPSQVDPLTgeiLLARVYLYSSFveysgA 92

                         90
                 ....*....|....*....
gi 255917952 133 LVLAVImAHEMGHNLGIHH 151
Cdd:cd04268   93 RLRNTA-EHELGHALGLRH 110
 
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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