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Conserved domains on  [gi|2118001525|ref|XP_044293308|]
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disintegrin and metalloproteinase domain-containing protein 9 [Varanus komodoensis]

Protein Classification

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 ...
 205-397 1.30e-88

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


:

Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 278.34  E-value: 1.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 205 RYVELFIVVDKERYQLLGQNETAVREEMVQLANYLDSMYVMLNIRIVLVGLEIWTVQNKIRLEGGAADVLANFVQWREQD 284
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 285 LVPRRRHDSAQFVLKKGF-GGTAGMAYVGTVCSKSHAGGINVFGTISVQMFASIVAHELGHNLGMNHDDErNCYCRTTNC 363
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2118001525 364 IMNSGAS-GARNFSSCSEEDFEKLTLNKGGSCLLN 397
Cdd:cd04269   160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
493-629 5.95e-59

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 196.81  E-value: 5.95e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525  493 QNGHPCHKEEAYCYNGVCQFYEAQCQAIFGSKAKAAPEICFSEVNSKGDRFGNCGYHGHDYKKCSSWNAMCGKLQCENVE 572
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2118001525  573 TLPVFGIQPAIIQSRIKGSTCWGVDFQLGSDvPDPGMVNEGTKCAPGKICKHSQCVD 629
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 38-159 5.16e-44

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: 155.16  E-value: 5.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525  38 EITVPKRVT--RDRREVPSSGSAQEEVSYVIAVEGREHILHLERNKQLLPKDFTVYTYNEDGTLRSDTPDLQGHCHYQGY 115
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2118001525 116 VEGILDSMAAISTCSGLRGLLQIENITYGIEP----TESPSGLQHLIY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
416-489 1.20e-34

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.20  E-value: 1.20e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118001525 416 DAGEECDCGSLEECKSDPCCEAGACRLRPGAECGYGDCCHNCRFVSKGTQCRESASECDLPEYCNGTAPFCPQD 489
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 616-660 9.77e-04

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


:

Pssm-ID: 460294  Cd Length: 52  Bit Score: 37.79  E-value: 9.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2118001525 616 CAPGKICKHSQCVDASILGYDCDIKNQCNGHGVCNSNRnCHCEPG 660
Cdd:pfam01683   1 CPPGQVLVNGQCVPKVAPGESCEADEQCPGGSVCVNGV-CQCPPG 44
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 205-397 1.30e-88

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 278.34  E-value: 1.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 205 RYVELFIVVDKERYQLLGQNETAVREEMVQLANYLDSMYVMLNIRIVLVGLEIWTVQNKIRLEGGAADVLANFVQWREQD 284
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 285 LVPRRRHDSAQFVLKKGF-GGTAGMAYVGTVCSKSHAGGINVFGTISVQMFASIVAHELGHNLGMNHDDErNCYCRTTNC 363
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2118001525 364 IMNSGAS-GARNFSSCSEEDFEKLTLNKGGSCLLN 397
Cdd:cd04269   160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 205-399 1.18e-84

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: 268.40  E-value: 1.18e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 205 RYVELFIVVDKERYQLLGQNETAVREEMVQLANYLDSMYVMLNIRIVLVGLEIWTVQNKIRLEGGAADVLANFVQWREQD 284
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 285 LVPRRRHDSAQFVLKKGFGG-TAGMAYVGTVCSKSHAGGINVFGTISVQMFASIVAHELGHNLGMNHDDE-RNCYCRTTN 362
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118001525 363 -CIMNS--GASGARNFSSCSEEDFEKLTLNKGGSCLLNIP 399
Cdd:pfam01421 161 gCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
493-629 5.95e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 196.81  E-value: 5.95e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525  493 QNGHPCHKEEAYCYNGVCQFYEAQCQAIFGSKAKAAPEICFSEVNSKGDRFGNCGYHGHDYKKCSSWNAMCGKLQCENVE 572
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2118001525  573 TLPVFGIQPAIIQSRIKGSTCWGVDFQLGSDvPDPGMVNEGTKCAPGKICKHSQCVD 629
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 494-598 2.07e-47

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: 163.56  E-value: 2.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 494 NGHPCHKEEAYCYNGVCQFYEAQCQAIFGSKAKAAPEICFSEVNSKGDRFGNCGYHGHDYKKCSSWNAMCGKLQCENVET 573
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 2118001525 574 LPVFGIQPAIIQSRIKGSTCWGVDF 598
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 38-159 5.16e-44

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: 155.16  E-value: 5.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525  38 EITVPKRVT--RDRREVPSSGSAQEEVSYVIAVEGREHILHLERNKQLLPKDFTVYTYNEDGTLRSDTPDLQGHCHYQGY 115
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2118001525 116 VEGILDSMAAISTCSGLRGLLQIENITYGIEP----TESPSGLQHLIY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
416-489 1.20e-34

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.20  E-value: 1.20e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118001525 416 DAGEECDCGSLEECKSDPCCEAGACRLRPGAECGYGDCCHNCRFVSKGTQCRESASECDLPEYCNGTAPFCPQD 489
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 416-490 1.25e-33

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: 123.57  E-value: 1.25e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118001525  416 DAGEECDCGSLEECKsDPCCEAGACRLRPGAECGYGDCCHNCRFVSKGTQCRESASECDLPEYCNGTAPFCPQDV 490
Cdd:smart00050   1 EEGEECDCGSPKECT-DPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDP 74
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 616-660 9.77e-04

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 37.79  E-value: 9.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2118001525 616 CAPGKICKHSQCVDASILGYDCDIKNQCNGHGVCNSNRnCHCEPG 660
Cdd:pfam01683   1 CPPGQVLVNGQCVPKVAPGESCEADEQCPGGSVCVNGV-CQCPPG 44
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 315-355 7.49e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 37.72  E-value: 7.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2118001525  315 CSKSHAGGINVFGTISVQMFA---SIVAHELGHNLGMNHDDERN 355
Cdd:smart00235  62 CTLSHAGRPGGDQHLSLGNGCintGVAAHELGHALGLYHEQSRS 105
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 205-397 1.30e-88

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 278.34  E-value: 1.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 205 RYVELFIVVDKERYQLLGQNETAVREEMVQLANYLDSMYVMLNIRIVLVGLEIWTVQNKIRLEGGAADVLANFVQWREQD 284
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 285 LVPRRRHDSAQFVLKKGF-GGTAGMAYVGTVCSKSHAGGINVFGTISVQMFASIVAHELGHNLGMNHDDErNCYCRTTNC 363
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2118001525 364 IMNSGAS-GARNFSSCSEEDFEKLTLNKGGSCLLN 397
Cdd:cd04269   160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 205-399 1.18e-84

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: 268.40  E-value: 1.18e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 205 RYVELFIVVDKERYQLLGQNETAVREEMVQLANYLDSMYVMLNIRIVLVGLEIWTVQNKIRLEGGAADVLANFVQWREQD 284
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 285 LVPRRRHDSAQFVLKKGFGG-TAGMAYVGTVCSKSHAGGINVFGTISVQMFASIVAHELGHNLGMNHDDE-RNCYCRTTN 362
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPPGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118001525 363 -CIMNS--GASGARNFSSCSEEDFEKLTLNKGGSCLLNIP 399
Cdd:pfam01421 161 gCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
493-629 5.95e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 196.81  E-value: 5.95e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525  493 QNGHPCHKEEAYCYNGVCQFYEAQCQAIFGSKAKAAPEICFSEVNSKGDRFGNCGYHGHDYKKCSSWNAMCGKLQCENVE 572
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2118001525  573 TLPVFGIQPAIIQSRIKGSTCWGVDFQLGSDvPDPGMVNEGTKCAPGKICKHSQCVD 629
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 494-598 2.07e-47

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: 163.56  E-value: 2.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 494 NGHPCHKEEAYCYNGVCQFYEAQCQAIFGSKAKAAPEICFSEVNSKGDRFGNCGYHGHDYKKCSSWNAMCGKLQCENVET 573
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 2118001525 574 LPVFGIQPAIIQSRIKGSTCWGVDF 598
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 38-159 5.16e-44

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: 155.16  E-value: 5.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525  38 EITVPKRVT--RDRREVPSSGSAQEEVSYVIAVEGREHILHLERNKQLLPKDFTVYTYNEDGTLRSDTPDLQGHCHYQGY 115
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2118001525 116 VEGILDSMAAISTCSGLRGLLQIENITYGIEP----TESPSGLQHLIY 159
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPlekySREEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
416-489 1.20e-34

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.20  E-value: 1.20e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118001525 416 DAGEECDCGSLEECKSDPCCEAGACRLRPGAECGYGDCCHNCRFVSKGTQCRESASECDLPEYCNGTAPFCPQD 489
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 416-490 1.25e-33

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: 123.57  E-value: 1.25e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118001525  416 DAGEECDCGSLEECKsDPCCEAGACRLRPGAECGYGDCCHNCRFVSKGTQCRESASECDLPEYCNGTAPFCPQDV 490
Cdd:smart00050   1 EEGEECDCGSPKECT-DPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDP 74
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 205-396 2.64e-28

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: 113.10  E-value: 2.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 205 RYVELFIVVDKERYQLLGQNETavrEEMV-QLANYLDSMY----VMLNIRIVLVGLEIWTVQNKIRLEGGAADV-LANFV 278
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDL---EHYIlTLMNIVASLYkdpsLGNSINIVVVRLIVLEDEESGLLISGNAQKsLKSFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 279 QWREQDLVPR----RRHDSA------QFVLKKGFGGTAGMAYVGTVCSKSHAGGINV---FGTisvqmfASIVAHELGHN 345
Cdd:cd04273    78 RWQKKLNPPNdsdpEHHDHAilltrqDICRSNGNCDTLGLAPVGGMCSPSRSCSINEdtgLSS------AFTIAHELGHV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2118001525 346 LGMNHDDERNcYCRTTN---CIM---NSGASGARNFSSCSEEDFEKLTLNKGGSCLL 396
Cdd:cd04273   152 LGMPHDGDGN-SCGPEGkdgHIMsptLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 207
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 205-379 4.86e-25

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: 103.27  E-value: 4.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 205 RYVELFIVVDKERYQLLGQNETAVREEMVQLANYLDSMY----VMLNIRIVLVGLEIW-TVQNKIRLEGGAADVLANFVQ 279
Cdd:cd04267     1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILkGEQFAPPIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 280 WREQDlvpRRRHDSAQFVLKKGF--GGTAGMAYVGTVCSKSHAGGInVFGTISVQMFASIVAHELGHNLGMNHD--DERN 355
Cdd:cd04267    81 WRAEG---PIRHDNAVLLTAQDFieGDILGLAYVGSMCNPYSSVGV-VEDTGFTLLTALTMAHELGHNLGAEHDggDELA 156

                         170       180
                  ....*....|....*....|....*..
gi 2118001525 356 CYCRTT-NCIMNSGASGARN--FSSCS 379
Cdd:cd04267   157 FECDGGgNYIMAPVDSGLNSyrFSQCS 183
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
204-376 3.96e-19

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 85.93  E-value: 3.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 204 TRYVELFIVVDKERYQLLGQNetAVREEMVQLANYLDS-MYVMLNIRIVLVGLEIWT----VQNKIRLEGGAADVLANFV 278
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDstcpYTPPACSTGDSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 279 ---QWREQDlvprrRHDSAQFVLKKGFGGTaGMAYVGTVCSKSHAGGINVFGTISVQMFAS-----IVAHELGHNLGMNH 350
Cdd:pfam13688  80 dfsAWRGTQ-----NDDLAYLFLMTNCSGG-GLAWLGQLCNSGSAGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVH 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2118001525 351 DDERNC---YCRTTN--------CIMN-SGASGARNFS 376
Cdd:pfam13688 154 DCDSSTssqCCPPSNstcpaggrYIMNpSSSPNSTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 230-351 3.55e-17

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: 78.18  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 230 EEMVQLANYLDSMYVM-LNIRIVLVGLEIWTVQNKIRLEGGAADVLANFVQWREQDLvPRRRHDSAQFVLKKGFGGTAGM 308
Cdd:pfam13582   1 ARIVSLVNRANTIYERdLGIRLQLAAIIITTSADTPYTSSDALEILDELQEVNDTRI-GQYGYDLGHLFTGRDGGGGGGI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2118001525 309 AYVGTVCSKSHAGGINVFGTISVQMFASIVAHELGHNLGMNHD 351
Cdd:pfam13582  80 AYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 206-395 7.68e-14

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 71.61  E-value: 7.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 206 YVELFIVVDKERYQLLGQNEtAVREEMVQLANYLDSMYVML---NIRIVLVGLEIWTVQ-NKIRLEGG------AADVLA 275
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSNE-QLIRYLAVMVNAANLRYRDLkspRIRLLLVGITISKDPdFEPYIHPInygyidAAETLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 276 NFVQW-REQDLvpRRRHDSAQFVLKKGFG---------GTAGMAYVGTVCSKSHAG----------GINVFgtisvqmfa 335
Cdd:cd04272    81 NFNEYvKKKRD--YFNPDVVFLVTGLDMStysggslqtGTGGYAYVGGACTENRVAmgedtpgsyyGVYTM--------- 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118001525 336 sivAHELGHNLGMNHD-DERNCYCR----TTNC------IMNSGASGARN--FSSCSEEDFEKLTLNKGGSCL 395
Cdd:cd04272   150 ---THELAHLLGAPHDgSPPPSWVKghpgSLDCpwddgyIMSYVVNGERQyrFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 205-379 7.75e-12

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: 64.47  E-value: 7.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 205 RYVELFIVVDKERYQllgqnETAVREEMVQLANYLDSMY-VMLNIRIVLVGLEIwtvqnkirleggaadvlanfvqwreq 283
Cdd:cd00203     1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIAMQIWrDYLNIRFVLVGVEI-------------------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 284 dlvprRRHDSAQFVLKKGF-GGTAGMAYVGTVCSKSHAGGINVFGTISVQMFASIVAHELGHNLGMNHDDERNCYCRTTN 362
Cdd:cd00203    50 -----DKADIAILVTRQDFdGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPT 124

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2118001525 363 -------------CIMNSGA---SGARN--FSSCS 379
Cdd:cd00203   125 iddtlnaedddyySVMSYTKgsfSDGQRkdFSQCD 159
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 227-379 2.03e-10

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: 60.72  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 227 AVREEMVQLANYLDSMYVM--LNIRIVLVGL-EI---------WTVQNKIRLEGGAADVLanFVQWR-EQDlvprrrHDS 293
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPddININGGLVNPgEIpattsasdsGNNYCNSPTTIVRRLNF--LSQWRgEQD------YCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 294 AQFVLKKGF-GGTAGMAYVGTVCSK-------------SHAGGINVFGTISVQmfasIVAHELGHNLGMNHDDERNCYCR 359
Cdd:pfam13574  74 AHLVTMGTFsGGELGLAYVGQICQKgasspktntglstTTNYGSFNYPTQEWD----VVAHEVGHNFGATHDCDGSQYAS 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2118001525 360 --------TTNC------IMN-SGASGARNFSSCS 379
Cdd:pfam13574 150 sgcernaaTSVCsangsfIMNpASKSNNDLFSPCS 184
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 274-379 6.17e-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: 51.27  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 274 LANFVQWREQdlvpRRRHDSAQFVLKKGF--GGTAGMAYVGTVCSK--SHAGGINVFGTISVQMFA---SIVAHELGHNL 346
Cdd:cd04271    82 LSIFSQWRGQ----QPDDGNAFWTLMTACpsGSEVGVAWLGQLCRTgaSDQGNETVAGTNVVVRTSnewQVFAHEIGHTF 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2118001525 347 GMNHD------------DERNCYCRTTNC------IMN-SGASGARNFSSCS 379
Cdd:cd04271   158 GAVHDctsgtcsdgsvgSQQCCPLSTSTCdangqyIMNpSSSSGITEFSPCT 209
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 303-379 1.32e-05

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: 46.84  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 303 GGTAGMAYVGTVCS---KSHAGGinvfGTISVQMFASIVAHELGHNLGMNHDDERNCyCRTT--------NCIMNSGASG 371
Cdd:pfam13583 105 GQNVGVAWVGALCSsarQNAKAS----GVARSRDEWDIFAHEIGHTFGAVHDCSSQG-EGLSsstedgsgQTIMSYASTA 179


                  ....*....
gi 2118001525 372 AR-NFSSCS 379
Cdd:pfam13583 180 SQtAFSPCT 188
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 303-394 4.00e-05

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: 45.83  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118001525 303 GGTAGMAYVGTVCSKSHaGGI---------------NVfGTISVQMFAS---------IVAHELGHNLGMNHDDErNCYC 358
Cdd:cd04270   114 MGTLGLAYVGSPRDNSA-GGIcekayyysngkkkylNT-GLTTTVNYGKrvptkesdlVTAHELGHNFGSPHDPD-IAEC 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2118001525 359 RTT-----NCIMNSGA-SGA----RNFSSCSEEDFEKLTLNKGGSC 394
Cdd:cd04270   191 APGesqggNYIMYARAtSGDkennKKFSPCSKKSISKVLEVKSNSC 236
EB pfam01683
EB module; This domain has no known function. It is found in several C. elegans proteins. The ...
 616-660 9.77e-04

EB module; This domain has no known function. It is found in several C. elegans proteins. The domain contains 8 conserved cysteines that probably form four disulphide bridges. This domain is found associated with kunitz domains pfam00014.


Pssm-ID: 460294  Cd Length: 52  Bit Score: 37.79  E-value: 9.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2118001525 616 CAPGKICKHSQCVDASILGYDCDIKNQCNGHGVCNSNRnCHCEPG 660
Cdd:pfam01683   1 CPPGQVLVNGQCVPKVAPGESCEADEQCPGGSVCVNGV-CQCPPG 44
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 285-350 2.34e-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: 39.79  E-value: 2.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118001525 285 LVPRRRHDSAQF---VLKKGFGGTAGMAYVGTVcSKSHAGGI--------NVFGTISVQMFASIVAHELGHNLGMNH 350
Cdd:cd04268    35 FKNANDVDPADIrysVIRWIPYNDGTWSYGPSQ-VDPLTGEIllarvylySSFVEYSGARLRNTAEHELGHALGLRH 110
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 338-385 3.62e-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: 39.20  E-value: 3.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2118001525 338 VAHELGHNLGMNHdderncyCRTTNCIMnsgasgarNFSSCSEEDFEK 385
Cdd:cd11375   127 AVHELGHLFGLDH-------CPYYACVM--------NFSNSLEETDRK 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 315-355 7.49e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 37.72  E-value: 7.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2118001525  315 CSKSHAGGINVFGTISVQMFA---SIVAHELGHNLGMNHDDERN 355
Cdd:smart00235  62 CTLSHAGRPGGDQHLSLGNGCintGVAAHELGHALGLYHEQSRS 105
 
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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