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Conserved domains on  [gi|767950756|ref|XP_011542781|]
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disintegrin and metalloproteinase domain-containing protein 2 isoform X2 [Homo sapiens]

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein( domain architecture ID 13660734)

protein containing domains Pep_M12B_propep, ZnMc_adamalysin_II_like, DISIN, and ACR

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACR smart00608
ADAM Cysteine-Rich Domain;
346-483 2.43e-49

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 167.92  E-value: 2.43e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756   346 QTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEADNLQCGKLICKYVG 425
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950756   426 KFLLQIPRATIIYANISGHLCIAVEFASDHaDSQKMWIKDGTSCGSNKVCRNQRCVSS 483
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGT-DPDIGMVKDGTKCGPGKVCINGQCVDV 137
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 267-344 3.11e-32

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: 118.95  E-value: 3.11e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950756   267 EAGEECDCGTEQDCaliGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHY 344
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 26-141 1.55e-27

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: 107.40  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756   26 QITVPEKIRSIIK-------EGIESQASYKIVIEGKPYTVNLMQ-KNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGY 97
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslaseSTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767950756   98 IEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLE----SSVGFEHVIY 141
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
Reprolysin super family cl29699
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 170-249 1.73e-27

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.


The actual alignment was detected with superfamily member pfam01421:

Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 109.70  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756  170 VEHPRtISLESLAVILAQLLSLSMGITYDDINK-CQC-SGAVCIMNPEAIHFSGVKiFSNCSFEDFAHFISKQKSQCLHN 247
Cdd:pfam01421 121 NEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCpPGGGCIMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFN 198


                  ..
gi 767950756  248 QP 249
Cdd:pfam01421 199 KP 200
 
Name Accession Description Interval E-value
ACR smart00608
ADAM Cysteine-Rich Domain;
346-483 2.43e-49

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 167.92  E-value: 2.43e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756   346 QTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEADNLQCGKLICKYVG 425
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950756   426 KFLLQIPRATIIYANISGHLCIAVEFASDHaDSQKMWIKDGTSCGSNKVCRNQRCVSS 483
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGT-DPDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 348-451 5.30e-34

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: 124.65  E-value: 5.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756  348 GHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEADNLQCGKLICKYVGKF 427
Cdd:pfam08516   2 GTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKEL 81

                          90       100
                  ....*....|....*....|....
gi 767950756  428 LLQIPRATIIYANISGHLCIAVEF 451
Cdd:pfam08516  82 PLLGEHATVIYTNINGVTCWGTDY 105
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 267-344 3.11e-32

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: 118.95  E-value: 3.11e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950756   267 EAGEECDCGTEQDCaliGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHY 344
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
267-342 6.94e-31

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 115.03  E-value: 6.94e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950756  267 EAGEECDCGTEQDCALigETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPEN 342
Cdd:pfam00200   1 EEGEECDCGSLEECTN--DPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 26-141 1.55e-27

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: 107.40  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756   26 QITVPEKIRSIIK-------EGIESQASYKIVIEGKPYTVNLMQ-KNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGY 97
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslaseSTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767950756   98 IEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLE----SSVGFEHVIY 141
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 170-249 1.73e-27

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: 109.70  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756  170 VEHPRtISLESLAVILAQLLSLSMGITYDDINK-CQC-SGAVCIMNPEAIHFSGVKiFSNCSFEDFAHFISKQKSQCLHN 247
Cdd:pfam01421 121 NEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCpPGGGCIMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFN 198


                  ..
gi 767950756  248 QP 249
Cdd:pfam01421 199 KP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 170-247 2.53e-21

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: 91.91  E-value: 2.53e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950756 170 VEHPRTiSLESLAVILAQLLSLSMGITYDDINkCQCSGAVCIMNPEAIHFSgvKIFSNCSFEDFAHFISKQKSQCLHN 247
Cdd:cd04269  121 VQDHSR-NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRSTCIMAPSPSSLT--DAFSNCSYEDYQKFLSRGGGQCLLN 194
 
Name Accession Description Interval E-value
ACR smart00608
ADAM Cysteine-Rich Domain;
346-483 2.43e-49

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 167.92  E-value: 2.43e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756   346 QTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEADNLQCGKLICKYVG 425
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950756   426 KFLLQIPRATIIYANISGHLCIAVEFASDHaDSQKMWIKDGTSCGSNKVCRNQRCVSS 483
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGT-DPDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 348-451 5.30e-34

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: 124.65  E-value: 5.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756  348 GHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEADNLQCGKLICKYVGKF 427
Cdd:pfam08516   2 GTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKEL 81

                          90       100
                  ....*....|....*....|....
gi 767950756  428 LLQIPRATIIYANISGHLCIAVEF 451
Cdd:pfam08516  82 PLLGEHATVIYTNINGVTCWGTDY 105
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 267-344 3.11e-32

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: 118.95  E-value: 3.11e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950756   267 EAGEECDCGTEQDCaliGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHY 344
Cdd:smart00050   1 EEGEECDCGSPKEC---TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Disintegrin pfam00200
Disintegrin;
267-342 6.94e-31

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 115.03  E-value: 6.94e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950756  267 EAGEECDCGTEQDCALigETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPEN 342
Cdd:pfam00200   1 EEGEECDCGSLEECTN--DPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 26-141 1.55e-27

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: 107.40  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756   26 QITVPEKIRSIIK-------EGIESQASYKIVIEGKPYTVNLMQ-KNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGY 97
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslaseSTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767950756   98 IEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLE----SSVGFEHVIY 141
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEkysrEEGGHPHVVY 128
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 170-249 1.73e-27

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: 109.70  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950756  170 VEHPRtISLESLAVILAQLLSLSMGITYDDINK-CQC-SGAVCIMNPEAIHFSGVKiFSNCSFEDFAHFISKQKSQCLHN 247
Cdd:pfam01421 121 NEDHS-KNLESFAVTMAHELGHNLGMQHDDFNGgCKCpPGGGCIMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFN 198


                  ..
gi 767950756  248 QP 249
Cdd:pfam01421 199 KP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 170-247 2.53e-21

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: 91.91  E-value: 2.53e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950756 170 VEHPRTiSLESLAVILAQLLSLSMGITYDDINkCQCSGAVCIMNPEAIHFSgvKIFSNCSFEDFAHFISKQKSQCLHN 247
Cdd:cd04269  121 VQDHSR-NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRSTCIMAPSPSSLT--DAFSNCSYEDYQKFLSRGGGQCLLN 194
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 180-246 1.39e-03

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: 40.30  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950756 180 SLAVILAQLLSLSMGITYDD-INKCQCSGAVC-IMNPEAIHFSGVKIFSNCSFEDFAHFISKQKSQCLH 246
Cdd:cd04273  139 SSAFTIAHELGHVLGMPHDGdGNSCGPEGKDGhIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 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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