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Conserved domains on  [gi|2462490099|ref|XP_054184828|]
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disintegrin and metalloproteinase domain-containing protein 32 isoform X8 [Homo sapiens]

Protein Classification

zinc metalloprotease; M10 family metallopeptidase domain-containing protein( domain architecture ID 10480921)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family| M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACR smart00608
ADAM Cysteine-Rich Domain;
349-486 1.34e-40

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 144.81  E-value: 1.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099  349 NGLSCKNNKFICYDGDCHDLDARCESVFGKGSRNAPFACYEEIQSQSDRFGNCGRDrNNKYVFCGWRNLICGRLVCTYPT 428
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462490099  429 RKPFHQENGDVIYAFVRDSVCITVDYKLpRTVPDPLAVKNGSQCDIGRVCVNRECVES 486
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHL-GTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 27-144 2.23e-29

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: 112.79  E-value: 2.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099  27 QIVIPEKIQTNTN----DSSEIEYEQISYIIPIDEKLYTVHLKQ-RYFLADNFMIYLY-NQGSMNTYSSDIQTQCYYQGN 100
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslASESTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462490099 101 IEGYPDSMVTLSTCSGLRGILQFENVSYGIEPLESAVE----FQHVLY 144
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSReeggHPHVVY 128
Disintegrin pfam00200
Disintegrin;
270-344 1.72e-27

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 105.79  E-value: 1.72e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462490099 270 EGNEICDCGTEAQCGPASCCDFRTCVLKDGAKCYKGLCCKDCQILQSGVECRPKAHpECDIAENCNGSSPECGPD 344
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 181-251 4.54e-20

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.


The actual alignment was detected with superfamily member cd04269:

Pssm-ID: 469599 [Multi-domain]  Cd Length: 194  Bit Score: 88.44  E-value: 4.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462490099 181 TLEAFAVIVTQMLALSLGISYDDPKkCQCSESTCIMNPEVvqSNGVKTFSSCSLRSFQNFISNVGVKCLQN 251
Cdd:cd04269   127 NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRSTCIMAPSP--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
DMP1 super family cl25845
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 584-656 5.37e-04

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


The actual alignment was detected with superfamily member pfam07263:

Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 42.99  E-value: 5.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462490099 584 EEEFPSSESKSEGSTQTYASQSSSEGStQTYASQTRSESSSQADTSkSKSEDSaeaytSRSKS-QDSTQTQSSS 656
Cdd:pfam07263 415 EESPESSEDENSSSQEGLQSHSASTES-QSEESQSEQDSQSEEDDE-SDSQDS-----SRSKEdSNSTESTSSS 481
 
Name Accession Description Interval E-value
ACR smart00608
ADAM Cysteine-Rich Domain;
349-486 1.34e-40

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 144.81  E-value: 1.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099  349 NGLSCKNNKFICYDGDCHDLDARCESVFGKGSRNAPFACYEEIQSQSDRFGNCGRDrNNKYVFCGWRNLICGRLVCTYPT 428
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462490099  429 RKPFHQENGDVIYAFVRDSVCITVDYKLpRTVPDPLAVKNGSQCDIGRVCVNRECVES 486
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHL-GTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 349-454 1.92e-38

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: 137.36  E-value: 1.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099 349 NGLSCKNNKFICYDGDCHDLDARCESVFGKGSRNAPFACYEEIQSQSDRFGNCGRDrNNKYVFCGWRNLICGRLVCTYPT 428
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRT-NGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100
                  ....*....|....*....|....*.
gi 2462490099 429 RKPFHQENGDVIYAFVRDSVCITVDY 454
Cdd:pfam08516  80 ELPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 27-144 2.23e-29

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: 112.79  E-value: 2.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099  27 QIVIPEKIQTNTN----DSSEIEYEQISYIIPIDEKLYTVHLKQ-RYFLADNFMIYLY-NQGSMNTYSSDIQTQCYYQGN 100
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslASESTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462490099 101 IEGYPDSMVTLSTCSGLRGILQFENVSYGIEPLESAVE----FQHVLY 144
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSReeggHPHVVY 128
Disintegrin pfam00200
Disintegrin;
270-344 1.72e-27

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 105.79  E-value: 1.72e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462490099 270 EGNEICDCGTEAQCGPASCCDFRTCVLKDGAKCYKGLCCKDCQILQSGVECRPKAHpECDIAENCNGSSPECGPD 344
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 181-251 4.54e-20

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: 88.44  E-value: 4.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462490099 181 TLEAFAVIVTQMLALSLGISYDDPKkCQCSESTCIMNPEVvqSNGVKTFSSCSLRSFQNFISNVGVKCLQN 251
Cdd:cd04269   127 NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRSTCIMAPSP--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 270-344 5.08e-20

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: 84.28  E-value: 5.08e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462490099  270 EGNEICDCGTEAQCGPaSCCDFRTCVLKDGAKCYKGLCCKDCQILQSGVECRPkAHPECDIAENCNGSSPECGPD 344
Cdd:smart00050   1 EEGEECDCGSPKECTD-PCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRP-SVDECDLPEYCNGTSADCPPD 73
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 174-253 1.33e-17

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: 81.58  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099 174 EKYPKeITLEAFAVIVTQMLALSLGISYDDP-KKCQCSES-TCIMNPEVVQSNGVKtFSSCSLRSFQNFISNVGVKCLQN 251
Cdd:pfam01421 121 NEDHS-KNLESFAVTMAHELGHNLGMQHDDFnGGCKCPPGgGCIMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFN 198


                  ..
gi 2462490099 252 KP 253
Cdd:pfam01421 199 KP 200
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 584-656 5.37e-04

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 42.99  E-value: 5.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462490099 584 EEEFPSSESKSEGSTQTYASQSSSEGStQTYASQTRSESSSQADTSkSKSEDSaeaytSRSKS-QDSTQTQSSS 656
Cdd:pfam07263 415 EESPESSEDENSSSQEGLQSHSASTES-QSEESQSEQDSQSEEDDE-SDSQDS-----SRSKEdSNSTESTSSS 481
 
Name Accession Description Interval E-value
ACR smart00608
ADAM Cysteine-Rich Domain;
349-486 1.34e-40

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 144.81  E-value: 1.34e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099  349 NGLSCKNNKFICYDGDCHDLDARCESVFGKGSRNAPFACYEEIQSQSDRFGNCGRDrNNKYVFCGWRNLICGRLVCTYPT 428
Cdd:smart00608   2 DGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRE-NGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462490099  429 RKPFHQENGDVIYAFVRDSVCITVDYKLpRTVPDPLAVKNGSQCDIGRVCVNRECVES 486
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHL-GTDPDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 349-454 1.92e-38

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: 137.36  E-value: 1.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099 349 NGLSCKNNKFICYDGDCHDLDARCESVFGKGSRNAPFACYEEIQSQSDRFGNCGRDrNNKYVFCGWRNLICGRLVCTYPT 428
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRT-NGGYVKCEKRDVLCGKLQCTNVK 79

                          90       100
                  ....*....|....*....|....*.
gi 2462490099 429 RKPFHQENGDVIYAFVRDSVCITVDY 454
Cdd:pfam08516  80 ELPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 27-144 2.23e-29

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: 112.79  E-value: 2.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099  27 QIVIPEKIQTNTN----DSSEIEYEQISYIIPIDEKLYTVHLKQ-RYFLADNFMIYLY-NQGSMNTYSSDIQTQCYYQGN 100
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslASESTYLDTLSYRLAAFGKKFHLHLTPnRLLLAPGFTVTYYlDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462490099 101 IEGYPDSMVTLSTCSGLRGILQFENVSYGIEPLESAVE----FQHVLY 144
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKYSReeggHPHVVY 128
Disintegrin pfam00200
Disintegrin;
270-344 1.72e-27

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 105.79  E-value: 1.72e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462490099 270 EGNEICDCGTEAQCGPASCCDFRTCVLKDGAKCYKGLCCKDCQILQSGVECRPKAHpECDIAENCNGSSPECGPD 344
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 181-251 4.54e-20

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: 88.44  E-value: 4.54e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462490099 181 TLEAFAVIVTQMLALSLGISYDDPKkCQCSESTCIMNPEVvqSNGVKTFSSCSLRSFQNFISNVGVKCLQN 251
Cdd:cd04269   127 NLLLFAVTMAHELGHNLGMEHDDGG-CTCGRSTCIMAPSP--SSLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 270-344 5.08e-20

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: 84.28  E-value: 5.08e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462490099  270 EGNEICDCGTEAQCGPaSCCDFRTCVLKDGAKCYKGLCCKDCQILQSGVECRPkAHPECDIAENCNGSSPECGPD 344
Cdd:smart00050   1 EEGEECDCGSPKECTD-PCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRP-SVDECDLPEYCNGTSADCPPD 73
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 174-253 1.33e-17

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: 81.58  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099 174 EKYPKeITLEAFAVIVTQMLALSLGISYDDP-KKCQCSES-TCIMNPEVVQSNGVKtFSSCSLRSFQNFISNVGVKCLQN 251
Cdd:pfam01421 121 NEDHS-KNLESFAVTMAHELGHNLGMQHDDFnGGCKCPPGgGCIMNPSAGSSFPRK-FSNCSQEDFEQFLTKQKGACLFN 198


                  ..
gi 2462490099 252 KP 253
Cdd:pfam01421 199 KP 200
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 584-656 5.37e-04

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 42.99  E-value: 5.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462490099 584 EEEFPSSESKSEGSTQTYASQSSSEGStQTYASQTRSESSSQADTSkSKSEDSaeaytSRSKS-QDSTQTQSSS 656
Cdd:pfam07263 415 EESPESSEDENSSSQEGLQSHSASTES-QSEESQSEQDSQSEEDDE-SDSQDS-----SRSKEdSNSTESTSSS 481
SEEEED pfam14797
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ...
 584-656 7.02e-04

Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.


Pssm-ID: 434218 [Multi-domain]  Cd Length: 111  Bit Score: 39.53  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462490099 584 EEEFPSSESKSEG-----STQTYASQSSSEGSTQTYASQTRSESSSQA-----------DTSKSKSEDsAEAYTSRSKSQ 647
Cdd:pfam14797  12 EEDSSDSSSDSESesgseSEEEGKEGSSSEDSSEDSSSEQESESGSESekkrtakrnskAKGKSDSED-GEKKNEKSKTS 90


                  ....*....
gi 2462490099 648 DSTQTQSSS 656
Cdd:pfam14797  91 DSSDTESSS 99
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 186-250 2.62e-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: 39.53  E-value: 2.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462490099 186 AVIVTQMLALSLGISYDDPKKcQCSEST---CIMNPEVVQSNGVKTFSSCSLRSFQNFISNVGVKCLQ 250
Cdd:cd04273   141 AFTIAHELGHVLGMPHDGDGN-SCGPEGkdgHIMSPTLGANTGPFTWSKCSRRYLTSFLDTGDGNCLL 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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