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Conserved domains on  [gi|525568385|gb|AGR55486|]
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a disintegrin and metallopeptidase domain 6a, partial [Mus musculus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Disintegrin pfam00200
Disintegrin;
10-82 4.02e-21

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 79.59  E-value: 4.02e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525568385   10 DNNEQCDCGSQKACYSDPCC-GNDCRLTPGSICDKELCCANCTYSPSGTLCRPIQNICDLPEYCSGSKFICPDD 82
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
ADAM_CR super family cl15456
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 86-109 3.98e-04

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.


The actual alignment was detected with superfamily member smart00608:

Pssm-ID: 472809  Cd Length: 137  Bit Score: 37.34  E-value: 3.98e-04
                           10        20
                   ....*....|....*....|....*
gi 525568385    86 QDGTPCSEE-GYCYKGNCTDRNIQC 109
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQC 25
 
Name Accession Description Interval E-value
Disintegrin pfam00200
Disintegrin;
10-82 4.02e-21

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 79.59  E-value: 4.02e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525568385   10 DNNEQCDCGSQKACYSDPCC-GNDCRLTPGSICDKELCCANCTYSPSGTLCRPIQNICDLPEYCSGSKFICPDD 82
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 12-84 6.12e-19

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: 74.26  E-value: 6.12e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525568385    12 NEQCDCGSQKACySDPCC-GNDCRLTPGSICDKELCCANCTYSPSGTLCRPIQNICDLPEYCSGSKFICPDDTY 84
Cdd:smart00050   3 GEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ACR smart00608
ADAM Cysteine-Rich Domain;
86-109 3.98e-04

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 37.34  E-value: 3.98e-04
                           10        20
                   ....*....|....*....|....*
gi 525568385    86 QDGTPCSEE-GYCYKGNCTDRNIQC 109
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQC 25
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 87-109 1.26e-03

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: 35.28  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....
gi 525568385   87 DGTPCSE-EGYCYKGNCTDRNIQC 109
Cdd:pfam08516   1 DGTPCNNgQAYCYNGRCRDRDQQC 24
 
Name Accession Description Interval E-value
Disintegrin pfam00200
Disintegrin;
10-82 4.02e-21

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 79.59  E-value: 4.02e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525568385   10 DNNEQCDCGSQKACYSDPCC-GNDCRLTPGSICDKELCCANCTYSPSGTLCRPIQNICDLPEYCSGSKFICPDD 82
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCdAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 12-84 6.12e-19

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: 74.26  E-value: 6.12e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525568385    12 NEQCDCGSQKACySDPCC-GNDCRLTPGSICDKELCCANCTYSPSGTLCRPIQNICDLPEYCSGSKFICPDDTY 84
Cdd:smart00050   3 GEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ACR smart00608
ADAM Cysteine-Rich Domain;
86-109 3.98e-04

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 37.34  E-value: 3.98e-04
                           10        20
                   ....*....|....*....|....*
gi 525568385    86 QDGTPCSEE-GYCYKGNCTDRNIQC 109
Cdd:smart00608   1 QDGTPCDNGqGYCYNGRCPTRDNQC 25
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 87-109 1.26e-03

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: 35.28  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....
gi 525568385   87 DGTPCSE-EGYCYKGNCTDRNIQC 109
Cdd:pfam08516   1 DGTPCNNgQAYCYNGRCRDRDQQC 24
 
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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