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Conserved domains on  [gi|525568298|gb|AGR55474|]
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a disintegrin and metallopeptidase domain 18, partial [Mus musculus domesticus]

Protein Classification

ZnMc and Disintegrin domain-containing protein( domain architecture ID 10446104)

ZnMc and Disintegrin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Disintegrin pfam00200
Disintegrin;
10-85 3.97e-20

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 77.28  E-value: 3.97e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525568298   10 EAGEECDCGNETECQFKECCDHETCRLKGSAQCGSGACCMpTCELSASGTPCRKAVDpECDFTEYCDGSSSHCVPD 85
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCT-NCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
ADAM_CR super family cl15456
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 90-113 1.91e-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 pfam08516:

Pssm-ID: 472809  Cd Length: 105  Bit Score: 37.59  E-value: 1.91e-04
                          10        20
                  ....*....|....*....|....
gi 525568298   90 NGHLCRLGSAYCYNGRCQALNDQC 113
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQC 24
 
Name Accession Description Interval E-value
Disintegrin pfam00200
Disintegrin;
10-85 3.97e-20

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 77.28  E-value: 3.97e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525568298   10 EAGEECDCGNETECQFKECCDHETCRLKGSAQCGSGACCMpTCELSASGTPCRKAVDpECDFTEYCDGSSSHCVPD 85
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCT-NCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 10-87 2.44e-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: 75.42  E-value: 2.44e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525568298    10 EAGEECDCGNETECQfKECCDHETCRLKGSAQCGSGACCMpTCELSASGTPCRKAVDpECDFTEYCDGSSSHCVPDTF 87
Cdd:smart00050   1 EEGEECDCGSPKECT-DPCCDPATCKLKPGAQCASGPCCD-NCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 90-113 1.91e-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.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 37.59  E-value: 1.91e-04
                          10        20
                  ....*....|....*....|....
gi 525568298   90 NGHLCRLGSAYCYNGRCQALNDQC 113
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQC 24
ACR smart00608
ADAM Cysteine-Rich Domain;
89-113 2.35e-04

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 38.11  E-value: 2.35e-04
                           10        20
                   ....*....|....*....|....*
gi 525568298    89 LNGHLCRLGSAYCYNGRCQALNDQC 113
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQC 25
 
Name Accession Description Interval E-value
Disintegrin pfam00200
Disintegrin;
10-85 3.97e-20

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 77.28  E-value: 3.97e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525568298   10 EAGEECDCGNETECQFKECCDHETCRLKGSAQCGSGACCMpTCELSASGTPCRKAVDpECDFTEYCDGSSSHCVPD 85
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCT-NCQFKPAGTVCRPSKD-ECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 10-87 2.44e-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: 75.42  E-value: 2.44e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525568298    10 EAGEECDCGNETECQfKECCDHETCRLKGSAQCGSGACCMpTCELSASGTPCRKAVDpECDFTEYCDGSSSHCVPDTF 87
Cdd:smart00050   1 EEGEECDCGSPKECT-DPCCDPATCKLKPGAQCASGPCCD-NCKFKPAGTLCRPSVD-ECDLPEYCNGTSADCPPDPY 75
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 90-113 1.91e-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.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 37.59  E-value: 1.91e-04
                          10        20
                  ....*....|....*....|....
gi 525568298   90 NGHLCRLGSAYCYNGRCQALNDQC 113
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQC 24
ACR smart00608
ADAM Cysteine-Rich Domain;
89-113 2.35e-04

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 38.11  E-value: 2.35e-04
                           10        20
                   ....*....|....*....|....*
gi 525568298    89 LNGHLCRLGSAYCYNGRCQALNDQC 113
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQC 25
 
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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