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Conserved domains on  [gi|48734396|gb|AAT46409|]
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tissue inhibitor of metalloproteinase 2, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTR_like super family cl02512
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 1-95 6.36e-55

NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex.


The actual alignment was detected with superfamily member cd03585:

Pssm-ID: 470599  Cd Length: 183  Bit Score: 168.37  E-value: 6.36e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396   1 SEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPD--KDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKMHITLCD 78
Cdd:cd03585  25 GEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDVNGKKEYLISGKVE-GGKVHITLCD 102

                        90
                ....*....|....*..
gi 48734396  79 FIVPWDTLSITQKKSLN 95
Cdd:cd03585 103 FVEPWDSLSLTQKKGLN 119
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 1-95 6.36e-55

NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. The levels of activated membrane-type MMPs, MMPs, and free TIMPs determine the balance between matrix degradation and matrix formation or stabilization. Consequently, TIMPs play roles in processes that require the remodeling and degradation of connective tissue, such as development, morphogenesis, wound healing, as well as in various diseases and pathological states such as tumor cell metastasis, arthritis, and artherosclerosis. Most TIMPs bind to a variety of MMPs. TIMP-1 and TIMP-2 appear to be multifunctional proteins with diverse biological action. They may exhibit growth factor-like activity and can inhibit angiogenesis. TIMP-3 has been implicated in apoptosis.


Pssm-ID: 239640  Cd Length: 183  Bit Score: 168.37  E-value: 6.36e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396   1 SEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPD--KDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKMHITLCD 78
Cdd:cd03585  25 GEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDVNGKKEYLISGKVE-GGKVHITLCD 102

                        90
                ....*....|....*..
gi 48734396  79 FIVPWDTLSITQKKSLN 95
Cdd:cd03585 103 FVEPWDSLSLTQKKGLN 119
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 1-95 1.74e-50

Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as collagenases, and irreversibly inactivate them.


Pssm-ID: 128502  Cd Length: 172  Bit Score: 156.47  E-value: 1.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396      1 SEKEVDSGndiygnPIKRIQYEIKQIKMFKGPDK--DIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKMHITLCD 78
Cdd:smart00206  25 GKKEVNEG------NTLYQRYEIKQTKMFKGFDKlgDIRFIYTPASESLCGYKLESQNKEEYLIAGRLE-DGKMHITLCS 97

                           90
                   ....*....|....*..
gi 48734396     79 FIVPWDTLSITQKKSLN 95
Cdd:smart00206  98 FVVPWDSLSLAQRKGLN 114
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 1-95 4.05e-49

Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular regions of vertebrate species


Pssm-ID: 460012  Cd Length: 183  Bit Score: 153.37  E-value: 4.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396     1 SEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDK-----DIEFIYTAPSSAVCGVSLDVGGKkEYLIAGKAEGDGKMHIT 75
Cdd:pfam00965  27 GEKEVKTGNDMYGPPIKNIVYEIKQIKMFKGPQLvgkaaDIQAVYTPPSSSLCGVTLELNGK-EYLIAGKLVSDGKLHVT 105

                          90       100
                  ....*....|....*....|
gi 48734396    76 LCDFIVPWDTLSITQKKSLN 95
Cdd:pfam00965 106 LCNFVEPWETLTLAQRRGLN 125
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 1-95 6.36e-55

NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. The levels of activated membrane-type MMPs, MMPs, and free TIMPs determine the balance between matrix degradation and matrix formation or stabilization. Consequently, TIMPs play roles in processes that require the remodeling and degradation of connective tissue, such as development, morphogenesis, wound healing, as well as in various diseases and pathological states such as tumor cell metastasis, arthritis, and artherosclerosis. Most TIMPs bind to a variety of MMPs. TIMP-1 and TIMP-2 appear to be multifunctional proteins with diverse biological action. They may exhibit growth factor-like activity and can inhibit angiogenesis. TIMP-3 has been implicated in apoptosis.


Pssm-ID: 239640  Cd Length: 183  Bit Score: 168.37  E-value: 6.36e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396   1 SEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPD--KDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKMHITLCD 78
Cdd:cd03585  25 GEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDVNGKKEYLISGKVE-GGKVHITLCD 102

                        90
                ....*....|....*..
gi 48734396  79 FIVPWDTLSITQKKSLN 95
Cdd:cd03585 103 FVEPWDSLSLTQKKGLN 119
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 1-95 1.74e-50

Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as collagenases, and irreversibly inactivate them.


Pssm-ID: 128502  Cd Length: 172  Bit Score: 156.47  E-value: 1.74e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396      1 SEKEVDSGndiygnPIKRIQYEIKQIKMFKGPDK--DIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKMHITLCD 78
Cdd:smart00206  25 GKKEVNEG------NTLYQRYEIKQTKMFKGFDKlgDIRFIYTPASESLCGYKLESQNKEEYLIAGRLE-DGKMHITLCS 97

                           90
                   ....*....|....*..
gi 48734396     79 FIVPWDTLSITQKKSLN 95
Cdd:smart00206  98 FVVPWDSLSLAQRKGLN 114
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 1-95 4.05e-49

Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular regions of vertebrate species


Pssm-ID: 460012  Cd Length: 183  Bit Score: 153.37  E-value: 4.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396     1 SEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDK-----DIEFIYTAPSSAVCGVSLDVGGKkEYLIAGKAEGDGKMHIT 75
Cdd:pfam00965  27 GEKEVKTGNDMYGPPIKNIVYEIKQIKMFKGPQLvgkaaDIQAVYTPPSSSLCGVTLELNGK-EYLIAGKLVSDGKLHVT 105

                          90       100
                  ....*....|....*....|
gi 48734396    76 LCDFIVPWDTLSITQKKSLN 95
Cdd:pfam00965 106 LCNFVEPWETLTLAQRRGLN 125
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 14-95 2.33e-24

NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. This group contains domains similar to the TIMP NTR domain, which binds MMPs. Members of this group may or may not function as MMP inhibitors.


Pssm-ID: 239632  Cd Length: 116  Bit Score: 88.57  E-value: 2.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396  14 NPIKRIQYEIKQIKMFKGPDKD--IEFIYTAPSSAVCGVSLDVGgkKEYLIAGKAEgDGKMHITLCDFIVPWDTLSITQK 91
Cdd:cd03577  30 GAGLNIRYTIEIKKVYKGSEKSllPITIYTPSDDSACGIPLLEG--KEYLIAGKVE-DGALHTTLCDGVAPWDDLTKEQK 106


                ....
gi 48734396  92 KSLN 95
Cdd:cd03577 107 RGLK 110
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 17-95 1.50e-20

NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex.


Pssm-ID: 239600  Cd Length: 105  Bit Score: 78.67  E-value: 1.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48734396  17 KRIQYEIKQIKMFKGPD-----KDIEFIYTAPSSAVCgvSLDVGGKKEYLIAGKAEGD-GKMHITLCDFIVPWDTLSITQ 90
Cdd:cd03523  22 DDVKYEVKIIKIYKTGKakadkADLRFYYTAPACCPC--HPILNPGREYLIMGKEEDSqGGLVLDPLSFVEPWSPLSLRQ 99


                ....*
gi 48734396  91 KKSLN 95
Cdd:cd03523 100 DRRLR 104
 
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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