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Conserved domains on  [gi|1622881792|ref|XP_028692704|]
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metalloproteinase inhibitor 2 isoform X2 [Macaca mulatta]

Protein Classification

NTR_TIMP domain-containing protein( domain architecture ID 10132426)

NTR_TIMP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 12-176 9.33e-105

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: 298.18  E-value: 9.33e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  12 IRAKAVSEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPE--KDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKM 89
Cdd:cd03585    19 IRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDVNGKKEYLISGKVE-GGKV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  90 HITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCA 169
Cdd:cd03585    97 HITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSINGHQAKHYACIKRSDGSCS 176


                  ....*..
gi 1622881792 170 WYRGAAP 176
Cdd:cd03585   177 WYRGGAP 183
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 12-176 9.33e-105

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: 298.18  E-value: 9.33e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  12 IRAKAVSEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPE--KDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKM 89
Cdd:cd03585    19 IRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDVNGKKEYLISGKVE-GGKV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  90 HITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCA 169
Cdd:cd03585    97 HITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSINGHQAKHYACIKRSDGSCS 176


                  ....*..
gi 1622881792 170 WYRGAAP 176
Cdd:cd03585   177 WYRGGAP 183
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 12-170 3.75e-95

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


Pssm-ID: 128502  Cd Length: 172  Bit Score: 273.57  E-value: 3.75e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792   12 IRAKAVSEKEVDSGndiygnPIKRIQYEIKQIKMFKGPEK--DIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKM 89
Cdd:smart00206  19 IRAKFVGKKEVNEG------NTLYQRYEIKQTKMFKGFDKlgDIRFIYTPASESLCGYKLESQNKEEYLIAGRLE-DGKM 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792   90 HITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCA 169
Cdd:smart00206  92 HITLCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSDTECLWTDQLLEGSEKGYQSKHYACIPREPGLCT 171


                   .
gi 1622881792  170 W 170
Cdd:smart00206 172 W 172
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 12-170 1.62e-88

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


Pssm-ID: 460012  Cd Length: 183  Bit Score: 257.37  E-value: 1.62e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  12 IRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEK-----DIEFIYTAPSSAVCGVSLDVGGKkEYLIAGKAEGD 86
Cdd:pfam00965  21 IRAKVVGEKEVKTGNDMYGPPIKNIVYEIKQIKMFKGPQLvgkaaDIQAVYTPPSSSLCGVTLELNGK-EYLIAGKLVSD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  87 GKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDG 166
Cdd:pfam00965 100 GKLHVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCSLSSPGECLWTDWVLEKDVNGCQAKHYACIKRSDG 179


                  ....
gi 1622881792 167 SCAW 170
Cdd:pfam00965 180 SCAW 183
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 12-176 9.33e-105

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: 298.18  E-value: 9.33e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  12 IRAKAVSEKEVDSGNDiYGNPIKRIQYEIKQIKMFKGPE--KDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKM 89
Cdd:cd03585    19 IRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFDkdKDIQYIYTPASSSLCGVKLDVNGKKEYLISGKVE-GGKV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  90 HITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCA 169
Cdd:cd03585    97 HITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSINGHQAKHYACIKRSDGSCS 176


                  ....*..
gi 1622881792 170 WYRGAAP 176
Cdd:cd03585   177 WYRGGAP 183
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 12-170 3.75e-95

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


Pssm-ID: 128502  Cd Length: 172  Bit Score: 273.57  E-value: 3.75e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792   12 IRAKAVSEKEVDSGndiygnPIKRIQYEIKQIKMFKGPEK--DIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEgDGKM 89
Cdd:smart00206  19 IRAKFVGKKEVNEG------NTLYQRYEIKQTKMFKGFDKlgDIRFIYTPASESLCGYKLESQNKEEYLIAGRLE-DGKM 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792   90 HITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCA 169
Cdd:smart00206  92 HITLCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSDTECLWTDQLLEGSEKGYQSKHYACIPREPGLCT 171


                   .
gi 1622881792  170 W 170
Cdd:smart00206 172 W 172
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 12-170 1.62e-88

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


Pssm-ID: 460012  Cd Length: 183  Bit Score: 257.37  E-value: 1.62e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  12 IRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEK-----DIEFIYTAPSSAVCGVSLDVGGKkEYLIAGKAEGD 86
Cdd:pfam00965  21 IRAKVVGEKEVKTGNDMYGPPIKNIVYEIKQIKMFKGPQLvgkaaDIQAVYTPPSSSLCGVTLELNGK-EYLIAGKLVSD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  87 GKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDG 166
Cdd:pfam00965 100 GKLHVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCSLSSPGECLWTDWVLEKDVNGCQAKHYACIKRSDG 179


                  ....
gi 1622881792 167 SCAW 170
Cdd:pfam00965 180 SCAW 183
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 12-118 6.34e-27

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: 98.58  E-value: 6.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  12 IRAKAVSEKEVDSGNdiygnpikRIQYEIKQIKMFKGPEKD--IEFIYTAPSSAVCGVSLDVGgkKEYLIAGKAEgDGKM 89
Cdd:cd03577    19 IKVKVLKKKLDGAGL--------NIRYTIEIKKVYKGSEKSllPITIYTPSDDSACGIPLLEG--KEYLIAGKVE-DGAL 87

                          90       100
                  ....*....|....*....|....*....
gi 1622881792  90 HITLCDFIVPWDTLSTTQKKSLNHRYQMG 118
Cdd:cd03577    88 HTTLCDGVAPWDDLTKEQKRGLKGLYKKG 116
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 12-113 2.18e-22

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: 86.37  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881792  12 IRAKAVSEKEVDsgndiygnpiKRIQYEIKQIKMFKGPE-----KDIEFIYTAPSSAVCgvSLDVGGKKEYLIAGKAEGD 86
Cdd:cd03523    10 VRAKIKEIKEEN----------DDVKYEVKIIKIYKTGKakadkADLRFYYTAPACCPC--HPILNPGREYLIMGKEEDS 77

                          90       100
                  ....*....|....*....|....*...
gi 1622881792  87 -GKMHITLCDFIVPWDTLSTTQKKSLNH 113
Cdd:cd03523    78 qGGLVLDPLSFVEPWSPLSLRQDRRLRE 105
 
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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