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Conserved domains on  [gi|1721879275|ref|XP_030229883|]
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metalloproteinase inhibitor 2-like isoform X1 [Gadus morhua]

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 ...
 39-221 1.37e-96

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: 279.69  E-value: 1.37e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  39 CSCSPAHPQQAFCSSDVVIRAKVIAMNKVDVGNDvYGNPVKQVKYDVKLIKMFKGP--VMDIEAIYTAPISALCGVTLDI 116
Cdd:cd03585     1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFdkDKDIQYIYTPASSSLCGVKLDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275 117 EGQMEYLITGKLEsDGNVHVTLCDFIEPWDAMSPIQKKSLPERYHMGCDCKIVRCETLPCALHADNECLWTDWVLENYIS 196
Cdd:cd03585    80 NGKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSIN 158

                         170       180
                  ....*....|....*....|....*
gi 1721879275 197 GPQAQHFACIQRRDGSCAWYRGAAQ 221
Cdd:cd03585   159 GHQAKHYACIKRSDGSCSWYRGGAP 183
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 39-221 1.37e-96

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: 279.69  E-value: 1.37e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  39 CSCSPAHPQQAFCSSDVVIRAKVIAMNKVDVGNDvYGNPVKQVKYDVKLIKMFKGP--VMDIEAIYTAPISALCGVTLDI 116
Cdd:cd03585     1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFdkDKDIQYIYTPASSSLCGVKLDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275 117 EGQMEYLITGKLEsDGNVHVTLCDFIEPWDAMSPIQKKSLPERYHMGCDCKIVRCETLPCALHADNECLWTDWVLENYIS 196
Cdd:cd03585    80 NGKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSIN 158

                         170       180
                  ....*....|....*....|....*
gi 1721879275 197 GPQAQHFACIQRRDGSCAWYRGAAQ 221
Cdd:cd03585   159 GHQAKHYACIKRSDGSCSWYRGGAP 183
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 37-215 7.63e-90

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


Pssm-ID: 460012  Cd Length: 183  Bit Score: 262.38  E-value: 7.63e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  37 EACSCSPAHPQQAFCSSDVVIRAKVIAMNKVDVGNDVYGNPVKQVKYDVKLIKMFKGP-----VMDIEAIYTAPISALCG 111
Cdd:pfam00965   1 EACSCSPSHPQQAFCNADVVIRAKVVGEKEVKTGNDMYGPPIKNIVYEIKQIKMFKGPqlvgkAADIQAVYTPPSSSLCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275 112 VTLDIEGQmEYLITGKLESDGNVHVTLCDFIEPWDAMSPIQKKSLPERYHMGCDCKIVRCETLPCALHADNECLWTDWVL 191
Cdd:pfam00965  81 VTLELNGK-EYLIAGKLVSDGKLHVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCSLSSPGECLWTDWVL 159

                         170       180
                  ....*....|....*....|....
gi 1721879275 192 ENYISGPQAQHFACIQRRDGSCAW 215
Cdd:pfam00965 160 EKDVNGCQAKHYACIKRSDGSCAW 183
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 39-215 4.45e-88

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


Pssm-ID: 128502  Cd Length: 172  Bit Score: 257.78  E-value: 4.45e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275   39 CSCSPAHPQQAFCSSDVVIRAKVIAMNKVDVGndvygnPVKQVKYDVKLIKMFKGP--VMDIEAIYTAPISALCGVTLDI 116
Cdd:smart00206   1 CSCSPPHPQTAFCNSDLVIRAKFVGKKEVNEG------NTLYQRYEIKQTKMFKGFdkLGDIRFIYTPASESLCGYKLES 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  117 EGQMEYLITGKLEsDGNVHVTLCDFIEPWDAMSPIQKKSLPERYHMGCDCKIVRCETLPCALHADNECLWTDWVLENYIS 196
Cdd:smart00206  75 QNKEEYLIAGRLE-DGKMHITLCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSDTECLWTDQLLEGSEK 153

                          170
                   ....*....|....*....
gi 1721879275  197 GPQAQHFACIQRRDGSCAW 215
Cdd:smart00206 154 GYQSKHYACIPREPGLCTW 172
 
Name Accession Description Interval E-value
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 39-221 1.37e-96

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: 279.69  E-value: 1.37e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  39 CSCSPAHPQQAFCSSDVVIRAKVIAMNKVDVGNDvYGNPVKQVKYDVKLIKMFKGP--VMDIEAIYTAPISALCGVTLDI 116
Cdd:cd03585     1 CSCAPVHPQQAFCNSDIVIRAKIVGEKEVDSGND-YGNPIKRIQYEIKQIKMFKGFdkDKDIQYIYTPASSSLCGVKLDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275 117 EGQMEYLITGKLEsDGNVHVTLCDFIEPWDAMSPIQKKSLPERYHMGCDCKIVRCETLPCALHADNECLWTDWVLENYIS 196
Cdd:cd03585    80 NGKKEYLISGKVE-GGKVHITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCFVSSPNECLWTDWLSEKSIN 158

                         170       180
                  ....*....|....*....|....*
gi 1721879275 197 GPQAQHFACIQRRDGSCAWYRGAAQ 221
Cdd:cd03585   159 GHQAKHYACIKRSDGSCSWYRGGAP 183
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 37-215 7.63e-90

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


Pssm-ID: 460012  Cd Length: 183  Bit Score: 262.38  E-value: 7.63e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  37 EACSCSPAHPQQAFCSSDVVIRAKVIAMNKVDVGNDVYGNPVKQVKYDVKLIKMFKGP-----VMDIEAIYTAPISALCG 111
Cdd:pfam00965   1 EACSCSPSHPQQAFCNADVVIRAKVVGEKEVKTGNDMYGPPIKNIVYEIKQIKMFKGPqlvgkAADIQAVYTPPSSSLCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275 112 VTLDIEGQmEYLITGKLESDGNVHVTLCDFIEPWDAMSPIQKKSLPERYHMGCDCKIVRCETLPCALHADNECLWTDWVL 191
Cdd:pfam00965  81 VTLELNGK-EYLIAGKLVSDGKLHVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCSLSSPGECLWTDWVL 159

                         170       180
                  ....*....|....*....|....
gi 1721879275 192 ENYISGPQAQHFACIQRRDGSCAW 215
Cdd:pfam00965 160 EKDVNGCQAKHYACIKRSDGSCAW 183
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 39-215 4.45e-88

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


Pssm-ID: 128502  Cd Length: 172  Bit Score: 257.78  E-value: 4.45e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275   39 CSCSPAHPQQAFCSSDVVIRAKVIAMNKVDVGndvygnPVKQVKYDVKLIKMFKGP--VMDIEAIYTAPISALCGVTLDI 116
Cdd:smart00206   1 CSCSPPHPQTAFCNSDLVIRAKFVGKKEVNEG------NTLYQRYEIKQTKMFKGFdkLGDIRFIYTPASESLCGYKLES 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  117 EGQMEYLITGKLEsDGNVHVTLCDFIEPWDAMSPIQKKSLPERYHMGCDCKIVRCETLPCALHADNECLWTDWVLENYIS 196
Cdd:smart00206  75 QNKEEYLIAGRLE-DGKMHITLCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSDTECLWTDQLLEGSEK 153

                          170
                   ....*....|....*....
gi 1721879275  197 GPQAQHFACIQRRDGSCAW 215
Cdd:smart00206 154 GYQSKHYACIPREPGLCTW 172
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 39-163 4.19e-32

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: 113.22  E-value: 4.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  39 CSCSPAHPQQAFCSSDVVIRAKVIAMNKVDVGNDVYgnpvkqvkYDVKLIKMFKGPVMD--IEAIYTAPISALCGVTLDI 116
Cdd:cd03577     1 CSCMPQHPQEKYCQADFVIKVKVLKKKLDGAGLNIR--------YTIEIKKVYKGSEKSllPITIYTPSDDSACGIPLLE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1721879275 117 EGqmEYLITGKLEsDGNVHVTLCDFIEPWDAMSPIQKKSLPERYHMG 163
Cdd:cd03577    73 GK--EYLIAGKVE-DGALHTTLCDGVAPWDDLTKEQKRGLKGLYKKG 116
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 48-158 1.56e-18

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: 77.89  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721879275  48 QAFCSSDVVIRAKVIAMNKVDVGndvygnpvkqVKYDVKLIKMFKGP-----VMDIEAIYTAPISALCgvTLDIEGQMEY 122
Cdd:cd03523     1 KAFCKSDYVVRAKIKEIKEENDD----------VKYEVKIIKIYKTGkakadKADLRFYYTAPACCPC--HPILNPGREY 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1721879275 123 LITGKLE-SDGNVHVTLCDFIEPWDAMSPIQKKSLPE 158
Cdd:cd03523    69 LIMGKEEdSQGGLVLDPLSFVEPWSPLSLRQDRRLRE 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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