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Conserved domains on  [gi|24645638|ref|NP_731461|]
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tissue inhibitor of metalloproteases [Drosophila melanogaster]

Protein Classification

NTR_TIMP_like domain-containing protein( domain architecture ID 10132415)

NTR_TIMP_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 28-141 3.25e-39

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: 130.56  E-value: 3.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638  28 CSCMPSHPQTHFAQADYVVQLRVLRKSDTIEPGRTTYKVHIKRTYKATSearRMLRDGRLSTPQDDAMCGINLDLGKVYI 107
Cdd:cd03577   1 CSCMPQHPQEKYCQADFVIKVKVLKKKLDGAGLNIRYTIEIKKVYKGSE---KSLLPITIYTPSDDSACGIPLLEGKEYL 77

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 24645638 108 VAGRM----PTLNICSYYKEYTRMTITERHGFSGGYAK 141
Cdd:cd03577  78 IAGKVedgaLHTTLCDGVAPWDDLTKEQKRGLKGLYKK 115
 
Name Accession Description Interval E-value
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 28-141 3.25e-39

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: 130.56  E-value: 3.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638  28 CSCMPSHPQTHFAQADYVVQLRVLRKSDTIEPGRTTYKVHIKRTYKATSearRMLRDGRLSTPQDDAMCGINLDLGKVYI 107
Cdd:cd03577   1 CSCMPQHPQEKYCQADFVIKVKVLKKKLDGAGLNIRYTIEIKKVYKGSE---KSLLPITIYTPSDDSACGIPLLEGKEYL 77

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 24645638 108 VAGRM----PTLNICSYYKEYTRMTITERHGFSGGYAK 141
Cdd:cd03577  78 IAGKVedgaLHTTLCDGVAPWDDLTKEQKRGLKGLYKK 115
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 26-184 2.10e-28

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


Pssm-ID: 460012  Cd Length: 183  Bit Score: 105.22  E-value: 2.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638    26 DACSCMPSHPQTHFAQADYVVQLRVLRKSDTIEP--------GRTTYKVHIKRTYKATSEARRMLRDGRLSTPQDDAMCG 97
Cdd:pfam00965   1 EACSCSPSHPQQAFCNADVVIRAKVVGEKEVKTGndmygppiKNIVYEIKQIKMFKGPQLVGKAADIQAVYTPPSSSLCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638    98 INLDL-GKVYIVAGRMPT-----LNICSYYKEYTRMTITERHGFSGGYAKATNCTVTPCFGERCFkgRNYADTCKWSP-- 169
Cdd:pfam00965  81 VTLELnGKEYLIAGKLVSdgklhVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCS--LSSPGECLWTDwv 158

                         170
                  ....*....|....*....
gi 24645638   170 ----FGKCETNYSACMPHK 184
Cdd:pfam00965 159 lekdVNGCQAKHYACIKRS 177
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 28-184 7.90e-16

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


Pssm-ID: 128502  Cd Length: 172  Bit Score: 71.73  E-value: 7.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638     28 CSCMPSHPQTHFAQADYVVQLRVLRKSDTIEP--GRTTYKVHIKRTYKATSEarrmLRDGR-LSTPQDDAMCGINLDLG- 103
Cdd:smart00206   1 CSCSPPHPQTAFCNSDLVIRAKFVGKKEVNEGntLYQRYEIKQTKMFKGFDK----LGDIRfIYTPASESLCGYKLESQn 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638    104 -KVYIVAGRMPTLNI----CSYYKEYTRMTITERHGFSGGYAKATNCTVTPCFGERCFKGRNyaDTCKWS------PFGK 172
Cdd:smart00206  77 kEEYLIAGRLEDGKMhitlCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSD--TECLWTdqllegSEKG 154

                          170
                   ....*....|..
gi 24645638    173 CETNYSACMPHK 184
Cdd:smart00206 155 YQSKHYACIPRE 166
 
Name Accession Description Interval E-value
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 28-141 3.25e-39

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: 130.56  E-value: 3.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638  28 CSCMPSHPQTHFAQADYVVQLRVLRKSDTIEPGRTTYKVHIKRTYKATSearRMLRDGRLSTPQDDAMCGINLDLGKVYI 107
Cdd:cd03577   1 CSCMPQHPQEKYCQADFVIKVKVLKKKLDGAGLNIRYTIEIKKVYKGSE---KSLLPITIYTPSDDSACGIPLLEGKEYL 77

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 24645638 108 VAGRM----PTLNICSYYKEYTRMTITERHGFSGGYAK 141
Cdd:cd03577  78 IAGKVedgaLHTTLCDGVAPWDDLTKEQKRGLKGLYKK 115
TIMP pfam00965
Tissue inhibitor of metalloproteinase; Members of this family are common in extracellular ...
 26-184 2.10e-28

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


Pssm-ID: 460012  Cd Length: 183  Bit Score: 105.22  E-value: 2.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638    26 DACSCMPSHPQTHFAQADYVVQLRVLRKSDTIEP--------GRTTYKVHIKRTYKATSEARRMLRDGRLSTPQDDAMCG 97
Cdd:pfam00965   1 EACSCSPSHPQQAFCNADVVIRAKVVGEKEVKTGndmygppiKNIVYEIKQIKMFKGPQLVGKAADIQAVYTPPSSSLCG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638    98 INLDL-GKVYIVAGRMPT-----LNICSYYKEYTRMTITERHGFSGGYAKATNCTVTPCFGERCFkgRNYADTCKWSP-- 169
Cdd:pfam00965  81 VTLELnGKEYLIAGKLVSdgklhVTLCNFVEPWETLTLAQRRGLNQRYGMGCDCKITPCSSIPCS--LSSPGECLWTDwv 158

                         170
                  ....*....|....*....
gi 24645638   170 ----FGKCETNYSACMPHK 184
Cdd:pfam00965 159 lekdVNGCQAKHYACIKRS 177
NTR smart00206
Tissue inhibitor of metalloproteinase family; Form complexes with metalloproteinases, such as ...
 28-184 7.90e-16

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


Pssm-ID: 128502  Cd Length: 172  Bit Score: 71.73  E-value: 7.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638     28 CSCMPSHPQTHFAQADYVVQLRVLRKSDTIEP--GRTTYKVHIKRTYKATSEarrmLRDGR-LSTPQDDAMCGINLDLG- 103
Cdd:smart00206   1 CSCSPPHPQTAFCNSDLVIRAKFVGKKEVNEGntLYQRYEIKQTKMFKGFDK----LGDIRfIYTPASESLCGYKLESQn 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638    104 -KVYIVAGRMPTLNI----CSYYKEYTRMTITERHGFSGGYAKATNCTVTPCFGERCFKGRNyaDTCKWS------PFGK 172
Cdd:smart00206  77 kEEYLIAGRLEDGKMhitlCSFVVPWDSLSLAQRKGLNKRYHAGCECKIFPCYSIPCKLSSD--TECLWTdqllegSEKG 154

                          170
                   ....*....|..
gi 24645638    173 CETNYSACMPHK 184
Cdd:smart00206 155 YQSKHYACIPRE 166
NTR_TIMP cd03585
NTR domain, TIMP subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
 28-156 9.91e-14

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: 66.67  E-value: 9.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638  28 CSCMPSHPQTHFAQADYVVQLRVLRK------SDTIEP-GRTTYKVHIKRTYKATSEARRMlrdGRLSTPQDDAMCGINL 100
Cdd:cd03585   1 CSCAPVHPQQAFCNSDIVIRAKIVGEkevdsgNDYGNPiKRIQYEIKQIKMFKGFDKDKDI---QYIYTPASSSLCGVKL 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24645638 101 DLG--KVYIVAGRMPT----LNICSYYKEYTRMTITERHGFSGGYAKATNCTVTPCFGERCF 156
Cdd:cd03585  78 DVNgkKEYLISGKVEGgkvhITLCDFVEPWDSLSLTQKKGLNHRYQMGCECKITPCYTIPCF 139
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 37-120 2.15e-06

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: 44.77  E-value: 2.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638  37 THFAQADYVVQLRVlrKSDTIEPGRTTYKVHIKRTYKaTSEARRMLRDGRL-STPQDDAMCGINLDLGKVYIVAGR---- 111
Cdd:cd03523   1 KAFCKSDYVVRAKI--KEIKEENDDVKYEVKIIKIYK-TGKAKADKADLRFyYTAPACCPCHPILNPGREYLIMGKeeds 77

                        90
                ....*....|.
gi 24645638 112 --MPTLNICSY 120
Cdd:cd03523  78 qgGLVLDPLSF 88
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 43-111 9.12e-04

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 37.32  E-value: 9.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638    43 DYVVQLRVLRKsdTIEPGRTTYKVHIKRTYKATSEARRmLRDGRLSTPqdDAMCG-INLDLGKVYIVAGR 111
Cdd:pfam01759   8 DYVYKVKVLSV--EEEGSFDKYTVKVKEVLKEGTDKIQ-RGKVRLFLK--RGDCRcPQLRLGKEYLIMGK 72
C345C smart00643
Netrin C-terminal Domain;
43-132 8.90e-03

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 35.04  E-value: 8.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645638     43 DYVVQLRVLRKsdTIEPGRTTYKVHIKRTYKATSE----ARRMLRDgRLSTPQddAMCGINLDLGKVYIVAGRMPTLnic 118
Cdd:smart00643  10 DYVYKVKVLSV--EEEGGFDKYTVKILEVIKSGTDelvrGKNKLRV-FISRAS--CRCPLLLKLGKSYLIMGKSGDL--- 81

                           90
                   ....*....|....
gi 24645638    119 SYYKEYTRMTITER 132
Cdd:smart00643  82 WDAKGRGQYVLGKN 95
 
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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