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Conserved domains on  [gi|767974273|ref|XP_011536658|]
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matrix metalloproteinase-17 isoform X1 [Homo sapiens]

Protein Classification

M10A family metallopeptidase( domain architecture ID 10477974)

M10A family metallopeptidase similar to matrix metalloproteinases with a C-terminal hemopexin repeat-containing domain that may be endopeptidases that degrade various components of the extracellular matrix

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 245-439 6.64e-75

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 234.90  E-value: 6.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 245 PHRCST-HFDAVAQIRGEAFFFKGKYFWRLtrDRHLVSLQPAQMHRFWRGLPlhlDSVDAVYERTSDHKIVFFKGDRYWV 323
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLP---SPVDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 324 FKDNNVEEGYPRPVSDFSLPP--GGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQ-SPLWRGVPSTLDDAMR 400
Cdd:cd00094   76 YTGKNLEPGYPKPISDLGFPPtvKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767974273 401 WSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVC 439
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 48-211 8.30e-72

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


:

Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 225.55  E-value: 8.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  48 KWNKRNLSWRVRTFPRDspLGHDTVRALMYYALKVWSDIAPLNFHEVAGSA-ADIQIDFSKADHNDGYPFDGPGGTVAHA 126
Cdd:cd04278    1 KWSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 127 FFPGhhHTAGDTHFDDDEAWTFrSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDplrYGLPYEDKVRV 206
Cdd:cd04278   79 FFPG--GIGGDIHFDDDEQWTL-GSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 767974273 207 WQLYG 211
Cdd:cd04278  153 QALYG 157
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 1-21 1.55e-03

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 36.72  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|.
gi 767974273    1 MQQFGGLEATGILDEATLALM 21
Cdd:pfam01471  37 FQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 245-439 6.64e-75

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 234.90  E-value: 6.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 245 PHRCST-HFDAVAQIRGEAFFFKGKYFWRLtrDRHLVSLQPAQMHRFWRGLPlhlDSVDAVYERTSDHKIVFFKGDRYWV 323
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLP---SPVDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 324 FKDNNVEEGYPRPVSDFSLPP--GGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQ-SPLWRGVPSTLDDAMR 400
Cdd:cd00094   76 YTGKNLEPGYPKPISDLGFPPtvKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767974273 401 WSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVC 439
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 48-211 8.30e-72

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 225.55  E-value: 8.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  48 KWNKRNLSWRVRTFPRDspLGHDTVRALMYYALKVWSDIAPLNFHEVAGSA-ADIQIDFSKADHNDGYPFDGPGGTVAHA 126
Cdd:cd04278    1 KWSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 127 FFPGhhHTAGDTHFDDDEAWTFrSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDplrYGLPYEDKVRV 206
Cdd:cd04278   79 FFPG--GIGGDIHFDDDEQWTL-GSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 767974273 207 WQLYG 211
Cdd:cd04278  153 QALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 48-211 4.34e-67

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 213.25  E-value: 4.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273   48 KWNKRNLSWRVRTFPRDspLGHDTVRALMYYALKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPFDGPGGTVAHAF 127
Cdd:pfam00413   1 KWRKKNLTYRILNYTPD--LPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  128 FPGhHHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGpvGDPLRYGLPYEDKVRVW 207
Cdd:pfam00413  79 FPG-PGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP--LDSKKFRLSQDDIKGIQ 155


                  ....
gi 767974273  208 QLYG 211
Cdd:pfam00413 156 QLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 47-211 1.19e-18

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 82.40  E-value: 1.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273    47 TKWNKRNLSWRVRTfprdSPLGhDTVRALMYYALKVWSDIAPLNFHEVAgSAADIQIDFSKADHndgypfdgpGGTVAHA 126
Cdd:smart00235   3 KKWPKGTVPYVIDS----SSLS-PEEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273   127 FFPGhhhtaGDTHFDDdeawtfrssdAHGMDLFAVAVHEFGHAIGLSHV---AAAHSIMRPYYQGPvgDPLRYGLPYEDK 203
Cdd:smart00235  68 GRPG-----GDQHLSL----------GNGCINTGVAAHELGHALGLYHEqsrSDRDNYMYINYTNI--DTRNFDLSEDDS 130


                   ....*...
gi 767974273   204 VRVWQLYG 211
Cdd:smart00235 131 LGIPYDYG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-393 2.35e-10

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 55.71  E-value: 2.35e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767974273   347 IDAAFSWaHNDRTYFFKDQLYWRYDDHTrhMDPGYPAQ-SPLWRGVPS 393
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKR--VDPGYPKLiSSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-344 3.64e-09

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 52.18  E-value: 3.64e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767974273  301 VDAVYERtSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDF-SLPP 344
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 1-21 1.55e-03

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 36.72  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|.
gi 767974273    1 MQQFGGLEATGILDEATLALM 21
Cdd:pfam01471  37 FQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 245-439 6.64e-75

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 234.90  E-value: 6.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 245 PHRCST-HFDAVAQIRGEAFFFKGKYFWRLtrDRHLVSLQPAQMHRFWRGLPlhlDSVDAVYERTSDHKIVFFKGDRYWV 323
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLP---SPVDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 324 FKDNNVEEGYPRPVSDFSLPP--GGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQ-SPLWRGVPSTLDDAMR 400
Cdd:cd00094   76 YTGKNLEPGYPKPISDLGFPPtvKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767974273 401 WSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVC 439
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 48-211 8.30e-72

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 225.55  E-value: 8.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  48 KWNKRNLSWRVRTFPRDspLGHDTVRALMYYALKVWSDIAPLNFHEVAGSA-ADIQIDFSKADHNDGYPFDGPGGTVAHA 126
Cdd:cd04278    1 KWSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 127 FFPGhhHTAGDTHFDDDEAWTFrSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDplrYGLPYEDKVRV 206
Cdd:cd04278   79 FFPG--GIGGDIHFDDDEQWTL-GSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 767974273 207 WQLYG 211
Cdd:cd04278  153 QALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 48-211 4.34e-67

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 213.25  E-value: 4.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273   48 KWNKRNLSWRVRTFPRDspLGHDTVRALMYYALKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPFDGPGGTVAHAF 127
Cdd:pfam00413   1 KWRKKNLTYRILNYTPD--LPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  128 FPGhHHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGpvGDPLRYGLPYEDKVRVW 207
Cdd:pfam00413  79 FPG-PGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP--LDSKKFRLSQDDIKGIQ 155


                  ....
gi 767974273  208 QLYG 211
Cdd:pfam00413 156 QLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 47-211 1.19e-18

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 82.40  E-value: 1.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273    47 TKWNKRNLSWRVRTfprdSPLGhDTVRALMYYALKVWSDIAPLNFHEVAgSAADIQIDFSKADHndgypfdgpGGTVAHA 126
Cdd:smart00235   3 KKWPKGTVPYVIDS----SSLS-PEEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273   127 FFPGhhhtaGDTHFDDdeawtfrssdAHGMDLFAVAVHEFGHAIGLSHV---AAAHSIMRPYYQGPvgDPLRYGLPYEDK 203
Cdd:smart00235  68 GRPG-----GDQHLSL----------GNGCINTGVAAHELGHALGLYHEqsrSDRDNYMYINYTNI--DTRNFDLSEDDS 130


                   ....*...
gi 767974273   204 VRVWQLYG 211
Cdd:smart00235 131 LGIPYDYG 138
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 78-174 1.78e-10

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 60.12  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  78 YALKVWSDIAPLNFHEVA-GSAADIQIDFSKADHNDGYpfdgpggtvAHAFFPG---HHHTAGDTHFDDDEAWTFRSSDA 153
Cdd:cd04277   41 DALEAWEDVADIDFVEVSdNSGADIRFGNSSDPDGNTA---------GYAYYPGsgsGTAYGGDIWFNSSYDTNSDSPGS 111

                         90       100
                 ....*....|....*....|.
gi 767974273 154 HGmdlFAVAVHEFGHAIGLSH 174
Cdd:cd04277  112 YG---YQTIIHEIGHALGLEH 129
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-393 2.35e-10

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 55.71  E-value: 2.35e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767974273   347 IDAAFSWaHNDRTYFFKDQLYWRYDDHTrhMDPGYPAQ-SPLWRGVPS 393
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKR--VDPGYPKLiSSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-340 2.69e-09

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 52.63  E-value: 2.69e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 767974273   301 VDAVYERtSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDF 340
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSF 39
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-344 3.64e-09

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 52.18  E-value: 3.64e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767974273  301 VDAVYERtSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDF-SLPP 344
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 51-193 6.16e-09

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 55.16  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  51 KRNLSWRVRTFPRDSPLGHDTVRALMYYALKVWSDIAPLNFHEVAGSA--ADIQIDFSKADHNDGYpfdgpGGTVAHAFF 128
Cdd:cd04279    1 KSPIRVYIDPTPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDndADIVIFFDRPPPVGGA-----GGGLARAGF 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767974273 129 PGHHHTAGDT--HFDDDEAWTFRSSDAhgmDLFAVAVHEFGHAIGLSHV-AAAHSIMRPYY-QGPVGDP 193
Cdd:cd04279   76 PLISDGNRKLfnRTDINLGPGQPRGAE---NLQAIALHELGHALGLWHHsDRPEDAMYPSQgQGPDGNP 141
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-393 1.66e-08

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 50.26  E-value: 1.66e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 767974273  347 IDAAFSWAHNdRTYFFKDQLYWRYDDhtRHMDPGYPAQSPLWRGVPS 393
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLPC 44
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 72-210 8.02e-07

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 49.06  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  72 VRALMYYALKVWSDIAPLNFHEVAG--SAADIQIDFSKADHNdgypfdgpGGTVAHAFFPG-HHHTAGDTHFDDDEAWTF 148
Cdd:cd00203   23 IQSLILIAMQIWRDYLNIRFVLVGVeiDKADIAILVTRQDFD--------GGTGGWAYLGRvCDSLRGVGVLQDNQSGTK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273 149 rssdahgmDLFAVAVHEFGHAIGLSH--------------------VAAAHSIMRPYYqGPVGDPLRYGLPYEDKVRVWQ 208
Cdd:cd00203   95 --------EGAQTIAHELGHALGFYHdhdrkdrddyptiddtlnaeDDDYYSVMSYTK-GSFSDGQRKDFSQCDIDQINK 165


                 ..
gi 767974273 209 LY 210
Cdd:cd00203  166 LY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 252-295 6.91e-06

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 43.00  E-value: 6.91e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767974273   252 FDAVAQIR-GEAFFFKGKYFWRLTRDRHLVSLqPAQMHRFWRGLP 295
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGY-PKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 395-436 1.56e-05

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 42.23  E-value: 1.56e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 767974273   395 LDDAMRWSDGASYFFRGQEYWKVLDGELEvaPGYPQSTARDW 436
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVD--PGYPKLISSFF 40
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 69-174 5.87e-05

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 44.29  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  69 HDTVRALMyyalKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPfdgpgGTVAHAFfPGHHHTAGdthFDDDEawtf 148
Cdd:cd04327   22 KDKVRAAA----REWLPYANLKFKFVTDADADIRISFTPGDGYWSYV-----GTDALLI-GADAPTMN---LGWFT---- 84

                         90       100
                 ....*....|....*....|....*.
gi 767974273 149 rsSDAHGMDLFAVAVHEFGHAIGLSH 174
Cdd:cd04327   85 --DDTPDPEFSRVVLHEFGHALGFIH 108
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 69-196 8.80e-04

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 40.17  E-value: 8.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974273  69 HDTVRALMYYALKVWSDIAPLNFHEVA-GSAADIQIdfskADHNDGYPFDGPGGTVAHAFFPGHhhtaGDTHFDDDEAWT 147
Cdd:cd04268   13 PDKLRAAILDAIEAWNKAFAIGFKNANdVDPADIRY----SVIRWIPYNDGTWSYGPSQVDPLT----GEILLARVYLYS 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767974273 148 FRSSDAHGmDLFAVAVHEFGHAIGLSHVAAAhSIMRPYYQGPVGDPLRY 196
Cdd:cd04268   85 SFVEYSGA-RLRNTAEHELGHALGLRHNFAA-SDRDDNVDLLAEKGDTS 131
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 395-436 1.10e-03

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 36.78  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 767974273  395 LDDAMRWSDGASYFFRGQEYWKVLDGELEvaPGYPQSTARDW 436
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVE--PGYPKLISDFP 40
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 252-274 1.54e-03

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 36.39  E-value: 1.54e-03
                          10        20
                  ....*....|....*....|....
gi 767974273  252 FDAVAQIR-GEAFFFKGKYFWRLT 274
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFD 24
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 1-21 1.55e-03

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 36.72  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|.
gi 767974273    1 MQQFGGLEATGILDEATLALM 21
Cdd:pfam01471  37 FQRAFGLPVDGIVDPETLAAL 57
 
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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