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Conserved domains on  [gi|157786912|ref|NP_001099395|]
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matrix metalloproteinase-17 precursor [Rattus norvegicus]

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
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 131-294 9.39e-75

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: 235.18  E-value: 9.39e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 131 KWSKRNLSWRVRTFPRDspLGRDTVRALMYYALKVWSDITPLNFHEVAGNM-ADIQIDFSKADHNDGYPFDGPGGTVAHA 209
Cdd:cd04278    1 KWSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 210 FFPGdhHTAGDTHFDDDEAWTFrSSDAHGMDLFAVAVHEFGHAIGLSHVAAPSSIMQPYYQGPVGDplrYGLPYEDRVRV 289
Cdd:cd04278   79 FFPG--GIGGDIHFDDDEQWTL-GSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 157786912 290 WQLYG 294
Cdd:cd04278  153 QALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-527 3.79e-74

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: 3.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 333 PHRCTA-HFDAVAQIRGEAFFFKGKYFWRLtrDRHLVSLQPAQMHRFWRGLPlhlDSVDAVYERTSDHKIVFFKGDRYWV 411
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLP---SPVDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 412 FKDNNVEEGYPRPVSDFSLPP--GGIDAVFSWAHNDRTYFFKDQLYWRYDDHTRRMDPGYPAQ-GPLWRGVPSVLDDAMR 488
Cdd:cd00094   76 YTGKNLEPGYPKPISDLGFPPtvKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157786912 489 WSDGASYFFRGQEYWKVLDGELEAAPGYPQSTARDWLVC 527
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 44-104 1.10e-08

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: 51.36  E-value: 1.10e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157786912   44 RAEDLSLGVEWLSKFGYLPpaDPATGQLQtqEELSKAITAMQQFGGLETTGILDEATLALM 104
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYP--GPVDGYFG--PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 131-294 9.39e-75

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: 235.18  E-value: 9.39e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 131 KWSKRNLSWRVRTFPRDspLGRDTVRALMYYALKVWSDITPLNFHEVAGNM-ADIQIDFSKADHNDGYPFDGPGGTVAHA 209
Cdd:cd04278    1 KWSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 210 FFPGdhHTAGDTHFDDDEAWTFrSSDAHGMDLFAVAVHEFGHAIGLSHVAAPSSIMQPYYQGPVGDplrYGLPYEDRVRV 289
Cdd:cd04278   79 FFPG--GIGGDIHFDDDEQWTL-GSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 157786912 290 WQLYG 294
Cdd:cd04278  153 QALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-527 3.79e-74

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: 3.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 333 PHRCTA-HFDAVAQIRGEAFFFKGKYFWRLtrDRHLVSLQPAQMHRFWRGLPlhlDSVDAVYERTSDHKIVFFKGDRYWV 411
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLP---SPVDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 412 FKDNNVEEGYPRPVSDFSLPP--GGIDAVFSWAHNDRTYFFKDQLYWRYDDHTRRMDPGYPAQ-GPLWRGVPSVLDDAMR 488
Cdd:cd00094   76 YTGKNLEPGYPKPISDLGFPPtvKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157786912 489 WSDGASYFFRGQEYWKVLDGELEAAPGYPQSTARDWLVC 527
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 131-294 9.51e-72

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: 227.11  E-value: 9.51e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912  131 KWSKRNLSWRVRTFPRDspLGRDTVRALMYYALKVWSDITPLNFHEVAGNMADIQIDFSKADHNDGYPFDGPGGTVAHAF 210
Cdd:pfam00413   1 KWRKKNLTYRILNYTPD--LPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912  211 FPGDhHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAPSSIMQPYYQGpvGDPLRYGLPYEDRVRVW 290
Cdd:pfam00413  79 FPGP-GLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP--LDSKKFRLSQDDIKGIQ 155


                  ....
gi 157786912  291 QLYG 294
Cdd:pfam00413 156 QLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-294 6.36e-22

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: 92.03  E-value: 6.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912   130 TKWSKRNLSWRVRTfprdSPLGRDtVRALMYYALKVWSDITPLNFHEVAGNmADIQIDFSKADHndgypfdgpGGTVAHA 209
Cdd:smart00235   3 KKWPKGTVPYVIDS----SSLSPE-EREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912   210 FFPGdhhtaGDTHFDDdeawtfrssdAHGMDLFAVAVHEFGHAIGLSHVAAPSS---IMQPYYQGPvgDPLRYGLPYEDR 286
Cdd:smart00235  68 GRPG-----GDQHLSL----------GNGCINTGVAAHELGHALGLYHEQSRSDrdnYMYINYTNI--DTRNFDLSEDDS 130


                   ....*...
gi 157786912   287 VRVWQLYG 294
Cdd:smart00235 131 LGIPYDYG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 435-481 1.06e-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: 54.17  E-value: 1.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 157786912   435 IDAVFSWaHNDRTYFFKDQLYWRYDDHtrRMDPGYPAQ-GPLWRGVPS 481
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPK--RVDPGYPKLiSSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 389-432 2.79e-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: 52.95  E-value: 2.79e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 157786912  389 VDAVYERtSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDF-SLPP 432
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 44-104 1.10e-08

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: 51.36  E-value: 1.10e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157786912   44 RAEDLSLGVEWLSKFGYLPpaDPATGQLQtqEELSKAITAMQQFGGLETTGILDEATLALM 104
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYP--GPVDGYFG--PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 131-294 9.39e-75

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: 235.18  E-value: 9.39e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 131 KWSKRNLSWRVRTFPRDspLGRDTVRALMYYALKVWSDITPLNFHEVAGNM-ADIQIDFSKADHNDGYPFDGPGGTVAHA 209
Cdd:cd04278    1 KWSKTNLTYRILNYPPD--LPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 210 FFPGdhHTAGDTHFDDDEAWTFrSSDAHGMDLFAVAVHEFGHAIGLSHVAAPSSIMQPYYQGPVGDplrYGLPYEDRVRV 289
Cdd:cd04278   79 FFPG--GIGGDIHFDDDEQWTL-GSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGI 152


                 ....*
gi 157786912 290 WQLYG 294
Cdd:cd04278  153 QALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-527 3.79e-74

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: 3.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 333 PHRCTA-HFDAVAQIRGEAFFFKGKYFWRLtrDRHLVSLQPAQMHRFWRGLPlhlDSVDAVYERTSDHKIVFFKGDRYWV 411
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRL--SPGKPPGSPFLISSFWPSLP---SPVDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 412 FKDNNVEEGYPRPVSDFSLPP--GGIDAVFSWAHNDRTYFFKDQLYWRYDDHTRRMDPGYPAQ-GPLWRGVPSVLDDAMR 488
Cdd:cd00094   76 YTGKNLEPGYPKPISDLGFPPtvKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157786912 489 WSDGASYFFRGQEYWKVLDGELEAAPGYPQSTARDWLVC 527
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 131-294 9.51e-72

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: 227.11  E-value: 9.51e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912  131 KWSKRNLSWRVRTFPRDspLGRDTVRALMYYALKVWSDITPLNFHEVAGNMADIQIDFSKADHNDGYPFDGPGGTVAHAF 210
Cdd:pfam00413   1 KWRKKNLTYRILNYTPD--LPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912  211 FPGDhHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAPSSIMQPYYQGpvGDPLRYGLPYEDRVRVW 290
Cdd:pfam00413  79 FPGP-GLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP--LDSKKFRLSQDDIKGIQ 155


                  ....
gi 157786912  291 QLYG 294
Cdd:pfam00413 156 QLYG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-294 6.36e-22

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: 92.03  E-value: 6.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912   130 TKWSKRNLSWRVRTfprdSPLGRDtVRALMYYALKVWSDITPLNFHEVAGNmADIQIDFSKADHndgypfdgpGGTVAHA 209
Cdd:smart00235   3 KKWPKGTVPYVIDS----SSLSPE-EREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912   210 FFPGdhhtaGDTHFDDdeawtfrssdAHGMDLFAVAVHEFGHAIGLSHVAAPSS---IMQPYYQGPvgDPLRYGLPYEDR 286
Cdd:smart00235  68 GRPG-----GDQHLSL----------GNGCINTGVAAHELGHALGLYHEQSRSDrdnYMYINYTNI--DTRNFDLSEDDS 130


                   ....*...
gi 157786912   287 VRVWQLYG 294
Cdd:smart00235 131 LGIPYDYG 138
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 161-257 4.07e-11

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: 62.05  E-value: 4.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 161 YALKVWSDITPLNFHEVA-GNMADIQIDFSKADHNDGYpfdgpggtvAHAFFPGDHHT---AGDTHFDDDEAWTFRSSDA 236
Cdd:cd04277   41 DALEAWEDVADIDFVEVSdNSGADIRFGNSSDPDGNTA---------GYAYYPGSGSGtayGGDIWFNSSYDTNSDSPGS 111

                         90       100
                 ....*....|....*....|.
gi 157786912 237 HGmdlFAVAVHEFGHAIGLSH 257
Cdd:cd04277  112 YG---YQTIIHEIGHALGLEH 129
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 162-276 5.35e-10

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: 58.24  E-value: 5.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 162 ALKVWSDITPLNFHEVAG--NMADIQIDFSKADHNDGYpfdgpGGTVAHAFFPGDHHTAGDT--HFDDDEAWTFRSSDAh 237
Cdd:cd04279   29 AAAEWENVGPLKFVYNPEedNDADIVIFFDRPPPVGGA-----GGGLARAGFPLISDGNRKLfnRTDINLGPGQPRGAE- 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 157786912 238 gmDLFAVAVHEFGHAIGLSHV-AAPSSIMQPYY-QGPVGDP 276
Cdd:cd04279  103 --NLQAIALHELGHALGLWHHsDRPEDAMYPSQgQGPDGNP 141
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 435-481 1.06e-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: 54.17  E-value: 1.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 157786912   435 IDAVFSWaHNDRTYFFKDQLYWRYDDHtrRMDPGYPAQ-GPLWRGVPS 481
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPK--RVDPGYPKLiSSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 389-428 1.98e-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: 53.40  E-value: 1.98e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 157786912   389 VDAVYERtSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDF 428
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSF 39
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 389-432 2.79e-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: 52.95  E-value: 2.79e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 157786912  389 VDAVYERtSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDF-SLPP 432
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 44-104 1.10e-08

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: 51.36  E-value: 1.10e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157786912   44 RAEDLSLGVEWLSKFGYLPpaDPATGQLQtqEELSKAITAMQQFGGLETTGILDEATLALM 104
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYP--GPVDGYFG--PSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 155-293 1.60e-08

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: 54.07  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 155 VRALMYYALKVWSDITPLNFHEVAGNM--ADIQIDFSKADHNdgypfdgpGGTVAHAFFPG--DHHTaGDTHFDDDEAWT 230
Cdd:cd00203   23 IQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDFD--------GGTGGWAYLGRvcDSLR-GVGVLQDNQSGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 231 FrssdahgmDLFAVAVHEFGHAIGLSH--------------------VAAPSSIMQPYYqGPVGDPLRYGLPYEDRVRVW 290
Cdd:cd00203   94 K--------EGAQTIAHELGHALGFYHdhdrkdrddyptiddtlnaeDDDYYSVMSYTK-GSFSDGQRKDFSQCDIDQIN 164


                 ...
gi 157786912 291 QLY 293
Cdd:cd00203  165 KLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 435-481 1.74e-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: 50.64  E-value: 1.74e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 157786912  435 IDAVFSWAHNdRTYFFKDQLYWRYDDhtRRMDPGYPAQGPLWRGVPS 481
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-383 5.49e-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: 43.39  E-value: 5.49e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 157786912   340 FDAVAQIR-GEAFFFKGKYFWRLTRDRHLVSLqPAQMHRFWRGLP 383
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGY-PKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 483-524 1.26e-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: 42.61  E-value: 1.26e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 157786912   483 LDDAMRWSDGASYFFRGQEYWKVLDGELEaaPGYPQSTARDW 524
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 ...
 152-257 1.48e-04

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: 43.14  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 152 RDTVRALMyyalKVWSDITPLNFHEVAGNMADIQIDFSKADHNDGYPfdgpgGTVAHAFfPGDHHTAGdthFDDDEawtf 231
Cdd:cd04327   22 KDKVRAAA----REWLPYANLKFKFVTDADADIRISFTPGDGYWSYV-----GTDALLI-GADAPTMN---LGWFT---- 84

                         90       100
                 ....*....|....*....|....*.
gi 157786912 232 rsSDAHGMDLFAVAVHEFGHAIGLSH 257
Cdd:cd04327   85 --DDTPDPEFSRVVLHEFGHALGFIH 108
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 483-527 9.38e-04

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: 37.16  E-value: 9.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 157786912  483 LDDAMRWSDGASYFFRGQEYWKVLDGELEaaPGYPQSTARD-WLVC 527
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVE--PGYPKLISDFpGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-362 1.34e-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: 1.34e-03
                          10        20
                  ....*....|....*....|....
gi 157786912  340 FDAVAQIR-GEAFFFKGKYFWRLT 362
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFD 24
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 153-293 5.17e-03

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: 38.25  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 153 DTVRALMYYALKVWSDITPLNFHEVAGNM-ADIQIDFSKadhndgypfDGPGGTVAHAFFPGDHHTAGDTHFDDDEAWTF 231
Cdd:cd04268   14 DKLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIR---------WIPYNDGTWSYGPSQVDPLTGEILLARVYLYS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157786912 232 RSSDAHGMDLFAVAVHEFGHAIGLSH----------------VAAPSSIMQPY---YQGPVGDPLRYGL-PYeDRVRVWQ 291
Cdd:cd04268   85 SFVEYSGARLRNTAEHELGHALGLRHnfaasdrddnvdllaeKGDTSSVMDYApsnFSIQLGDGQKYTIgPY-DIAAIKK 163


                 ..
gi 157786912 292 LY 293
Cdd:cd04268  164 LY 165
 
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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