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Conserved domains on  [gi|461764|sp|P33435|]
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RecName: Full=Collagenase 3; AltName: Full=Matrix metalloproteinase-13; Short=MMP-13; Flags: Precursor

Protein Classification

matrix metalloproteinase( domain architecture ID 12021147)

matrix metalloproteinase is an M10A family metallopeptidase with a C-terminal hemopexin repeat-containing domain, such as stromelysin-1 (matrix metalloproteinase-3), which can degrade fibronectin, laminin, type I, III, IV, and V gelatins, collagens III, IV, X, and IX, as well as cartilage proteoglycans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 113-268 3.79e-96

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: 286.82  E-value: 3.79e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764     113 KWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPP 192
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 461764     193 GPNYGGDAHFDDDETWT---SSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQFLYG 268
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 282-472 3.50e-77

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: 239.52  E-value: 3.50e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   282 PEKCDPaLSLDAITSLRGETMIFKDRFFWRLHPQQVEAELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGY 361
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   362 DILEGYPRKISDLGFPKEVKRLSAAVHFENTGKTLFFSENHVWSYDDVNQTMDKDYPRLIEEEFPGIGNKVDAVYE-KNG 440
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 461764   441 YIYFFNGPIQFEYSIWS--NRIVRVMPTNS-ILWC 472
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-92 4.62e-07

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: 46.74  E-value: 4.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 461764      33 SEEDLVFAEHYLKSY-YHPATLAGILkkstVTSTVDRLREMQSFFGLEVTGKLDDPTLDIM 92
Cdd:pfam01471   1 SGEDVKELQRYLNRLgYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 113-268 3.79e-96

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: 286.82  E-value: 3.79e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764     113 KWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPP 192
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 461764     193 GPNYGGDAHFDDDETWT---SSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQFLYG 268
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 113-268 7.33e-83

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: 252.51  E-value: 7.33e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   113 KWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDG-TADIMISFGTKEHGDFYPFDGPSGLLAHAFP 191
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 461764   192 PGPnYGGDAHFDDDETWT--SSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTgKSHFMLPDDDVQGIQFLYG 268
Cdd:cd04278  81 PGG-IGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGP-VPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 282-472 3.50e-77

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: 239.52  E-value: 3.50e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   282 PEKCDPaLSLDAITSLRGETMIFKDRFFWRLHPQQVEAELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGY 361
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   362 DILEGYPRKISDLGFPKEVKRLSAAVHFENTGKTLFFSENHVWSYDDVNQTMDKDYPRLIEEEFPGIGNKVDAVYE-KNG 440
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 461764   441 YIYFFNGPIQFEYSIWS--NRIVRVMPTNS-ILWC 472
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-269 1.97e-33

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: 122.84  E-value: 1.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764      112 LKWSQTNLTYRIvnYTPDMShSEVEKAFRKAFKVWSDVTPLNFTRIyDGTADIMISFGTKEHGDFYpfdgpsgllAHAFP 191
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLS-PEEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSGCTL---------SHAGR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764      192 PGpnygGDAHFDDdETWTSSskgynlFIVAAHELGHSLGLDHSKDPGA---LMFPIYTYTGKSHFMLPDDDVQGIQFLYG 268
Cdd:smart00235  70 PG----GDQHLSL-GNGCIN------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138


                   .
gi 461764      269 P 269
Cdd:smart00235 139 S 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-92 4.62e-07

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: 46.74  E-value: 4.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 461764      33 SEEDLVFAEHYLKSY-YHPATLAGILkkstVTSTVDRLREMQSFFGLEVTGKLDDPTLDIM 92
Cdd:pfam01471   1 SGEDVKELQRYLNRLgYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 335-377 4.95e-07

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: 46.02  E-value: 4.95e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 461764     335 VDAAYEHPsRDLMFIFRGRKFWALNGYDILEGYPRKISDL-GFP 377
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 383-429 6.57e-07

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: 45.70  E-value: 6.57e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 461764      383 LSAAVHFENtGKTLFFSENHVWSYDdvNQTMDKDYPRLIEEEFPGIG 429
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFD--PKRVDPGYPKLISSFFPGLP 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
220-243 1.05e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 1.05e-03
                        10        20
                ....*....|....*....|....
gi 461764   220 VAAHELGHSLGLDHSKDPGALMFP 243
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 105-246 2.70e-03

fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This enzyme is a Zn metalloprotease. Three distinct subtypes included in this family all are produced by enterotoxigenic (by definition) strains of Bacteroides fragilis. [Cellular processes, Pathogenesis]


Pssm-ID: 188450 [Multi-domain]  Cd Length: 386  Bit Score: 39.95  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764     105 YNVFPRTLKWSQ---TNLTYRIVN--------YTPDMSHS----EVE--KAFRKAFKVWSDVtplnftRIYDGTADIMIS 167
Cdd:TIGR03935 228 STGYPHEVTAQMqdaANSLKRLVNnhfvlveyTTEYSCPSggadESKglDGFTASLKSNPKA------KGYDKQIYILIR 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 461764     168 FGTKEHGdfypFDGPSGLLAHAFPPGPNYGGDAHfdddeTWTSSSKGYNLfivaAHELGHSLGLDHSKDPGALMFPIYT 246
Cdd:TIGR03935 302 WGTWDNN----ILGIGWLNSYNVNTASNFEASGM-----STTQLMYPGTL----AHELGHILGAEHTDNEKDLMYTWYT 367
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 113-268 3.79e-96

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: 286.82  E-value: 3.79e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764     113 KWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPP 192
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 461764     193 GPNYGGDAHFDDDETWT---SSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQFLYG 268
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 113-268 7.33e-83

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: 252.51  E-value: 7.33e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   113 KWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDG-TADIMISFGTKEHGDFYPFDGPSGLLAHAFP 191
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 461764   192 PGPnYGGDAHFDDDETWT--SSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTgKSHFMLPDDDVQGIQFLYG 268
Cdd:cd04278  81 PGG-IGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGP-VPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 282-472 3.50e-77

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: 239.52  E-value: 3.50e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   282 PEKCDPaLSLDAITSLRGETMIFKDRFFWRLHPQQVEAELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGY 361
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   362 DILEGYPRKISDLGFPKEVKRLSAAVHFENTGKTLFFSENHVWSYDDVNQTMDKDYPRLIEEEFPGIGNKVDAVYE-KNG 440
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 461764   441 YIYFFNGPIQFEYSIWS--NRIVRVMPTNS-ILWC 472
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-269 1.97e-33

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: 122.84  E-value: 1.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764      112 LKWSQTNLTYRIvnYTPDMShSEVEKAFRKAFKVWSDVTPLNFTRIyDGTADIMISFGTKEHGDFYpfdgpsgllAHAFP 191
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLS-PEEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSGCTL---------SHAGR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764      192 PGpnygGDAHFDDdETWTSSskgynlFIVAAHELGHSLGLDHSKDPGA---LMFPIYTYTGKSHFMLPDDDVQGIQFLYG 268
Cdd:smart00235  70 PG----GDQHLSL-GNGCIN------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138


                   .
gi 461764      269 P 269
Cdd:smart00235 139 S 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 121-268 3.56e-17

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: 79.38  E-value: 3.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   121 YRIVNYTPDMSHSEVEKAF-RKAFKVWSDVTPLNFTRIYDGT-ADIMISFGTKEHGDFYpfdgpsgllAHAFPPGPN--- 195
Cdd:cd04277  20 GREEDTTNTAALSAAQQAAaRDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNTA---------GYAYYPGSGsgt 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   196 -YGGDAHFDDDETWTSSSKG-YNlFIVAAHELGHSLGLDHSKDPGA----------------LM---FPIYTYTGKSH-- 252
Cdd:cd04277  91 aYGGDIWFNSSYDTNSDSPGsYG-YQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynSGYGNGASAGGgy 169

                       170
                ....*....|....*....
gi 461764   253 ---FMLpdDDVQGIQFLYG 268
Cdd:cd04277 170 pqtPML--LDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 107-268 1.03e-14

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: 71.33  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   107 VFPRTLKWSQTNLTyrivnytPDMSHSEVEKAFRKAFKVWSDVtpLNFTRIYDGT----ADIMISFGTKEHGDfypfdGP 182
Cdd:cd04279   1 KSPIRVYIDPTPAP-------PDSRAQSWLQAVKQAAAEWENV--GPLKFVYNPEedndADIVIFFDRPPPVG-----GA 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   183 SGLLAHAFPPGPNYGGDA---HFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKD-PGALMFPIYTYTGKSHFMLPDD 258
Cdd:cd04279  67 GGGLARAGFPLISDGNRKlfnRTDINLGPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSAR 146

                       170
                ....*....|
gi 461764   259 DVQGIQFLYG 268
Cdd:cd04279 147 DVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 119-267 3.73e-10

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: 58.69  E-value: 3.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   119 LTYRIVNYTPDMSHS----EVEKAFRKAFKVWSDVTPLNFT--RIYDGTADIMISFgtkehgdfYPFDGPSGLLAHAFPP 192
Cdd:cd00203   3 IPYVVVADDRDVEEEnlsaQIQSLILIAMQIWRDYLNIRFVlvGVEIDKADIAILV--------TRQDFDGGTGGWAYLG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   193 G--PNYGGDAHFDDDETWTssskgYNLFIVAAHELGHSLGLDHS--------------------KDPGALMFPIYT-YTG 249
Cdd:cd00203  75 RvcDSLRGVGVLQDNQSGT-----KEGAQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSYTKGsFSD 149

                       170
                ....*....|....*...
gi 461764   250 KSHFMLPDDDVQGIQFLY 267
Cdd:cd00203 150 GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 119-275 1.31e-08

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: 54.04  E-value: 1.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   119 LTYRIVNYTPDmshsEVEKAFRKAFKVWSDVTPLNFTRIYDG-TADIMISFGTKEHGDfypfDGPSGLLAHAFPPGpnyG 197
Cdd:cd04268   4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIRWIPYN----DGTWSYGPSQVDPL---T 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   198 GDAHfDDDETWTSSSKGYN---LFIVAAHELGHSLGLDHSKDpGALMFPIYTYTGKSH----FMLPDDD----VQGIQFL 266
Cdd:cd04268  73 GEIL-LARVYLYSSFVEYSgarLRNTAEHELGHALGLRHNFA-ASDRDDNVDLLAEKGdtssVMDYAPSnfsiQLGDGQK 150


                ....*....
gi 461764   267 YGPGDEDPN 275
Cdd:cd04268 151 YTIGPYDIA 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-92 4.62e-07

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: 46.74  E-value: 4.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 461764      33 SEEDLVFAEHYLKSY-YHPATLAGILkkstVTSTVDRLREMQSFFGLEVTGKLDDPTLDIM 92
Cdd:pfam01471   1 SGEDVKELQRYLNRLgYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 335-377 4.95e-07

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: 46.02  E-value: 4.95e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 461764     335 VDAAYEHPsRDLMFIFRGRKFWALNGYDILEGYPRKISDL-GFP 377
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 383-429 6.57e-07

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: 45.70  E-value: 6.57e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 461764      383 LSAAVHFENtGKTLFFSENHVWSYDdvNQTMDKDYPRLIEEEFPGIG 429
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFD--PKRVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 335-377 1.30e-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: 1.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 461764      335 VDAAYEHPsRDLMFIFRGRKFWALNGYDILEGYPRKISDL--GFP 377
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-332 3.54e-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: 41.07  E-value: 3.54e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 461764      291 LDAITSLR-GETMIFKDRFFWRLHPQQVEA-ELFLTKSFWPELP 332
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPgYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 386-430 1.92e-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: 38.70  E-value: 1.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 461764     386 AVHFENTGKTLFFSENHVWSYDdvNQTMDKDYPRLIeEEFPGIGN 430
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFD--PQRVEPGYPKLI-SDFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-318 4.70e-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: 37.93  E-value: 4.70e-04
                          10        20
                  ....*....|....*....|....*....
gi 461764     291 LDAITSLR-GETMIFKDRFFWRLHPQQVE 318
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVE 29
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
220-243 1.05e-03

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 1.05e-03
                        10        20
                ....*....|....*....|....
gi 461764   220 VAAHELGHSLGLDHSKDPGALMFP 243
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 217-265 1.15e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 39.59  E-value: 1.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 461764   217 LFIVAAHELGHSLGLDHSKDPGALMFPIYTytgkshfmLPDDDVQGIQF 265
Cdd:cd11375 123 LLKEAVHELGHLFGLDHCPYYACVMNFSNS--------LEETDRKPPYL 163
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 134-233 2.13e-03

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: 39.29  E-value: 2.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764   134 EVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFgtKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSssk 213
Cdd:cd04327  20 FLKDKVRAAAREWLPYANLKFKFVTDADADIRISF--TPGDGYWSYVGTDALLIGADAPTMNLGWFTDDTPDPEFSR--- 94

                        90       100
                ....*....|....*....|
gi 461764   214 gynlfiVAAHELGHSLGLDH 233
Cdd:cd04327  95 ------VVLHEFGHALGFIH 108
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 105-246 2.70e-03

fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This enzyme is a Zn metalloprotease. Three distinct subtypes included in this family all are produced by enterotoxigenic (by definition) strains of Bacteroides fragilis. [Cellular processes, Pathogenesis]


Pssm-ID: 188450 [Multi-domain]  Cd Length: 386  Bit Score: 39.95  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 461764     105 YNVFPRTLKWSQ---TNLTYRIVN--------YTPDMSHS----EVE--KAFRKAFKVWSDVtplnftRIYDGTADIMIS 167
Cdd:TIGR03935 228 STGYPHEVTAQMqdaANSLKRLVNnhfvlveyTTEYSCPSggadESKglDGFTASLKSNPKA------KGYDKQIYILIR 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 461764     168 FGTKEHGdfypFDGPSGLLAHAFPPGPNYGGDAHfdddeTWTSSSKGYNLfivaAHELGHSLGLDHSKDPGALMFPIYT 246
Cdd:TIGR03935 302 WGTWDNN----ILGIGWLNSYNVNTASNFEASGM-----STTQLMYPGTL----AHELGHILGAEHTDNEKDLMYTWYT 367
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 209-234 4.68e-03

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 36.96  E-value: 4.68e-03
                          10        20
                  ....*....|....*....|....*...
gi 461764     209 TSSSKGYNLF--IVAAHELGHSLGLDHS 234
Cdd:pfam13582  95 NSGSGPVGDTgaDTFAHEIGHNFGLNHT 122
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 175-233 8.80e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 37.70  E-value: 8.80e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 461764   175 DFYPFDGpSGLLAHAFPPGPNYGGDAHFD----DDET--WTSSSKgYNLFIVAAHELGHSLGLDH 233
Cdd:cd04275  91 YVANFLG-GGLLGYATFPDSLVSLAFITDgvviNPSSlpGGSAAP-YNLGDTATHEVGHWLGLYH 153
 
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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