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Conserved domains on  [gi|7305275|ref|NP_038931|]
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matrix metalloproteinase-20 preproprotein [Mus musculus]

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 ...
 115-270 1.14e-93

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: 280.66  E-value: 1.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275    115 KWKKNILTYRISKYTPSMSPTEVDKAIQMALHAWSTAVPLNFVRINSGEADIMISFETGDHGDSYPFDGPRGTLAHAFAP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305275    195 GEGLGGDTHFDNAEKWTMGT---NGFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALYG 270
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 292-482 6.37e-64

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: 205.62  E-value: 6.37e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  292 PDLCDSSSsFDAVTMLGKELLFFKDRIFWRRQVHLPtGIRPSTITSSFPQLMSNVDAAYEVAERGIAFFFKGPHYWVTRG 371
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  372 FHMQ-GPPRTIYDFGFPRHVQRIDAAVYLKEPQKTLFFVGEEYYSYDERKKKMEKDYPKNTEEEFSGVSGHIDAAVE-LN 449
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7305275  450 GYIYFFSGRKTFKYDT---EKEDVVSVVKSSSWIGC 482
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 39-94 4.95e-04

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: 38.27  E-value: 4.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 7305275     39 LAQAYLDKYYTKKGGP--QAGEMVAResnpmirRIKELQIFFGLKVTGKLDQNTMNVI 94
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVdgYFGPSTEA-------AVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-270 1.14e-93

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: 280.66  E-value: 1.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275    115 KWKKNILTYRISKYTPSMSPTEVDKAIQMALHAWSTAVPLNFVRINSGEADIMISFETGDHGDSYPFDGPRGTLAHAFAP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305275    195 GEGLGGDTHFDNAEKWTMGT---NGFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALYG 270
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-270 6.95e-82

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: 250.20  E-value: 6.95e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  115 KWKKNILTYRISKYTPSMSPTEVDKAIQMALHAWSTAVPLNFVRINSG-EADIMISFETGDHGDSYPFDGPRGTLAHAFA 193
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305275  194 PGeGLGGDTHFDNAEKWTMGTN--GFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYrFHLPKDDVKGIQALYG 270
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 292-482 6.37e-64

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: 205.62  E-value: 6.37e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  292 PDLCDSSSsFDAVTMLGKELLFFKDRIFWRRQVHLPtGIRPSTITSSFPQLMSNVDAAYEVAERGIAFFFKGPHYWVTRG 371
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  372 FHMQ-GPPRTIYDFGFPRHVQRIDAAVYLKEPQKTLFFVGEEYYSYDERKKKMEKDYPKNTEEEFSGVSGHIDAAVE-LN 449
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7305275  450 GYIYFFSGRKTFKYDT---EKEDVVSVVKSSSWIGC 482
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-271 4.50e-39

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: 138.25  E-value: 4.50e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275     112 GEPKWKKNILTYRIskYTPSMSPTEvDKAIQMALHAWSTAVPLNFVRiNSGEADIMISFETGDHGdsyPFdgprgtLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275     192 FAPGeglgGDTHFDNaEKWTMGTNgfnlftVAAHEFGHALGLGHSTDPSA---LMYPTYKYQNPYRFHLPKDDVKGIQAL 268
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 7305275     269 YGP 271
Cdd:smart00235 137 YGS 139
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 139-245 9.94e-08

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 9.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  139 KAIQMALHAWSTAVPLNFVRiNSGEADIMISFETGDHGDSyPFDGPRGTLAHAfapgeglggDTHFDNAEKWTM------ 212
Cdd:COG5549 104 AAVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNPPLTAS-PNPETGARSAET---------TYEFYDTGNILShrftil 172

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 7305275  213 -GTNGFNLFTVAA--HEFGHALGL-GHSTDPSALMYP 245
Cdd:COG5549 173 lSPNQTGKYLLATarHELGHALGIwGHSPSPTDAMYF 209
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 393-438 6.51e-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: 40.30  E-value: 6.51e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 7305275     393 IDAAVYLKEpQKTLFFVGEEYYSYDErkKKMEKDYPKNTEEEFSGV 438
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-387 3.86e-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: 3.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 7305275    346 VDAAYEVaERGIAFFFKGPHYWVTRGFHMQ-GPPRTIYDF-GFP 387
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEpGYPKLISDFpGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 39-94 4.95e-04

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: 38.27  E-value: 4.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 7305275     39 LAQAYLDKYYTKKGGP--QAGEMVAResnpmirRIKELQIFFGLKVTGKLDQNTMNVI 94
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVdgYFGPSTEA-------AVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-270 1.14e-93

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: 280.66  E-value: 1.14e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275    115 KWKKNILTYRISKYTPSMSPTEVDKAIQMALHAWSTAVPLNFVRINSGEADIMISFETGDHGDSYPFDGPRGTLAHAFAP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305275    195 GEGLGGDTHFDNAEKWTMGT---NGFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALYG 270
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-270 6.95e-82

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: 250.20  E-value: 6.95e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  115 KWKKNILTYRISKYTPSMSPTEVDKAIQMALHAWSTAVPLNFVRINSG-EADIMISFETGDHGDSYPFDGPRGTLAHAFA 193
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305275  194 PGeGLGGDTHFDNAEKWTMGTN--GFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYrFHLPKDDVKGIQALYG 270
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 292-482 6.37e-64

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: 205.62  E-value: 6.37e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  292 PDLCDSSSsFDAVTMLGKELLFFKDRIFWRRQVHLPtGIRPSTITSSFPQLMSNVDAAYEVAERGIAFFFKGPHYWVTRG 371
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  372 FHMQ-GPPRTIYDFGFPRHVQRIDAAVYLKEPQKTLFFVGEEYYSYDERKKKMEKDYPKNTEEEFSGVSGHIDAAVE-LN 449
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7305275  450 GYIYFFSGRKTFKYDT---EKEDVVSVVKSSSWIGC 482
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-271 4.50e-39

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: 138.25  E-value: 4.50e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275     112 GEPKWKKNILTYRIskYTPSMSPTEvDKAIQMALHAWSTAVPLNFVRiNSGEADIMISFETGDHGdsyPFdgprgtLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275     192 FAPGeglgGDTHFDNaEKWTMGTNgfnlftVAAHEFGHALGLGHSTDPSA---LMYPTYKYQNPYRFHLPKDDVKGIQAL 268
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 7305275     269 YGP 271
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 118-270 3.20e-17

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: 78.65  E-value: 3.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  118 KNILTYRIS--KYTPSMSPTEVDKAIQMALHAWSTAVPLNFVRI--NSGEADIMISFetgdhGDSYPFDGPRGTLAHAFA 193
Cdd:cd04279   1 KSPIRVYIDptPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIFF-----DRPPPVGGAGGGLARAGF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  194 PGEGLGGDTHFDNAEKW---TMGTNGFNLFTVAAHEFGHALGL-GHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALY 269
Cdd:cd04279  76 PLISDGNRKLFNRTDINlgpGQPRGAENLQAIALHELGHALGLwHHSDRPEDAMYPSQGQGPDGNPTLSARDVATLKRLY 155


                .
gi 7305275  270 G 270
Cdd:cd04279 156 G 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 131-269 3.13e-13

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: 67.55  E-value: 3.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  131 SMSPTEVDKAIQMALHAWSTAVPLNFV--RINSGEADIMISFETGDHgdsypfdgPRGTLAHAFAPG--EGLGGDTHFDn 206
Cdd:cd00203  17 ENLSAQIQSLILIAMQIWRDYLNIRFVlvGVEIDKADIAILVTRQDF--------DGGTGGWAYLGRvcDSLRGVGVLQ- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  207 aekwTMGTNGFNLFTVAAHEFGHALGLGHSTDPSA--------------------LMYPTY-KYQNPYRFHLPKDDVKGI 265
Cdd:cd00203  88 ----DNQSGTKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQI 163


                ....
gi 7305275  266 QALY 269
Cdd:cd00203 164 NKLY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 123-270 2.03e-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: 59.74  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  123 YRISKYTPSMSPTEVDK-AIQMALHAWSTAVPLNFVRINSGE-ADIMISFETGDHGDSYpfdgprgtlAHAFAPGEG--- 197
Cdd:cd04277  20 GREEDTTNTAALSAAQQaAARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNTA---------GYAYYPGSGsgt 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  198 -LGGDTHFDNAEKWTMGTNGFNLFTVAAHEFGHALGLGHSTDPSAL--MYPTYK----------YQNPYRFHLPKD---- 260
Cdd:cd04277  91 aYGGDIWFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGdpVPPTYAldsreytvmsYNSGYGNGASAGggyp 170

                       170
                ....*....|....*.
gi 7305275  261 ------DVKGIQALYG 270
Cdd:cd04277 171 qtpmllDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 117-269 1.53e-09

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: 56.74  E-value: 1.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  117 KKNIlTYRISKYTPSmsptEVDKAIQMALHAWSTAVPLNFVRINSG-EADIMIS----FETGDHGDSYpfdGPRGTLAHA 191
Cdd:cd04268   1 KKPI-TYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSvirwIPYNDGTWSY---GPSQVDPLT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  192 fapGEGLGGDTHFDNAEKWTMGTNgfnLFTVAAHEFGHALGLGHS----------------TDPSALMYPTYKYQNP--- 252
Cdd:cd04268  73 ---GEILLARVYLYSSFVEYSGAR---LRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNFSIqlg 146

                       170
                ....*....|....*....
gi 7305275  253 --YRFHLPKDDVKGIQALY 269
Cdd:cd04268 147 dgQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 131-235 4.72e-08

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: 53.15  E-value: 4.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  131 SMSPTEVDKAIQMAlHAWSTAVPLNFVRINSGEADIMISFETGDHGDSYpfdgprgtlahafapgegLGGDTHFDNAEKW 210
Cdd:cd04327  16 GPDAFLKDKVRAAA-REWLPYANLKFKFVTDADADIRISFTPGDGYWSY------------------VGTDALLIGADAP 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 7305275  211 TMGTNGFNLFT-------VAAHEFGHALGLGH 235
Cdd:cd04327  77 TMNLGWFTDDTpdpefsrVVLHEFGHALGFIH 108
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 139-245 9.94e-08

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 9.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305275  139 KAIQMALHAWSTAVPLNFVRiNSGEADIMISFETGDHGDSyPFDGPRGTLAHAfapgeglggDTHFDNAEKWTM------ 212
Cdd:COG5549 104 AAVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNPPLTAS-PNPETGARSAET---------TYEFYDTGNILShrftil 172

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 7305275  213 -GTNGFNLFTVAA--HEFGHALGL-GHSTDPSALMYP 245
Cdd:COG5549 173 lSPNQTGKYLLATarHELGHALGIwGHSPSPTDAMYF 209
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 393-438 6.51e-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: 40.30  E-value: 6.51e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 7305275     393 IDAAVYLKEpQKTLFFVGEEYYSYDErkKKMEKDYPKNTEEEFSGV 438
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-388 1.40e-04

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: 39.15  E-value: 1.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 7305275     346 VDAAYEVaERGIAFFFKGPHYWVTRGFHMQ-GPPRTIYDF--GFPR 388
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDpGYPKLISSFfpGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-344 3.27e-04

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: 38.38  E-value: 3.27e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 7305275     301 FDAVTML-GKELLFFKDRIFWRRQVHLPTGIRPSTITSSFPQLMS 344
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-387 3.86e-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: 3.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 7305275    346 VDAAYEVaERGIAFFFKGPHYWVTRGFHMQ-GPPRTIYDF-GFP 387
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEpGYPKLISDFpGLP 43
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
219-246 4.63e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 4.63e-04
                        10        20
                ....*....|....*....|....*...
gi 7305275  219 LFTVAAHEFGHALGLGHSTDPSALMYPT 246
Cdd:COG1913 123 VLKEAVHELGHLFGLGHCPNPRCVMHFS 150
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 39-94 4.95e-04

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: 38.27  E-value: 4.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 7305275     39 LAQAYLDKYYTKKGGP--QAGEMVAResnpmirRIKELQIFFGLKVTGKLDQNTMNVI 94
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVdgYFGPSTEA-------AVKAFQRAFGLPVDGIVDPETLAAL 57
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 219-246 1.07e-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: 39.97  E-value: 1.07e-03
                        10        20
                ....*....|....*....|....*...
gi 7305275  219 LFTVAAHEFGHALGLGHSTDPSALMYPT 246
Cdd:cd11375 123 LLKEAVHELGHLFGLDHCPYYACVMNFS 150
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 442-469 5.64e-03

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: 34.91  E-value: 5.64e-03
                           10        20
                   ....*....|....*....|....*....
gi 7305275     442 IDAAVEL-NGYIYFFSGRKTFKYDTEKED 469
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKRVD 29
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 442-467 7.43e-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: 34.46  E-value: 7.43e-03
                          10        20
                  ....*....|....*....|....*..
gi 7305275    442 IDAAVEL-NGYIYFFSGRKTFKYDTEK 467
Cdd:pfam00045   1 IDAAFEDrDGKTYFFKGRKYWRFDPQR 27
 
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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