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Conserved domains on  [gi|157817855|ref|NP_001100270|]
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matrix metalloproteinase-20 precursor [Rattus norvegicus]

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 5.44e-92

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: 276.42  E-value: 5.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855  115 KWKKNILTYRVSKYTPSMSPTEVDKAVHMALHAWSTAVPLIFVRINSGEADIMISFETGDHGDSYPFDGPRGTLAHAFAP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817855  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. ...
 292-464 2.53e-63

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: 204.08  E-value: 2.53e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 292 PDLCDSSSsFDAVTMLGKELLFFKDRIFWRRRVHLPAGIrPSTITSSFPQLMSNVDAAYEVAERGIAFFFKGPHYWVTRG 371
Cdd:cd00094    1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKPPGS-PFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 372 FQMQ-GPPRTIYDFGFPRHVQRIDAAVYLKEPQKTLFFVGEEYYSYDERKKKMEKDYPKSTEEEFSGVSGHIDAAVE-LN 449
Cdd:cd00094   79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                        170
                 ....*....|....*
gi 157817855 450 GYIYFFSGPKTFKYD 464
Cdd:cd00094  159 GYYYFFKGDQYWRFD 173
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 39-94 3.33e-06

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: 44.04  E-value: 3.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817855   39 LAQAYLDKYYTKKGGP--QAGEMvaresnpTVRKIKELQTFFGLRVTGKLDQNTMDVI 94
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVdgYFGPS-------TEAAVKAFQRAFGLPVDGIVDPETLAAL 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 5.44e-92

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: 276.42  E-value: 5.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855  115 KWKKNILTYRVSKYTPSMSPTEVDKAVHMALHAWSTAVPLIFVRINSGEADIMISFETGDHGDSYPFDGPRGTLAHAFAP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817855  195 GEGLGGDTHFDNAEKWTMGT---NGFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALYG 270
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-270 4.03e-80

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: 245.96  E-value: 4.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 115 KWKKNILTYRVSKYTPSMSPTEVDKAVHMALHAWSTAVPLIFVRINSG-EADIMISFETGDHGDSYPFDGPRGTLAHAFA 193
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817855 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. ...
 292-464 2.53e-63

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: 204.08  E-value: 2.53e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 292 PDLCDSSSsFDAVTMLGKELLFFKDRIFWRRRVHLPAGIrPSTITSSFPQLMSNVDAAYEVAERGIAFFFKGPHYWVTRG 371
Cdd:cd00094    1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKPPGS-PFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 372 FQMQ-GPPRTIYDFGFPRHVQRIDAAVYLKEPQKTLFFVGEEYYSYDERKKKMEKDYPKSTEEEFSGVSGHIDAAVE-LN 449
Cdd:cd00094   79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                        170
                 ....*....|....*
gi 157817855 450 GYIYFFSGPKTFKYD 464
Cdd:cd00094  159 GYYYFFKGDQYWRFD 173
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-271 5.23e-37

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: 132.86  E-value: 5.23e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855   112 GEPKWKKNILTYRVskYTPSMSPTEvDKAVHMALHAWSTAVPLIFVRiNSGEADIMISFETGDHGdsyPFdgprgtLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855   192 FAPGeglgGDTHFDNaEKWTMGTNgfnlftVAAHEFGHALGLGHSTDPSA---LMYPTYKYQNPYRFHLPKDDVKGIQAL 268
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 157817855   269 YGP 271
Cdd:smart00235 137 YGS 139
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 139-245 7.05e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 50.07  E-value: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 139 KAVHMALHAWSTAVPLIFVRiNSGEADIMISFETGDHGDSyPFDGPRGTLAHAfapgeglggDTHFDNAEKWTM------ 212
Cdd:COG5549  104 AAVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNPPLTAS-PNPETGARSAET---------TYEFYDTGNILShrftil 172

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157817855 213 -GTNGFNLFTVAA--HEFGHALGL-GHSTDPSALMYP 245
Cdd:COG5549  173 lSPNQTGKYLLATarHELGHALGIwGHSPSPTDAMYF 209
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 39-94 3.33e-06

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: 44.04  E-value: 3.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817855   39 LAQAYLDKYYTKKGGP--QAGEMvaresnpTVRKIKELQTFFGLRVTGKLDQNTMDVI 94
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVdgYFGPS-------TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-388 6.98e-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: 6.98e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 157817855   346 VDAAYEVaERGIAFFFKGPHYWVTRGFQMQ-GPPRTIYDF--GFPR 388
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDpGYPKLISSFfpGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-387 1.50e-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: 39.09  E-value: 1.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 157817855  346 VDAAYEVaERGIAFFFKGPHYWVTRGFQMQ-GPPRTIYDF-GFP 387
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEpGYPKLISDFpGLP 43
 
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 5.44e-92

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: 276.42  E-value: 5.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855  115 KWKKNILTYRVSKYTPSMSPTEVDKAVHMALHAWSTAVPLIFVRINSGEADIMISFETGDHGDSYPFDGPRGTLAHAFAP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817855  195 GEGLGGDTHFDNAEKWTMGT---NGFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALYG 270
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-270 4.03e-80

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: 245.96  E-value: 4.03e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 115 KWKKNILTYRVSKYTPSMSPTEVDKAVHMALHAWSTAVPLIFVRINSG-EADIMISFETGDHGDSYPFDGPRGTLAHAFA 193
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157817855 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. ...
 292-464 2.53e-63

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: 204.08  E-value: 2.53e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 292 PDLCDSSSsFDAVTMLGKELLFFKDRIFWRRRVHLPAGIrPSTITSSFPQLMSNVDAAYEVAERGIAFFFKGPHYWVTRG 371
Cdd:cd00094    1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKPPGS-PFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 372 FQMQ-GPPRTIYDFGFPRHVQRIDAAVYLKEPQKTLFFVGEEYYSYDERKKKMEKDYPKSTEEEFSGVSGHIDAAVE-LN 449
Cdd:cd00094   79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                        170
                 ....*....|....*
gi 157817855 450 GYIYFFSGPKTFKYD 464
Cdd:cd00094  159 GYYYFFKGDQYWRFD 173
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-271 5.23e-37

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: 132.86  E-value: 5.23e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855   112 GEPKWKKNILTYRVskYTPSMSPTEvDKAVHMALHAWSTAVPLIFVRiNSGEADIMISFETGDHGdsyPFdgprgtLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855   192 FAPGeglgGDTHFDNaEKWTMGTNgfnlftVAAHEFGHALGLGHSTDPSA---LMYPTYKYQNPYRFHLPKDDVKGIQAL 268
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 157817855   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 ...
 130-270 1.54e-15

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: 74.03  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 130 PSMSPTEVDKAVHMALHAWSTAVPLIFVRI--NSGEADIMISFetgdhGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNA 207
Cdd:cd04279   15 PDSRAQSWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKLFNRT 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817855 208 EKW---TMGTNGFNLFTVAAHEFGHALGL-GHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALYG 270
Cdd:cd04279   90 DINlgpGQPRGAENLQAIALHELGHALGLwHHSDRPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 131-269 4.75e-12

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: 64.08  E-value: 4.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 131 SMSPTEVDKAVHMALHAWSTAVPLIFV--RINSGEADIMISFETGDHgdsypfdgPRGTLAHAFAPG--EGLGGDTHFDn 206
Cdd:cd00203   17 ENLSAQIQSLILIAMQIWRDYLNIRFVlvGVEIDKADIAILVTRQDF--------DGGTGGWAYLGRvcDSLRGVGVLQ- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 207 aekwTMGTNGFNLFTVAAHEFGHALGLGHSTDPSA--------------------LMYPTY-KYQNPYRFHLPKDDVKGI 265
Cdd:cd00203   88 ----DNQSGTKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQI 163


                 ....
gi 157817855 266 QALY 269
Cdd:cd00203  164 NKLY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 128-270 2.22e-09

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: 56.66  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 128 YTPSMSPTEVDKAVHmALHAWSTAVPLIFVRINSGE-ADIMISFETGDHGDSYpfdgprgtlAHAFAPGEG----LGGDT 202
Cdd:cd04277   27 NTAALSAAQQAAARD-ALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNTA---------GYAYYPGSGsgtaYGGDI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 203 HFDNAEKWTMGTNGFNLFTVAAHEFGHALGLGHSTDPSAL--MYPTYK----------YQNPYRFHLPKD---------- 260
Cdd:cd04277   97 WFNSSYDTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGGdpVPPTYAldsreytvmsYNSGYGNGASAGggypqtpmll 176

                        170
                 ....*....|
gi 157817855 261 DVKGIQALYG 270
Cdd:cd04277  177 DIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 117-269 8.56e-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: 54.81  E-value: 8.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 117 KKNIlTYRVSKYTPSmsptEVDKAVHMALHAWSTAVPLIFVRINSG-EADIMIS----FETGDHGDSYpfdGPRGTLAHA 191
Cdd:cd04268    1 KKPI-TYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSvirwIPYNDGTWSY---GPSQVDPLT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 192 fapGEGLGGDTHFDNAEKWTMGTNgfnLFTVAAHEFGHALGLGHS----------------TDPSALMYPTYKYQNP--- 252
Cdd:cd04268   73 ---GEILLARVYLYSSFVEYSGAR---LRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNFSIqlg 146

                        170
                 ....*....|....*....
gi 157817855 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 ...
 133-235 2.77e-07

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: 50.84  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 133 SPTEVDKAVHMALHAWSTAVPLIFVRINSGEADIMISFETGDHGDSYpfdgprgtlahafapgegLGGDTHFDNAEKWTM 212
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGDGYWSY------------------VGTDALLIGADAPTM 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 157817855 213 GTNGFNLFT-------VAAHEFGHALGLGH 235
Cdd:cd04327   79 NLGWFTDDTpdpefsrVVLHEFGHALGFIH 108
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 139-245 7.05e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 50.07  E-value: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817855 139 KAVHMALHAWSTAVPLIFVRiNSGEADIMISFETGDHGDSyPFDGPRGTLAHAfapgeglggDTHFDNAEKWTM------ 212
Cdd:COG5549  104 AAVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNPPLTAS-PNPETGARSAET---------TYEFYDTGNILShrftil 172

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157817855 213 -GTNGFNLFTVAA--HEFGHALGL-GHSTDPSALMYP 245
Cdd:COG5549  173 lSPNQTGKYLLATarHELGHALGIwGHSPSPTDAMYF 209
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 39-94 3.33e-06

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: 44.04  E-value: 3.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817855   39 LAQAYLDKYYTKKGGP--QAGEMvaresnpTVRKIKELQTFFGLRVTGKLDQNTMDVI 94
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVdgYFGPS-------TEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-388 6.98e-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: 6.98e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 157817855   346 VDAAYEVaERGIAFFFKGPHYWVTRGFQMQ-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. ...
 393-438 7.70e-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: 39.92  E-value: 7.70e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 157817855   393 IDAAVYLKEpQKTLFFVGEEYYSYDErkKKMEKDYPKSTEEEFSGV 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 1.50e-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: 39.09  E-value: 1.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 157817855  346 VDAAYEVaERGIAFFFKGPHYWVTRGFQMQ-GPPRTIYDF-GFP 387
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEpGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-344 1.64e-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: 1.64e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 157817855   301 FDAVTML-GKELLFFKDRIFWRRRVHLPAGIRPSTITSSFPQLMS 344
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
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 157817855 219 LFTVAAHEFGHALGLGHSTDPSALMYPT 246
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVMHFS 150
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 219-246 1.23e-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: 1.23e-03
                         10        20
                 ....*....|....*....|....*...
gi 157817855 219 LFTVAAHEFGHALGLGHSTDPSALMYPT 246
Cdd:cd11375  123 LLKEAVHELGHLFGLDHCPYYACVMNFS 150
 
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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