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Conserved domains on  [gi|78099009|sp|Q9EPL5|]
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RecName: Full=Interstitial collagenase A; AltName: Full=Matrix metalloproteinase-1a; Short=MMP-1a; AltName: Full=Mcol-A; 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 ...
 105-259 1.10e-78

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: 241.75  E-value: 1.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009   105 RWTKTHLTYSILNYTPYLPKAVVEDAIARAFRVWSDVTPLTFQRVFEEEGDIVLSFHRGDHGDNNPFDGPNYKLAHTFQP 184
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78099009   185 GPGLGGDVHYDLDETWTNSSEN---FNLFYVTAHELGHSLGLTHSSDIGALMFPSYTWY-TEDFVLNQDDINRIQDLYG 259
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLdSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 273-464 4.79e-67

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: 212.94  E-value: 4.79e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 273 PHPCNGdLTFDAITTFRGEVFFFKGRFYIRVNRFMPEPELNLIGILWPNLPVKLDAAYEASMIDQVRYFKGSKVWAVQEQ 352
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 353 SVLRGFPRDIHSfFGFPSNVTHIDAAVCEEETGKTYFFVDHMYWRYDENTQSMDPGYPRLTAEDFPGIDDKVDDVFQ-KG 431
Cdd:cd00094  80 NLEPGYPKPISD-LGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 78099009 432 ENFYFFHQSVQHRFNLQIRRVDDSRD---SSTWFNC 464
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPlkiSSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-84 1.53e-09

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: 53.67  E-value: 1.53e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78099009    26 RQNVETVWKYLENYYNLgknmqAKNVNGK--EMMAEKLRQMQQLFGLKVTGNSDPETLRAM 84
Cdd:pfam01471   2 GEDVKELQRYLNRLGYY-----PGPVDGYfgPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 105-259 1.10e-78

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: 241.75  E-value: 1.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009   105 RWTKTHLTYSILNYTPYLPKAVVEDAIARAFRVWSDVTPLTFQRVFEEEGDIVLSFHRGDHGDNNPFDGPNYKLAHTFQP 184
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78099009   185 GPGLGGDVHYDLDETWTNSSEN---FNLFYVTAHELGHSLGLTHSSDIGALMFPSYTWY-TEDFVLNQDDINRIQDLYG 259
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLdSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 105-259 2.55e-75

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


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 232.86  E-value: 2.55e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 105 RWTKTHLTYSILNYTPYLPKAVVEDAIARAFRVWSDVTPLTFQRVF-EEEGDIVLSFHRGDHGDNNPFDGPNYKLAHTFQ 183
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTsGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78099009 184 PGpGLGGDVHYDLDETWT--NSSENFNLFYVTAHELGHSLGLTHSSDIGALMFPSYTWYTEDFVLNQDDINRIQDLYG 259
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 273-464 4.79e-67

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: 212.94  E-value: 4.79e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 273 PHPCNGdLTFDAITTFRGEVFFFKGRFYIRVNRFMPEPELNLIGILWPNLPVKLDAAYEASMIDQVRYFKGSKVWAVQEQ 352
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 353 SVLRGFPRDIHSfFGFPSNVTHIDAAVCEEETGKTYFFVDHMYWRYDENTQSMDPGYPRLTAEDFPGIDDKVDDVFQ-KG 431
Cdd:cd00094  80 NLEPGYPKPISD-LGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 78099009 432 ENFYFFHQSVQHRFNLQIRRVDDSRD---SSTWFNC 464
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPlkiSSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 102-260 1.10e-27

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: 107.44  E-value: 1.10e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009    102 NNPRWTKTHLTYSIlnYTPYLPKAVVEdAIARAFRVWSDVTPLTFQRVFEEEgDIVLSFHRGDHGdnnPFdgpnykLAHT 181
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGTA-DIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009    182 FQPGpglgGDVHYDLdETWTNSsenfnlFYVTAHELGHSLGLTHSSDIGA---LMFPSYTWY-TEDFVLNQDDINRIQDL 257
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCIN------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIdTRNFDLSEDDSLGIPYD 136


                   ...
gi 78099009    258 YGP 260
Cdd:smart00235 137 YGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 375-420 7.96e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 54.17  E-value: 7.96e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 78099009    375 IDAAVCEEEtGKTYFFVDHMYWRYDEntQSMDPGYPRLTAEDFPGI 420
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-84 1.53e-09

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: 53.67  E-value: 1.53e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78099009    26 RQNVETVWKYLENYYNLgknmqAKNVNGK--EMMAEKLRQMQQLFGLKVTGNSDPETLRAM 84
Cdd:pfam01471   2 GEDVKELQRYLNRLGYY-----PGPVDGYfgPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 375-420 1.57e-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: 47.56  E-value: 1.57e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 78099009   375 IDAAVcEEETGKTYFFVDHMYWRYDENTqsMDPGYPRLTAeDFPGI 420
Cdd:pfam00045   1 IDAAF-EDRDGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGL 42
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
196-236 1.35e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.56  E-value: 1.35e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 78099009 196 LDETWTNSSENFNLFY-----VTAHELGHSLGLTHSSDIGALMFPS 236
Cdd:COG1913 105 LRPEFYGLPPDEELFLervlkEAVHELGHLFGLGHCPNPRCVMHFS 150
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 211-254 1.53e-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: 40.72  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 78099009   211 YVTAHELGHSLGLTHSSDIGALMFPSYTWYTEDFVLNQDDINRI 254
Cdd:TIGR03935 340 GTLAHELGHILGAEHTDNEKDLMYTWYTGYWRLNHLSEKNMVRI 383
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 105-259 1.10e-78

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: 241.75  E-value: 1.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009   105 RWTKTHLTYSILNYTPYLPKAVVEDAIARAFRVWSDVTPLTFQRVFEEEGDIVLSFHRGDHGDNNPFDGPNYKLAHTFQP 184
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78099009   185 GPGLGGDVHYDLDETWTNSSEN---FNLFYVTAHELGHSLGLTHSSDIGALMFPSYTWY-TEDFVLNQDDINRIQDLYG 259
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLdSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 105-259 2.55e-75

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


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 232.86  E-value: 2.55e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 105 RWTKTHLTYSILNYTPYLPKAVVEDAIARAFRVWSDVTPLTFQRVF-EEEGDIVLSFHRGDHGDNNPFDGPNYKLAHTFQ 183
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTsGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78099009 184 PGpGLGGDVHYDLDETWT--NSSENFNLFYVTAHELGHSLGLTHSSDIGALMFPSYTWYTEDFVLNQDDINRIQDLYG 259
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 273-464 4.79e-67

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: 212.94  E-value: 4.79e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 273 PHPCNGdLTFDAITTFRGEVFFFKGRFYIRVNRFMPEPELNLIGILWPNLPVKLDAAYEASMIDQVRYFKGSKVWAVQEQ 352
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 353 SVLRGFPRDIHSfFGFPSNVTHIDAAVCEEETGKTYFFVDHMYWRYDENTQSMDPGYPRLTAEDFPGIDDKVDDVFQ-KG 431
Cdd:cd00094  80 NLEPGYPKPISD-LGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 78099009 432 ENFYFFHQSVQHRFNLQIRRVDDSRD---SSTWFNC 464
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPlkiSSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 102-260 1.10e-27

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: 107.44  E-value: 1.10e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009    102 NNPRWTKTHLTYSIlnYTPYLPKAVVEdAIARAFRVWSDVTPLTFQRVFEEEgDIVLSFHRGDHGdnnPFdgpnykLAHT 181
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGTA-DIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009    182 FQPGpglgGDVHYDLdETWTNSsenfnlFYVTAHELGHSLGLTHSSDIGA---LMFPSYTWY-TEDFVLNQDDINRIQDL 257
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCIN------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIdTRNFDLSEDDSLGIPYD 136


                   ...
gi 78099009    258 YGP 260
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 129-259 5.57e-12

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: 63.63  E-value: 5.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 129 DAIARAFRVWSDVTPLTF--QRVFEEEGDIVLSFHRGDHGDNNPFdgpnyKLAHTFQPGPGLGGDV---HYDLDETWTNS 203
Cdd:cd04279  24 QAVKQAAAEWENVGPLKFvyNPEEDNDADIVIFFDRPPPVGGAGG-----GLARAGFPLISDGNRKlfnRTDINLGPGQP 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 78099009 204 SENFNLFYVTAHELGHSLGLTHSSDIGA-LMFPSYTwYTEDF--VLNQDDINRIQDLYG 259
Cdd:cd04279  99 RGAENLQAIALHELGHALGLWHHSDRPEdAMYPSQG-QGPDGnpTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 109-259 1.25e-11

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 63.20  E-value: 1.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 109 THLTYSI---------------LNYTPYLPKAVVEDAIARAFRVWSDVTPLTFQRVFEEE-GDIVLsfhrgdhGDNNPFD 172
Cdd:cd04277   2 TTLTYSFsntggpysygygreeDTTNTAALSAAQQAAARDALEAWEDVADIDFVEVSDNSgADIRF-------GNSSDPD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 173 GPNYKLAhtFQPGPG----LGGDVHYDLDETWTNSSENfNLFYVTA-HELGHSLGLTHSSDIGA---------------- 231
Cdd:cd04277  75 GNTAGYA--YYPGSGsgtaYGGDIWFNSSYDTNSDSPG-SYGYQTIiHEIGHALGLEHPGDYNGgdpvpptyaldsreyt 151

                       170       180       190
                ....*....|....*....|....*....|....*
gi 78099009 232 LM---FPSYTWYTEDFVLNQ----DDINRIQDLYG 259
Cdd:cd04277 152 VMsynSGYGNGASAGGGYPQtpmlLDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 375-420 7.96e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 54.17  E-value: 7.96e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 78099009    375 IDAAVCEEEtGKTYFFVDHMYWRYDEntQSMDPGYPRLTAEDFPGI 420
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-84 1.53e-09

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: 53.67  E-value: 1.53e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78099009    26 RQNVETVWKYLENYYNLgknmqAKNVNGK--EMMAEKLRQMQQLFGLKVTGNSDPETLRAM 84
Cdd:pfam01471   2 GEDVKELQRYLNRLGYY-----PGPVDGYfgPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 130-258 8.47e-09

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


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 54.84  E-value: 8.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 130 AIARAFRVWSDVTPLTFQRVFEEEG--DIVLSFHRGDhgdnnpFDGPNYKLAHTFQPGPGLGGDVHYDldetwTNSSENF 207
Cdd:cd00203  26 LILIAMQIWRDYLNIRFVLVGVEIDkaDIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQ-----DNQSGTK 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78099009 208 NLFYVTAHELGHSLGLTHSSD--------------------IGALMfpSYTWYTEDFV----LNQDDINRIQDLY 258
Cdd:cd00203  95 EGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVM--SYTKGSFSDGqrkdFSQCDIDQINKLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 375-420 1.57e-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: 47.56  E-value: 1.57e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 78099009   375 IDAAVcEEETGKTYFFVDHMYWRYDENTqsMDPGYPRLTAeDFPGI 420
Cdd:pfam00045   1 IDAAF-EDRDGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGL 42
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 111-275 2.11e-07

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: 50.57  E-value: 2.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 111 LTYSILNYTPylpkAVVEDAIARAFRVWSDVTPLTFQRVFEE-EGDIVLSFHRgdhgDNNPFDGPNYKLAHTFQPgpgLG 189
Cdd:cd04268   4 ITYYIDDSVP----DKLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIR----WIPYNDGTWSYGPSQVDP---LT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 190 GDVHYD---LDETWTNSSENFnLFYVTAHELGHSLGLTHSSDigalmfPSYTWYTEDFVLNQDDINRIQDlYGPSPNPIQ 266
Cdd:cd04268  73 GEILLArvyLYSSFVEYSGAR-LRNTAEHELGHALGLRHNFA------ASDRDDNVDLLAEKGDTSSVMD-YAPSNFSIQ 144


                ....*....
gi 78099009 267 PTGATTPHP 275
Cdd:cd04268 145 LGDGQKYTI 153
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 326-370 6.23e-06

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: 42.94  E-value: 6.23e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 78099009   326 LDAAYEASmIDQVRYFKGSKVWAVQEQSVLRGFPRDIHSFFGFPS 370
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFPGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 326-370 3.62e-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: 3.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 78099009    326 LDAAYEaSMIDQVRYFKGSKVWAVQEQSVLRGFPRDIHSFF-GFPS 370
Cdd:smart00120   1 IDAAFE-LRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFpGLPC 45
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
196-236 1.35e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.56  E-value: 1.35e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 78099009 196 LDETWTNSSENFNLFY-----VTAHELGHSLGLTHSSDIGALMFPS 236
Cdd:COG1913 105 LRPEFYGLPPDEELFLervlkEAVHELGHLFGLGHCPNPRCVMHFS 150
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 211-254 1.53e-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: 40.72  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 78099009   211 YVTAHELGHSLGLTHSSDIGALMFPSYTWYTEDFVLNQDDINRI 254
Cdd:TIGR03935 340 GTLAHELGHILGAEHTDNEKDLMYTWYTGYWRLNHLSEKNMVRI 383
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 282-323 3.03e-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: 35.68  E-value: 3.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 78099009    282 FDAITTFR-GEVFFFKGRFYIRVNRF-MPEPELNLIGILWPNLP 323
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKrVDPGYPKLISSFFPGLP 44
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 123-225 7.49e-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: 37.74  E-value: 7.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099009 123 PKAVVEDAIARAFRVWSDVTPLTFQRVFEEEGDIVLSFHRGDhgDNNPFDGPNYKLAHTFQPGPGLGGDVHYDLDETWTN 202
Cdd:cd04327  17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGD--GYWSYVGTDALLIGADAPTMNLGWFTDDTPDPEFSR 94

                        90       100
                ....*....|....*....|...
gi 78099009 203 ssenfnlfyVTAHELGHSLGLTH 225
Cdd:cd04327  95 ---------VVLHEFGHALGFIH 108
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
162-231 8.83e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 37.40  E-value: 8.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78099009   162 RGDHGDNN-----PFDGPNYKLAHTFQPGP-GLGGDVHYDLDETWTNSSeNFNLFYVTAHELGHSLGLTHSSDIGA 231
Cdd:pfam13688  85 RGTQNDDLaylflMTNCSGGGLAWLGQLCNsGSAGSVSTRVSGNNVVVS-TATEWQVFAHEIGHNFGAVHDCDSST 159
 
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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