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Conserved domains on  [gi|3183022|sp|P91953|]
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RecName: Full=50 kDa hatching enzyme; Short=HE; Short=HEZ; AltName: Full=Envelysin; AltName: Full=Sea-urchin-hatching proteinase; Contains: RecName: Full=38 kDa hatching enzyme; Contains: RecName: Full=32 kDa hatching enzyme non-specific; Contains: RecName: Full=15 kDa peptide; 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 ...
 176-330 7.42e-76

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: 237.90  E-value: 7.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022    176 AWPRNVaVTYSFGTLSNDLSQTAIKNELRRAFQVWDDVSSLTFREVvDSSSVDIRIKFGSYEHGDGISFDGQGGVLAHAF 255
Cdd:pfam00413   1 KWRKKN-LTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022    256 LP---RNGDAHFDDSERWTIGT--NSGTNLFQVAAHEFGHSLGLYHSDVQSALMYPYYRGYNP-NFNLDRDDIAGITSLY 329
Cdd:pfam00413  79 FPgpgLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkKFRLSQDDIKGIQQLY 158


                  .
gi 3183022    330 G 330
Cdd:pfam00413 159 G 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 380-574 3.35e-45

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: 158.63  E-value: 3.35e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  380 RQACTG-SFDAVIKDnSDRIYALAGRYYWRLDQASPSWGV--VRNRFGFdLPENVDASFQNGI--FSYFFSGCYYYYQTS 454
Cdd:cd00094   1 PDACDPlSFDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPflISSFWPS-LPSPVDAAFERPDtgKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  455 T--RRRFPRTPFNRRWVGLPCDIDAVYKSGDSGTTYFFKGRFVYKFSSSNQLQRRSpISSYFRNTPYALRDGVEAVVRVD 532
Cdd:cd00094  79 KnlEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPG-YPKLIETDFPGVPDKVDAAFRWL 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 3183022  533 DVYLHFYRDGRYYRMIESTKQfvnfpNGLSYRDVIDTLIPQC 574
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKE-----VRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 104-157 7.84e-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: 43.27  E-value: 7.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 3183022    104 VVKLKANLEQFGYVPLGST--FGEANinyTSAILEYQQNGGINQTGILDAETAALL 157
Cdd:pfam01471   5 VKELQRYLNRLGYYPGPVDgyFGPST---EAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 176-330 7.42e-76

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: 237.90  E-value: 7.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022    176 AWPRNVaVTYSFGTLSNDLSQTAIKNELRRAFQVWDDVSSLTFREVvDSSSVDIRIKFGSYEHGDGISFDGQGGVLAHAF 255
Cdd:pfam00413   1 KWRKKN-LTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022    256 LP---RNGDAHFDDSERWTIGT--NSGTNLFQVAAHEFGHSLGLYHSDVQSALMYPYYRGYNP-NFNLDRDDIAGITSLY 329
Cdd:pfam00413  79 FPgpgLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkKFRLSQDDIKGIQQLY 158


                  .
gi 3183022    330 G 330
Cdd:pfam00413 159 G 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 177-330 1.81e-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: 237.10  E-value: 1.81e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  177 WPRNVaVTYSFGTLSNDLSQTAIKNELRRAFQVWDDVSSLTFREVVDSSSVDIRIKFGSYEHGDGISFDGQGGVLAHAFL 256
Cdd:cd04278   2 WSKTN-LTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3183022  257 P--RNGDAHFDDSERWTIGTNS-GTNLFQVAAHEFGHSLGLYHSDVQSALMYPYYRGYNPNFNLDRDDIAGITSLYG 330
Cdd:cd04278  81 PggIGGDIHFDDDEQWTLGSDSgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 380-574 3.35e-45

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: 158.63  E-value: 3.35e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  380 RQACTG-SFDAVIKDnSDRIYALAGRYYWRLDQASPSWGV--VRNRFGFdLPENVDASFQNGI--FSYFFSGCYYYYQTS 454
Cdd:cd00094   1 PDACDPlSFDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPflISSFWPS-LPSPVDAAFERPDtgKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  455 T--RRRFPRTPFNRRWVGLPCDIDAVYKSGDSGTTYFFKGRFVYKFSSSNQLQRRSpISSYFRNTPYALRDGVEAVVRVD 532
Cdd:cd00094  79 KnlEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPG-YPKLIETDFPGVPDKVDAAFRWL 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 3183022  533 DVYLHFYRDGRYYRMIESTKQfvnfpNGLSYRDVIDTLIPQC 574
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKE-----VRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 177-330 5.10e-30

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: 114.76  E-value: 5.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022     177 WPRNVaVTYSFgtLSNDLSQTAiKNELRRAFQVWDDVSSLTFREVvdSSSVDIRIKFGSYEHGdgisfdgqgGVLAHAFL 256
Cdd:smart00235   5 WPKGT-VPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVER--TGTADIYISFGSGDSG---------CTLSHAGR 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3183022     257 PrNGDAHFDDsERWTIGtnsgtnlFQVAAHEFGHSLGLYHSDVQSA---LMYPYYRGYNP-NFNLDRDDIAGITSLYG 330
Cdd:smart00235  70 P-GGDQHLSL-GNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTrNFDLSEDDSLGIPYDYG 138
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 104-157 7.84e-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: 43.27  E-value: 7.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 3183022    104 VVKLKANLEQFGYVPLGST--FGEANinyTSAILEYQQNGGINQTGILDAETAALL 157
Cdd:pfam01471   5 VKELQRYLNRLGYYPGPVDgyFGPST---EAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 475-518 2.25e-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: 41.84  E-value: 2.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 3183022     475 IDAVYKSGDsGTTYFFKGRFVYKFSSSNQLQ-RRSPISSYFRNTP 518
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKRVDPgYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 475-513 1.27e-03

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 36.78  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 3183022    475 IDAVYKSGDsGTTYFFKGRFVYKFSSSNQLQR-RSPISSY 513
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRVEPGyPKLISDF 39
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 283-321 7.75e-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: 38.79  E-value: 7.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 3183022    283 VAAHEFGHSLGLYHSDVQSALMYPYYRGYNPNFNLDRDD 321
Cdd:TIGR03935 341 TLAHELGHILGAEHTDNEKDLMYTWYTGYWRLNHLSEKN 379
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 176-330 7.42e-76

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: 237.90  E-value: 7.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022    176 AWPRNVaVTYSFGTLSNDLSQTAIKNELRRAFQVWDDVSSLTFREVvDSSSVDIRIKFGSYEHGDGISFDGQGGVLAHAF 255
Cdd:pfam00413   1 KWRKKN-LTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEV-STGEADIMIGFGRGDHGDGYPFDGPGGVLAHAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022    256 LP---RNGDAHFDDSERWTIGT--NSGTNLFQVAAHEFGHSLGLYHSDVQSALMYPYYRGYNP-NFNLDRDDIAGITSLY 329
Cdd:pfam00413  79 FPgpgLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkKFRLSQDDIKGIQQLY 158


                  .
gi 3183022    330 G 330
Cdd:pfam00413 159 G 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 177-330 1.81e-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: 237.10  E-value: 1.81e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  177 WPRNVaVTYSFGTLSNDLSQTAIKNELRRAFQVWDDVSSLTFREVVDSSSVDIRIKFGSYEHGDGISFDGQGGVLAHAFL 256
Cdd:cd04278   2 WSKTN-LTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3183022  257 P--RNGDAHFDDSERWTIGTNS-GTNLFQVAAHEFGHSLGLYHSDVQSALMYPYYRGYNPNFNLDRDDIAGITSLYG 330
Cdd:cd04278  81 PggIGGDIHFDDDEQWTLGSDSgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 380-574 3.35e-45

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: 158.63  E-value: 3.35e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  380 RQACTG-SFDAVIKDnSDRIYALAGRYYWRLDQASPSWGV--VRNRFGFdLPENVDASFQNGI--FSYFFSGCYYYYQTS 454
Cdd:cd00094   1 PDACDPlSFDAVTTL-RGELYFFKGRYFWRLSPGKPPGSPflISSFWPS-LPSPVDAAFERPDtgKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  455 T--RRRFPRTPFNRRWVGLPCDIDAVYKSGDSGTTYFFKGRFVYKFSSSNQLQRRSpISSYFRNTPYALRDGVEAVVRVD 532
Cdd:cd00094  79 KnlEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPG-YPKLIETDFPGVPDKVDAAFRWL 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 3183022  533 DVYLHFYRDGRYYRMIESTKQfvnfpNGLSYRDVIDTLIPQC 574
Cdd:cd00094 158 DGYYYFFKGDQYWRFDPRSKE-----VRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 177-330 5.10e-30

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: 114.76  E-value: 5.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022     177 WPRNVaVTYSFgtLSNDLSQTAiKNELRRAFQVWDDVSSLTFREVvdSSSVDIRIKFGSYEHGdgisfdgqgGVLAHAFL 256
Cdd:smart00235   5 WPKGT-VPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVER--TGTADIYISFGSGDSG---------CTLSHAGR 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3183022     257 PrNGDAHFDDsERWTIGtnsgtnlFQVAAHEFGHSLGLYHSDVQSA---LMYPYYRGYNP-NFNLDRDDIAGITSLYG 330
Cdd:smart00235  70 P-GGDQHLSL-GNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTrNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 203-330 4.90e-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: 72.87  E-value: 4.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  203 LRRAFQVWDDVSSLTFREVVDSSSV-DIRIKFGSYEHGDGIsfdgqGGVLAHAFLPRNGDAHFDDSERWTIGTNSG---- 277
Cdd:cd04279  26 VKQAAAEWENVGPLKFVYNPEEDNDaDIVIFFDRPPPVGGA-----GGGLARAGFPLISDGNRKLFNRTDINLGPGqprg 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3183022  278 -TNLFQVAAHEFGHSLGLYH-SDVQSALMYPYYrGYNPNFN--LDRDDIAGITSLYG 330
Cdd:cd04279 101 aENLQAIALHELGHALGLWHhSDRPEDAMYPSQ-GQGPDGNptLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 183-329 1.32e-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: 66.01  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  183 VTYSFGTL----SNDLSQTAIKNELRRAFQVWDDVSSLTFREV-VDSSSVDIRIKFgsyehgdgISFDGQGGVLAHAFLP 257
Cdd:cd00203   3 IPYVVVADdrdvEEENLSAQIQSLILIAMQIWRDYLNIRFVLVgVEIDKADIAILV--------TRQDFDGGTGGWAYLG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  258 RNGDAHFDDSerWTIGTNSGTNLF-QVAAHEFGHSLGLYHS--------------------DVQSALMYPYYRGYNP--N 314
Cdd:cd00203  75 RVCDSLRGVG--VLQDNQSGTKEGaQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSYTKGSFSDgqR 152

                       170
                ....*....|....*
gi 3183022  315 FNLDRDDIAGITSLY 329
Cdd:cd00203 153 KDFSQCDIDQINKLY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 180-318 2.77e-12

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: 65.51  E-value: 2.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  180 NVAVTYSFGTLSNDLSQ---------------TAIKNELRRAFQVWDDVSSLTFREVVDSSSVDIRIKFGSYEHGDGISF 244
Cdd:cd04277   1 DTTLTYSFSNTGGPYSYgygreedttntaalsAAQQAAARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGY 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3183022  245 DGQGGVLAHafLPRNGDAHFDDSERWTIGTNSGTNlFQVAAHEFGHSLGLYHSDVqsalmYPYYRGYNPNFNLD 318
Cdd:cd04277  81 AYYPGSGSG--TAYGGDIWFNSSYDTNSDSPGSYG-YQTIIHEIGHALGLEHPGD-----YNGGDPVPPTYALD 146
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 183-329 1.17e-11

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: 63.28  E-value: 1.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  183 VTYSFGTLSNDlsqtAIKNELRRAFQVWDDVSSLTFREVVDSSSVDIRIKFGSYEHGDgisfDGQGGVLAHAFLPRNGDA 262
Cdd:cd04268   4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYN----DGTWSYGPSQVDPLTGEI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  263 HFDDSERWTIGTN-SGTNLFQVAAHEFGHSLGLYHS----------------DVQSALMYPYYRGYNPNF------NLDR 319
Cdd:cd04268  76 LLARVYLYSSFVEySGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNFSIQLgdgqkyTIGP 155

                       170
                ....*....|
gi 3183022  320 DDIAGITSLY 329
Cdd:cd04268 156 YDIAAIKKLY 165
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 104-157 7.84e-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: 43.27  E-value: 7.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 3183022    104 VVKLKANLEQFGYVPLGST--FGEANinyTSAILEYQQNGGINQTGILDAETAALL 157
Cdd:pfam01471   5 VKELQRYLNRLGYYPGPVDgyFGPST---EAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 475-518 2.25e-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: 41.84  E-value: 2.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 3183022     475 IDAVYKSGDsGTTYFFKGRFVYKFSSSNQLQ-RRSPISSYFRNTP 518
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKRVDPgYPKLISSFFPGLP 44
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 200-332 9.23e-04

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 40.83  E-value: 9.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022  200 KNELRRAFQVWDDVSSLTFREVVDSSSvDIRIKFgsyEHGDGI-SFDGQGGVLAHAflprngDAH---FDdserWTIGTN 275
Cdd:cd04327  22 KDKVRAAAREWLPYANLKFKFVTDADA-DIRISF---TPGDGYwSYVGTDALLIGA------DAPtmnLG----WFTDDT 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3183022  276 SGTNLFQVAAHEFGHSLGLYHS----------DVQSAlmYPYYRG---------YNPNFNLDRDDIAGITSLYGRN 332
Cdd:cd04327  88 PDPEFSRVVLHEFGHALGFIHEhqspaanipwDKEAV--YAYFSGppnwdretvINHNVFAKLDDGDVAYSPYDPD 161
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 475-513 1.27e-03

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 36.78  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 3183022    475 IDAVYKSGDsGTTYFFKGRFVYKFSSSNQLQR-RSPISSY 513
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRVEPGyPKLISDF 39
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-426 4.53e-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: 35.23  E-value: 4.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 3183022    387 FDAVIKDNSDRIYALAGRYYWRLDQASPSWGVVRNRFGFD 426
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFP 40
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 177-296 7.32e-03

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 38.03  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3183022    177 WPRNVaVTYSFGTLSNDLSQTAIKNelrrAFQVWDDVSSLTFREVVDSSSVDiRIKFGSyehGDGI-SFDGqggvlahaf 255
Cdd:pfam01400   3 WPNGP-IPYVIDGSLTGLARALIRQ----AMRHWENKTCIRFVERTPAPDNN-YLFFFK---GDGCySYVG--------- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 3183022    256 lpRNGDAHfddserwTIGTNSGTNLFQVAAHEFGHSLGLYH 296
Cdd:pfam01400  65 --RVGGRQ-------PVSIGDGCDKFGIIVHELGHALGFFH 96
fragilysin TIGR03935
fragilysin; Members of this family are fragilysin, the Bacteroides fragilis enterotoxin. This ...
 283-321 7.75e-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: 38.79  E-value: 7.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 3183022    283 VAAHEFGHSLGLYHSDVQSALMYPYYRGYNPNFNLDRDD 321
Cdd:TIGR03935 341 TLAHELGHILGAEHTDNEKDLMYTWYTGYWRLNHLSEKN 379
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-428 8.77e-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: 34.53  E-value: 8.77e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 3183022     387 FDAVIKDNSDRIYALAGRYYWRLDQASPSWGVVR--NRFGFDLP 428
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKliSSFFPGLP 44
 
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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