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Conserved domains on  [gi|6678894|ref|NP_032632|]
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stromelysin-3 preproprotein [Mus musculus]

Protein Classification

M10A family metallopeptidase( domain architecture ID 11995186)

M10A family metallopeptidase similar to matrix metalloproteinases with a C-terminal hemopexin repeat-containing domain that may be endopeptidases that degrade various components of the extracellular matrix

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 ...
 108-262 3.95e-80

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: 246.37  E-value: 3.95e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894    108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALQVWSEVTPLTFTEVHEGRADIMIDFARYWHGDNLPFDGPGGILAHAFFP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678894    188 KTHREGDVHFDYDETWTIGD--NQGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYP--LSLSPDDRRGIQHLYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 295-484 4.52e-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: 213.71  E-value: 4.52e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  295 PDVCET-SFDAVSTIRGELFFFKAGFVWRLRSGRlQPGYPALASRHWQGLPSPVDAAFEDAQ-GQIWFFQGAQYWVYDGE 372
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  373 -KPVLGPAPLSKLGLQGSP--VHAALVWGPEKnKIYFFRGGDYWRFHPRTQRVDNPVPRR-STDWRGVPSEIDAAFQDAE 448
Cdd:cd00094  80 nLEPGYPKPISDLGFPPTVkqIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFRWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6678894  449 GYAYFLRGHLYWKFDPVKVKVLEGFPRPVGPDFFDC 484
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-262 3.95e-80

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: 246.37  E-value: 3.95e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894    108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALQVWSEVTPLTFTEVHEGRADIMIDFARYWHGDNLPFDGPGGILAHAFFP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678894    188 KTHREGDVHFDYDETWTIGD--NQGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYP--LSLSPDDRRGIQHLYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-262 8.62e-77

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: 237.49  E-value: 8.62e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALQVWSEVTPLTFTEVHEG-RADIMIDFARYWHGDNLPFDGPGGILAHAFF 186
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678894  187 PKTHReGDVHFDYDETWTIGDNQ-GTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPL-SLSPDDRRGIQHLYG 262
Cdd:cd04278  81 PGGIG-GDIHFDDDEQWTLGSDSgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKfKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 295-484 4.52e-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: 213.71  E-value: 4.52e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  295 PDVCET-SFDAVSTIRGELFFFKAGFVWRLRSGRlQPGYPALASRHWQGLPSPVDAAFEDAQ-GQIWFFQGAQYWVYDGE 372
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  373 -KPVLGPAPLSKLGLQGSP--VHAALVWGPEKnKIYFFRGGDYWRFHPRTQRVDNPVPRR-STDWRGVPSEIDAAFQDAE 448
Cdd:cd00094  80 nLEPGYPKPISDLGFPPTVkqIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFRWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6678894  449 GYAYFLRGHLYWKFDPVKVKVLEGFPRPVGPDFFDC 484
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 108-262 1.66e-31

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: 118.22  E-value: 1.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894     108 RWEKTDLTYRIlrFPWQLVREQvRQTVAEALQVWSEVTPLTFTEVHEGrADIMIDFARYWHGdnlPFdgpggiLAHAFFP 187
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894     188 KthreGDVHFDyDETWTIGDNqgtdllqVAAHEFGHVLGLQHTTAAKA---LMSPFYTF--RYPLSLSPDDRRGIQHLYG 262
Cdd:smart00235  71 G----GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 302-345 1.33e-08

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: 50.70  E-value: 1.33e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 6678894     302 FDAVSTIR-GELFFFKAGFVWRLRSGRLQPGYPALASRHWQGLPS 345
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 302-345 4.03e-08

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: 49.10  E-value: 4.03e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6678894    302 FDAVSTIR-GELFFFKAGFVWRLRSGRLQPGYPALASrHWQGLPS 345
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLIS-DFPGLPC 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
213-256 5.56e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 5.56e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6678894  213 LLQVAAHEFGHVLGLQHTTAAKALMspfytfRYPLSLSPDDRRG 256
Cdd:COG1913 123 VLKEAVHELGHLFGLGHCPNPRCVM------HFSNSLEELDRKP 160
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-262 3.95e-80

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: 246.37  E-value: 3.95e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894    108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALQVWSEVTPLTFTEVHEGRADIMIDFARYWHGDNLPFDGPGGILAHAFFP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678894    188 KTHREGDVHFDYDETWTIGD--NQGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYP--LSLSPDDRRGIQHLYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSkkFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-262 8.62e-77

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: 237.49  E-value: 8.62e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  108 RWEKTDLTYRILRFPWQLVREQVRQTVAEALQVWSEVTPLTFTEVHEG-RADIMIDFARYWHGDNLPFDGPGGILAHAFF 186
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678894  187 PKTHReGDVHFDYDETWTIGDNQ-GTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPL-SLSPDDRRGIQHLYG 262
Cdd:cd04278  81 PGGIG-GDIHFDDDEQWTLGSDSgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKfKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 295-484 4.52e-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: 213.71  E-value: 4.52e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  295 PDVCET-SFDAVSTIRGELFFFKAGFVWRLRSGRlQPGYPALASRHWQGLPSPVDAAFEDAQ-GQIWFFQGAQYWVYDGE 372
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  373 -KPVLGPAPLSKLGLQGSP--VHAALVWGPEKnKIYFFRGGDYWRFHPRTQRVDNPVPRR-STDWRGVPSEIDAAFQDAE 448
Cdd:cd00094  80 nLEPGYPKPISDLGFPPTVkqIDAALRWPDNG-KTYFFKGDKYWRYDEKTQKMDPGYPKLiETDFPGVPDKVDAAFRWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6678894  449 GYAYFLRGHLYWKFDPVKVKVLEGFPRPVGPDFFDC 484
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 108-262 1.66e-31

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: 118.22  E-value: 1.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894     108 RWEKTDLTYRIlrFPWQLVREQvRQTVAEALQVWSEVTPLTFTEVHEGrADIMIDFARYWHGdnlPFdgpggiLAHAFFP 187
Cdd:smart00235   4 KWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894     188 KthreGDVHFDyDETWTIGDNqgtdllqVAAHEFGHVLGLQHTTAAKA---LMSPFYTF--RYPLSLSPDDRRGIQHLYG 262
Cdd:smart00235  71 G----GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 129-262 1.13e-14

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 71.33  E-value: 1.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  129 QVRQTVAEALQVWSEVTPLTF--TEVHEGRADIMIDFARYWHGDNLpfdgpGGILAHAFFPKTHREGDV---HFDYDETW 203
Cdd:cd04279  21 SWLQAVKQAAAEWENVGPLKFvyNPEEDNDADIVIFFDRPPPVGGA-----GGGLARAGFPLISDGNRKlfnRTDINLGP 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678894  204 TIGdNQGTDLLQVAAHEFGHVLGLQHTTAAKA-LMSPFY--TFRYPLSLSPDDRRGIQHLYG 262
Cdd:cd04279  96 GQP-RGAENLQAIALHELGHALGLWHHSDRPEdAMYPSQgqGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 127-261 2.81e-13

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


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 67.55  E-value: 2.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  127 REQVRQTVAEALQVWSEVTPLTFTEVHEG--RADIMIDFARYwhgdnlpfDGPGGILAHAFFPKT--HREGDVHFDYDET 202
Cdd:cd00203  20 SAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTRQ--------DFDGGTGGWAYLGRVcdSLRGVGVLQDNQS 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  203 WTIgdnqgtDLLQVAAHEFGHVLGLQH--------------------TTAAKALMSPFYTFR---YPLSLSPDDRRGIQH 259
Cdd:cd00203  92 GTK------EGAQTIAHELGHALGFYHdhdrkdrddyptiddtlnaeDDDYYSVMSYTKGSFsdgQRKDFSQCDIDQINK 165


                ..
gi 6678894  260 LY 261
Cdd:cd00203 166 LY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 121-262 4.78e-13

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: 67.44  E-value: 4.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  121 FPWQLVREQVRQTVAEALQVWSEVTPLTFTEV-HEGRADIMIDFarywhgdnlpFDGP-GGILAHAFFPK----THREGD 194
Cdd:cd04277  26 TNTAALSAAQQAAARDALEAWEDVADIDFVEVsDNSGADIRFGN----------SSDPdGNTAGYAYYPGsgsgTAYGGD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  195 VHFDYDETWTIGDNqGTDLLQVAAHEFGHVLGLQH-----------TTAAKA-----LMS--------PFYTFRYPLSLS 250
Cdd:cd04277  96 IWFNSSYDTNSDSP-GSYGYQTIIHEIGHALGLEHpgdynggdpvpPTYALDsreytVMSynsgygngASAGGGYPQTPM 174

                       170
                ....*....|..
gi 6678894  251 PDDRRGIQHLYG 262
Cdd:cd04277 175 LLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 111-235 1.27e-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: 57.12  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678894  111 KTDLTYRILR-FPwqlvrEQVRQTVAEALQVWSEVTPLTFTEVHEGR-ADIMIDFARYWHGDnlpfDGPGGILAHAFFPK 188
Cdd:cd04268   1 KKPITYYIDDsVP-----DKLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYN----DGTWSYGPSQVDPL 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6678894  189 TH--REGDVHFDYDETWTIGDNqgtdLLQVAAHEFGHVLGLQHTTAAKA 235
Cdd:cd04268  72 TGeiLLARVYLYSSFVEYSGAR----LRNTAEHELGHALGLRHNFAASD 116
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 302-345 1.33e-08

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: 50.70  E-value: 1.33e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 6678894     302 FDAVSTIR-GELFFFKAGFVWRLRSGRLQPGYPALASRHWQGLPS 345
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 302-345 4.03e-08

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: 49.10  E-value: 4.03e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6678894    302 FDAVSTIR-GELFFFKAGFVWRLRSGRLQPGYPALASrHWQGLPS 345
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLIS-DFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-438 2.42e-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: 47.18  E-value: 2.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 6678894    391 VHAALVWGPekNKIYFFRGGDYWRFHPrtQRVDNPVPRRSTDWRGVPS 438
Cdd:pfam00045   1 IDAAFEDRD--GKTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-384 8.93e-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: 45.64  E-value: 8.93e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 6678894    347 VDAAFEDAQGQIWFFQGAQYWVYDGEKPVLG-PAPLSKL 384
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGyPKLISDF 39
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 440-482 1.66e-06

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: 44.93  E-value: 1.66e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 6678894     440 IDAAFQDAEGYAYFLRGHLYWKFDPVKVKvlEGFPRPVGPDFF 482
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVD--PGYPKLISSFFP 41
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-438 1.86e-06

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: 44.54  E-value: 1.86e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6678894     391 VHAALVWgpEKNKIYFFRGGDYWRFHPrtQRVDNPVPRR-STDWRGVPS 438
Cdd:smart00120   1 IDAAFEL--RDGKTYFFKGDKYWRFDP--KRVDPGYPKLiSSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 440-477 1.49e-05

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: 42.17  E-value: 1.49e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6678894    440 IDAAFQDAEGYAYFLRGHLYWKFDPvkVKVLEGFPRPV 477
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDP--QRVEPGYPKLI 36
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-384 2.15e-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: 41.46  E-value: 2.15e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 6678894     347 VDAAFEDAQGQIWFFQGAQYWVYDGEKPVLG-PAPLSKL 384
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGyPKLISSF 39
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
213-256 5.56e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 5.56e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6678894  213 LLQVAAHEFGHVLGLQHTTAAKALMspfytfRYPLSLSPDDRRG 256
Cdd:COG1913 123 VLKEAVHELGHLFGLGHCPNPRCVM------HFSNSLEELDRKP 160
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 213-242 9.37e-03

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 37.30  E-value: 9.37e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 6678894  213 LLQVAAHEFGHVLGLQHTTAAKALMSPFYT 242
Cdd:cd04276 116 LRYLLAHEVGHTLGLRHNFKASSDGSNEEL 145
 
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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