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Conserved domains on  [gi|998074870|ref|NP_001307187|]
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matrix metalloproteinase-25 isoform 2 [Mus musculus]

Protein Classification

ZnMc_MMP and HX domain-containing protein( domain architecture ID 10136642)

ZnMc_MMP and HX domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 2-123 2.72e-61

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: 195.12  E-value: 2.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870   2 EEVNSQyQEPDIIIHFARAYHQDSYPFDGSGGTLAHAFFPGEhpISGDTHFDDEETWTFGStDDNGIDLFAVAVHEFGHA 81
Cdd:cd04278   43 REVTSG-QEADIRISFARGNHGDGYPFDGPGGTLAHAFFPGG--IGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHA 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 998074870  82 LGLGHSSAPNSIMRPFYQGPVGDpatYRLPQDDRDGLQQLYG 123
Cdd:cd04278  119 LGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 157-351 4.65e-53

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: 175.19  E-value: 4.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870 157 PDRCEG-NFDAVANIRGEIFLFKGPWFWRLQPSGQLVSPRPAglHRFWEGLPTHvkvIQAAYARPLDGRIILFSGPQFWV 235
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLI--SSFWPSLPSP---VDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870 236 FQERQLE-GAARPLVEFGLPPGED-VDAVFSWPHNGKTYLIRGQKYWRYDEVAARPDPGYPRALS-LWDGAPFAPDDVTI 312
Cdd:cd00094   76 YTGKNLEpGYPKPISDLGFPPTVKqIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 998074870 313 SNTGDTYFFKGTHFWRFAEGSVKAESDSPQPIGPKWLDC 351
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 2-123 2.72e-61

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: 195.12  E-value: 2.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870   2 EEVNSQyQEPDIIIHFARAYHQDSYPFDGSGGTLAHAFFPGEhpISGDTHFDDEETWTFGStDDNGIDLFAVAVHEFGHA 81
Cdd:cd04278   43 REVTSG-QEADIRISFARGNHGDGYPFDGPGGTLAHAFFPGG--IGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHA 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 998074870  82 LGLGHSSAPNSIMRPFYQGPVGDpatYRLPQDDRDGLQQLYG 123
Cdd:cd04278  119 LGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 7-123 2.19e-58

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: 187.44  E-value: 2.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870    7 QYQEPDIIIHFARAYHQDSYPFDGSGGTLAHAFFPGEHpISGDTHFDDEETWTFGSTDDNGIDLFAVAVHEFGHALGLGH 86
Cdd:pfam00413  46 STGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPGPG-LGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGH 124

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 998074870   87 SSAPNSIMRPFYQGpvGDPATYRLPQDDRDGLQQLYG 123
Cdd:pfam00413 125 SSDPGAIMYPTYSP--LDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 157-351 4.65e-53

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: 175.19  E-value: 4.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870 157 PDRCEG-NFDAVANIRGEIFLFKGPWFWRLQPSGQLVSPRPAglHRFWEGLPTHvkvIQAAYARPLDGRIILFSGPQFWV 235
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLI--SSFWPSLPSP---VDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870 236 FQERQLE-GAARPLVEFGLPPGED-VDAVFSWPHNGKTYLIRGQKYWRYDEVAARPDPGYPRALS-LWDGAPFAPDDVTI 312
Cdd:cd00094   76 YTGKNLEpGYPKPISDLGFPPTVKqIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 998074870 313 SNTGDTYFFKGTHFWRFAEGSVKAESDSPQPIGPKWLDC 351
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 9-123 3.31e-16

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: 74.69  E-value: 3.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870     9 QEPDIIIHFARAYHqdsypfdgsGGTLAHAFFPGehpisGDTHFDDEetwtfgstddNGIDLFAVAVHEFGHALGLGHSS 88
Cdd:smart00235  47 GTADIYISFGSGDS---------GCTLSHAGRPG-----GDQHLSLG----------NGCINTGVAAHELGHALGLYHEQ 102

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 998074870    89 APNS---IMRPFYQGPvgDPATYRLPQDDRDGLQQLYG 123
Cdd:smart00235 103 SRSDrdnYMYINYTNI--DTRNFDLSEDDSLGIPYDYG 138
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 259-304 4.67e-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: 48.72  E-value: 4.67e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 998074870  259 VDAVFSWPHnGKTYLIRGQKYWRYDEvaARPDPGYPRALSLWDGAP 304
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 259-304 4.75e-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: 48.78  E-value: 4.75e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 998074870   259 VDAVFSWPhNGKTYLIRGQKYWRYDEvaARPDPGYPRALS-LWDGAP 304
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 62-122 5.62e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 47.37  E-value: 5.62e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998074870  62 STDDNGIDLFAVAVHEFGHALGL-GHSSAPNSIMrpFYQGpVGDPatYRLPQDDRDGLQQLY 122
Cdd:COG5549  174 SPNQTGKYLLATARHELGHALGIwGHSPSPTDAM--YFSQ-VRNP--PPISPRDINTLKRIY 230
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 2-123 2.72e-61

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: 195.12  E-value: 2.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870   2 EEVNSQyQEPDIIIHFARAYHQDSYPFDGSGGTLAHAFFPGEhpISGDTHFDDEETWTFGStDDNGIDLFAVAVHEFGHA 81
Cdd:cd04278   43 REVTSG-QEADIRISFARGNHGDGYPFDGPGGTLAHAFFPGG--IGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHA 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 998074870  82 LGLGHSSAPNSIMRPFYQGPVGDpatYRLPQDDRDGLQQLYG 123
Cdd:cd04278  119 LGLGHSSDPDSIMYPYYQGPVPK---FKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 7-123 2.19e-58

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: 187.44  E-value: 2.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870    7 QYQEPDIIIHFARAYHQDSYPFDGSGGTLAHAFFPGEHpISGDTHFDDEETWTFGSTDDNGIDLFAVAVHEFGHALGLGH 86
Cdd:pfam00413  46 STGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPGPG-LGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGH 124

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 998074870   87 SSAPNSIMRPFYQGpvGDPATYRLPQDDRDGLQQLYG 123
Cdd:pfam00413 125 SSDPGAIMYPTYSP--LDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 157-351 4.65e-53

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: 175.19  E-value: 4.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870 157 PDRCEG-NFDAVANIRGEIFLFKGPWFWRLQPSGQLVSPRPAglHRFWEGLPTHvkvIQAAYARPLDGRIILFSGPQFWV 235
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLI--SSFWPSLPSP---VDAAFERPDTGKIYFFKGDKYWV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870 236 FQERQLE-GAARPLVEFGLPPGED-VDAVFSWPHNGKTYLIRGQKYWRYDEVAARPDPGYPRALS-LWDGAPFAPDDVTI 312
Cdd:cd00094   76 YTGKNLEpGYPKPISDLGFPPTVKqIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFR 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 998074870 313 SNTGDTYFFKGTHFWRFAEGSVKAESDSPQPIGPKWLDC 351
Cdd:cd00094  156 WLDGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 9-123 3.31e-16

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: 74.69  E-value: 3.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870     9 QEPDIIIHFARAYHqdsypfdgsGGTLAHAFFPGehpisGDTHFDDEetwtfgstddNGIDLFAVAVHEFGHALGLGHSS 88
Cdd:smart00235  47 GTADIYISFGSGDS---------GCTLSHAGRPG-----GDQHLSLG----------NGCINTGVAAHELGHALGLYHEQ 102

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 998074870    89 APNS---IMRPFYQGPvgDPATYRLPQDDRDGLQQLYG 123
Cdd:smart00235 103 SRSDrdnYMYINYTNI--DTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 12-123 8.22e-13

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: 65.56  E-value: 8.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870  12 DIIIhfaraYHQDSYPFDGSGGTLAHAFFPGEHPISGDT--HFDDEETWTFGSTDDNgidLFAVAVHEFGHALGLGHSSA 89
Cdd:cd04279   52 DIVI-----FFDRPPPVGGAGGGLARAGFPLISDGNRKLfnRTDINLGPGQPRGAEN---LQAIALHELGHALGLWHHSD 123

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 998074870  90 -PNSIMRPFY-QGPVGDPatyRLPQDDRDGLQQLYG 123
Cdd:cd04279  124 rPEDAMYPSQgQGPDGNP---TLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 3-122 1.35e-08

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: 53.68  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870   3 EVNSQYQEPDIIIHFARAyhqdsypfDGSGGTLAHAFFPG-EHPISGDTHFDDEETWTFgstddngiDLFAVAVHEFGHA 81
Cdd:cd00203   44 LVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLGRvCDSLRGVGVLQDNQSGTK--------EGAQTIAHELGHA 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998074870  82 LGLGHSS--------------------APNSIMRPFYqGPVGDPATYRLPQDDRDGLQQLY 122
Cdd:cd00203  108 LGFYHDHdrkdrddyptiddtlnaeddDYYSVMSYTK-GSFSDGQRKDFSQCDIDQINKLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 259-304 4.67e-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: 48.72  E-value: 4.67e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 998074870  259 VDAVFSWPHnGKTYLIRGQKYWRYDEvaARPDPGYPRALSLWDGAP 304
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 259-304 4.75e-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: 48.78  E-value: 4.75e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 998074870   259 VDAVFSWPhNGKTYLIRGQKYWRYDEvaARPDPGYPRALS-LWDGAP 304
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 29-123 5.17e-08

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: 52.42  E-value: 5.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870  29 DGSGGTLAHAFFPG---EHPISGDTHFDDEETWTFGStddNGIDLFAVAVHEFGHALGLGHS----------------SA 89
Cdd:cd04277   72 DPDGNTAGYAYYPGsgsGTAYGGDIWFNSSYDTNSDS---PGSYGYQTIIHEIGHALGLEHPgdynggdpvpptyaldSR 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 998074870  90 PNSIMRpfYQGPVGDP--ATYRLPQ----DDRDGLQQLYG 123
Cdd:cd04277  149 EYTVMS--YNSGYGNGasAGGGYPQtpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 8-122 1.93e-06

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: 47.49  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998074870   8 YQEPDIIIHFARayhqDSYPFDGSGGTLAHAFFPGEHPISgdthfDDEETWTFGSTDDNGIDLFAVAVHEFGHALGLGHS 87
Cdd:cd04268   41 VDPADIRYSVIR----WIPYNDGTWSYGPSQVDPLTGEIL-----LARVYLYSSFVEYSGARLRNTAEHELGHALGLRHN 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 998074870  88 SA----------------PNSIM---RPFYQGPVGDPATYRLPQDDRDGLQQLY 122
Cdd:cd04268  112 FAasdrddnvdllaekgdTSSVMdyaPSNFSIQLGDGQKYTIGPYDIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 62-122 5.62e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 47.37  E-value: 5.62e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998074870  62 STDDNGIDLFAVAVHEFGHALGL-GHSSAPNSIMrpFYQGpVGDPatYRLPQDDRDGLQQLY 122
Cdd:COG5549  174 SPNQTGKYLLATARHELGHALGIwGHSPSPTDAM--YFSQ-VRNP--PPISPRDINTLKRIY 230
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 164-207 6.57e-05

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 39.92  E-value: 6.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 998074870   164 FDAVA-NIRGEIFLFKGPWFWRLQPsGQLVSPRPAGLHRFWEGLP 207
Cdd:smart00120   1 IDAAFeLRDGKTYFFKGDKYWRFDP-KRVDPGYPKLISSFFPGLP 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
70-96 9.45e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 9.45e-04
                         10        20
                 ....*....|....*....|....*..
gi 998074870  70 LFAVAVHEFGHALGLGHSSAPNSIMRP 96
Cdd:COG1913  123 VLKEAVHELGHLFGLGHCPNPRCVMHF 149
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 54-86 5.35e-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: 5.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 998074870  54 DEETWTFGSTDDNGIDLF--AVAVHEFGHALGLGH 86
Cdd:cd04327   74 DAPTMNLGWFTDDTPDPEfsRVVLHEFGHALGFIH 108
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 164-207 5.86e-03

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 34.46  E-value: 5.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 998074870  164 FDAVANIR-GEIFLFKGPWFWRLQPsGQLVSPRPAGLHRFWeGLP 207
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDP-QRVEPGYPKLISDFP-GLP 43
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 73-96 1.00e-02

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 36.89  E-value: 1.00e-02
                         10        20
                 ....*....|....*....|....
gi 998074870  73 VAVHEFGHALGLGHSSAPNSIMRP 96
Cdd:cd11375  126 EAVHELGHLFGLDHCPYYACVMNF 149
 
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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