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Conserved domains on  [gi|767995855|ref|XP_011523529|]
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matrix metalloproteinase-28 isoform X3 [Homo sapiens]

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 ...
 44-199 1.50e-73

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: 227.47  E-value: 1.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  44 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 123
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995855 124 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYG 199
Cdd:cd04278   79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 236-425 9.77e-32

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: 119.72  E-value: 9.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 236 PKYCHS-SFDAITVDRQQqLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGP 314
Cdd:cd00094    1 PDACDPlSFDAVTTLRGE-LYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 315 KPVWGLPQLCRAGGLPRHP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRP 388
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWL 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767995855 389 DGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 425
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 44-199 1.50e-73

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: 227.47  E-value: 1.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  44 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 123
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995855 124 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYG 199
Cdd:cd04278   79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 44-199 8.46e-66

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: 207.47  E-value: 8.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855   44 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLgnAFDGPGGALAHA 123
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGY--PFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  124 FLP---RRGEAHFDQDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDAL-LSWDDVLAVQSL 197
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  ..
gi 767995855  198 YG 199
Cdd:pfam00413 158 YG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 236-425 9.77e-32

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: 119.72  E-value: 9.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 236 PKYCHS-SFDAITVDRQQqLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGP 314
Cdd:cd00094    1 PDACDPlSFDAVTTLRGE-LYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 315 KPVWGLPQLCRAGGLPRHP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRP 388
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWL 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767995855 389 DGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 425
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 44-200 1.32e-23

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: 95.88  E-value: 1.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855    44 KWYKQHLSYRLVNWPEhlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglgnafdgpGGALAHA 123
Cdd:smart00235   4 KWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855   124 FLPRrGEAHFDqDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKRLGRDAL-LSWDDVLAVQSLYG 199
Cdd:smart00235  68 GRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPYDYG 138


                   .
gi 767995855   200 K 200
Cdd:smart00235 139 S 139
Zn_serralysin NF035945
serralysin family metalloprotease;
73-199 2.31e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 46.51  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  73 AFQLWSNVSALEFWEAPATGPADIrlTFfqgdhndglGNaFDGpgGALAHAFLPRRGEAhfdQDERWSLSRRR------- 145
Cdd:NF035945  88 SLQSWSDVANITFTEVSAGQKANI--TF---------GN-YSD--SGQAYAYLPGTSDV---SGQSWYNYNSDyirnltp 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 146 -----GRNLFvvlAHEIGHTLGLTHsPA--------PRALMAPY-----------Y---KRLGRD--------ALLswDD 190
Cdd:NF035945 151 dlgnyGRQTL---THEIGHTLGLSH-PGdynagegnPTYKDATYaedtrqysvmsYwseSNTGQDfkghyasaPLL--DD 224


                 ....*....
gi 767995855 191 VLAVQSLYG 199
Cdd:NF035945 225 IAAIQKLYG 233
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
116-175 8.33e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 43.02  E-value: 8.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 116 PGGALAHAFLPRRGEAHFDQDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 175
Cdd:COG1913   93 LGGRVAVVSTARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 381-425 2.72e-04

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 38.38  E-value: 2.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767995855   381 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 425
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-323 4.37e-04

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 37.93  E-value: 4.37e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 767995855  291 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 323
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKL 35
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
155-173 2.49e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 2.49e-03
                         10
                 ....*....|....*....
gi 767995855 155 HEIGHTLGLTHSPAPRALM 173
Cdd:NF033823 128 HELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 155-173 9.71e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.92  E-value: 9.71e-03
                         10
                 ....*....|....*....
gi 767995855 155 HEIGHTLGLTHSPAPRALM 173
Cdd:PRK13267 131 HELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 44-199 1.50e-73

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: 227.47  E-value: 1.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  44 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 123
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995855 124 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYG 199
Cdd:cd04278   79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 44-199 8.46e-66

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: 207.47  E-value: 8.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855   44 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLgnAFDGPGGALAHA 123
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGY--PFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  124 FLP---RRGEAHFDQDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDAL-LSWDDVLAVQSL 197
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  ..
gi 767995855  198 YG 199
Cdd:pfam00413 158 YG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 236-425 9.77e-32

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: 119.72  E-value: 9.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 236 PKYCHS-SFDAITVDRQQqLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGP 314
Cdd:cd00094    1 PDACDPlSFDAVTTLRGE-LYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 315 KPVWGLPQLCRAGGLPRHP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRP 388
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWL 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767995855 389 DGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 425
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 44-200 1.32e-23

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: 95.88  E-value: 1.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855    44 KWYKQHLSYRLVNWPEhlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglgnafdgpGGALAHA 123
Cdd:smart00235   4 KWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855   124 FLPRrGEAHFDqDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKRLGRDAL-LSWDDVLAVQSLYG 199
Cdd:smart00235  68 GRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPYDYG 138


                   .
gi 767995855   200 K 200
Cdd:smart00235 139 S 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 69-199 9.88e-14

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: 69.37  E-value: 9.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  69 AVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFDGPGGAlahaFLPRRGEAHFDQDERWSLSRRRGRN 148
Cdd:cd04277   38 AARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAYYPGSGS----GTAYGGDIWFNSSYDTNSDSPGSYG 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995855 149 LFVVLaHEIGHTLGLTHS-------PAPRA---------LMA----PYYKRLGRDALLSW---DDVLAVQSLYG 199
Cdd:cd04277  114 YQTII-HEIGHALGLEHPgdynggdPVPPTyaldsreytVMSynsgYGNGASAGGGYPQTpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 64-222 1.06e-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: 62.90  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  64 PAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFdGPGGALahaflPRRGEAHFDQDERWS--- 140
Cdd:cd04268   14 DKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSY-GPSQVD-----PLTGEILLARVYLYSsfv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 141 -LSRRRGRNlfvVLAHEIGHTLGLTHSPApRALMAPYYkrlgrDALLSWDDVLAVQSlygkPLGGSVAVQLPGKLFTDFE 219
Cdd:cd04268   88 eYSGARLRN---TAEHELGHALGLRHNFA-ASDRDDNV-----DLLAEKGDTSSVMD----YAPSNFSIQLGDGQKYTIG 154


                 ...
gi 767995855 220 TWD 222
Cdd:cd04268  155 PYD 157
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 65-198 4.11e-11

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: 61.38  E-value: 4.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  65 AVRGAVRAAFQLWSNVSALEFWEAPAT-GPADIRLTFFQGDHNdglgnafdgpGGALAHAFLPR-----RGEAHFDQDER 138
Cdd:cd00203   22 QIQSLILIAMQIWRDYLNIRFVLVGVEiDKADIAILVTRQDFD----------GGTGGWAYLGRvcdslRGVGVLQDNQS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 139 WslsrrrGRNLFVVLAHEIGHTLGLTHSP--------------------APRALMAPYYKR--LGRDALLSWDDVLAVQS 196
Cdd:cd00203   92 G------TKEGAQTIAHELGHALGFYHDHdrkdrddyptiddtlnaeddDYYSVMSYTKGSfsDGQRKDFSQCDIDQINK 165


                 ..
gi 767995855 197 LY 198
Cdd:cd00203  166 LY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 56-199 1.43e-08

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: 53.61  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  56 NWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGP-ADIRLtFFQGDHNDGLGnafdgpGGALAHAFLPrrgeahFD 134
Cdd:cd04279   12 PAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDNdADIVI-FFDRPPPVGGA------GGGLARAGFP------LI 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767995855 135 QDERWSLS-----------RRRGRNLFVVLAHEIGHTLGLTH-SPAPRALMAPYYKRLG-RDALLSWDDVLAVQSLYG 199
Cdd:cd04279   79 SDGNRKLFnrtdinlgpgqPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPdGNPTLSARDVATLKRLYG 156
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 62-165 1.07e-05

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: 46.16  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  62 PEPaVRGAVRAAFQLW---------SNVSALEFWEAPATgPADIRLTFFQGDHNDGLGNAFdgpGGALAHaflPRRGE-- 130
Cdd:cd04276   19 PEK-YRDAIREGVLYWnkafekagfKNAIIVKVLPDDAD-PGDIRYNVIRWIHSPNGGWAY---GPSVVD---PRTGEil 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767995855 131 -------AHF---DQDERWSLSRRRGRNLfvvLAHEIGHTLGLTH 165
Cdd:cd04276   91 kadvilySGFlrqDQLWYEDLLAASLRYL---LAHEVGHTLGLRH 132
Zn_serralysin NF035945
serralysin family metalloprotease;
73-199 2.31e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 46.51  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  73 AFQLWSNVSALEFWEAPATGPADIrlTFfqgdhndglGNaFDGpgGALAHAFLPRRGEAhfdQDERWSLSRRR------- 145
Cdd:NF035945  88 SLQSWSDVANITFTEVSAGQKANI--TF---------GN-YSD--SGQAYAYLPGTSDV---SGQSWYNYNSDyirnltp 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 146 -----GRNLFvvlAHEIGHTLGLTHsPA--------PRALMAPY-----------Y---KRLGRD--------ALLswDD 190
Cdd:NF035945 151 dlgnyGRQTL---THEIGHTLGLSH-PGdynagegnPTYKDATYaedtrqysvmsYwseSNTGQDfkghyasaPLL--DD 224


                 ....*....
gi 767995855 191 VLAVQSLYG 199
Cdd:NF035945 225 IAAIQKLYG 233
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
116-175 8.33e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 43.02  E-value: 8.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855 116 PGGALAHAFLPRRGEAHFDQDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 175
Cdd:COG1913   93 LGGRVAVVSTARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 381-425 2.72e-04

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 38.38  E-value: 2.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767995855   381 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 425
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 243-286 3.52e-04

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 37.99  E-value: 3.52e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767995855   243 FDAITVDRQQQLYIFKGSHFWEV-AADGNVSEPRPLQERWVGLPP 286
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFdPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-323 4.37e-04

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 37.93  E-value: 4.37e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 767995855  291 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 323
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKL 35
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-323 1.16e-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: 36.45  E-value: 1.16e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767995855   291 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 323
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKL 35
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 140-175 2.10e-03

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


Pssm-ID: 213029  Cd Length: 173  Bit Score: 38.82  E-value: 2.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767995855 140 SLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 175
Cdd:cd11375  117 GLFLER---LLKEAVHELGHLFGLDHCPYYACVMNF 149
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
155-173 2.49e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 2.49e-03
                         10
                 ....*....|....*....
gi 767995855 155 HEIGHTLGLTHSPAPRALM 173
Cdd:NF033823 128 HELGHLLGLGHCPNPRCVM 146
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 62-168 4.01e-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: 38.52  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995855  62 PEPAVRGAVRAAFQLWSNVSALEFWEApATGPADIRLTFFQGDHN------DGLGNAFDGPGGALAhaflprrgeahfdq 135
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFV-TDADADIRISFTPGDGYwsyvgtDALLIGADAPTMNLG-------------- 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767995855 136 derWSLSRRRGRNLFVVLAHEIGHTLGLTH---SPA 168
Cdd:cd04327   82 ---WFTDDTPDPEFSRVVLHEFGHALGFIHehqSPA 114
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 152-165 5.12e-03

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 38.77  E-value: 5.12e-03
                          10
                  ....*....|....
gi 767995855  152 VLAHEIGHTLGLTH 165
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 243-286 5.18e-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: 34.85  E-value: 5.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 767995855  243 FDAITVDRQQQLYIFKGSHFWEVaaDGNVSE---PRPLQErWVGLPP 286
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRF--DPQRVEpgyPKLISD-FPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 381-425 8.83e-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: 34.08  E-value: 8.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767995855  381 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSgRWATELPWMGC 425
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYP-KLISDFPGLPC 44
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 155-173 9.71e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.92  E-value: 9.71e-03
                         10
                 ....*....|....*....
gi 767995855 155 HEIGHTLGLTHSPAPRALM 173
Cdd:PRK13267 131 HELGHTLGLEHCDNPRCVM 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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