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Conserved domains on  [gi|767995851|ref|XP_011523527|]
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matrix metalloproteinase-28 isoform X2 [Homo sapiens]

Protein Classification

PG_binding_1 and HX domain-containing protein( domain architecture ID 10478050)

protein containing domains PG_binding_1, ZnMc, and HX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 126-209 1.59e-38

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.


The actual alignment was detected with superfamily member cd04278:

Pssm-ID: 469599 [Multi-domain]  Cd Length: 157  Bit Score: 136.57  E-value: 1.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 126 QGGALAHAFLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVL 202
Cdd:cd04278   71 PGGTLAHAFFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIR 150


                 ....*..
gi 767995851 203 AVQSLYG 209
Cdd:cd04278  151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 246-435 2.46e-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: 121.26  E-value: 2.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 246 PKYCHS-SFDAITVDRQQqLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGP 324
Cdd:cd00094    1 PDACDPlSFDAVTTLRGE-LYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 325 KPVWGLPQLCRAGGLPRHP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRP 398
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWL 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767995851 399 DGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 435
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 2.51e-07

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 47.12  E-value: 2.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851   31 ELRKEAEAFLEKYGYLNEqvpkaPTSTRFS----DAIRAFQWVSQLPVSGVLDRATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFGpsteAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 126-209 1.59e-38

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: 136.57  E-value: 1.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 126 QGGALAHAFLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVL 202
Cdd:cd04278   71 PGGTLAHAFFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIR 150


                 ....*..
gi 767995851 203 AVQSLYG 209
Cdd:cd04278  151 GIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 127-209 9.76e-34

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: 123.88  E-value: 9.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851  127 GGALAHAFLP---RRGEAHFDQDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDAL-LSWDD 200
Cdd:pfam00413  71 GGVLAHAFFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDD 150


                  ....*....
gi 767995851  201 VLAVQSLYG 209
Cdd:pfam00413 151 IKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 246-435 2.46e-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: 121.26  E-value: 2.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 246 PKYCHS-SFDAITVDRQQqLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGP 324
Cdd:cd00094    1 PDACDPlSFDAVTTLRGE-LYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 325 KPVWGLPQLCRAGGLPRHP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRP 398
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWL 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767995851 399 DGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 435
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 122-210 7.81e-12

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: 62.75  E-value: 7.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851   122 RFAK--QGGALAHAFLPRrGEAHFDqDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKRLGRDAL- 195
Cdd:smart00235  54 SFGSgdSGCTLSHAGRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFd 124

                           90
                   ....*....|....*
gi 767995851   196 LSWDDVLAVQSLYGK 210
Cdd:smart00235 125 LSEDDSLGIPYDYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 2.51e-07

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 47.12  E-value: 2.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851   31 ELRKEAEAFLEKYGYLNEqvpkaPTSTRFS----DAIRAFQWVSQLPVSGVLDRATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFGpsteAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
63-185 1.62e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 45.33  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851  63 IRAFQW-VSQLPVSGVLDRatLRQMTRPRC----GVTDtnsyaawaeriSDLFARHRTkmrrkkrF----AKQGGALAHA 133
Cdd:COG1913   41 LEAYDPeRGQYDAEALLDF--LSRLKEEDGdkvlGVTD-----------VDLYAPGLN-------FvfglAYLGGRVAVV 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767995851 134 FLPRRGEAHFDQDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 185
Cdd:COG1913  101 STARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-435 1.86e-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: 38.76  E-value: 1.86e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767995851   391 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 435
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-333 3.43e-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: 3.43e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 767995851  301 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 333
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKL 35
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
165-183 2.56e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 2.56e-03
                         10
                 ....*....|....*....
gi 767995851 165 HEIGHTLGLTHSPAPRALM 183
Cdd:NF033823 128 HELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 165-183 1.00e-02

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.92  E-value: 1.00e-02
                         10
                 ....*....|....*....
gi 767995851 165 HEIGHTLGLTHSPAPRALM 183
Cdd:PRK13267 131 HELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 126-209 1.59e-38

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: 136.57  E-value: 1.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 126 QGGALAHAFLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVL 202
Cdd:cd04278   71 PGGTLAHAFFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIR 150


                 ....*..
gi 767995851 203 AVQSLYG 209
Cdd:cd04278  151 GIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 127-209 9.76e-34

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: 123.88  E-value: 9.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851  127 GGALAHAFLP---RRGEAHFDQDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDAL-LSWDD 200
Cdd:pfam00413  71 GGVLAHAFFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDD 150


                  ....*....
gi 767995851  201 VLAVQSLYG 209
Cdd:pfam00413 151 IKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 246-435 2.46e-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: 121.26  E-value: 2.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 246 PKYCHS-SFDAITVDRQQqLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGP 324
Cdd:cd00094    1 PDACDPlSFDAVTTLRGE-LYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 325 KPVWGLPQLCRAGGLPRHP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRP 398
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWL 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767995851 399 DGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 435
Cdd:cd00094  158 DGYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 122-210 7.81e-12

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: 62.75  E-value: 7.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851   122 RFAK--QGGALAHAFLPRrGEAHFDqDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKRLGRDAL- 195
Cdd:smart00235  54 SFGSgdSGCTLSHAGRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFd 124

                           90
                   ....*....|....*
gi 767995851   196 LSWDDVLAVQSLYGK 210
Cdd:smart00235 125 LSEDDSLGIPYDYGS 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 2.51e-07

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 47.12  E-value: 2.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851   31 ELRKEAEAFLEKYGYLNEqvpkaPTSTRFS----DAIRAFQWVSQLPVSGVLDRATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFGpsteAAVKAFQRAFGLPVDGIVDPETLAAL 57
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 23-185 2.63e-06

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: 47.29  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851  23 QPAERGGQELRKEAEAFLEKYGYLNEQVPKAPtstrFSDAIRAFQWV-SQLPVSGVLDraTLRQMTRPR----CGVTDTN 97
Cdd:cd11375    5 VPIGSVDPDLLDELKERLSAFFGLPVEVLPSI----PVPPLEAYNPSrGQYLADDILD--ALLKLKPPDadcvLGVTDVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851  98 SYaawaerISDL---FARHRTKMRRkkrfakqgGALAHAflprRGEAHFDQDERW-SLSRRRgrnLFVVLAHEIGHTLGL 173
Cdd:cd11375   79 LY------EPGLnfvFGLADGGSGV--------AVVSTA----RLRPEFYGLPPDeGLFLER---LLKEAVHELGHLFGL 137

                        170
                 ....*....|..
gi 767995851 174 THSPAPRALMAP 185
Cdd:cd11375  138 DHCPYYACVMNF 149
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 121-208 2.91e-06

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: 47.13  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 121 KRFAKQGGALAHAFLPR-----RGEAHFDQDERWslsrrrGRNLFVVLAHEIGHTLGLTHSP------------------ 177
Cdd:cd00203   59 TRQDFDGGTGGWAYLGRvcdslRGVGVLQDNQSG------TKEGAQTIAHELGHALGFYHDHdrkdrddyptiddtlnae 132

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767995851 178 --APRALMAPYYKR--LGRDALLSWDDVLAVQSLY 208
Cdd:cd00203  133 ddDYYSVMSYTKGSfsDGQRKDFSQCDIDQINKLY 167
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
63-185 1.62e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 45.33  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851  63 IRAFQW-VSQLPVSGVLDRatLRQMTRPRC----GVTDtnsyaawaeriSDLFARHRTkmrrkkrF----AKQGGALAHA 133
Cdd:COG1913   41 LEAYDPeRGQYDAEALLDF--LSRLKEEDGdkvlGVTD-----------VDLYAPGLN-------FvfglAYLGGRVAVV 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767995851 134 FLPRRGEAHFDQDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 185
Cdd:COG1913  101 STARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 150-209 6.51e-05

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: 43.21  E-value: 6.51e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995851 150 SLSRRRGRNLFVVLAHEIGHTLGLTH-SPAPRALMAPYYKRLG-RDALLSWDDVLAVQSLYG 209
Cdd:cd04279   95 PGQPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPdGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 126-209 7.25e-05

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: 43.56  E-value: 7.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 126 QGGALAHAFLP-------RRGEAHFDQDERWSLSRRRGRNLFVVLaHEIGHTLGLTHS-------PAPRA---------L 182
Cdd:cd04277   74 DGNTAGYAYYPgsgsgtaYGGDIWFNSSYDTNSDSPGSYGYQTII-HEIGHALGLEHPgdynggdPVPPTyaldsreytV 152

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767995851 183 MA----PYYKRLGRDALLSW---DDVLAVQSLYG 209
Cdd:cd04277  153 MSynsgYGNGASAGGGYPQTpmlLDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-435 1.86e-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: 38.76  E-value: 1.86e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767995851   391 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 435
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 253-296 2.31e-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: 38.76  E-value: 2.31e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767995851   253 FDAITVDRQQQLYIFKGSHFWEV-AADGNVSEPRPLQERWVGLPP 296
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFdPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-333 3.43e-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: 3.43e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 767995851  301 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 333
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKL 35
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 136-232 6.33e-04

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: 40.17  E-value: 6.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995851 136 PRRGEAHFDQDERWS----LSRRRGRNlfvVLAHEIGHTLGLTHSPApRALMAPYYkrlgrDALLSWDDVLAVQSlygkP 211
Cdd:cd04268   70 PLTGEILLARVYLYSsfveYSGARLRN---TAEHELGHALGLRHNFA-ASDRDDNV-----DLLAEKGDTSSVMD----Y 136

                         90       100
                 ....*....|....*....|.
gi 767995851 212 LGGSVAVQLPGKLFTDFETWD 232
Cdd:cd04268  137 APSNFSIQLGDGQKYTIGPYD 157
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 301-333 7.84e-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: 37.22  E-value: 7.84e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767995851   301 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 333
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKL 35
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 127-175 1.47e-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: 39.62  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995851 127 GGALAHAFL-PRRGE---------AHF---DQDERWSLSRRRGRNLfvvLAHEIGHTLGLTH 175
Cdd:cd04276   74 GWAYGPSVVdPRTGEilkadvilySGFlrqDQLWYEDLLAASLRYL---LAHEVGHTLGLRH 132
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
165-183 2.56e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 2.56e-03
                         10
                 ....*....|....*....
gi 767995851 165 HEIGHTLGLTHSPAPRALM 183
Cdd:NF033823 128 HELGHLLGLGHCPNPRCVM 146
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 253-296 3.47e-03

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 35.23  E-value: 3.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 767995851  253 FDAITVDRQQQLYIFKGSHFWEVaaDGNVSE---PRPLQErWVGLPP 296
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRF--DPQRVEpgyPKLISD-FPGLPC 44
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 162-175 4.97e-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: 4.97e-03
                          10
                  ....*....|....
gi 767995851  162 VLAHEIGHTLGLTH 175
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-435 6.52e-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: 6.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767995851  391 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSgRWATELPWMGC 435
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYP-KLISDFPGLPC 44
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 165-183 1.00e-02

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.92  E-value: 1.00e-02
                         10
                 ....*....|....*....
gi 767995851 165 HEIGHTLGLTHSPAPRALM 183
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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