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Conserved domains on  [gi|1034601225|ref|XP_016880553|]
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matrix metalloproteinase-28 isoform X6 [Homo sapiens]

Protein Classification

PG_binding_1 and ZnMc_MMP domain-containing protein( domain architecture ID 10477963)

PG_binding_1 and ZnMc_MMP 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 ...
 129-284 4.62e-76

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: 232.09  E-value: 4.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 208
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601225 209 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYG 284
Cdd:cd04278    79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 1.33e-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: 47.90  E-value: 1.33e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225  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 ...
 129-284 4.62e-76

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: 232.09  E-value: 4.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 208
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601225 209 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYG 284
Cdd:cd04278    79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 129-284 3.33e-68

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: 212.09  E-value: 3.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLgnAFDGPGGALAHA 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGY--PFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 209 FLP---RRGEAHFDQDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDAL-LSWDDVLAVQSL 282
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  ..
gi 1034601225 283 YG 284
Cdd:pfam00413 158 YG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 129-285 1.75e-24

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: 97.42  E-value: 1.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225  129 KWYKQHLSYRLVNWPEhlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglgnafdgpGGALAHA 208
Cdd:smart00235   4 KWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225  209 FLPRrGEAHFDqDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKRLGRDAL-LSWDDVLAVQSLYG 284
Cdd:smart00235  68 GRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPYDYG 138


                   .
gi 1034601225  285 K 285
Cdd:smart00235 139 S 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 1.33e-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: 47.90  E-value: 1.33e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225  31 ELRKEAEAFLEKYGYLNEqvpkaPTSTRFS----DAIRAFQWVSQLPVSGVLDRATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFGpsteAAVKAFQRAFGLPVDGIVDPETLAAL 57
Zn_serralysin NF035945
serralysin family metalloprotease;
158-284 1.30e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 46.89  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 158 AFQLWSNVSALEFWEAPATGPADIrlTFfqgdhndglGNaFDGpgGALAHAFLPRRGEAhfdQDERWSLSRRR------- 230
Cdd:NF035945   88 SLQSWSDVANITFTEVSAGQKANI--TF---------GN-YSD--SGQAYAYLPGTSDV---SGQSWYNYNSDyirnltp 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 231 -----GRNLFvvlAHEIGHTLGLTHsPA--------PRALMAPY-----------Y---KRLGRD--------ALLswDD 275
Cdd:NF035945  151 dlgnyGRQTL---THEIGHTLGLSH-PGdynagegnPTYKDATYaedtrqysvmsYwseSNTGQDfkghyasaPLL--DD 224


                  ....*....
gi 1034601225 276 VLAVQSLYG 284
Cdd:NF035945  225 IAAIQKLYG 233
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
201-260 5.58e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 43.41  E-value: 5.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 201 PGGALAHAFLPRRGEAHFDQDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:COG1913    93 LGGRVAVVSTARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
240-258 2.08e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 2.08e-03
                          10
                  ....*....|....*....
gi 1034601225 240 HEIGHTLGLTHSPAPRALM 258
Cdd:NF033823  128 HELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 240-258 8.11e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.92  E-value: 8.11e-03
                          10
                  ....*....|....*....
gi 1034601225 240 HEIGHTLGLTHSPAPRALM 258
Cdd:PRK13267  131 HELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 129-284 4.62e-76

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: 232.09  E-value: 4.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 208
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601225 209 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYG 284
Cdd:cd04278    79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALYG 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 129-284 3.33e-68

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: 212.09  E-value: 3.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLgnAFDGPGGALAHA 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGY--PFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 209 FLP---RRGEAHFDQDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDAL-LSWDDVLAVQSL 282
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  ..
gi 1034601225 283 YG 284
Cdd:pfam00413 158 YG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 129-285 1.75e-24

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: 97.42  E-value: 1.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225  129 KWYKQHLSYRLVNWPEhlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglgnafdgpGGALAHA 208
Cdd:smart00235   4 KWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225  209 FLPRrGEAHFDqDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKRLGRDAL-LSWDDVLAVQSLYG 284
Cdd:smart00235  68 GRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPYDYG 138


                   .
gi 1034601225  285 K 285
Cdd:smart00235 139 S 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 154-284 1.72e-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: 71.29  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 154 AVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFDGPGGAlahaFLPRRGEAHFDQDERWSLSRRRGRN 233
Cdd:cd04277    38 AARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAYYPGSGS----GTAYGGDIWFNSSYDTNSDSPGSYG 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034601225 234 LFVVLaHEIGHTLGLTHS-------PAPRA---------LMA----PYYKRLGRDALLSW---DDVLAVQSLYG 284
Cdd:cd04277   114 YQTII-HEIGHALGLEHPgdynggdPVPPTyaldsreytVMSynsgYGNGASAGGGYPQTpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 149-307 3.16e-12

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: 64.05  E-value: 3.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 149 PAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFdGPGGALahaflPRRGEAHFDQDERWS--- 225
Cdd:cd04268    14 DKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSY-GPSQVD-----PLTGEILLARVYLYSsfv 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 226 -LSRRRGRNlfvVLAHEIGHTLGLTHSPApRALMAPYYkrlgrDALLSWDDVLAVQSlygkPLGGSVAVQLPGKLFTDFE 304
Cdd:cd04268    88 eYSGARLRN---TAEHELGHALGLRHNFA-ASDRDDNV-----DLLAEKGDTSSVMD----YAPSNFSIQLGDGQKYTIG 154


                  ...
gi 1034601225 305 TWD 307
Cdd:cd04268   155 PYD 157
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 150-283 3.34e-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: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 150 AVRGAVRAAFQLWSNVSALEFWEAPAT-GPADIRLTFFQGDHNdglgnafdgpGGALAHAFLPR-----RGEAHFDQDER 223
Cdd:cd00203    22 QIQSLILIAMQIWRDYLNIRFVLVGVEiDKADIAILVTRQDFD----------GGTGGWAYLGRvcdslRGVGVLQDNQS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 224 WslsrrrGRNLFVVLAHEIGHTLGLTHSP--------------------APRALMAPYYKR--LGRDALLSWDDVLAVQS 281
Cdd:cd00203    92 G------TKEGAQTIAHELGHALGFYHDHdrkdrddyptiddtlnaeddDYYSVMSYTKGSfsDGQRKDFSQCDIDQINK 165


                  ..
gi 1034601225 282 LY 283
Cdd:cd00203   166 LY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 141-284 3.14e-09

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: 55.16  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 141 NWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGP-ADIRLtFFQGDHNDGLGnafdgpGGALAHAFLPrrgeahFD 219
Cdd:cd04279    12 PAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDNdADIVI-FFDRPPPVGGA------GGGLARAGFP------LI 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601225 220 QDERWSLS-----------RRRGRNLFVVLAHEIGHTLGLTH-SPAPRALMAPYYKRLG-RDALLSWDDVLAVQSLYG 284
Cdd:cd04279    79 SDGNRKLFnrtdinlgpgqPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPdGNPTLSARDVATLKRLYG 156
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 1.33e-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: 47.90  E-value: 1.33e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225  31 ELRKEAEAFLEKYGYLNEqvpkaPTSTRFS----DAIRAFQWVSQLPVSGVLDRATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFGpsteAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 147-250 1.84e-06

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: 48.09  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 147 PEPaVRGAVRAAFQLW---------SNVSALEFWEAPATgPADIRLTFFQGDHNDGLGNAFdgpGGALAHaflPRRGE-- 215
Cdd:cd04276    19 PEK-YRDAIREGVLYWnkafekagfKNAIIVKVLPDDAD-PGDIRYNVIRWIHSPNGGWAY---GPSVVD---PRTGEil 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034601225 216 -------AHF---DQDERWSLSRRRGRNLfvvLAHEIGHTLGLTH 250
Cdd:cd04276    91 kadvilySGFlrqDQLWYEDLLAASLRYL---LAHEVGHTLGLRH 132
Zn_serralysin NF035945
serralysin family metalloprotease;
158-284 1.30e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 46.89  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 158 AFQLWSNVSALEFWEAPATGPADIrlTFfqgdhndglGNaFDGpgGALAHAFLPRRGEAhfdQDERWSLSRRR------- 230
Cdd:NF035945   88 SLQSWSDVANITFTEVSAGQKANI--TF---------GN-YSD--SGQAYAYLPGTSDV---SGQSWYNYNSDyirnltp 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 231 -----GRNLFvvlAHEIGHTLGLTHsPA--------PRALMAPY-----------Y---KRLGRD--------ALLswDD 275
Cdd:NF035945  151 dlgnyGRQTL---THEIGHTLGLSH-PGdynagegnPTYKDATYaedtrqysvmsYwseSNTGQDfkghyasaPLL--DD 224


                  ....*....
gi 1034601225 276 VLAVQSLYG 284
Cdd:NF035945  225 IAAIQKLYG 233
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
201-260 5.58e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 43.41  E-value: 5.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 201 PGGALAHAFLPRRGEAHFDQDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:COG1913    93 LGGRVAVVSTARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 225-260 1.38e-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: 39.20  E-value: 1.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1034601225 225 SLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:cd11375   117 GLFLER---LLKEAVHELGHLFGLDHCPYYACVMNF 149
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 147-253 1.46e-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: 39.29  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601225 147 PEPAVRGAVRAAFQLWSNVSALEFWEApATGPADIRLTFFQGDHN------DGLGNAFDGPGGALAhaflprrgeahfdq 220
Cdd:cd04327    17 PDAFLKDKVRAAAREWLPYANLKFKFV-TDADADIRISFTPGDGYwsyvgtDALLIGADAPTMNLG-------------- 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034601225 221 derWSLSRRRGRNLFVVLAHEIGHTLGLTH---SPA 253
Cdd:cd04327    82 ---WFTDDTPDPEFSRVVLHEFGHALGFIHehqSPA 114
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
240-258 2.08e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 2.08e-03
                          10
                  ....*....|....*....
gi 1034601225 240 HEIGHTLGLTHSPAPRALM 258
Cdd:NF033823  128 HELGHLLGLGHCPNPRCVM 146
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 237-250 2.90e-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: 39.16  E-value: 2.90e-03
                          10
                  ....*....|....
gi 1034601225 237 VLAHEIGHTLGLTH 250
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
188-253 5.42e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 37.78  E-value: 5.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034601225 188 GDHNDGLGNAF---DGPGGALAHAF-LPRRGEAHF-DQDERWSLSRRRGRNLFVVLAHEIGHTLGLTHSPA 253
Cdd:pfam13688  86 GTQNDDLAYLFlmtNCSGGGLAWLGqLCNSGSAGSvSTRVSGNNVVVSTATEWQVFAHEIGHNFGAVHDCD 156
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 240-258 8.11e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 36.92  E-value: 8.11e-03
                          10
                  ....*....|....*....
gi 1034601225 240 HEIGHTLGLTHSPAPRALM 258
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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