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Conserved domains on  [gi|1034601215|ref|XP_011523534|]
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matrix metalloproteinase-28 isoform X1 [Homo sapiens]

Protein Classification

PG_binding_1 and ZnMc_MMP domain-containing protein( domain architecture ID 10477998)

protein containing domains PG_binding_1, ZnMc_MMP, and HX

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 ...
 129-283 5.53e-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: 227.86  E-value: 5.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 208
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601215 209 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLY 283
Cdd:cd04278    79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156
HX super family cl02471
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 311-484 2.83e-27

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.


The actual alignment was detected with superfamily member cd00094:

Pssm-ID: 413329 [Multi-domain]  Cd Length: 194  Bit Score: 108.17  E-value: 2.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 311 QQLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQLCRAGGLPR 390
Cdd:cd00094    17 GELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGYPKPISDLGFPP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 391 HP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRPDGSIIFFRDDRYWRLDQ 464
Cdd:cd00094    97 TVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWLDGYYYFFKGDQYWRFDP 174

                         170       180
                  ....*....|....*....|
gi 1034601215 465 AKLQATTSGRWATELPWMGC 484
Cdd:cd00094   175 RSKEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 2.49e-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: 47.51  E-value: 2.49e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215  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 ...
 129-283 5.53e-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: 227.86  E-value: 5.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 208
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601215 209 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLY 283
Cdd:cd04278    79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 129-283 2.80e-65

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: 207.85  E-value: 2.80e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLgnAFDGPGGALAHA 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGY--PFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 209 FLP---RRGEAHFDQDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDAL-LSWDDVLAVQSL 282
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  .
gi 1034601215 283 Y 283
Cdd:pfam00413 158 Y 158
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 311-484 2.83e-27

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: 108.17  E-value: 2.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 311 QQLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQLCRAGGLPR 390
Cdd:cd00094    17 GELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGYPKPISDLGFPP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 391 HP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRPDGSIIFFRDDRYWRLDQ 464
Cdd:cd00094    97 TVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWLDGYYYFFKGDQYWRFDP 174

                         170       180
                  ....*....|....*....|
gi 1034601215 465 AKLQATTSGRWATELPWMGC 484
Cdd:cd00094   175 RSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 129-285 2.55e-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: 95.50  E-value: 2.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215  129 KWYKQHLSYRLVNWPEhlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglgnafdgpGGALAHA 208
Cdd:smart00235   4 KWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215  209 FLPRrGEAHFDqDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKRLGRDAL-LSWDDVLAVQSLYV 284
Cdd:smart00235  68 GRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPYDYG 138


                   .
gi 1034601215  285 S 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 2.49e-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: 47.51  E-value: 2.49e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215  31 ELRKEAEAFLEKYGYLNEqvpkaPTSTRFS----DAIRAFQWVSQLPVSGVLDRATLRQM 86
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPG-----PVDGYFGpsteAAVKAFQRAFGLPVDGIVDPETLAAL 57
Zn_serralysin NF035945
serralysin family metalloprotease;
158-250 4.26e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 45.73  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 158 AFQLWSNVSALEFWEAPATGPADIrlTFfqgdhndglGNaFDGpgGALAHAFLPRRGEAhfdQDERWSLSRRR------- 230
Cdd:NF035945   88 SLQSWSDVANITFTEVSAGQKANI--TF---------GN-YSD--SGQAYAYLPGTSDV---SGQSWYNYNSDyirnltp 150

                          90       100
                  ....*....|....*....|....*
gi 1034601215 231 -----GRNLFvvlAHEIGHTLGLTH 250
Cdd:NF035945  151 dlgnyGRQTL---THEIGHTLGLSH 172
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
201-260 9.24e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 43.02  E-value: 9.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 201 PGGALAHAFLPRRGEAHFDQDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:COG1913    93 LGGRVAVVSTARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 440-484 2.09e-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: 2.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034601215  440 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 484
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-382 3.73e-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: 3.73e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034601215 350 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 382
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKL 35
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
240-258 2.92e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 2.92e-03
                          10
                  ....*....|....*....
gi 1034601215 240 HEIGHTLGLTHSPAPRALM 258
Cdd:NF033823  128 HELGHLLGLGHCPNPRCVM 146
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 129-283 5.53e-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: 227.86  E-value: 5.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGlgNAFDGPGGALAHA 208
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQEADIRISFARGNHGDG--YPFDGPGGTLAHA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601215 209 FLP--RRGEAHFDQDERWSL-SRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLY 283
Cdd:cd04278    79 FFPggIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 129-283 2.80e-65

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: 207.85  E-value: 2.80e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 129 KWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPaTGPADIRLTFFQGDHNDGLgnAFDGPGGALAHA 208
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVS-TGEADIMIGFGRGDHGDGY--PFDGPGGVLAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 209 FLP---RRGEAHFDQDERWSLS--RRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDAL-LSWDDVLAVQSL 282
Cdd:pfam00413  78 FFPgpgLGGDIHFDDDETWTVGsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFrLSQDDIKGIQQL 157


                  .
gi 1034601215 283 Y 283
Cdd:pfam00413 158 Y 158
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 311-484 2.83e-27

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: 108.17  E-value: 2.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 311 QQLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQLCRAGGLPR 390
Cdd:cd00094    17 GELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGYPKPISDLGFPP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 391 HP---DAALFFPPLRRLILFKG---ARYYVLARggLQVEPYYPRSLQDWGGIPEEVSGALPRPDGSIIFFRDDRYWRLDQ 464
Cdd:cd00094    97 TVkqiDAALRWPDNGKTYFFKGdkyWRYDEKTQ--KMDPGYPKLIETDFPGVPDKVDAAFRWLDGYYYFFKGDQYWRFDP 174

                         170       180
                  ....*....|....*....|
gi 1034601215 465 AKLQATTSGRWATELPWMGC 484
Cdd:cd00094   175 RSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 129-285 2.55e-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: 95.50  E-value: 2.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215  129 KWYKQHLSYRLVNWPEhlpEPAVRGAVRAAFQLWSNVSALEFweAPATGPADIRLTFFQGDHndglgnafdgpGGALAHA 208
Cdd:smart00235   4 KWPKGTVPYVIDSSSL---SPEEREAIAKALAEWSDVTCIRF--VERTGTADIYISFGSGDS-----------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215  209 FLPRrGEAHFDqDERWSLSrrrgrnlFVVLAHEIGHTLGLTHSPAPRA---LMAPYYKRLGRDAL-LSWDDVLAVQSLYV 284
Cdd:smart00235  68 GRPG-GDQHLS-LGNGCIN-------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFdLSEDDSLGIPYDYG 138


                   .
gi 1034601215  285 S 285
Cdd:smart00235 139 S 139
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 351-483 8.44e-18

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: 81.59  E-value: 8.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 351 AVSLNDGDFYFFKGGRCWRFRGPKPVWGlPQLCRA--GGLPRHPDAALFFPPLRRLILFKGARYYVLArgGLQVEPYYPR 428
Cdd:cd00094    11 AVTTLRGELYFFKGRYFWRLSPGKPPGS-PFLISSfwPSLPSPVDAAFERPDTGKIYFFKGDKYWVYT--GKNLEPGYPK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 429 SLQDWGGIPEE--VSGALPRPD-GSIIFFRDDRYWRLD--QAKLQATTSGRWATELPWMG 483
Cdd:cd00094    88 PISDLGFPPTVkqIDAALRWPDnGKTYFFKGDKYWRYDekTQKMDPGYPKLIETDFPGVP 147
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 154-283 2.93e-13

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 68.21  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 154 AVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFDGPGGAlahaFLPRRGEAHFDQDERWSLSRRRGRN 233
Cdd:cd04277    38 AARDALEAWEDVADIDFVEVSDNSGADIRFGNSSDPDGNTAGYAYYPGSGS----GTAYGGDIWFNSSYDTNSDSPGSYG 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034601215 234 LFVVLaHEIGHTLGLTHS-------PAPRA---------LMA----PYYKRLGRDALLSW---DDVLAVQSLY 283
Cdd:cd04277   114 YQTII-HEIGHALGLEHPgdynggdPVPPTyaldsreytVMSynsgYGNGASAGGGYPQTpmlLDIAALQYLY 185
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 149-253 1.08e-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: 63.28  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 149 PAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFdGPGGALahaflPRRGEAHFDQDERWS--- 225
Cdd:cd04268    14 DKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIPYNDGTWSY-GPSQVD-----PLTGEILLARVYLYSsfv 87

                          90       100
                  ....*....|....*....|....*....
gi 1034601215 226 -LSRRRGRNlfvVLAHEIGHTLGLTHSPA 253
Cdd:cd04268    88 eYSGARLRN---TAEHELGHALGLRHNFA 113
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 150-283 4.85e-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: 4.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 150 AVRGAVRAAFQLWSNVSALEFWEAPAT-GPADIRLTFFQGDHNdglgnafdgpGGALAHAFLPR-----RGEAHFDQDER 223
Cdd:cd00203    22 QIQSLILIAMQIWRDYLNIRFVLVGVEiDKADIAILVTRQDFD----------GGTGGWAYLGRvcdslRGVGVLQDNQS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 224 WslsrrrGRNLFVVLAHEIGHTLGLTHSP--------------------APRALMAPYYKR--LGRDALLSWDDVLAVQS 281
Cdd:cd00203    92 G------TKEGAQTIAHELGHALGFYHDHdrkdrddyptiddtlnaeddDYYSVMSYTKGSfsDGQRKDFSQCDIDQINK 165


                  ..
gi 1034601215 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 ...
 141-283 3.41e-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: 52.84  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 141 NWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGP-ADIRLtFFQGDHNDGLGnafdgpGGALAHAFLPrrgeahFD 219
Cdd:cd04279    12 PAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNPEEDNdADIVI-FFDRPPPVGGA------GGGLARAGFP------LI 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034601215 220 QDERWSLS-----------RRRGRNLFVVLAHEIGHTLGLTH-SPAPRALMAPYYKRLG-RDALLSWDDVLAVQSLY 283
Cdd:cd04279    79 SDGNRKLFnrtdinlgpgqPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPdGNPTLSARDVATLKRLY 155
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 2.49e-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: 47.51  E-value: 2.49e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215  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 9.11e-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: 46.55  E-value: 9.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 147 PEPaVRGAVRAAFQLW---------SNVSALEFWEAPATgPADIRLTFFQGDHNDGLGNAFdgpGGALAHaflPRRGE-- 215
Cdd:cd04276    19 PEK-YRDAIREGVLYWnkafekagfKNAIIVKVLPDDAD-PGDIRYNVIRWIHSPNGGWAY---GPSVVD---PRTGEil 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034601215 216 -------AHF---DQDERWSLSRRRGRNLfvvLAHEIGHTLGLTH 250
Cdd:cd04276    91 kadvilySGFlrqDQLWYEDLLAASLRYL---LAHEVGHTLGLRH 132
Zn_serralysin NF035945
serralysin family metalloprotease;
158-250 4.26e-05

serralysin family metalloprotease;


Pssm-ID: 468274 [Multi-domain]  Cd Length: 457  Bit Score: 45.73  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 158 AFQLWSNVSALEFWEAPATGPADIrlTFfqgdhndglGNaFDGpgGALAHAFLPRRGEAhfdQDERWSLSRRR------- 230
Cdd:NF035945   88 SLQSWSDVANITFTEVSAGQKANI--TF---------GN-YSD--SGQAYAYLPGTSDV---SGQSWYNYNSDyirnltp 150

                          90       100
                  ....*....|....*....|....*
gi 1034601215 231 -----GRNLFvvlAHEIGHTLGLTH 250
Cdd:NF035945  151 dlgnyGRQTL---THEIGHTLGLSH 172
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
201-260 9.24e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 43.02  E-value: 9.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 201 PGGALAHAFLPRRGEAHFDQDERWSLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:COG1913    93 LGGRVAVVSTARLRPEFYGLPPDEELFLER---VLKEAVHELGHLFGLGHCPNPRCVMHF 149
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 440-484 2.09e-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: 2.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034601215  440 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGC 484
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-382 3.73e-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: 3.73e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034601215 350 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 382
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKL 35
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-382 8.71e-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: 8.71e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034601215  350 AAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQL 382
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKL 35
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 225-260 2.08e-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: 2.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1034601215 225 SLSRRRgrnLFVVLAHEIGHTLGLTHSPAPRALMAP 260
Cdd:cd11375   117 GLFLER---LLKEAVHELGHLFGLDHCPYYACVMNF 149
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
240-258 2.92e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 38.75  E-value: 2.92e-03
                          10
                  ....*....|....*....
gi 1034601215 240 HEIGHTLGLTHSPAPRALM 258
Cdd:NF033823  128 HELGHLLGLGHCPNPRCVM 146
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 147-253 3.61e-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: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601215 147 PEPAVRGAVRAAFQLWSNVSALEFWEApATGPADIRLTFFQGDHN------DGLGNAFDGPGGALAhaflprrgeahfdq 220
Cdd:cd04327    17 PDAFLKDKVRAAAREWLPYANLKFKFV-TDADADIRISFTPGDGYwsyvgtDALLIGADAPTMNLG-------------- 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034601215 221 derWSLSRRRGRNLFVVLAHEIGHTLGLTH---SPA 253
Cdd:cd04327    82 ---WFTDDTPDPEFSRVVLHEFGHALGFIHehqSPA 114
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 237-250 6.32e-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: 6.32e-03
                          10
                  ....*....|....
gi 1034601215 237 VLAHEIGHTLGLTH 250
Cdd:pfam16313  16 VSAHEVGHTLGLRH 29
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 440-484 7.10e-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: 7.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034601215 440 VSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSgRWATELPWMGC 484
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYP-KLISDFPGLPC 44
 
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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