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Conserved domains on  [gi|1149122726|ref|NP_999404|]
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matrix metalloproteinase-14 precursor [Sus scrofa]

Protein Classification

ZnMc_MMP and HX domain-containing protein( domain architecture ID 12021149)

protein containing domains PG_binding_1, ZnMc_MMP, HX, and DUF3377

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 116-282 1.17e-89

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: 273.34  E-value: 1.17e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 116 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyireghekQADIMIFFAEGFHGDSTPFDGEGG 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 196 FLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRR 275
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 1149122726 276 GIQQLYG 282
Cdd:pfam00413 153 GIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 314-506 5.68e-77

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: 241.83  E-value: 5.68e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 314 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRkNQVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 391
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLS-PGKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 392 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 470
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1149122726 471 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 506
Cdd:cd00094   160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 super family cl13321
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 558-580 5.39e-09

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


The actual alignment was detected with superfamily member pfam11857:

Pssm-ID: 463374  Cd Length: 72  Bit Score: 52.71  E-value: 5.39e-09
                          10        20
                  ....*....|....*....|...
gi 1149122726 558 FFFRRHGTPKRLLYCQRSLLDKV 580
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-86 6.12e-09

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: 52.13  E-value: 6.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1149122726  34 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQRFYGLRVTGKADADTMKAM 86
Cdd:pfam01471   9 QRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 116-282 1.17e-89

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: 273.34  E-value: 1.17e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 116 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyireghekQADIMIFFAEGFHGDSTPFDGEGG 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 196 FLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRR 275
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 1149122726 276 GIQQLYG 282
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 116-282 5.13e-81

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: 250.97  E-value: 5.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 116 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyiregheKQADIMIFFAEGFHGDSTPFDGEGG 195
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-------QEADIRISFARGNHGDGYPFDGPGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 196 FLAHAYFPGPnIGGDTHFDSAEPWTVRNEDlNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTeNFVLPDDDRR 275
Cdd:cd04278    74 TLAHAFFPGG-IGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                  ....*..
gi 1149122726 276 GIQQLYG 282
Cdd:cd04278   151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 314-506 5.68e-77

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: 241.83  E-value: 5.68e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 314 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRkNQVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 391
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLS-PGKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 392 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 470
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1149122726 471 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 506
Cdd:cd00094   160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 115-283 5.88e-35

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: 128.62  E-value: 5.88e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726  115 LKWQHNEITFCIqnYTPKVGEYATfEAIRKAFRVWESATPLRFREVPYAyireghekqADIMIFFAEGFHGdstpfdgeg 194
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEER-EAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726  195 GFLAHAYFPGpnigGDTHFDsAEPWTVRnedlngndiFLVAVHELGHALGLEHSNDPSA---IMAPFYQWMDTENFVLPD 271
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|..
gi 1149122726  272 DDRRGIQQLYGS 283
Cdd:smart00235 128 DDSLGIPYDYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 366-409 3.74e-10

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: 55.33  E-value: 3.74e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1149122726  366 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLP 409
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 366-409 8.26e-10

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: 54.11  E-value: 8.26e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1149122726 366 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELgRGLP 409
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 558-580 5.39e-09

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


Pssm-ID: 463374  Cd Length: 72  Bit Score: 52.71  E-value: 5.39e-09
                          10        20
                  ....*....|....*....|...
gi 1149122726 558 FFFRRHGTPKRLLYCQRSLLDKV 580
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-86 6.12e-09

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: 52.13  E-value: 6.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1149122726  34 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQRFYGLRVTGKADADTMKAM 86
Cdd:pfam01471   9 QRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
235-255 1.79e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.61  E-value: 1.79e-04
                          10        20
                  ....*....|....*....|.
gi 1149122726 235 AVHELGHALGLEHSNDPSAIM 255
Cdd:NF033823  126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
234-257 5.00e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 5.00e-04
                          10        20
                  ....*....|....*....|....
gi 1149122726 234 VAVHELGHALGLEHSNDPSAIMAP 257
Cdd:COG1913   126 EAVHELGHLFGLGHCPNPRCVMHF 149
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 35-88 5.44e-04

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 38.74  E-value: 5.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149122726  35 AWLQQYGYLPP---GDLRTHTQrspqslsAAIAAMQRFYGLRVTGKADADTMKAMRR 88
Cdd:COG3409    20 QRLNALGYYPGpvdGIFGPATE-------AAVRAFQRANGLPVDGIVGPATWAALRA 69
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 235-255 2.03e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.62  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|.
gi 1149122726 235 AVHELGHALGLEHSNDPSAIM 255
Cdd:PRK13267  129 VTHELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 116-282 1.17e-89

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: 273.34  E-value: 1.17e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 116 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyireghekQADIMIFFAEGFHGDSTPFDGEGG 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 196 FLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRR 275
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 1149122726 276 GIQQLYG 282
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 116-282 5.13e-81

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: 250.97  E-value: 5.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 116 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyiregheKQADIMIFFAEGFHGDSTPFDGEGG 195
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-------QEADIRISFARGNHGDGYPFDGPGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 196 FLAHAYFPGPnIGGDTHFDSAEPWTVRNEDlNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTeNFVLPDDDRR 275
Cdd:cd04278    74 TLAHAFFPGG-IGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                  ....*..
gi 1149122726 276 GIQQLYG 282
Cdd:cd04278   151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 314-506 5.68e-77

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: 241.83  E-value: 5.68e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 314 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRkNQVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 391
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLS-PGKPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 392 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 470
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1149122726 471 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 506
Cdd:cd00094   160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 115-283 5.88e-35

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: 128.62  E-value: 5.88e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726  115 LKWQHNEITFCIqnYTPKVGEYATfEAIRKAFRVWESATPLRFREVPYAyireghekqADIMIFFAEGFHGdstpfdgeg 194
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEER-EAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726  195 GFLAHAYFPGpnigGDTHFDsAEPWTVRnedlngndiFLVAVHELGHALGLEHSNDPSA---IMAPFYQWMDTENFVLPD 271
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|..
gi 1149122726  272 DDRRGIQQLYGS 283
Cdd:smart00235 128 DDSLGIPYDYGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 122-282 3.75e-18

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: 81.73  E-value: 3.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 122 ITFCIQNYTPKVGEYAT--FEAIRKAFRVWESATPLRFREVPyayireGHEKQADIMIFFaegfhGDSTPFDGEGGFLAH 199
Cdd:cd04279     4 IRVYIDPTPAPPDSRAQswLQAVKQAAAEWENVGPLKFVYNP------EEDNDADIVIFF-----DRPPPVGGAGGGLAR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 200 AYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSND-PSAIMAPFYQWMDTENFVLPDDDRRGIQ 278
Cdd:cd04279    73 AGFPLISDGNRKLFNRTDINLGPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLK 152


                  ....
gi 1149122726 279 QLYG 282
Cdd:cd04279   153 RLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 140-282 1.39e-16

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: 78.23  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 140 EAIRKAFRVWESATPLRFREVPYayireghEKQADIMIffaegfhGDSTpfDGEGGFLAHAYFPGPNI----GGDTHFDS 215
Cdd:cd04277    37 AAARDALEAWEDVADIDFVEVSD-------NSGADIRF-------GNSS--DPDGNTAGYAYYPGSGSgtayGGDIWFNS 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 216 AEPWtvrNEDLNGNDIFLVAVHELGHALGLEHSND-----PSAIMAPFYQWMDT-------------ENFVLPDD----D 273
Cdd:cd04277   101 SYDT---NSDSPGSYGYQTIIHEIGHALGLEHPGDynggdPVPPTYALDSREYTvmsynsgygngasAGGGYPQTpmllD 177


                  ....*....
gi 1149122726 274 RRGIQQLYG 282
Cdd:cd04277   178 IAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 140-293 6.33e-12

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: 64.08  E-value: 6.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 140 EAIRKAFRVWESATPLRFREVPyayireGHEKQADIMIFFaegfhgdsTPFDGEGGFLAHAYFPGPNIGGdthfdSAEPW 219
Cdd:cd00203    25 SLILIAMQIWRDYLNIRFVLVG------VEIDKADIAILV--------TRQDFDGGTGGWAYLGRVCDSL-----RGVGV 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149122726 220 TVRNEdLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENfvlPDDDRRGIQQlYGSESGFPTKMPP 293
Cdd:cd00203    86 LQDNQ-SGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDTLNA---EDDDYYSVMS-YTKGSFSDGQRKD 154
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 366-409 3.74e-10

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: 55.33  E-value: 3.74e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1149122726  366 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLP 409
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 413-458 5.75e-10

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: 54.94  E-value: 5.75e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1149122726  413 IDAAlFWMPNGKTYFFRGNKYYRFNEELraVDSEYPKNI-KVWEGIP 458
Cdd:smart00120   1 IDAA-FELRDGKTYFFKGDKYWRFDPKR--VDPGYPKLIsSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 366-409 8.26e-10

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: 54.11  E-value: 8.26e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1149122726 366 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELgRGLP 409
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 413-458 1.84e-09

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: 53.34  E-value: 1.84e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1149122726 413 IDAALFWmPNGKTYFFRGNKYYRFNEElrAVDSEYPKNIKVWEGIP 458
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQ--RVEPGYPKLISDFPGLP 43
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 120-254 3.68e-09

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: 55.97  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149122726 120 NEITFCIQNYTPKvgeyATFEAIRKAFRVWESATPLRFREVpyayiREGHekQADIMIFFAEGFHGDstpfDGEGGFLAH 199
Cdd:cd04268     2 KPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNA-----NDVD--PADIRYSVIRWIPYN----DGTWSYGPS 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1149122726 200 AYFPGpniGGDTHFDSAEPWTVRNEdLNGNDIFLVAVHELGHALGLEHSNDPSAI 254
Cdd:cd04268    67 QVDPL---TGEILLARVYLYSSFVE-YSGARLRNTAEHELGHALGLRHNFAASDR 117
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 558-580 5.39e-09

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


Pssm-ID: 463374  Cd Length: 72  Bit Score: 52.71  E-value: 5.39e-09
                          10        20
                  ....*....|....*....|...
gi 1149122726 558 FFFRRHGTPKRLLYCQRSLLDKV 580
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-86 6.12e-09

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: 52.13  E-value: 6.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1149122726  34 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQRFYGLRVTGKADADTMKAM 86
Cdd:pfam01471   9 QRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 321-363 1.02e-06

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: 45.64  E-value: 1.02e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1149122726 321 FDTVAMLR-GEMFVFKERWFWRVRKNQVMDGYPMPIGQFwRGLP 363
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 321-363 1.59e-06

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: 44.93  E-value: 1.59e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1149122726  321 FDTVAMLR-GEMFVFKERWFWRVRKNQVMDGYPMPIGQFWRGLP 363
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 472-508 4.50e-06

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: 43.77  E-value: 4.50e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1149122726  472 FTYFYKGNKYWKFNNQklKVEPGYPKSALRDWMGCPS 508
Cdd:smart00120  11 KTYFFKGDKYWRFDPK--RVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 472-506 8.94e-06

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: 42.94  E-value: 8.94e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1149122726 472 FTYFYKGNKYWKFNNQklKVEPGYPKSALRD-WMGC 506
Cdd:pfam00045  11 KTYFFKGRKYWRFDPQ--RVEPGYPKLISDFpGLPC 44
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
235-255 1.79e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.61  E-value: 1.79e-04
                          10        20
                  ....*....|....*....|.
gi 1149122726 235 AVHELGHALGLEHSNDPSAIM 255
Cdd:NF033823  126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
234-257 5.00e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 5.00e-04
                          10        20
                  ....*....|....*....|....
gi 1149122726 234 VAVHELGHALGLEHSNDPSAIMAP 257
Cdd:COG1913   126 EAVHELGHLFGLGHCPNPRCVMHF 149
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 35-88 5.44e-04

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 38.74  E-value: 5.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149122726  35 AWLQQYGYLPP---GDLRTHTQrspqslsAAIAAMQRFYGLRVTGKADADTMKAMRR 88
Cdd:COG3409    20 QRLNALGYYPGpvdGIFGPATE-------AAVRAFQRANGLPVDGIVGPATWAALRA 69
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 234-276 1.08e-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: 40.36  E-value: 1.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1149122726 234 VAVHELGHALGLEHSNDPSAIMapfyqwmdteNFV--LPDDDRRG 276
Cdd:cd11375   126 EAVHELGHLFGLDHCPYYACVM----------NFSnsLEETDRKP 160
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 228-257 1.96e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 40.05  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1149122726 228 GNDIFLVAVHELGHALGLE-HSNDPSAIMAP 257
Cdd:COG5549   179 GKYLLATARHELGHALGIWgHSPSPTDAMYF 209
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 235-255 2.03e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.62  E-value: 2.03e-03
                          10        20
                  ....*....|....*....|.
gi 1149122726 235 AVHELGHALGLEHSNDPSAIM 255
Cdd:PRK13267  129 VTHELGHTLGLEHCDNPRCVM 149
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 223-258 8.90e-03

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 37.59  E-value: 8.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1149122726 223 NEDLNGNdIFLVAV---HELGHALGLEHSN------DPSAIMAPF 258
Cdd:cd04269   121 VQDHSRN-LLLFAVtmaHELGHNLGMEHDDggctcgRSTCIMAPS 164
 
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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