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Conserved domains on  [gi|4826834|ref|NP_004986|]
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matrix metalloproteinase-14 preproprotein [Homo sapiens]

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 ...
 118-284 5.15e-90

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: 274.49  E-value: 5.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834    118 KWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAyireghekQADIMIFFAEGFHGDSTPFDGEGG 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834    198 FLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRR 277
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 4826834    278 GIQQLYG 284
Cdd:pfam00413 153 GIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 316-508 7.18e-78

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: 244.53  E-value: 7.18e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  316 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRNNqVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 393
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  394 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 472
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4826834  473 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 508
Cdd:cd00094 160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 super family cl13321
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 560-582 2.33e-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: 53.86  E-value: 2.33e-09
                          10        20
                  ....*....|....*....|...
gi 4826834    560 FFFRRHGTPRRLLYCQRSLLDKV 582
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 36-88 3.38e-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: 52.90  E-value: 3.38e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4826834     36 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAM 88
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 ...
 118-284 5.15e-90

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: 274.49  E-value: 5.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834    118 KWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAyireghekQADIMIFFAEGFHGDSTPFDGEGG 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834    198 FLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRR 277
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 4826834    278 GIQQLYG 284
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-284 1.30e-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: 252.51  E-value: 1.30e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  118 KWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAyiregheKQADIMIFFAEGFHGDSTPFDGEGG 197
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-------QEADIRISFARGNHGDGYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  198 FLAHAYFPGPnIGGDTHFDSAEPWTVRNEDlNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTeNFVLPDDDRR 277
Cdd:cd04278  74 TLAHAFFPGG-IGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                ....*..
gi 4826834  278 GIQQLYG 284
Cdd:cd04278 151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 316-508 7.18e-78

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: 244.53  E-value: 7.18e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  316 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRNNqVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 393
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  394 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 472
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4826834  473 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 508
Cdd:cd00094 160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 117-284 5.41e-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: 5.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834     117 LKWQHNEITFCIqnYTPKVGEYAtYEAIRKAFRVWESATPLRFREVPYAyireghekqADIMIFFAEGFHGdstpfdgeg 196
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834     197 GFLAHAYFPGpnigGDTHFDsAEPWTVRnedlngndiFLVAVHELGHALGLEHSSDPSA---IMAPFYQWMDTENFVLPD 273
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|.
gi 4826834     274 DDRRGIQQLYG 284
Cdd:smart00235 128 DDSLGIPYDYG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-411 2.44e-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: 55.71  E-value: 2.44e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4826834     368 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLP 411
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-411 5.50e-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: 54.88  E-value: 5.50e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4826834    368 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELgRGLP 411
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 560-582 2.33e-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: 53.86  E-value: 2.33e-09
                          10        20
                  ....*....|....*....|...
gi 4826834    560 FFFRRHGTPRRLLYCQRSLLDKV 582
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 36-88 3.38e-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: 52.90  E-value: 3.38e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4826834     36 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAM 88
Cdd:pfam01471   9 QRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
237-257 1.26e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.99  E-value: 1.26e-04
                         10        20
                 ....*....|....*....|.
gi 4826834   237 AVHELGHALGLEHSSDPSAIM 257
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
236-259 6.23e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 6.23e-04
                        10        20
                ....*....|....*....|....
gi 4826834  236 VAVHELGHALGLEHSSDPSAIMAP 259
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 37-90 7.12e-04

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 38.35  E-value: 7.12e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4826834   37 AWLQQYGYLPP---GDLRTHTQrspqslsAAIAAMQKFYGLQVTGKADADTMKAMRR 90
Cdd:COG3409  20 QRLNALGYYPGpvdGIFGPATE-------AAVRAFQRANGLPVDGIVGPATWAALRA 69
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 237-257 8.80e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 37.69  E-value: 8.80e-03
                         10        20
                 ....*....|....*....|.
gi 4826834   237 AVHELGHALGLEHSSDPSAIM 257
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 ...
 118-284 5.15e-90

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: 274.49  E-value: 5.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834    118 KWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAyireghekQADIMIFFAEGFHGDSTPFDGEGG 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834    198 FLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRR 277
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 4826834    278 GIQQLYG 284
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-284 1.30e-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: 252.51  E-value: 1.30e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  118 KWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAyiregheKQADIMIFFAEGFHGDSTPFDGEGG 197
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-------QEADIRISFARGNHGDGYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  198 FLAHAYFPGPnIGGDTHFDSAEPWTVRNEDlNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTeNFVLPDDDRR 277
Cdd:cd04278  74 TLAHAFFPGG-IGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                ....*..
gi 4826834  278 GIQQLYG 284
Cdd:cd04278 151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 316-508 7.18e-78

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: 244.53  E-value: 7.18e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  316 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRNNqVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 393
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  394 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 472
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4826834  473 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 508
Cdd:cd00094 160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 117-284 5.41e-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: 5.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834     117 LKWQHNEITFCIqnYTPKVGEYAtYEAIRKAFRVWESATPLRFREVPYAyireghekqADIMIFFAEGFHGdstpfdgeg 196
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834     197 GFLAHAYFPGpnigGDTHFDsAEPWTVRnedlngndiFLVAVHELGHALGLEHSSDPSA---IMAPFYQWMDTENFVLPD 273
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|.
gi 4826834     274 DDRRGIQQLYG 284
Cdd:smart00235 128 DDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 124-284 2.37e-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: 82.12  E-value: 2.37e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  124 ITFCIQNYTPKVGEYAT--YEAIRKAFRVWESATPLRFREVPyayireGHEKQADIMIFFaegfhGDSTPFDGEGGFLAH 201
Cdd:cd04279   4 IRVYIDPTPAPPDSRAQswLQAVKQAAAEWENVGPLKFVYNP------EEDNDADIVIFF-----DRPPPVGGAGGGLAR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  202 AYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSD-PSAIMAPFYQWMDTENFVLPDDDRRGIQ 280
Cdd:cd04279  73 AGFPLISDGNRKLFNRTDINLGPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLK 152


                ....
gi 4826834  281 QLYG 284
Cdd:cd04279 153 RLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 139-284 2.12e-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: 77.46  E-value: 2.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  139 ATYEAIRKAFRVWESATPLRFREVPYayireghEKQADIMIffaegfhGDSTpfDGEGGFLAHAYFPGPNI----GGDTH 214
Cdd:cd04277  34 AQQAAARDALEAWEDVADIDFVEVSD-------NSGADIRF-------GNSS--DPDGNTAGYAYYPGSGSgtayGGDIW 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  215 FDSAEPWtvrNEDLNGNDIFLVAVHELGHALGLEHS-----SDPSAIMAPFYQWMDT-------------ENFVLPD--- 273
Cdd:cd04277  98 FNSSYDT---NSDSPGSYGYQTIIHEIGHALGLEHPgdyngGDPVPPTYALDSREYTvmsynsgygngasAGGGYPQtpm 174

                       170
                ....*....|..
gi 4826834  274 -DDRRGIQQLYG 284
Cdd:cd04277 175 lLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 141-283 2.09e-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: 65.62  E-value: 2.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  141 YEAIRKAFRVWESATPLRFREVPyayireGHEKQADIMIFFaegfhgdsTPFDGEGGFLAHAYFPGPNIGGdthfdSAEP 220
Cdd:cd00203  24 QSLILIAMQIWRDYLNIRFVLVG------VEIDKADIAILV--------TRQDFDGGTGGWAYLGRVCDSL-----RGVG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  221 WTVRNEdLNGNDIFLVAVHELGHALGLEHSSDPSA--------------------IMAPFY-QWMDTENFVLPDDDRRGI 279
Cdd:cd00203  85 VLQDNQ-SGTKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQI 163


                ....
gi 4826834  280 QQLY 283
Cdd:cd00203 164 NKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-411 2.44e-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: 55.71  E-value: 2.44e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4826834     368 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLP 411
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 415-460 3.37e-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: 3.37e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 4826834     415 IDAAlFWMPNGKTYFFRGNKYYRFNEELraVDSEYPKNI-KVWEGIP 460
Cdd:smart00120   1 IDAA-FELRDGKTYFFKGDKYWRFDPKR--VDPGYPKLIsSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-411 5.50e-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: 54.88  E-value: 5.50e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4826834    368 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELgRGLP 411
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 415-460 1.14e-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: 53.72  E-value: 1.14e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 4826834    415 IDAALFWmPNGKTYFFRGNKYYRFNEElrAVDSEYPKNIKVWEGIP 460
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQ--RVEPGYPKLISDFPGLP 43
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 122-256 1.42e-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: 57.12  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826834  122 NEITFCIQNYTPKvgeyATYEAIRKAFRVWESATPLRFREVpyayiREGHekQADIMIFFAEGFHGDstpfDGEGGFLAH 201
Cdd:cd04268   2 KPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNA-----NDVD--PADIRYSVIRWIPYN----DGTWSYGPS 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4826834  202 AYFPGpniGGDTHFDSAEPWTVRNEdLNGNDIFLVAVHELGHALGLEHSSDPSAI 256
Cdd:cd04268  67 QVDPL---TGEILLARVYLYSSFVE-YSGARLRNTAEHELGHALGLRHNFAASDR 117
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 560-582 2.33e-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: 53.86  E-value: 2.33e-09
                          10        20
                  ....*....|....*....|...
gi 4826834    560 FFFRRHGTPRRLLYCQRSLLDKV 582
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 36-88 3.38e-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: 52.90  E-value: 3.38e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4826834     36 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAM 88
Cdd:pfam01471   9 QRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 323-365 7.27e-08

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: 48.72  E-value: 7.27e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4826834    323 FDTVAMLR-GEMFVFKERWFWRVRNNQVMDGYPMPIGQFwRGLP 365
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 323-365 2.12e-07

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: 47.62  E-value: 2.12e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4826834     323 FDTVAMLR-GEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLP 365
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 474-510 3.08e-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: 44.16  E-value: 3.08e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 4826834     474 FTYFYKGNKYWKFNNQklKVEPGYPKSALRDWMGCPS 510
Cdd:smart00120  11 KTYFFKGDKYWRFDPK--RVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 474-508 6.37e-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: 43.32  E-value: 6.37e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 4826834    474 FTYFYKGNKYWKFNNQklKVEPGYPKSALRD-WMGC 508
Cdd:pfam00045  11 KTYFFKGRKYWRFDPQ--RVEPGYPKLISDFpGLPC 44
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
237-257 1.26e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.99  E-value: 1.26e-04
                         10        20
                 ....*....|....*....|.
gi 4826834   237 AVHELGHALGLEHSSDPSAIM 257
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
236-259 6.23e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 6.23e-04
                        10        20
                ....*....|....*....|....
gi 4826834  236 VAVHELGHALGLEHSSDPSAIMAP 259
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 236-278 6.40e-04

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: 40.74  E-value: 6.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 4826834  236 VAVHELGHALGLEHSSDPSAIMapfyqwmdteNFV--LPDDDRRG 278
Cdd:cd11375 126 EAVHELGHLFGLDHCPYYACVM----------NFSnsLEETDRKP 160
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 37-90 7.12e-04

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 38.35  E-value: 7.12e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4826834   37 AWLQQYGYLPP---GDLRTHTQrspqslsAAIAAMQKFYGLQVTGKADADTMKAMRR 90
Cdd:COG3409  20 QRLNALGYYPGpvdGIFGPATE-------AAVRAFQRANGLPVDGIVGPATWAALRA 69
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 230-259 3.12e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 39.67  E-value: 3.12e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 4826834  230 GNDIFLVAVHELGHALGLE-HSSDPSAIMAP 259
Cdd:COG5549 179 GKYLLATARHELGHALGIWgHSPSPTDAMYF 209
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 237-257 8.80e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 37.69  E-value: 8.80e-03
                         10        20
                 ....*....|....*....|.
gi 4826834   237 AVHELGHALGLEHSSDPSAIM 257
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 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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