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Conserved domains on  [gi|13591995|ref|NP_112318|]
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matrix metalloproteinase-14 precursor [Rattus norvegicus]

Protein Classification

S41 family peptidase( domain architecture ID 12021149)

peptidase family S41 such as C-terminal processing protease (CTPase or CtpA) that contains the PDZ domain; active site consists of a serine/lysine catalytic dyad

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 3.24e-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: 274.88  E-value: 3.24e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995   118 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyireghekQADIMILFAEGFHGDSTPFDGEGG 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995   198 FLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRR 277
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 13591995   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 6.49e-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: 6.49e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 316 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRNNqVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 393
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 394 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 472
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 13591995 473 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 508
Cdd:cd00094 160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 36-88 2.49e-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: 53.29  E-value: 2.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13591995    36 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQRFYGLQVTGKADSDTMKAM 88
Cdd:pfam01471   9 QRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
DUF3377 super family cl13321
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 560-582 5.41e-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: 5.41e-09
                          10        20
                  ....*....|....*....|...
gi 13591995   560 FFFRRHGTPKRLLYCQRSLLDKV 582
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
 
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 3.24e-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: 274.88  E-value: 3.24e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995   118 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyireghekQADIMILFAEGFHGDSTPFDGEGG 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995   198 FLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRR 277
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 13591995   278 GIQQLYG 284
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-284 3.12e-80

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: 249.04  E-value: 3.12e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 118 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyiregheKQADIMILFAEGFHGDSTPFDGEGG 197
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-------QEADIRISFARGNHGDGYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 198 FLAHAYFPGPnIGGDTHFDSAEPWTVQNEDlNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTeNFVLPDDDRR 277
Cdd:cd04278  74 TLAHAFFPGG-IGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                ....*..
gi 13591995 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 6.49e-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: 6.49e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 316 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRNNqVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 393
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 394 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 472
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 13591995 473 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 508
Cdd:cd00094 160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 117-285 2.37e-34

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: 126.70  E-value: 2.37e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995    117 LKWQHNEITFCIqnYTPKVGEYATfEAIRKAFRVWESATPLRFREVPYAyireghekqADIMILFAEGFHGdstpfdgeg 196
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEER-EAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995    197 GFLAHAYFPGpnigGDTHFDsAEPWTvqnedlngnDIFLVAVHELGHALGLEHSNDPSA---IMAPFYQWMDTENFVLPD 273
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGC---------INTGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|..
gi 13591995    274 DDRRGIQQLYGS 285
Cdd:smart00235 128 DDSLGIPYDYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-411 3.24e-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: 3.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 13591995    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 6.56e-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: 54.49  E-value: 6.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 13591995   368 INTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELgRGLP 411
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 36-88 2.49e-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: 53.29  E-value: 2.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13591995    36 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQRFYGLQVTGKADSDTMKAM 88
Cdd:pfam01471   9 QRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 560-582 5.41e-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: 5.41e-09
                          10        20
                  ....*....|....*....|...
gi 13591995   560 FFFRRHGTPKRLLYCQRSLLDKV 582
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
237-257 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 13591995  237 AVHELGHALGLEHSNDPSAIM 257
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
236-259 5.02e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 5.02e-04
                        10        20
                ....*....|....*....|....
gi 13591995 236 VAVHELGHALGLEHSNDPSAIMAP 259
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 37-90 7.55e-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: 7.55e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13591995  37 AWLQQYGYLPP---GDLRTHTQrspqslsAAIAAMQRFYGLQVTGKADSDTMKAMRR 90
Cdd:COG3409  20 QRLNALGYYPGpvdGIFGPATE-------AAVRAFQRANGLPVDGIVGPATWAALRA 69
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 237-257 1.76e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.62  E-value: 1.76e-03
                         10        20
                 ....*....|....*....|.
gi 13591995  237 AVHELGHALGLEHSNDPSAIM 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 3.24e-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: 274.88  E-value: 3.24e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995   118 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyireghekQADIMILFAEGFHGDSTPFDGEGG 197
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995   198 FLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRR 277
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 13591995   278 GIQQLYG 284
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 118-284 3.12e-80

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: 249.04  E-value: 3.12e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 118 KWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAyiregheKQADIMILFAEGFHGDSTPFDGEGG 197
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSG-------QEADIRISFARGNHGDGYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 198 FLAHAYFPGPnIGGDTHFDSAEPWTVQNEDlNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTeNFVLPDDDRR 277
Cdd:cd04278  74 TLAHAFFPGG-IGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                ....*..
gi 13591995 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 6.49e-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: 6.49e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 316 PNICDG-NFDTVAMLRGEMFVFKERWFWRVRNNqVMDGYPMPIGQFWRGLPASINTAYERKD-GKFVFFKGDKHWVFDEA 393
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 394 SLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNI-KVWEGIPESPRGSFMGSDE 472
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 13591995 473 vFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGC 508
Cdd:cd00094 160 -YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 117-285 2.37e-34

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: 126.70  E-value: 2.37e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995    117 LKWQHNEITFCIqnYTPKVGEYATfEAIRKAFRVWESATPLRFREVPYAyireghekqADIMILFAEGFHGdstpfdgeg 196
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEER-EAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995    197 GFLAHAYFPGpnigGDTHFDsAEPWTvqnedlngnDIFLVAVHELGHALGLEHSNDPSA---IMAPFYQWMDTENFVLPD 273
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGC---------INTGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|..
gi 13591995    274 DDRRGIQQLYGS 285
Cdd:smart00235 128 DDSLGIPYDYGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 124-284 1.13e-17

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: 80.19  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 124 ITFCIQNYTPKVGEYAT--FEAIRKAFRVWESATPLRFREVPyayireGHEKQADIMILFaegfhGDSTPFDGEGGFLAH 201
Cdd:cd04279   4 IRVYIDPTPAPPDSRAQswLQAVKQAAAEWENVGPLKFVYNP------EEDNDADIVIFF-----DRPPPVGGAGGGLAR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 202 AYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSND-PSAIMAPFYQWMDTENFVLPDDDRRGIQ 280
Cdd:cd04279  73 AGFPLISDGNRKLFNRTDINLGPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLK 152


                ....
gi 13591995 281 QLYG 284
Cdd:cd04279 153 RLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 142-284 2.21e-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: 2.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 142 EAIRKAFRVWESATPLRFREVPYayireghEKQADIMIlfaegfhGDSTpfDGEGGFLAHAYFPGPNI----GGDTHFDS 217
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSD-------NSGADIRF-------GNSS--DPDGNTAGYAYYPGSGSgtayGGDIWFNS 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 218 AEpwtVQNEDLNGNDIFLVAVHELGHALGLEHSND-----PSAIMAPFYQWMDT-------------ENFVLPD----DD 275
Cdd:cd04277 101 SY---DTNSDSPGSYGYQTIIHEIGHALGLEHPGDynggdPVPPTYALDSREYTvmsynsgygngasAGGGYPQtpmlLD 177


                ....*....
gi 13591995 276 RRGIQQLYG 284
Cdd:cd04277 178 IAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 142-295 1.55e-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: 62.92  E-value: 1.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 142 EAIRKAFRVWESATPLRFREVPyayireGHEKQADIMILFaegfhgdsTPFDGEGGFLAHAYFPG--PNIGGDTHFDSAE 219
Cdd:cd00203  25 SLILIAMQIWRDYLNIRFVLVG------VEIDKADIAILV--------TRQDFDGGTGGWAYLGRvcDSLRGVGVLQDNQ 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591995 220 PWTVQNedlngndiFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENfvlPDDDRRGIQQlYGSKSGSPTKMPP 295
Cdd:cd00203  91 SGTKEG--------AQTIAHELGHALGFYHDHDRKDRDDYPTIDDTLNA---EDDDYYSVMS-YTKGSFSDGQRKD 154
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-411 3.24e-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: 3.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 13591995    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 4.89e-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: 4.89e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 13591995    415 IDAAlFWMPNGKTYFFRGNKYYRFNEEfrAVDSEYPKNI-KVWEGIP 460
Cdd:smart00120   1 IDAA-FELRDGKTYFFKGDKYWRFDPK--RVDPGYPKLIsSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 368-411 6.56e-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: 54.49  E-value: 6.56e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 13591995   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 1.45e-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: 1.45e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 13591995   415 IDAALFWmPNGKTYFFRGNKYYRFNEEfrAVDSEYPKNIKVWEGIP 460
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQ--RVEPGYPKLISDFPGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 36-88 2.49e-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: 53.29  E-value: 2.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13591995    36 EAWLQQYGYLPPGDlrthTQRSPQSLSAAIAAMQRFYGLQVTGKADSDTMKAM 88
Cdd:pfam01471   9 QRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 560-582 5.41e-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: 5.41e-09
                          10        20
                  ....*....|....*....|...
gi 13591995   560 FFFRRHGTPKRLLYCQRSLLDKV 582
Cdd:pfam11857  50 VQFQRKGTPRRLLYCKRSLQDWV 72
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 122-256 1.08e-08

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: 54.81  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591995 122 NEITFCIQNYTPKvgeyATFEAIRKAFRVWESATPLRFREVpyayiREGHekQADIMIlfaeGFHGDSTPFDGEGGFLAH 201
Cdd:cd04268   2 KPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNA-----NDVD--PADIRY----SVIRWIPYNDGTWSYGPS 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13591995 202 AYFP--GPNIGGDTHFDSaepwtvQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAI 256
Cdd:cd04268  67 QVDPltGEILLARVYLYS------SFVEYSGARLRNTAEHELGHALGLRHNFAASDR 117
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 323-365 8.59e-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: 8.59e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 13591995   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 2.73e-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: 47.24  E-value: 2.73e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 13591995    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 3.90e-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: 3.90e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 13591995    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 7.60e-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: 7.60e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 13591995   474 FTYFYKGNKYWKFNNQklKVEPGYPKSALRD-WMGC 508
Cdd:pfam00045  11 KTYFFKGRKYWRFDPQ--RVEPGYPKLISDFpGLPC 44
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
237-257 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 13591995  237 AVHELGHALGLEHSNDPSAIM 257
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
236-259 5.02e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.10  E-value: 5.02e-04
                        10        20
                ....*....|....*....|....
gi 13591995 236 VAVHELGHALGLEHSNDPSAIMAP 259
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 37-90 7.55e-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: 7.55e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13591995  37 AWLQQYGYLPP---GDLRTHTQrspqslsAAIAAMQRFYGLQVTGKADSDTMKAMRR 90
Cdd:COG3409  20 QRLNALGYYPGpvdGIFGPATE-------AAVRAFQRANGLPVDGIVGPATWAALRA 69
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 236-278 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 13591995 236 VAVHELGHALGLEHSNDPSAIMapfyqwmdteNFV--LPDDDRRG 278
Cdd:cd11375 126 EAVHELGHLFGLDHCPYYACVM----------NFSnsLEETDRKP 160
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 237-257 1.76e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.62  E-value: 1.76e-03
                         10        20
                 ....*....|....*....|.
gi 13591995  237 AVHELGHALGLEHSNDPSAIM 257
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 230-259 1.97e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 40.05  E-value: 1.97e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 13591995 230 GNDIFLVAVHELGHALGLE-HSNDPSAIMAP 259
Cdd:COG5549 179 GKYLLATARHELGHALGIWgHSPSPTDAMYF 209
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 225-260 8.94e-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: 8.94e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 13591995 225 NEDLNGNdIFLVAV---HELGHALGLEHSN------DPSAIMAPF 260
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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