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Conserved domains on  [gi|35903106|ref|NP_919395|]
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matrix metalloproteinase-14b precursor [Danio rerio]

Protein Classification

M10A family metallopeptidase( domain architecture ID 12021161)

M10A family metallopeptidase similar to matrix metalloproteinases with a C-terminal hemopexin repeat-containing domain that may be endopeptidases that degrade various components of the extracellular matrix; also contains a possible peptidoglycan binding domain at the N-terminus and a DUF3377 domain at the C-terminal end

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 ...
 111-277 4.66e-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: 272.95  E-value: 4.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   111 KWDKNEITFCIQNYTPKVGEYETFEAIRKAFKVWESVTPLRFREISYSDirdkvvdfADIMLFFADGFHGDASPFDGEGG 190
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGE--------ADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   191 FLAHAYFPGNGIGGDTHFDAAEPWTIGNKDLLGNDVFLVAVHELGHALGMEHSNDPSAIMAPFYQWMETDHFVLPDDDRK 270
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 35903106   271 GIQKLYG 277
Cdd:pfam00413 153 GIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 311-503 2.87e-72

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: 230.66  E-value: 2.87e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 311 PNICEG-HFDTIGIFRGEMFVFKGKWFWRVRNNqVMENYPMPIGHFWRGLPTDINAAYERED-GKFVFFKGDRHWVFTES 388
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 389 NLEPGYPKVLGELGTGVPKDKLDAALLYTPTGYTYFFRGNKYYRYNEDTHSVDPDYPKPISK-WQGVPDNIKAAFMSRDq 467
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETdFPGVPDKVDAAFRWLD- 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 35903106 468 GYTYFYKANKYWKFNNQLLKVEPGYPKSALKDWMGC 503
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 563-621 3.84e-25

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: 98.93  E-value: 3.84e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   563 VLIIEVEDAPSSRG-GAAAVVVPLMLLVCVIFTLGALLFFRRYGTPRRLLYCQRSLLDKV 621
Cdd:pfam11857  13 VDIVVVIDDVASGTvNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-81 1.11e-08

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: 51.36  E-value: 1.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 35903106    29 EAWLQQYGYLPP---GDLRTHTArspqsvpSAIAAMQRFYGLTVTGNLDANTLEAM 81
Cdd:pfam01471   9 QRYLNRLGYYPGpvdGYFGPSTE-------AAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 111-277 4.66e-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: 272.95  E-value: 4.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   111 KWDKNEITFCIQNYTPKVGEYETFEAIRKAFKVWESVTPLRFREISYSDirdkvvdfADIMLFFADGFHGDASPFDGEGG 190
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGE--------ADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   191 FLAHAYFPGNGIGGDTHFDAAEPWTIGNKDLLGNDVFLVAVHELGHALGMEHSNDPSAIMAPFYQWMETDHFVLPDDDRK 270
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 35903106   271 GIQKLYG 277
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 111-277 1.97e-76

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 240.18  E-value: 1.97e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 111 KWDKNEITFCIQNYTPKVGEYETFEAIRKAFKVWESVTPLRFREISYSDirdkvvdFADIMLFFADGFHGDASPFDGEGG 190
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ-------EADIRISFARGNHGDGYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 191 FLAHAYFPGnGIGGDTHFDAAEPWTIGNKDLlGNDVFLVAVHELGHALGMEHSNDPSAIMAPFYQWMETdHFVLPDDDRK 270
Cdd:cd04278  74 TLAHAFFPG-GIGGDIHFDDDEQWTLGSDSG-GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                ....*..
gi 35903106 271 GIQKLYG 277
Cdd:cd04278 151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 311-503 2.87e-72

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: 230.66  E-value: 2.87e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 311 PNICEG-HFDTIGIFRGEMFVFKGKWFWRVRNNqVMENYPMPIGHFWRGLPTDINAAYERED-GKFVFFKGDRHWVFTES 388
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 389 NLEPGYPKVLGELGTGVPKDKLDAALLYTPTGYTYFFRGNKYYRYNEDTHSVDPDYPKPISK-WQGVPDNIKAAFMSRDq 467
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETdFPGVPDKVDAAFRWLD- 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 35903106 468 GYTYFYKANKYWKFNNQLLKVEPGYPKSALKDWMGC 503
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 110-278 3.69e-33

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: 124.00  E-value: 3.69e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106    110 LKWDKNEITFCIqnYTPKVGEYETfEAIRKAFKVWESVTPLRFREISysdirdkvvDFADIMLFFADGFHGdaspfdgeg 189
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEER-EAIAKALAEWSDVTCIRFVERT---------GTADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106    190 GFLAHAYFPGngigGDTHFDAaEPWTIGNKdllgndvflVAVHELGHALGMEHSNDPSA---IMAPFYQWMETDHFVLPD 266
Cdd:smart00235  62 CTLSHAGRPG----GDQHLSL-GNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|..
gi 35903106    267 DDRKGIQKLYGP 278
Cdd:smart00235 128 DDSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 563-621 3.84e-25

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: 98.93  E-value: 3.84e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   563 VLIIEVEDAPSSRG-GAAAVVVPLMLLVCVIFTLGALLFFRRYGTPRRLLYCQRSLLDKV 621
Cdd:pfam11857  13 VDIVVVIDDVASGTvNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 363-406 4.07e-09

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: 52.24  E-value: 4.07e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 35903106    363 INAAYEREDGKFVFFKGDRHWVFTESNLEPGYPKVLGELGTGVP 406
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-81 1.11e-08

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: 51.36  E-value: 1.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 35903106    29 EAWLQQYGYLPP---GDLRTHTArspqsvpSAIAAMQRFYGLTVTGNLDANTLEAM 81
Cdd:pfam01471   9 QRYLNRLGYYPGpvdGYFGPSTE-------AAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 363-396 2.17e-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: 50.26  E-value: 2.17e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 35903106   363 INAAYEREDGKFVFFKGDRHWVFTESNLEPGYPK 396
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPK 34
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
218-250 2.54e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.14  E-value: 2.54e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 35903106  218 NKDLLGNDVFLVAVHELGHALGMEHSNDPSAIM 250
Cdd:NF033823 114 DEDLFLERLAKEAVHELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 218-250 2.54e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.24  E-value: 2.54e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 35903106  218 NKDLLGNDVFLVAVHELGHALGMEHSNDPSAIM 250
Cdd:PRK13267 117 DSELFEERVRKEVTHELGHTLGLEHCDNPRCVM 149
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 215-252 3.44e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 39.67  E-value: 3.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 35903106 215 TIG-NKDLLGNDVFLVAVHELGHALG-MEHSNDPSAIMAP 252
Cdd:COG5549 170 TILlSPNQTGKYLLATARHELGHALGiWGHSPSPTDAMYF 209
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 30-83 7.76e-03

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 35.27  E-value: 7.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35903106  30 AWLQQYGYLPP---GDLRTHTARspqsvpsAIAAMQRFYGLTVTGNLDANTLEAMKR 83
Cdd:COG3409  20 QRLNALGYYPGpvdGIFGPATEA-------AVRAFQRANGLPVDGIVGPATWAALRA 69
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 111-277 4.66e-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: 272.95  E-value: 4.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   111 KWDKNEITFCIQNYTPKVGEYETFEAIRKAFKVWESVTPLRFREISYSDirdkvvdfADIMLFFADGFHGDASPFDGEGG 190
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGE--------ADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   191 FLAHAYFPGNGIGGDTHFDAAEPWTIGNKDLLGNDVFLVAVHELGHALGMEHSNDPSAIMAPFYQWMETDHFVLPDDDRK 270
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 35903106   271 GIQKLYG 277
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 111-277 1.97e-76

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 240.18  E-value: 1.97e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 111 KWDKNEITFCIQNYTPKVGEYETFEAIRKAFKVWESVTPLRFREISYSDirdkvvdFADIMLFFADGFHGDASPFDGEGG 190
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ-------EADIRISFARGNHGDGYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 191 FLAHAYFPGnGIGGDTHFDAAEPWTIGNKDLlGNDVFLVAVHELGHALGMEHSNDPSAIMAPFYQWMETdHFVLPDDDRK 270
Cdd:cd04278  74 TLAHAFFPG-GIGGDIHFDDDEQWTLGSDSG-GTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                ....*..
gi 35903106 271 GIQKLYG 277
Cdd:cd04278 151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 311-503 2.87e-72

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: 230.66  E-value: 2.87e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 311 PNICEG-HFDTIGIFRGEMFVFKGKWFWRVRNNqVMENYPMPIGHFWRGLPTDINAAYERED-GKFVFFKGDRHWVFTES 388
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPG-KPPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 389 NLEPGYPKVLGELGTGVPKDKLDAALLYTPTGYTYFFRGNKYYRYNEDTHSVDPDYPKPISK-WQGVPDNIKAAFMSRDq 467
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETdFPGVPDKVDAAFRWLD- 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 35903106 468 GYTYFYKANKYWKFNNQLLKVEPGYPKSALKDWMGC 503
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 110-278 3.69e-33

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: 124.00  E-value: 3.69e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106    110 LKWDKNEITFCIqnYTPKVGEYETfEAIRKAFKVWESVTPLRFREISysdirdkvvDFADIMLFFADGFHGdaspfdgeg 189
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEER-EAIAKALAEWSDVTCIRFVERT---------GTADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106    190 GFLAHAYFPGngigGDTHFDAaEPWTIGNKdllgndvflVAVHELGHALGMEHSNDPSA---IMAPFYQWMETDHFVLPD 266
Cdd:smart00235  62 CTLSHAGRPG----GDQHLSL-GNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|..
gi 35903106    267 DDRKGIQKLYGP 278
Cdd:smart00235 128 DDSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 563-621 3.84e-25

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: 98.93  E-value: 3.84e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106   563 VLIIEVEDAPSSRG-GAAAVVVPLMLLVCVIFTLGALLFFRRYGTPRRLLYCQRSLLDKV 621
Cdd:pfam11857  13 VDIVVVIDDVASGTvNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 135-277 5.84e-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: 76.30  E-value: 5.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 135 EAIRKAFKVWESVTPLRFREISYSDirdkvvdFADIMLFFADGFHGdaspfdgegGFLAHAYFPGNGI----GGDTHFDA 210
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNS-------GADIRFGNSSDPDG---------NTAGYAYYPGSGSgtayGGDIWFNS 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 211 AEpwtIGNKDLLGNDVFLVAVHELGHALGMEHSND-----PSAIMAPFYQWMET-------------DHFVLPD----DD 268
Cdd:cd04277 101 SY---DTNSDSPGSYGYQTIIHEIGHALGLEHPGDynggdPVPPTYALDSREYTvmsynsgygngasAGGGYPQtpmlLD 177


                ....*....
gi 35903106 269 RKGIQKLYG 277
Cdd:cd04277 178 IAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 117-277 2.36e-14

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: 70.95  E-value: 2.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 117 ITFCIQNYTPKVGEYET--FEAIRKAFKVWESVTPLRFREISYSDIRdkvvdfADIMLFFADGFHGDASpfdgeGGFLAH 194
Cdd:cd04279   4 IRVYIDPTPAPPDSRAQswLQAVKQAAAEWENVGPLKFVYNPEEDND------ADIVIFFDRPPPVGGA-----GGGLAR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 195 AYFPGNGIGGDTHFDAAEPWtiGNKDLLGNDVFL--VAVHELGHALGMEHSND-PSAIMAPFYQWMETDHFVLPDDDRKG 271
Cdd:cd04279  73 AGFPLISDGNRKLFNRTDIN--LGPGQPRGAENLqaIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVAT 150


                ....*.
gi 35903106 272 IQKLYG 277
Cdd:cd04279 151 LKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 135-287 3.72e-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: 64.85  E-value: 3.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 135 EAIRKAFKVWESVTPLRFREisysdiRDKVVDFADIMLFFADGfhgdaspfDGEGGFLAHAYFPG--NGIGGDTHFDAAE 212
Cdd:cd00203  25 SLILIAMQIWRDYLNIRFVL------VGVEIDKADIAILVTRQ--------DFDGGTGGWAYLGRvcDSLRGVGVLQDNQ 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35903106 213 PWTignkdllgNDVFLVAVHELGHALGMEHSNDPSAImapFYQWMETDHFVLPDDDRKGIQKlYGPGSGGHPRPP 287
Cdd:cd00203  91 SGT--------KEGAQTIAHELGHALGFYHDHDRKDR---DDYPTIDDTLNAEDDDYYSVMS-YTKGSFSDGQRK 153
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 114-276 6.27e-11

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 61.36  E-value: 6.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 114 KNEITFCIQNYTPKvgEYEtfEAIRKAFKVWESVTPLRFREIsysdirdKVVDFADIMLFFADGFHGDaspfDGEGGFLA 193
Cdd:cd04268   1 KKPITYYIDDSVPD--KLR--AAILDAIEAWNKAFAIGFKNA-------NDVDPADIRYSVIRWIPYN----DGTWSYGP 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903106 194 HAYFPGNGiggdTHFDAAEPWTIGNKDLLGNDVFLVAVHELGHALGMEHSNDPSA----------------IM--APFYQ 255
Cdd:cd04268  66 SQVDPLTG----EILLARVYLYSSFVEYSGARLRNTAEHELGHALGLRHNFAASDrddnvdllaekgdtssVMdyAPSNF 141

                       170       180
                ....*....|....*....|....
gi 35903106 256 WMETDHFVLPD---DDRKGIQKLY 276
Cdd:cd04268 142 SIQLGDGQKYTigpYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 363-406 4.07e-09

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: 52.24  E-value: 4.07e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 35903106    363 INAAYEREDGKFVFFKGDRHWVFTESNLEPGYPKVLGELGTGVP 406
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 410-455 6.08e-09

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: 51.86  E-value: 6.08e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 35903106    410 LDAALLYtPTGYTYFFRGNKYYRYNEdtHSVDPDYPKPISK-WQGVP 455
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDP--KRVDPGYPKLISSfFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-81 1.11e-08

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: 51.36  E-value: 1.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 35903106    29 EAWLQQYGYLPP---GDLRTHTArspqsvpSAIAAMQRFYGLTVTGNLDANTLEAM 81
Cdd:pfam01471   9 QRYLNRLGYYPGpvdGYFGPSTE-------AAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 363-396 2.17e-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: 50.26  E-value: 2.17e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 35903106   363 INAAYEREDGKFVFFKGDRHWVFTESNLEPGYPK 396
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPK 34
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 410-455 4.31e-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: 49.49  E-value: 4.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 35903106   410 LDAALLYtPTGYTYFFRGNKYYRYNEDThsVDPDYPKPISKWQGVP 455
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQR--VEPGYPKLISDFPGLP 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 458-503 7.61e-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: 7.61e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 35903106   458 IKAAFMSRDqGYTYFYKANKYWKFNNQllKVEPGYPKSALKD-WMGC 503
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQ--RVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 458-502 2.64e-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: 2.64e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 35903106    458 IKAAFMSRDqGYTYFYKANKYWKFNNQllKVEPGYPKSALKDWMG 502
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPK--RVDPGYPKLISSFFPG 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 325-360 3.83e-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: 46.85  E-value: 3.83e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 35903106    325 RGEMFVFKGKWFWRVRNNQVMENYPMPIGHFWRGLP 360
Cdd:smart00120   9 DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 323-360 1.32e-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: 45.25  E-value: 1.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 35903106   323 IFRGEMFVFKGKWFWRVRNNQVMENYPMPIGHFwRGLP 360
Cdd:pfam00045   7 DRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 229-271 2.07e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 39.59  E-value: 2.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 35903106 229 VAVHELGHALGMEHSNDPSAIMapfyqwmetdHFV--LPDDDRKG 271
Cdd:cd11375 126 EAVHELGHLFGLDHCPYYACVM----------NFSnsLEETDRKP 160
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
218-250 2.54e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.14  E-value: 2.54e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 35903106  218 NKDLLGNDVFLVAVHELGHALGMEHSNDPSAIM 250
Cdd:NF033823 114 DEDLFLERLAKEAVHELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 218-250 2.54e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.24  E-value: 2.54e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 35903106  218 NKDLLGNDVFLVAVHELGHALGMEHSNDPSAIM 250
Cdd:PRK13267 117 DSELFEERVRKEVTHELGHTLGLEHCDNPRCVM 149
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 215-252 3.44e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 39.67  E-value: 3.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 35903106 215 TIG-NKDLLGNDVFLVAVHELGHALG-MEHSNDPSAIMAP 252
Cdd:COG5549 170 TILlSPNQTGKYLLATARHELGHALGiWGHSPSPTDAMYF 209
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
217-252 3.52e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.78  E-value: 3.52e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 35903106 217 GNKDLLGNDVFLVAVHELGHALGMEHSNDPSAIMAP 252
Cdd:COG1913 114 PDEELFLERVLKEAVHELGHLFGLGHCPNPRCVMHF 149
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 222-253 4.89e-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: 38.75  E-value: 4.89e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 35903106 222 LGNDVFLVAV---HELGHALGMEHSN------DPSAIMAPF 253
Cdd:cd04269 124 HSRNLLLFAVtmaHELGHNLGMEHDDggctcgRSTCIMAPS 164
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 30-83 7.76e-03

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


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 35.27  E-value: 7.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35903106  30 AWLQQYGYLPP---GDLRTHTARspqsvpsAIAAMQRFYGLTVTGNLDANTLEAMKR 83
Cdd:COG3409  20 QRLNALGYYPGpvdGIFGPATEA-------AVRAFQRANGLPVDGIVGPATWAALRA 69
 
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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